OMIM Entry - +141800 - HEMOGLOBIN--ALPHA LOCUS 1; HBA1

+141800 ICD+

ICD10CM: D56.0,
SNOMEDCT: 48553001,
SNOMEDCT: 68913001

ICD10CM: D56.0, SNOMEDCT: 48553001, SNOMEDCT: 68913001

HEMOGLOBIN--ALPHA LOCUS 1; HBA1

Alternative titles; symbols

3-PRIME ALPHA-GLOBIN GENE
MINOR ALPHA-GLOBIN LOCUS

Other entities represented in this entry:

METHEMOGLOBINEMIA, ALPHA-GLOBIN TYPE, INCLUDED

ERYTHREMIA, ALPHA-GLOBIN TYPE, INCLUDED

HGNC Approved Gene Symbol: HBA1

Cytogenetic location: 16p13.3 Genomic coordinates (GRCh37): 16:226,678 - 227,519 (from NCBI)

Gene Phenotype Relationships

Location	Phenotype	Phenotype MIM number
16p13.3	Erythremias, alpha-
	Heinz body anemias, alpha-	140700
	Hemoglobin H disease, nondeletional	613978
	Methemoglobinemias, alpha-
	Thalassemias, alpha-	604131

Clinical Synopsis

TEXT

The alpha and beta loci determine the structure of the 2 types of polypeptide chains in the tetrameric adult hemoglobin, Hb A, alpha-2/beta-2. The alpha locus also determines a polypeptide chain, the alpha chain, in fetal hemoglobin (alpha-2/gamma-2), in hemoglobin A2(alpha-2/delta-2), and in embryonic hemoglobin (alpha-2/epsilon-2). The number of normal alpha genes (3, 2, 1 or none) in Asian cases of alpha-thalassemia (604131) results in 4 different alpha-thalassemia syndromes (Kan et al., 1976). Three normal alpha genes gives a silent carrier state. Two normal alpha genes results in microcytosis (so-called heterozygous alpha-thalassemia). One normal alpha gene results in microcytosis and hemolysis (so-called Hb H disease, 613978). No normal alpha gene results in 'homozygous alpha-thalassemia' manifested as fatal hydrops fetalis.

By studies of somatic cell hybrids, Deisseroth et al. (1976) showed that the alpha and beta loci are on different chromosomes. Gandini et al. (1977) concluded, incorrectly as it turned out, that the alpha loci are on the long arm of chromosome 4 (4q28-q34). The conclusion was based on a finding of excessive synthesis of alpha chains in patients with duplication of this region. Deisseroth et al. (1977) combined the methods of somatic cell hybridization and DNA-cDNA hybridization to establish assignment of the alpha-globin locus to chromosome 16. This represents an extension of the cell hybridization method permitting mapping of genes that are not functional in the cultured cell. Weitkamp et al. (1977) presented data concerning linkage of the alpha and beta loci to 34 marker loci. Data on alpha-thalassemia, combined with those on the Hopkins-2 variant, excluded linkage of alpha and haptoglobin at a recombination fraction less than 0.15. Deisseroth and Hendrick (1978) confirmed the assignment of the alpha locus to chromosome 16 by means of cotransfer of this gene with the human APRT gene, known to be on 16 (see 102600), into mouse erythroleukemia cells. (The APRT gene is on the long arm of chromosome 16.) On the basis of findings in a case of partial trisomy 16, Wainscoat et al. (1981) concluded that the alpha-globin genes are on segment 16pter-p12. By combining somatic cell hybridization with a cDNA probe in the study of a cell line with reciprocal translocation between 16q and 11q, Koeffler et al. (1981) showed that the alpha-globin genes are on the short arm of 16. Gerhard et al. (1981) used an improved method of in situ hybridization to confirm the assignment of the alpha-globin cluster to chromosome 16p. The evidence on the precise location of HBAC is conflicting, with assignments from 16p13.33 to 16p13.11 (Reeders, 1986). The fact that adult polycystic kidney disease (APKD; 173900) is proximal to HBAC and is on the 5-prime side of HBAC appears to indicate that the order is 16cen--APKD--5-prime HBZ1--HBA1--3-prime HVR--pter. (3-prime HVR is the hypervariable region used in mapping APKD to 16p.) On the basis of the findings in a fetus with an unbalanced translocation involving 16p, Breuning et al. (1987) concluded that the HBA cluster is distal to PGP. By a combination of in situ hybridization, Southern blot analysis, and linkage analysis using the fragile site 16p12.3 and translocation breakpoints within band 16p13.1, Simmers et al. (1987) mapped the alpha-globin gene complex to 16pter-p13.2. Buckle et al. (1988) described a child in whom cytogenetic analysis indicated monosomy for 16pter-p13.3. DNA studies showed that the patient had not inherited either maternal alpha-globin allele. The child had the alpha-thalassemia trait as well as moderate mental retardation and dysmorphic features. They determined that the gene is located in the 16pter-p13.3 segment. After reviewing earlier data placing the alpha-globin cluster slightly more proximal, they concluded that the findings in this child may be more reliable.

Orkin (1978) identified alpha-globin gene fragments in restriction endonuclease digests of total DNA after electrophoresis by hybridization with P32-labeled cDNA probes. The data indicated that the alpha genes occur in duplicate and that the 2 copies lie close together. Thus direct physical evidence is provided for the duplication deduced from the findings with mutant alpha chains and with the alpha-thalassemias and the kinetics of hybridization in solution. The 2 alpha chains lie about 3.7 kilobases apart. Leder et al. (1978) presented evidence that the alpha and beta genes of all adult mammalian hemoglobins have 2 intervening sequences at analogous positions. Wilson et al. (1977) described a possible nucleotide polymorphism in the untranslated 3-prime region of the alpha-globin gene and suggested that the heterogeneity is related to the existence of 2 alpha gene loci. Musumeci et al. (1978) pointed out that the combination of alpha-thalassemia and beta-thalassemia leads to less severe clinical expression of homozygous beta-thalassemia. The rarity of a chromosome 16 with both alpha loci deleted (as demonstrated by the restriction endonuclease mapping technique of Southern) explains the rarity of severe forms of alpha-thalassemia in Africans, e.g., Hb H disease which requires loss of 3 alpha loci and homozygous alpha-thalassemia which requires loss of 4 alpha loci (Dozy et al., 1979). By restriction endonuclease mapping, Goossens et al. (1980) identified 12 persons heterozygous for a chromosome carrying 3 alpha genes. There were no hematologic abnormalities. The frequency was 0.0036 in American Blacks and 0.05 in Greek Cypriots. They had previously shown a frequency of 0.16 for the single alpha-globin locus in black Americans. The single locus had a frequency of 0.18 in Sardinians, but none of 125 Sardinians had a triple alpha locus, suggesting that the former had a selective advantage. Greek Cypriots have a frequency of 0.07 for the single alpha locus. Among 645 Japanese subjects studied, Nakashima et al. (1990) found 10 persons heterozygous for a chromosome with the triplicated alpha-globin locus. Thus, the frequency of the triplicate alpha locus was 0.008 in this population, while that of the single alpha-locus, i.e., the alpha-thalassemia-2 gene, may be lower than 0.0008. Analysis of haplotypes suggested that the triple alpha loci may have had multiple origins. Nakashima et al. (1990) commented on the fact that in Melanesia the frequency of the triplicated genotype is about the same (Flint et al., 1986) as in Japan, whereas the frequency of the single alpha gene is much higher, compatible with a selective advantage vis-a-vis malaria. Liebhaber et al. (1981) found identity of the alpha-1-globin genes from an Asian and a Caucasian. Furthermore, the alpha-1 and alpha-2 genes have a much higher degree of homology than would be predicted from the timing of the duplication before the bird-mammal divergence (about 300 Myr ago). Liebhaber et al. (1981) presented this as evidence for the existence of mechanisms for suppression of allelic polymorphisms and for exchange of genetic information within the alpha-globin gene complex. See 142200 for a discussion of gene conversion in relation to a comparably surprising homology of the 2 gamma-globin genes.

Lehmann and Carrell (1984) suggested the use of the following nomenclature for alpha-thalassemias based on the number of alpha-globin genes that are missing or abnormal: 1-alpha-thalassemia (silent type); 2-alpha-thalassemia, trans or cis (thalassemia trait); 3-alpha-thalassemia (Hb H disease); and 4-alpha-thalassemia (Hb Bart's hydrops fetalis). In this scheme, homozygous Hb Constant Spring is a 2-alpha-thalassemia which, if combined with a cis 2-alpha-thalassemia heterozygous Hb Constant Spring, gives a 3-alpha-thalassemia and results in Hb H disease. Lehmann and Carrell (1984) also proposed that the 2 alpha-globin genes be designated as 5-prime (now alpha-2) and 3-prime (now alpha-1). Liebhaber and Cash (1985) described a method for identifying whether the alpha-1 or alpha-2 locus is the site of particular alpha-globin mutations. Rubin and Kan (1985) described a sensitive method for determining how many alpha-globin genes are present. It had the advantages of not requiring restriction enzyme digestion and gel electrophoresis and using the much more stable isotope (35)S rather than 32(P) for labeling. Only a small sample of DNA is needed. Application of the approach to diagnosis of Down syndrome was proposed. Assum et al. (1985) added a fourth restriction site polymorphism in the alpha-globin gene cluster. Compared to the beta-globin cluster, the alpha-globin cluster seemed to show a poverty of DNA polymorphism; however, Higgs et al. (1986) demonstrated a remarkable degree of DNA polymorphism in the alpha-globin gene cluster. In addition, the RFLP haplotype is associated with hypervariable regions of DNA.

Pseudo-alpha-1 (HBAP1), a pseudogene, is defective in several respects, including splice junction mutations and premature termination codons. Hardison et al. (1986) identified a previously undetected pseudogene in the alpha-globin cluster. It was not detected by hybridization studies but was found only on sequence analysis. Hardison et al. (1986) suggested that 'divergent copies of a large number of genes may comprise a substantial fraction of the slowly renaturing DNA of mammalian genomes.' The newly detected pseudogene, which will be symbolized HBAP2, is only 65 bp 3-prime to the polyadenylation site of zeta-1 (HBZP). The sequence is: 5-prime--HBZ--HBZP--HBAP2--HBA2--HBA1--3-prime. (The functional Hba gene of the mouse is on chromosome 11, but pseudogenes are dispersed to other chromosomes (e.g., Hba-ps3 to mouse chromosome 15) (Popp et al., 1981; Leder et al., 1981; Eicher and Lee, 1991).)

Vandenplas et al. (1987) described a new form of alpha-0 thalassemia in a South African family ascertained through a case of Hb H disease. A novel deletion of 22.8-23.7 kb of DNA removed 3 pseudogenes as well as the alpha-2 and alpha-1 genes. Since the alpha-2-globin gene encodes the majority of alpha-globin, a thalassemic mutation of the alpha-1-globin gene would be expected to result in a less severe loss of alpha-chain synthesis.

Moi et al. (1987) described an initiation codon mutation, AUG-to-GUG, in the alpha-1-globin gene. As predicted, the degree of interference with alpha-globin synthesis was less in this mutation than in the mutation in the initiation codon of the alpha-2-globin gene (see 141850).

Hill et al. (1987) described a unique nondeletion form of Hb H disease in Papua New Guinea: all 4 alpha genes were intact. Hill et al. (1987) commented on the striking difference in the hemoglobinopathies that occur in Southeast Asia and in Melanesia. In the former area, Hb E, Hb Constant Spring, and the Southeast Asian form of deletion alpha-0-thalassemia are all common, whereas these forms have never been found in Melanesians or Polynesians.

Jarman and Higgs (1988) identified a highly polymorphic region approximately 100 kb upstream of the alpha-globin genes and referred to it as 5-prime HVR. This is a valuable genetic marker for 16p. Higgs et al. (1989) gave a comprehensive review of the molecular genetics of the alpha-globin gene cluster, including its diseases.

Hatton et al. (1990) presented evidence for the existence of an alpha-locus control region (LCRA; 152422). This would be comparable to the beta-LCR which controls expression of the beta-like genes; see 152424. Liebhaber et al. (1990) identified an individual with alpha-thalassemia in whom structurally normal alpha-globin genes were inactivated in cis by a discrete de novo 35-kb deletion located about 30 kb 5-prime to the alpha-globin gene cluster. They concluded that the deletion inactivates expression of the alpha-globin genes by removing one or more of the previously identified upstream regulatory sequences that are critical to expression of the alpha-globin genes.

Hemoglobinopathies of alpha-globin can result from missense mutations at either of the 2 alpha-globin loci, HBA1 or HBA2. Since the normal HBA1 and HBA2 genes encode an identical alpha globin, these mutants cannot be assigned to their specific loci on the basis of protein structural analysis. A clue to the encoding locus, HBA1 versus HBA2, is provided by the relative concentration of the alpha-globin mutant in the erythrocyte based on the 2- to 3-fold higher level of expression of the HBA2 gene (Liebhaber et al., 1986). However, since variables such as protein stability, efficiency of hemoglobin tetramer formation, and other factors can affect the steady-state levels of globin mutants, a definitive locus assignment must be directly determined. Cash et al. (1989) quantitated the expression of 2 alpha-globin structural mutants found in the Caribbean basin, Fort de France and Spanish Town, and showed that they are HBA1 and HBA2 mutants, respectively, on the basis of low or high expression.

Wilkie et al. (1991) described major polymorphic length variation in the terminal region of 16p (16p13.3) by physically linking the alpha-globin locus with probes to telomere-associated repeats. They found 3 alleles in which the alpha-globin genes lie 170 kb, 350 kb, or 430 kb from the telomere. The 2 most common alleles were found to contain different terminal segments, starting 145 kb distal to the alpha-globin genes. Beyond this boundary these alleles are nonhomologous, yet each contains sequences related to other, different chromosome termini. This chromosome-size polymorphism probably arose by occasional exchanges between the subtelomeric regions of nonhomologous chromosomes. Wilkie et al. (1991) raised the possibility that the high frequency of trisomy 16 may be related to this nonhomology of the 2 common 16pter alleles in their subtelomeric region.

Huisman et al. (1996) found that of the 141 codons of the alpha-globin genes (there are no sequence differences between the coding regions of the alpha-2 and alpha-1 genes), as many as 99 have been found to be mutated; for several, 3 or 4 mutations have been discovered, while 5 mutations are known for codons 23, 75, and 94, and 6 for codon 141. The mutations appear to occur at random; thus, either one of the 3 bases are replaced in the 199 known alpha-globin gene mutants.

The suggestion that alpha(+)-thalassemia has achieved a high frequency in some populations as a result of selection by malaria is based on a number of epidemiologic studies. In the southwest Pacific region, there is a striking geographic correlation between the frequency of alpha(+)-thalassemia and the endemicity of Plasmodium falciparum. Allen et al. (1997) undertook a prospective case-control study of children with severe malaria on the north coast of Papua New Guinea, where malaria transmission is intense and alpha(+)-thalassemia affects more than 90% of the population (homozygotes comprise approximately 55% and heterozygotes 37% of the population). Compared with normal children, the risk of having severe malaria was 0.40 in alpha(+)-thalassemia homozygotes and 0.66 in heterozygotes. Unexpectedly, the risk of hospital admission with infections other than malaria also was reduced to a similar degree in homozygotes (0.36) and heterozygotes (0.63). This clinical study demonstrated that a malaria resistance gene protects against disease caused by infections other than malaria. A reduction in mortality greater than that attributable directly to malaria had been observed after the prevention of malaria by insecticides, chemoprophylaxis, and insecticide-impregnated bed nets. Previous observations that direct malaria mortality cannot account for observed hemoglobin S gene frequencies suggest that the findings of this study may apply equally to other malaria resistance genes.

Fung et al. (1999) reported 3 cases of homozygous alpha-thalassemia who survived beyond the newborn period, all with hypospadias. Review of the literature identified 2 additional cases. Fung et al. (1999) suggested that the hypospadias may have been secondary to the in utero edema leading to failure of fusion of urogenital folds or due to defect or deletion of another gene at 16p13.3.

For a review of hydrops fetalis caused by alpha-thalassemia, see Chui and Waye (1998).

From work on the mouse model of alpha-thalassemia, Leder et al. (1999) demonstrated that a normal beta-globin allele can act as a modifying gene ameliorating the severity of alpha-thalassemia. They found that the phenotype of alpha-thalassemia was strongly influenced by the genetic background in which the mutation resided; when both mutant genes were on a chromosome derived from strain 129, the phenotype was severe, whereas it was mild when the gene was on a 129 chromosome and a C57BL/6 chromosome. Linkage mapping indicated that the modifying gene is very tightly linked to the beta-globin locus (lod score = 13.3). Furthermore, the severity of the phenotype correlated with the size of beta-globin-containing inclusion bodies, which accumulate in red blood cells and likely accelerate their destruction. The beta-major globin chains encoded by the 2 strains differed by 3 amino acids, one of which is a glycine-to-cysteine substitution at position 13. The cys13 should be available for interchain disulfide bridging and consequent aggregation between excess beta chains. This normal polymorphic variation between murine beta-globin chains could account for the modifying action of the unlinked beta-globin locus. Here, the variation in severity of the phenotype would not depend on a change in the ratio between alpha and beta chains but on the chemical nature of the normal beta chain, which is in excess. This work also indicated that modifying genes can be normal variants that, absent an apparent physiologic rationale, may be difficult to identify on the basis of structure alone.

De Gobbi et al. (2006) identified a pathogenetic mechanism underlying a variant form of the inherited blood disorder alpha-thalassemia. Association studies of affected individuals from Melanesia localized the disease trait to the telomeric region of human chromosome 16, which includes the alpha-globin gene cluster, but no molecular defects were detected by conventional approaches. After resequencing and using a combination of chromatin immunoprecipitation and expression analysis on a tiled oligonucleotide array, De Gobbi et al. (2006) identified a gain-of-function regulatory single-nucleotide polymorphism (rSNP) (141800.0218) in a nongenic region between the alpha-globin genes and their upstream regulatory elements. The rSNP creates a new promoter-like element that interferes with normal activation of all downstream alpha-like globin genes. De Gobbi et al. (2006) concluded that their work illustrates a strategy for distinguishing between neutral and functionally important rSNPs, and it also identifies a pathogenetic mechanism that could potentially underlie other genetic diseases.

Schoenfelder et al. (2010) found that mouse Hbb and Hba associated with hundreds of active genes from nearly all chromosomes in nuclear foci that they called 'transcription factories.' The 2 globin genes preferentially associated with a specific and partially overlapping subset of active genes. Schoenfelder et al. (2010) also noted that expression of the Hbb locus is dependent upon Klf1 (600599), while expression of the Hba locus is only partially dependent on Klf1. Immunofluorescence analysis of mouse erythroid cells showed that most Klf1 localized to the cytoplasm and that nuclear Klf1 was present in discrete sites that overlapped with RNAII foci. Klf1 knockout in mouse erythroid cells specifically disrupted the association of Klf1-regulated genes within the Hbb-associated network. Klf1 knockout more weakly disrupted interactions within the specific Hba network. Schoenfelder et al. (2010) concluded that transcriptional regulation involves a complex 3-dimensional network rather than factors acting on single genes in isolation.

N.B.: Alpha-globin variants for which it is unknown whether HBA1 or HBA2 is involved have arbitrarily been included in this entry. Carver and Kutlar (1995) listed 191 alpha-globin variants as of January 1995. The syllabus by Huisman et al. (1996) listed 199 alpha-chain hemoglobin variants as of January 1996. These included single-base mutations in the alpha-2 and alpha-1 genes as well as 2-base mutations. Not included in their syllabus were deletions in mutations that result in alpha-thalassemia, even if such a change (point mutation or frameshift) occurred in one of the coding regions of the gene. Information about the alpha-thalassemias was provided by Higgs et al. (1989).

ALLELIC VARIANTS (Selected Examples):

Table View

.0001 HEMOGLOBIN AICHI

HBA1, HIS50ARG [dbSNP:rs33967561]

See Harano et al. (1984) and Baudin et al. (1987).

.0002 HEMOGLOBIN ALBANY-GEORGIA

HEMOGLOBIN ALBANY-SUMA

HBA1, LYS11ASN [dbSNP:rs33996902]

This was found in a clinically normal black female in Albany, Georgia (Webber et al., 1983). See also Shimasaki et al. (1983).

.0003 HEMOGLOBIN ANANTHARAJ

HBA1, LYS11GLU [dbSNP:rs33938574]

See Pootrakul et al. (1975).

.0004 HEMOGLOBIN ANN ARBOR

HBA1, LEU80ARG [dbSNP:rs34071856]

See Adams et al. (1972) and Adams (1974).

.0005 HEMOGLOBIN ARYA

HBA1, ASP47ASN [dbSNP:rs34269448]

See Rahbar et al. (1975).

.0006 HEMOGLOBIN ATAGO

HBA1, ASP85TYR [dbSNP:rs33915947] [dbSNP:rs63750958]

See Fujiwara (1970) and Fujiwara et al. (1971).

.0007 HEMOGLOBIN ATTLEBORO

HBA1, SER138PRO [dbSNP:rs34011123] [dbSNP:rs63750801]

See McDonald et al. (1990).

.0008 HEMOGLOBIN AZTEC

HBA1, MET76THR [dbSNP:rs33969953]

See Shelton et al. (1985).

.0009 HEMOGLOBIN BARI

HBA1, HIS45GLN [dbSNP:rs35687532]

See Marinucci et al. (1980).

.0010 HEMOGLOBIN BEIJING

HBA1, LYS16ASN [dbSNP:rs33923844]

See Liang et al. (1982).

.0011 HEMOGLOBIN BIBBA

HBA1, LEU136PRO [dbSNP:rs34635364]

See Kleihauer et al. (1968). (This is actually an allelic variant of the HBA2 gene; see 141850.0030.)

.0012 HEMOGLOBIN BOURMEDES

HBA1, PRO37ARG [dbSNP:rs35776155]

See Dahmane-Arbane et al. (1987).

.0014 HEMOGLOBIN BROUSSAIS

HEMOGLOBIN J (BROUSSAIS)
HEMOGLOBIN TAGAWA I

HBA1, LYS90ASN [dbSNP:rs33914470]

See de Traverse et al. (1966), Yanase et al. (1968), Vella et al. (1970), and Fleming et al. (1978).

.0015 HEMOGLOBIN CATONSVILLE

HBA1, INS GLU, PRO37/GLU/THR38 [dbSNP:rs34667595]

See Virshup et al. (1988). Moo-Penn et al. (1989) identified insertion of a glutamic acid residue between proline-37 and threonine-38 in an unstable hemoglobin variant. The PCR-amplified fragment of the variant gene showed insertion of a GAA codon. In the normal alpha-globin gene cluster, GAG is the codon for glutamic acid. Moo-Penn et al. (1989) suggested that this mutation may have resulted from nonhomologous nonallelic gene conversion.

.0016 HEMOGLOBIN CHAD

HBA1, GLU23LYS [dbSNP:rs33939620]

See Boyer et al. (1968).

.0017 HEMOGLOBIN CHAPEL HILL

HBA1, ASP74GLY [dbSNP:rs33921047]

See Orringer et al. (1976).

.0018 HEMOGLOBIN CHESAPEAKE

HBA1, ARG92LEU [dbSNP:rs33991779]

See Clegg et al. (1966) and Harano et al. (1983). Polycythemia is the only clinical feature. This was the first polycythemia-producing variant to be described (Charache et al., 1966).

.0019 HEMOGLOBIN CHIAPAS

HBA1, PRO114ARG [dbSNP:rs33910377] [dbSNP:rs63750388]

See Jones et al. (1968).

.0020 HEMOGLOBIN CHICAGO

HBA1, LEU136MET [dbSNP:rs41364652]

See Bowman et al. (1986).

.0021 HEMOGLOBIN CHONGQING

HBA1, LEU2ARG [dbSNP:rs36030576] [dbSNP:rs63750585]

See Zeng et al. (1984).

.0022 HEMOGLOBIN CONTALDO

HBA1, HIS103ARG [dbSNP:rs35329201] [dbSNP:rs63750752]

Unstable hemoglobin due to disruption of hydrogen bond between alpha 103 (his) and beta 108 (asn) (Sciarratta et al., 1984).

.0023 HEMOGLOBIN CORDELE

HBA1, ASP47ALA [dbSNP:rs33944368]

See Nakatsuji et al. (1984).

.0024 HEMOGLOBIN DAGESTAN

HBA1, LYS60GLU [dbSNP:rs34259907]

See Spivak et al. (1981) and Lacombe et al. (1987).

.0025 HEMOGLOBIN DALLAS

HBA1, ASN97LYS [dbSNP:rs41338947]

See Dysert et al. (1982).

.0026 HEMOGLOBIN DANESHGAH-TEHRAN

HBA1, HIS72ARG [dbSNP:rs35859529]

See Rahbar et al. (1973) and de Weinstein et al. (1985).

.0027 HEMOGLOBIN DENMARK HILL

HBA1, PRO95ALA [dbSNP:rs33984621]

See Wiltshire et al. (1972).

.0028 HEMOGLOBIN DUAN

HBA1, ASP75ALA [dbSNP:rs33991223]

See Liang et al. (1981, 1988).

.0029 HEMOGLOBIN DUNN

HBA1, ASP6ASN [dbSNP:rs33961916]

See Jue et al. (1979) and Baklouti et al. (1988).

.0030 HEMOGLOBIN ETOBICOKE

HBA1, SER84ARG [dbSNP:rs33926206] [dbSNP:rs33996798]

See Crookston et al. (1969) and Headlee et al. (1983).

.0031 HEMOGLOBIN EVANSTON

HBA1, TRP14ARG [dbSNP:rs33964317]

Honig et al. (1982) first described Hb Evanston in 2 black families. See also Moo-Penn et al. (1983).

Harteveld et al. (2004) found this rare variant alone and in the presence of common alpha-thalassemia deletions in 3 independent Asian cases.

.0032 HEMOGLOBIN FERNDOWN

HBA1, ASP6VAL [dbSNP:rs33986902]

See Lee-Potter et al. (1981).

.0033 HEMOGLOBIN FONTAINEBLEAU

HBA1, ALA21PRO [dbSNP:rs34324664]

Wajcman et al. (1989) found this substitution in an Italian family. The substitution produced no change in the stability or oxygen binding properties of the hemoglobin molecule. The electrophoretic properties were, furthermore, identical to those of Hb A, with the exception of isoelectric focusing in which the variant migrated like Hb A1c. Hb J(Nyanza), another substitution at position alpha-21, likewise causes no hematologic disorder.

.0034 HEMOGLOBIN FORT DE FRANCE

HBA1, HIS45ARG [dbSNP:rs28928883]

See Braconnier et al. (1977). Cash et al. (1989) confirmed that this is a mutant of the HBA1 gene.

.0035 HEMOGLOBIN G (AUDHALI)

HBA1, GLU23VAL [dbSNP:rs33939421]

See Marengo-Rowe et al. (1968).

.0037 HEMOGLOBIN G (FORT WORTH)

HEMOGLOBIN FORT WORTH

HBA1, GLU27GLY [dbSNP:rs33964507]

This variant was described in 2 black families. Unusually low (5%) concentration was found in heterozygotes, perhaps because of decreased ability of the abnormal alpha chain to form dimers with beta chains. See Schneider et al. (1971) and Carstairs et al. (1985).

.0038 HEMOGLOBIN G (GEORGIA)

HBA1, PRO95LEU [dbSNP:rs33931314]

See Huisman et al. (1970).

.0039 MOVED TO 141850.0054

.0040 HEMOGLOBIN G (NORFOLK)

HBA1, ASP85ASN [dbSNP:rs33915947] [dbSNP:rs63750958]

See Cohen-Solal et al. (1975) and Lorkin et al. (1975).

.0041 HEMOGLOBIN G (PEST)

HBA1, ASP74ASN [dbSNP:rs28928875]

Hb G (Pest) and Hb J (Buda) (141850.0008), both alpha-chain mutants, occurred together in a Hungarian male with erythrocytosis. The occurrence of some normal Hb A in this man showed the existence of at least 2 alpha loci. See Brimhall et al. (1970, 1974) and Hollan et al. (1972). Using polymerase chain reaction (PCR) to amplify selectively alpha-1 and alpha-2-globin cDNAs, Mamalaki et al. (1990) then hybridized the cDNAs to synthetic oligonucleotides specific for either the normal or the mutated sequence. Using this approach, the alpha-globin structural mutants J-Buda and G-Pest were found to be encoded by the alpha-2 and the alpha-1-globin genes, respectively. The substitution in G-Pest was a change from GAC to AAC at codon 74.

.0042 HEMOGLOBIN G (TAICHUNG)

HEMOGLOBIN Q
HEMOGLOBIN Q (THAILAND)
HEMOGLOBIN MAHIDOL
HEMOGLOBIN ASABARA
HEMOGLOBIN KURASHIKI

HBA1, ASP74HIS [dbSNP:rs28928875]

See Vella et al. (1958), Gammack et al. (1961), Lie-Injo et al. (1966, 1979); Blackwell and Liu (1970), Pootrakul and Dixon (1970), Lorkin et al. (1970), Iuchi et al. (1978), and Higgs et al. (1980). Zeng et al. (1992) demonstrated that the mutation is due to a GAC-to-CAC change in codon 74 of the HBA1 gene. They developed a simple and accurate method for diagnosis of the Hb Q (Thailand) variant based on restriction enzyme analysis.

.0043 HEMOGLOBIN G (WAIMANALO)

HEMOGLOBIN AIDA

HBA1, ASP64ASN [dbSNP:rs33984024]

See Blackwell et al. (1973) and Bunn et al. (1978). Schiliro et al. (1991) found this variant in a Filipino mother and child living in Sicily. They showed no hematologic abnormalities.

.0044 HEMOGLOBIN GARDEN STATE

HBA1, ALA82ASP [dbSNP:rs34879587]

See Winter et al. (1978).

.0045 HEMOGLOBIN GRADY

HEMOGLOBIN DAKAR

HBA1, 3AA INS, 118THR-GLU-PHE119

At the time it was first studied by Huisman et al. (1974), hemoglobin Grady was unique in having an insertion of threonine-glutamic acid-phenylalanine between amino acids 118 and 119 of the alpha chain. Several hemoglobins with deletions were then known (Leiden, Lyon, Freiburg, Niteroi, Tochigi, St. Antoine, Tours and Gun Hill). Scott et al. (1981) found no evidence of an extra (fifth) alpha gene. They argued, therefore, that if, as supposed, Hb Grady arose by unequal crossing over, the event occurred between alleles rather than between the separate alpha-1 and alpha-2 loci. The glu-phe-thr insertion is a repeat of normal residues 116, 117 and 118. See Cleek et al. (1983). Substitution of glutamine for histidine at alpha 112 was thought to be the change in hemoglobin Dakar; however, on restudy the hemoglobin was found to be identical to Hb Grady (Garel et al., 1976).

.0046 HEMOGLOBIN GUANGZHOU

HEMOGLOBIN HANGZHOU

HBA1, ASP64GLY [dbSNP:rs35873730]

See Jen and Liu (1987), Zhou et al. (1987), and Li et al. (1990).

.0047 HEMOGLOBIN GUIZHOU

HEMOGLOBIN UTSUNOMIYA

HBA1, PRO77ARG [dbSNP:rs34019158]

See Hattori et al. (1985).

.0048 HEMOGLOBIN HANDA

HEMOGLOBIN MUNAKATA

HBA1, LYS90MET [dbSNP:rs33911106]

See Harano et al. (1982) and Sugihara et al. (1983).

.0049 HEMOGLOBIN HANDSWORTH

HBA1, GLY18ARG [dbSNP:rs34504387] [dbSNP:rs63750294]

See Griffiths et al. (1977), Chih-chuan et al. (1981), and Al-Awamy et al. (1985).

.0050 HEMOGLOBIN HARBIN

HBA1, LYS16MET [dbSNP:rs35210126]

See Zeng et al. (1984).

.0051 HEMOGLOBIN HEKINAN

HBA1, GLU27ASP [dbSNP:rs41530750]

See Harano et al. (1988). Using dot-blot analysis of amplified DNA with (32)p-labeled probes, Zhao et al. (1990) located the mutation in codon 27 of the minor alpha-1 globin gene and showed that the change involved a GAG (glutamic acid)-to-GAT (aspartic acid) mutation. Their patients were 3 Chinese women from Macau.

In Thailand, Ngiwsara et al. (2004) described 2 unrelated cases of compound heterozygosity for Hb Hekinan and alpha-thalassemia.

.0052 HEMOGLOBIN HIROSAKI

HBA1, PHE43LEU [dbSNP:rs41491146]

See Ohba et al. (1975, 1978).

.0053 HEMOGLOBIN HOBART

HBA1, HIS20ARG [dbSNP:rs33943087]

See Fleming et al. (1987).

.0054 HEMOGLOBIN HOPKINS 2

HBA1, HIS112ASP [dbSNP:rs34830032] [dbSNP:rs63749881]

Fast hemoglobin. See Smith and Torbert (1958), Itano and Robinson (1960), Bradley et al. (1961), Ostertag et al. (1972), Clegg and Charache (1978).

.0055 HEMOGLOBIN I

HEMOGLOBIN I (BURLINGTON)
HEMOGLOBIN I (PHILADELPHIA)
HEMOGLOBIN I (SKAMANIA)
HEMOGLOBIN I (TEXAS)

HBA1, LYS16GLU [dbSNP:rs41407250]

Fast hemoglobin. Substitution of aspartic acid for lysine at alpha 16 was first reported by Murayama (1962). However, Crick pointed out that this substitution could not be accomplished by change in one base. Restudy by Beale and Lehmann (1965) and by Schneider et al. (1966) showed substitution of glutamic acid for lysine. Hemoglobin I was thought to show sickling but this has been shown to be due to faulty technique (Schneider et al., 1967). See Rucknagel et al. (1955), Schwartz et al. (1957), Itano and Robinson (1959, 1960), Ranney et al. (1962), O'Brien et al. (1964), Thompson et al. (1965), Schneider et al. (1966), Bowman and Barnett (1967), Baur (1968), Labossiere and Vella (1971), Fleming et al. (1978), and Liebhaber et al. (1984). The hemoglobin I mutation is curious in that the mutation is present in HBA2 (141850.0011) as well as in HBA1.

.0057 HEMOGLOBIN IWATA

HBA1, HIS87ARG [dbSNP:rs33976776]

See Shibata et al. (1980) and Liu et al. (1983).

.0058 HEMOGLOBIN J (ABIDJAN)

HBA1, GLY51ASP [dbSNP:rs35934411]

See Cabannes et al. (1972).

.0059 HEMOGLOBIN J (ANATOLIA)

HBA1, LYS61THR [dbSNP:rs41381645]

See Giordano et al. (1990).

.0060 HEMOGLOBIN J (BIRMINGHAM)

HEMOGLOBIN J (MEERUT)

HBA1, ALA120GLU [dbSNP:rs36075744] [dbSNP:rs63749927]

See Kamuzora and Lehmann (1974) and Blackwell et al. (1974).

.0062 HEMOGLOBIN J (CAMAGUEY)

HBA1, ARG141GLY [dbSNP:rs33991910] [dbSNP:rs63750134]

See Martinez et al. (1978). Romero et al. (1995) found this hemoglobin variant in 3 Spanish families. The original description by Martinez et al. (1978) was in a Cuban family of Spanish ancestry.

.0063 HEMOGLOBIN J (CAPE TOWN)

HBA1, ARG92GLN [dbSNP:rs33991779]

See Botha et al. (1966), Harano et al. (1983), and Lambridis et al. (1986).

.0064 HEMOGLOBIN J (CUBUJUQUI)

HBA1, ARG141SER [dbSNP:rs33991910] [dbSNP:rs63750134]

See Saenz et al. (1977) and Moo-Penn et al. (1981).

.0065 HEMOGLOBIN J (HABANA)

HBA1, ALA71GLU [dbSNP:rs3180281]

See Colombo et al. (1974) and Ohba et al. (1983).

.0066 HEMOGLOBIN J (KUROSH)

HBA1, ALA19ASP

See Rahbar et al. (1976).

.0067 HEMOGLOBIN J (MEDELLIN)

HBA1, GLY22ASP [dbSNP:rs34608326]

See Gottlieb et al. (1964).

.0068 HEMOGLOBIN J (NYANZA)

HBA1, ALA21ASP [dbSNP:rs11548605]

See Kendall et al. (1973).

.0070 HEMOGLOBIN J (PARIS 1)

HEMOGLOBIN J (ALJEZUR)

HBA1, ALA12ASP [dbSNP:rs35615982]

See Rosa et al. (1966), Trincao et al. (1968), and Marinucci et al. (1979).

.0071 HEMOGLOBIN J (RAJAPPEN)

HBA1, LYS90THR [dbSNP:rs33911106]

See Hyde et al. (1971).

.0072 HEMOGLOBIN J (ROVIGO)

HBA1, ALA53ASP [dbSNP:rs34574239]

See Alberti et al. (1974) and Moo-Penn et al. (1978).

.0074 HEMOGLOBIN J (SINGA)

HBA1, ASN78ASP [dbSNP:rs33964623]

See Wong et al. (1984).

.0075 HEMOGLOBIN J (SINGAPORE)

HBA1, ASN78ASP AND ALA79GLY [dbSNP:rs35692096]

Since no simple frameshift mechanism could be imagined, the possibility of 2 separate mutations was favored by Blackwell et al. (1972), who suggested that 2 separate hemoglobins, appropriately called Hb J (Singa) and Hb J (Pore), will be discovered eventually. Double mutation on the same chromosome would seem more likely than crossing-over in a compound heterozygote since the 2 codons involved are contiguous.

.0076 HEMOGLOBIN J (TASHIKUERGAN)

HBA1, ALA19GLU [dbSNP:rs35628685]

See Houjun et al. (1984). Li et al. (1990) found this variant in populations in the Silk Road region of China.

.0077 HEMOGLOBIN J (TONGARIKI)

HBA1, ALA115ASP [dbSNP:rs34204059] [dbSNP:rs63750290]

See Gajdusek et al. (1967) and Beaven et al. (1972). A homozygous individual had only anomalous hemoglobin suggesting the existence of only one alpha locus in Melanesians (Abramson et al., 1970).

.0078 HEMOGLOBIN J (TORONTO)

HBA1, ALA5ASP [dbSNP:rs34090856]

See Crookston et al. (1965).

.0079 HEMOGLOBIN JACKSON

HBA1, LYS127ASN [dbSNP:rs33972894] [dbSNP:rs63749865]

See Moo-Penn et al. (1976).

.0080 HEMOGLOBIN KARACHI

HBA1, ALA5PRO [dbSNP:rs34751764]

See Ahmad et al. (1986).

.0081 HEMOGLOBIN KARIYA

HBA1, LYS40GLU [dbSNP:rs34492931]

See Harano et al. (1983) and Imai et al. (1989).

.0082 HEMOGLOBIN KAWACHI

HBA1, PRO44ARG [dbSNP:rs33978134]

See Harano et al. (1982).

.0083 HEMOGLOBIN KOELLIKER

HEMOGLOBIN F (KOELLIKER)

HBA1, ARG141DEL

Not a genetic change. The C-terminal amino acid, 141, of the alpha chain (arginine) is missing, probably from the action of a carboxypeptidase present in normal plasma. This unusual fast hemoglobin is observed in persons with hemolysis. The change can occur in fetal hemoglobin also (Kohne et al., 1977). See Marti et al. (1967) and Schiliro et al. (1982).

.0084 HEMOGLOBIN KOKURA

HEMOGLOBIN BEILINSON
HEMOGLOBIN MICHIGAN-I
HEMOGLOBIN MICHIGAN-II
HEMOGLOBIN L (GASLINI)
HEMOGLOBIN TAGAWA II
HEMOGLOBIN UMI
HEMOGLOBIN MUGINO
HEMOGLOBIN YUKUHASHI-2

HBA1, ASP47GLY [dbSNP:rs33944368]

See Yamaoka et al. (1960), Ooya et al. (1961), Sumida (1975), and Ohba et al. (1982). The change is in TP IV (DeVries et al., 1963).

.0086 HEMOGLOBIN L (PERSIAN GULF)

HBA1, GLY57ARG [dbSNP:rs35252931]

See Rahbar et al. (1969).

.0087 HEMOGLOBIN LEGNANO

HBA1, ARG141LEU [dbSNP:rs33935328] [dbSNP:rs63751282]

See Mavilio et al. (1978).

.0088 HEMOGLOBIN LE LAMENTIN

HBA1, HIS20GLN [dbSNP:rs41525149]

See Sellaye et al. (1982), Harano et al. (1983), and Malcorra-Azpiazu et al. (1988).

.0089 HEMOGLOBIN LILLE

HBA1, ASP74ALA [dbSNP:rs33921047]

See Djoumessi et al. (1981) and Lu et al. (1984).

.0090 HEMOGLOBIN LOIRE

HBA1, ALA88SER [dbSNP:rs35239527]

This variant was discovered in a 10-year-old Algerian boy born in Loire. The child had erythrocytosis and microcytosis, the latter being due to iron deficiency (Baklouti et al., 1988).

.0091 HEMOGLOBIN LUXEMBOURG

HBA1, TYR24HIS [dbSNP:rs34743106]

Groff et al. (1989) found this substitution in association with mild hemolytic anemia and increased indirect bilirubinemia in a family originating from the Netherlands.

.0092 HEMOGLOBIN M (BOSTON)

HEMOGLOBIN GOTHENBURG
HEMOGLOBIN M (GOTHENBURG)
HEMOGLOBIN M (OSAKA)
HEMOGLOBIN M (KISKUNHALAS)

HBA1, HIS58TYR [dbSNP:rs35213748]

The aberrant hemoglobins associated with methemoglobinemia are referred to as hemoglobin M. Most of the hemoglobin M variants have substitutions of histidine at alpha 58, alpha 87, beta 63, or beta 92. These 4 amino acids are critical to the binding of the heme group. The exception is hemoglobin M (Milwaukee-1). See Gerald et al. (1957), Hansen et al. (1960), Gerald and Efron (1961), Betke (1962), Hayashi et al. (1964), Shimizu et al. (1965), Suzuki et al. (1965), Hollan et al. (1967), and Pulsinelli et al. (1973).

.0093 HEMOGLOBIN M (IWATE)

HEMOGLOBIN M (KANKAKEE)
HEMOGLOBIN M (OLDENBURG)
HEMOGLOBIN M (SENDAI)

HBA1, HIS87TYR [dbSNP:rs28928876]

Hb Iwate was the first variant hemoglobin found in Japan (Shibata et al., 1960). Familial cyanosis had been recognized for about 200 years in the prefecture of Iwate in Honshu, where about 70 affected persons were identified in the 1950s. It was called 'kuchikuro,' or 'blackmouth.' In each form of methemoglobinemia, the heme iron is stabilized in the ferric form. Patients with the Hb M alpha forms are cyanotic at birth; those with the Hb M beta forms are usually not cyanotic until they are 3 months of age. Horst et al. (1987) showed that the Iwate mutation involves the alpha-1 globin gene. Specifically, they demonstrated a CAC-to-TAC mutation in codon 87 of that gene. They showed that the Iwate mutation can be identified directly on RsaI digestion. See Meyering et al. (1960), Shibata et al. (1961), Gerald and Efron (1961), Miyaji et al. (1962), Heller (1962), Heller et al. (1962), Tonz et al. (1962), Shibata (1964), Tamura (1964), Shimizu et al. (1965), Pik and Tonz (1966), Maggio et al. (1981), and Mayne et al. (1986).

Ameri et al. (1999) likewise determined that the molecular defect in 2 patients with Hb M (Kankakee) was his87 to tyr in the HBA1 gene. The proportion of Hb M (Kankakee) observed was higher than that predicted for an alpha-1-globin variant. They presented evidence suggesting that the greater-than-expected proportion of Hb M (Kankakee) results from preferential association of the electronegative beta-globin chains with the alpha-(M)-globin chains that are more electropositive than normal alpha-globin chains.

.0094 MOVED TO 141850.0047

.0095 HEMOGLOBIN MATSUE-OKI

HBA1, ASP75ASN [dbSNP:rs33977363]

See Ohba et al. (1977) and Yi-Tao et al. (1982).

.0096 HEMOGLOBIN MEMPHIS

HBA1, GLU23GLN [dbSNP:rs33939620]

Substitution of glutamine for glutamic acid at alpha 23. A hemoglobin S homozygote who also carries this abnormal hemoglobin has a mild form of sickle cell anemia. See Kraus et al. (1965, 1967) and Cooper et al. (1973).

.0097 HEMOGLOBIN MEXICO

HEMOGLOBIN J
HEMOGLOBIN J (MEXICO)
HEMOGLOBIN J (PARIS 2)
HEMOGLOBIN UPPSALA

HBA1, GLN54GLU [dbSNP:rs35317336]

Fast hemoglobin. See Jones et al. (1963, 1968), Beckman et al. (1966), Labie and Rosa (1966), Quattrin and Ventruto (1967), Fessas et al. (1969), and Trabuchet et al. (1982).

.0098 HEMOGLOBIN MILLEDGEVILLE

HBA1, PRO44LEU [dbSNP:rs33978134]

See Honig et al. (1980).

.0099 HEMOGLOBIN MIYANO

HBA1, THR41SER [dbSNP:rs34462388] [dbSNP:rs34890875]

See Ohba et al. (1989).

.0100 HEMOGLOBIN MIZUSHI

HBA1, ASP75GLY [dbSNP:rs33991223]

No hematologic abnormality. See Iuchi et al. (1980).

.0101 HEMOGLOBIN MOABIT

HBA1, LEU86ARG [dbSNP:rs35548338]

See Knuth et al. (1979).

.0104 HEMOGLOBIN NECKER ENFANTS-MALADES

HBA1, HIS20TYR [dbSNP:rs34708054]

This variant was detected by chromatography in the course of screening diabetics for Hb A1c (Wajcman et al., 1980).

.0105 HEMOGLOBIN NIGERIA

HBA1, SER81CYS [dbSNP:rs34936612]

See Honig et al. (1978).

.0106 HEMOGLOBIN NOKO

HBA1, MET76LYS [dbSNP:rs33969953]

See Shibata et al. (1981).

.0107 HEMOGLOBIN NORFOLK

HEMOGLOBIN J (NORFOLK)
HEMOGLOBIN KAGOSHIMA
HEMOGLOBIN NISHIK

HBA1, GLY57ASP [dbSNP:rs36062788]

Fast hemoglobin. See Ager et al. (1958), Baglioni (1962), Huntsman et al. (1963), Hanada et al. (1964), Imamura (1966), and Lehmann and Carrell (1969).

.0108 HEMOGLOBIN NOUAKCHOTT

HBA1, PRO114LEU [dbSNP:rs33910377] [dbSNP:rs63750388]

See Wajcman et al. (1989).

.0109 HEMOGLOBIN NUNOBIKI

HBA1, ARG141CYS [dbSNP:rs33991910] [dbSNP:rs63750134]

This hemoglobin showed an extremely high oxygen affinity. The patient, who had 'marginal erythrocytosis,' was shown to have 13.1% Hb Nunobiki (Shimasaki, 1985).

.0110 HEMOGLOBIN O (INDONESIA)

HEMOGLOBIN O (BUGINESE-X)
HEMOGLOBIN BUGINESE-X
HEMOGLOBIN O (OLIVIERE)
HEMOGLOBIN OLIVIERE

HBA1, GLU116LYS [dbSNP:rs33987053] [dbSNP:rs63749882]

See Lie-Injo and Sadono (1958), Baglioni and Lehmann (1962), and Sansone et al. (1970).

Daud et al. (2001) investigated the occurrence of hemoglobin O (Indonesia) in related ethnic populations of the Indonesian archipelago. Nineteen individuals heterozygous for this variant were identified in 4 ethnic populations. The level of Hb O (Indonesia) in 17 of the individuals was 11.6 +/- 1.0%, significantly lower than the expected 17 to 22%, indicating the instability of Hb O (Indonesia).

.0111 HEMOGLOBIN O (PADOVA)

HBA1, GLU30LYS [dbSNP:rs33993166]

See Vettore et al. (1974), Kilinc et al. (1985), and Martin et al. (1990). Schnedl et al. (1997) showed that the silent hemoglobin O Padova mutation causes an additional peak on high performance liquid chromatography (HPLC) and falsely low HbA(1c) values (glycated hemoglobin) when measured by HPLC. HPLC is the gold standard for evaluation of glycated hemoglobin in diabetes mellitus.

.0112 HEMOGLOBIN OGI

HEMOGLOBIN QUEENS

HBA1, LEU34ARG [dbSNP:rs35203445]

See Sugihara et al. (1982), Moo-Penn et al. (1982), and Yongsuwan et al. (1987). This has been shown to be a mutation of the HBA1 gene (Cash et al., 1989).

.0113 HEMOGLOBIN OLEANDER

HBA1, GLU116GLN [dbSNP:rs33987053] [dbSNP:rs63749882]

See Schneider et al. (1980).

.0114 HEMOGLOBIN OTTAWA

HEMOGLOBIN SIAM

HBA1, GLY15ARG [dbSNP:rs35816645]

See Vella et al. (1974) and Pootrakul et al. (1974).

Yodsowan et al. (2000) studied this variant in a 21-year-old Thai female and her mother. Turbpaiboon et al. (2002) reported a fourth case of Hb Siam in a healthy Thai female and concluded that there is no alpha-thalassemic effect of the variant.

.0115 HEMOGLOBIN OWARI

HBA1, VAL121MET [dbSNP:rs35187567] [dbSNP:rs63751008]

This is a neutral-to-neutral change; it was detected in the course of mass screening by isoelectric focusing (Harano et al., 1986).

.0116 HEMOGLOBIN PERSPOLIS

HBA1, ASP64TYR [dbSNP:rs33984024]

See Rahbar et al. (1976).

.0117 HEMOGLOBIN PETAH TIKVA

HBA1, ALA110ASP [dbSNP:rs63749948]

See Honig et al. (1981).

.0118 HEMOGLOBIN PONTOISE

HEMOGLOBIN J (PONTOISE)

HBA1, ALA63ASP [dbSNP:rs34502246]

See Thillet et al. (1977) and Gonzalez-Redondo et al. (1987).

.0119 HEMOGLOBIN PORT PHILLIP

HBA1, LEU91PRO [dbSNP:rs34684963]

See Brennan et al. (1977).

.0120 MOVED TO 141850.0055

.0121 HEMOGLOBIN Q (INDIA)

HBA1, ASP64HIS [dbSNP:rs33984024]

See Sukumaran et al. (1972) and Schmidt et al. (1976).

.0122 HEMOGLOBIN Q (IRAN)

HBA1, ASP75HIS [dbSNP:rs33977363]

See Lorkin et al. (1970), Lie-Injo et al. (1979), and Higgs et al. (1980).

.0123 MOVED TO 141850.0052

.0124 HEMOGLOBIN REIMS

HBA1, GLU23GLY [dbSNP:rs33939421]

See Bardakdjian-Michau et al. (1989).

.0125 HEMOGLOBIN RUSS

HBA1, GLY51ARG [dbSNP:rs33960522]

See Huisman and Sydenstricker (1962) and Reynolds and Huisman (1966). This has been shown to be a mutation of the HBA1 gene (Cash et al., 1989).

.0126 HEMOGLOBIN SASSARI

HBA1, ASP126HIS [dbSNP:rs63750950]

Masala et al. (1987) first described this variant as an electrophoretically slow-moving hemoglobin in 2 brothers affected by erythrocytosis with slight microcytosis. In a large screening program involving 20,000 people in the city of Sassari and its surrounding area in Sardinia, Masala (1992) found the variant in 3 other apparently unrelated subjects. A male of German origin was identified by Bardakdjian-Michau et al. (1990) as a carrier of the same mutation. Sanna et al. (1994) demonstrated that the adult variant has increased oxygen affinity, a dramatic reduction of homotropic interactions, and a significant decrease of the effect of 2,3-diphosphoglycerate (35% lower than that observed for Hb A). The fetal variant also showed increased oxygen affinity compared with normal Hb F and an almost abolished heme-heme interaction.

Paglietti et al. (1998) demonstrated that Hb Sassari results from a GAC (asp)-to-CAC (his) mutation in the HBA1 gene.

.0127 HEMOGLOBIN SAVARIA

HBA1, SER49ARG [dbSNP:rs41518249]

See Szelenyi et al. (1980), Juricic et al. (1985), Ojwang et al. (1985), and Suarez et al. (1985).

.0128 HEMOGLOBIN SAWARA

HBA1, ASP6ALA [dbSNP:rs33986902]

No pathologic effects were observed (Sumida et al., 1973; Sumida, 1975).

.0130 HEMOGLOBIN SETIF

HBA1, ASP94TYR [dbSNP:rs34102339]

See Wajcman et al. (1972), Nozari et al. (1977), Al-Awamy et al. (1985), and Abdo (1989). Schiliro et al. (1991) found this hemoglobin variant in Sicily.

Dincol et al. (2003) stated that Hb Setif was first described in an Algerian family (Wajcman et al., 1972) and subsequently in Iranian, African, Saudi Arabian, and Maltese populations. They identified the variant in a Turkish family. Heterozygotes were asymptomatic.

.0131 HEMOGLOBIN SHAARE ZEDEK

HBA1, LYS56GLU [dbSNP:rs34182019]

See Abramov et al. (1980).

.0132 HEMOGLOBIN SHENYANG

HBA1, ALA26GLU [dbSNP:rs35477770]

See Zeng et al. (1982) and Yi et al. (1989).

.0133 HEMOGLOBIN SHIMONOSEKI

HEMOGLOBIN HIKOSHIMA

HBA1, GLN54ARG [dbSNP:rs36024711]

See Yamaoka et al. (1960) and Hanada and Rucknagel (1964).

.0134 HEMOGLOBIN SHUANGFENG

HBA1, GLU27LYS [dbSNP:rs34776279]

See Liang et al. (1981).

.0135 HEMOGLOBIN SINGAPORE

HBA1, ARG141PRO [dbSNP:rs33935328] [dbSNP:rs63751282]

See Clegg et al. (1969).

.0137 HEMOGLOBIN ST. CLAUDE

HBA1, LYS127THR [dbSNP:rs35431217] [dbSNP:rs63751308]

See Vella et al. (1974).

.0138 HEMOGLOBIN ST. LUKE'S

HBA1, PRO95ARG [dbSNP:rs33931314]

See Bannister et al. (1972).

Felice (2003) cited evidence that Hb St. Luke's is a mutation of the HBA1 gene.

.0139 HEMOGLOBIN STANLEYVILLE-II

HBA1, ASN78LYS [dbSNP:rs34440919]

See Van Ros et al. (1968), North et al. (1980), and Rhoda et al. (1983). Costa et al. (1991) described a family with 1 homozygote and 3 heterozygotes for Hb Stanleyville II. The pattern of restriction fragments demonstrated an associated 3.7-kb alpha-globin gene deletion.

.0140 HEMOGLOBIN STRUMICA

HEMOGLOBIN SERBIA

HBA1, HIS112ARG [dbSNP:rs34713708] [dbSNP:rs63750546]

See Niazi et al. (1975) and Beksedic et al. (1975).

.0143 HEMOGLOBIN SUNSHINE SETH

HBA1, ASP94HIS [dbSNP:rs34102339]

See Schroeder et al. (1979).

.0144 HEMOGLOBIN SURESNES

HBA1, ARG141HIS [dbSNP:rs33935328] [dbSNP:rs63751282]

See Poyart et al. (1976) and Saenz et al. (1978).

.0145 HEMOGLOBIN SWAN RIVER

HBA1, ASP6GLY [dbSNP:rs33986902]

See Moo-Penn et al. (1987). Harano et al. (1996) observed this variant in a Japanese man with mild polycythemia.

.0147 HEMOGLOBIN THAILAND

HBA1, LYS56THR [dbSNP:rs33949106]

See Pootrakul et al. (1977).

.0148 HEMOGLOBIN TITUSVILLE

HBA1, ASP94ASN [dbSNP:rs34102339]

See Schneider et al. (1975).

.0149 HEMOGLOBIN TOKONAME

HBA1, LYS139THR [dbSNP:rs34849179] [dbSNP:rs56348461]

See Harano et al. (1983).

.0150 HEMOGLOBIN TORINO

HBA1, PHE43VAL [dbSNP:rs35511459]

See Beretta et al. (1968) and Prato et al. (1970).

.0151 HEMOGLOBIN TOTTORI

HBA1, GLY59VAL [dbSNP:rs28928878]

See Nakatsuji et al. (1981).

.0152 HEMOGLOBIN TOYAMA

HEINZ BODY HEMOLYTIC ANEMIA

HBA1, LEU136ARG [dbSNP:rs34635364] [dbSNP:rs41469945]

This hemoglobin variant is associated with congenital Heinz body anemia (Ohba et al., 1987).

.0153 HEMOGLOBIN TWIN PEAKS

HBA1, LEU113HIS [dbSNP:rs35654345] [dbSNP:rs63751116]

See Guis et al. (1985). This has been shown to be a mutation of the HBA1 gene (Cash et al., 1989).

.0154 HEMOGLOBIN UBE-2

HBA1, ASN68ASP [dbSNP:rs34823698]

See Miyaji et al. (1967). In Turkey, Bilginer et al. (1984) found the first instance of Hb Ube-2 outside Japan. It occurred in other members of the family.

Cotton et al. (2000) found this rare variant during universal neonatal screening. The patients had normal hematologic parameters. The variant was found in twins and an older sister and in the father; both parents were of Belgian ancestry.

Shin et al. (2002) described the disorder in a Taiwanese subject.

.0155 HEMOGLOBIN UBE-4

HBA1, GLU116ALA [dbSNP:rs35932809] [dbSNP:rs63750606]

See Ohba et al. (1978).

.0156 HEMOGLOBIN WESTMEAD

HBA1, HIS122GLN [dbSNP:rs41479347]

This variant was found in a Chinese woman (Fleming et al., 1980). See Liang et al. (1988).

.0157 HEMOGLOBIN WINNIPEG

HBA1, ASP75TYR [dbSNP:rs33977363]

See Vella et al. (1973) and Nakatsuji et al. (1983). This has been shown to be a mutation of the HBA1 gene (Cash et al., 1989).

.0158 HEMOGLOBIN WOODVILLE

HBA1, ASP6TYR [dbSNP:rs33961916]

Since alpha-6 asp is involved in salt linkage with alpha-127 lys of the same chain, the increased oxygen affinity of hemoglobin variants at this position probably reflects loss of this salt bridge in the deoxy state. Similar changes have been observed for Hb St. Claude which also cannot form the salt bridge because of substitution of threonine for lysine at alpha-127. See Como et al. (1986).

.0159 HEMOGLOBIN WUMING

HEMOGLOBIN J (WENCHANG-WUMING)

HBA1, LYS11GLN [dbSNP:rs33938574]

See Zeng et al. (1981). Qualtieri et al. (1995) found this fast-migrating hemoglobin variant in a pregnant woman living in Italy.

.0160 HEMOGLOBIN ZAMBIA

HBA1, LYS60ASN [dbSNP:rs28928887]

See Barclay et al. (1969).

.0161 HEMOGLOBIN BELLIARD

HBA1, LYS56ASN [dbSNP:rs33959483]

See Wajcman et al. (1990).

.0162 HEMOGLOBIN TONOSHO

HBA1, ALA110THR [dbSNP:rs34629158] [dbSNP:rs63750629]

In the course of measuring hemoglobin A1c by automated cation exchange high performance liquid chromatography, Ohba et al. (1990) detected a new alpha-chain variant: substitution of alanine by threonine at position 110. The abnormal alpha chain comprised about 14% of the total alpha chain.

.0163 HEMOGLOBIN FUKUTOMI

HBA1, ASP126VAL [dbSNP:rs33957766] [dbSNP:rs63750467]

This hemoglobin, which has a high affinity for oxygen, was detected in a Japanese male during a screening survey. The proband was a 53-year-old man with liver cirrhosis and hemorrhagic gastritis (Hidaka et al., 1990).

.0164 HEMOGLOBIN PORT HURON

HBA1, LYS56ARG [dbSNP:rs33949106]

Zwerdling et al. (1991) investigated the structural abnormality of a putative Hb E detected in an African American family with no apparent Asian ancestry. The tryptic peptide map formed by high performance liquid chromatography showed that the electrophoretic variant was indeed the beta glu26-to-lys mutation of Hb E. In addition, however, the tryptic map showed an abnormal alpha peptide. The second mutation was a substitution of arginine for lysine at residue 56 of the alpha chain. The variant was clinically silent.

.0166 HEMOGLOBIN PAVIE

HBA1, VAL135GLU [dbSNP:rs35994191] [dbSNP:rs63749809]

See Wajcman et al. (1990).

.0167 HEMOGLOBIN QUESTEMBERT

HBA1, SER131PRO [dbSNP:rs35974739] [dbSNP:rs63751417]

See Wajcman et al. (1990, 1993).

.0168 HEMOGLOBIN THIONVILLE

HBA1, NH2 EXTENSION, VAL1GLU [dbSNP:rs63750609]

See Vasseur et al. (1990). Substitution of glutamic acid for valine as the first residue in the mature protein is accompanied by retention of the initiator methionine residue. This may be the only known hemoglobin variant with an NH2-extension in the alpha-globin chain. Hb Marseille (141900.0171), Hb Doha (141900.0069), and Hb South Florida (141900.0266) are examples of hemoglobin variants with an NH2-extension due to retention of the initiator methionine in the beta-globin chain. Each is due to mutation in the first or second residue of the mature protein. Vasseur et al. (1992) found that elongation of the NH2-terminus of the alpha-chain, due to inhibition of cleavage of the initiator methionine which is then acetylated, modifies the 3-dimensional structure of hemoglobin at a region that is known to have an important role in the allosteric regulation of oxygen binding. Hb Thionville has a lowered affinity for oxygen. In contrast, response to 2,3-diphosphoglycerate is normal.

.0169 HEMOGLOBIN KANAGAWA

HBA1, LYS40MET [dbSNP:rs41416747]

In the course of a high performance liquid chromatography survey of Hb A1c, Miyashita et al. (1992) detected a new hemoglobin in a 70-year-old Japanese male with cerebral infarction and erythremia. Further studies revealed a lys40-to-met mutation. The variant showed increased oxygen affinity, decreased heme-heme interaction, and a lowered 2,3-diphosphoglycerate effect.

(Erythemia, a now almost obsolete synonym for polycythemia and erythrocytosis, means increased red blood cell mass.)

.0170 HEMOGLOBIN TURRIFF

HBA1, LYS99GLU [dbSNP:rs34806456]

In a diabetic woman of Scottish ancestry, Langdown et al. (1992) detected a new hemoglobin variant in the course of determining Hb A1c by high performance liquid chromatography. The abnormal hemoglobin chromatographed with the Hb A1c fraction. Family studies showed that a lys99-to-glu mutation, which was not associated with any hematologic disturbance, had occurred de novo. An AAG-to-GAG mutation was presumed and was not assigned to either the alpha-2- or alpha-1-globin chain.

The Hb A(1c) level in the patient of Langdown et al. (1992) was found to be very high. In a Japanese individual, Harano et al. (2003) likewise found an unexpectedly high Hb A(1c) level as measured by an automatic Hb A(1c) analyzer and found by DNA sequencing a change in the first nucleotide of codon 99 (AAG-GAG) of the Hb A1 gene.

.0171 HEMOGLOBIN ZAIRE

HBA1, 15-BP TANDEM REPEAT

Hemoglobin Zaire was found in a 36-year-old patient from Zaire during a systematic hemoglobin study. Wajcman et al. (1992) demonstrated that the abnormality was the insertion of 5 amino acids--his, leu, pro, ala, glu--between glu116 and phe117 of the alpha-globin chain. This sequence represented a tandem repeat of the 5 amino acid residues from 112 through 116, located at the end of the GH corner of the molecule. Hemoglobin Grady (141800.0045) involves the insertion of 3 amino acids as repeats of residues 116, 117 and 118. Unequal crossing over between alleles rather than between the separate alpha-1 and alpha-2 loci was thought to be the mechanism in that case and possibly in the case of Hb Zaire as well.

.0172 HEMOGLOBIN LUTON

HBA1, HIS89LEU [dbSNP:rs33944813]

In a newborn infant and the father, a 35-year-old Pakistani man, Williamson et al. (1992) described a new hemoglobin with high oxygen affinity. The high affinity hemoglobin mutation was identified by HPLC peptide mapping and amino acid sequencing; leucine was substituted for histidine at amino acid position 89. The mutation occurred at the end of the F helix (FG1), a part of the hemoglobin structure critical in determining oxygen affinity since it is directly linked to the heme iron through the proximal histidine residue F8. This was the first example of a mutation at this position of the alpha chain of hemoglobin, although there were 2 high affinity mutants that involved the structurally equivalent amino acid (beta94 asp) of the beta chain: Hb Barcelona (beta94 his; 141900.0016) and Hb Bunbury (beta94 asn; 141900.0035). The new hemoglobin was called Hb Luton for the name of the hospital where the proband was originally treated. The proband was a neonate in whom 2 abnormal hemoglobin bands were found, the 2 bands being the mutant forms of fetal and adult hemoglobins containing the anomalous alpha globin. The father had microcytosis as well as mild polycythemia and was shown to have an accompanying alpha-thalassemia trait due to deletion of a single alpha-globin gene.

.0173 HEMOGLOBIN OZIERI

HBA1, ALA71VAL [dbSNP:rs3180281]

During a screening for hemoglobinopathies in Sardinia, Ferranti et al. (1993) found a new 'silent' hemoglobin variant in 5 apparently unrelated newborn babies. The variant was detected by means of isoelectric focusing (IEF), and further study revealed a valine for alanine substitution at position 71 of the alpha-globin chain. The substitution indicated that a C-to-T transition had occurred in the GCG codon for alanine which contains one of the 35 unmethylated CpG dinucleotides of the HBA1 gene. This observation brought to 13 the number of variants due to mutation in the CpGs of the HBA1 gene and raised the possibility that unmethylated CpGs, like methylated ones, may be hotspots for mutations.

.0174 HEMOGLOBIN ADANA

HEMOGLOBIN H DISEASE, NONDELETIONAL, INCLUDED

HBA1, GLY59ASP [dbSNP:rs28928878]

In 3 Turkish children with severe thalassemia, Curuk et al. (1992) found a GGC-to-GAC mutation in codon 59 of the HBA1 gene resulting in a replacement of glycine by aspartic acid. The combination of an alpha-thal-1 deletion with the unstable Hb Adana resulted in a severe type of Hb H disease (613978).

.0175 HEMOGLOBIN AL-AIN ABU DHABI

HBA1, GLY18ASP [dbSNP:rs35993097] [dbSNP:rs63750679]

During a routine program of hemoglobin screening performed in the United Arab Emirates, Abbes et al. (1992) found an electrophoretically fast-moving variant in a 9-month-old girl and in several members of her family. Amino acid sequencing demonstrated that the new variant had a gly18-to-asp substitution. Its functional properties were normal.

.0176 HEMOGLOBIN POITIERS

HBA1, HIS45ASP [dbSNP:rs33931984]

Hb Poitiers was discovered by Bardakdjian et al. (1994) in a 9-year-old French Caucasian boy who suffered from chronic anemia. The molecular defect consists of a missense mutation at codon 45 of the HBA1 gene, changing histidine to aspartate. Hb Poitiers displays a 2-fold increased oxygen affinity, a slightly decreased heme-heme interaction, and a slightly faster autooxidation rate. In adult hemoglobin (Hb A), the histidine residue at position 45 of the alpha-globin gene is the only polar contact between the heme group and globin. This position, however, seems to allow for moderate variation without dramatic consequences on the function of hemoglobin. His45 is replaced by glutamine in Hb Bari (141800.0009) and by arginine in Hb Fort de France (141800.0034).

.0177 MOVED TO 141850.0062

.0178 HEMOGLOBIN CAEN

HBA1, VAL132GLY [dbSNP:rs35166834] [dbSNP:rs63750708]

Wajcman et al. (1993) discovered the Hb Caen variant in a 25-year-old French Caucasian woman suffering from a mild chronic hemolytic anemia. Trypsin degradation of the isolated hemoglobin alpha chain followed by high performance liquid chromatography indicated that the valine residue at position 132 was replaced by glycine.

.0179 HEMOGLOBIN YUDA

HBA1, ALA130ASP [dbSNP:rs41528545]

Hb Yuda was discovered in a 65-year-old Japanese female with noninsulin-dependent diabetes mellitus (Fujisawa et al., 1992). Gas phase Edman degradation indicated that the abnormal hemoglobin alpha chain has a substitution of aspartic acid for alanine at residue 130. Hb Yuda has a very low oxygen affinity and slightly decreased cooperative subunit interaction.

.0180 HEMOGLOBIN CAPA

HBA1, ASP94GLY [dbSNP:rs28928879]

Hb Capa was discovered in a 28-year-old female in Turkey who was being treated for chronic iron deficiency anemia. The hemoglobin showed abnormal electrophoretic mobility and was mildly unstable in a heat denaturation test. The molecular change was a GAC-to-GGC transition in codon 94, resulting in substitution of glycine for aspartic acid. Three other substitutions of asp-94 are known: Hb Setif (141800.0130), Hb Titusville (141800.0148), and Hb Sunshine Seth (141800.0143). All 4 variants exhibit mild instability.

.0181 HEMOGLOBIN MONTEFIORE

HBA1, ASP126TYR [dbSNP:rs33933481] [dbSNP:rs63750950]

Wajcman et al. (1992) demonstrated an asp126-to-tyr change in the HBA1 gene in an individual of Puerto Rican descent. At physiologic pH (7.4), the oxygen binding of the patient's red blood cells revealed a 40% reduction. Hb Montefiore appears to have lower cooperativity than other characterized alpha-126 mutants: aspartic acid is replaced by asparagine in Hb Tarrant (141800.0146), by histidine in Hb Sassari (141800.0126), and by valine in Hb Fukutomi (141800.0163).

.0182 HEMOGLOBIN ROUEN

HEMOGLOBIN ETHIOPIA

HBA1, TYR140HIS [dbSNP:rs35723200] [dbSNP:rs55870409]

A tyr140-to-his mutation in the HBA1 gene was discovered and characterized in a French patient with polycythemia vera by Wajcman et al. (1992) and in a newborn baby of Ethiopian descent by Webber et al. (1992). This mutation provides an example of an alteration of the C-terminus of the alpha chain, a region involved in the mechanisms of allosteric regulation. Hb Rouen has increased oxygen affinity and decreased cooperativity. A complementary tyr145-to-his mutation (Hb Bethesda; 141900.0022) in the hemoglobin beta chain has more dramatic effects, suggesting that the alpha and beta chains play unequal roles in the overall function of hemoglobin.

.0183 HEMOGLOBIN MELUSINE

HBA1, PRO114SER [dbSNP:rs34472107] [dbSNP:rs63751114]

Hb Melusine was found in an Algerian patient during a systematic screening for hemoglobinopathies in Luxembourg. Using isoelectric focusing and reverse phase high performance liquid chromatography (RP-HPLC), Wajcman et al. (1993) determined that the molecular mutation at amino acid position 114 of the HBA1 gene changed the residue from proline to serine.

.0184 HEMOGLOBIN TAYBE

HBA1, THR38DEL OR THR39DEL [dbSNP:rs63751150]

Girodon et al. (1992) reported the characterization of Hb Taybe, a hemoglobin variant discovered in a young Arabic woman suffering since birth from a severe and highly regenerative hemolytic anemia. DNA amplification and sequencing of the HBA1 gene indicated a 3-bp deletion (encoding threonine) at amino acid position 38 or 39. This variant increases the hydrophobicity of the amino acid chain, and it is quite unstable.

.0185 HEMOGLOBIN CEMENELUM

HBA1, ARG92TRP [dbSNP:rs34868036]

Wajcman et al. (1994) described a missense mutation involving the same codon as that involved in Hb Chesapeake (141800.0018), the first high oxygen affinity hemoglobin variant to be described in association with polycythemia (Charache et al., 1966). Hb Chesapeake has an arg92-to-leu substitution; Hb Cemenelum has an arg92-to-trp substitution. Hb J (Cape Town) (141800.0063) has a substitution (arg92-to-gln) in the same codon. Hb Cemenelum was discovered in a French diabetic patient with no hematologic abnormalities. The purified abnormal hemoglobin, like Hb J (Cape Town), displayed only a 1.5- to 2-fold increased oxygen affinity. The findings demonstrate that the degree to which the functional properties are altered by changes in key residues at the alpha-beta interface depends upon the specific residue occupying this position.

.0186 HEMOGLOBIN RAMONA

HBA1, TYR24CYS [dbSNP:rs28928880]

Hb Ramona was accidentally detected by isoelectrofocusing in a pregnant woman of part Spanish descent; its mobility was slightly faster than that of Hb A. A TAT-to-TGT change was found at codon 24, corresponding to a replacement of tyrosine by cysteine.

.0187 HEMOGLOBIN TATRAS

HBA1, LYS7ASN [dbSNP:rs34410516]

In a 72-year-old woman born in Czechoslovakia, Wajcman et al. (1994) found a lys7-to-asn mutation when investigating the basis for an abnormal level of Hb A1c. No abnormal hematologic features were observed.

.0188 HEMOGLOBIN LISBON

HBA1, GLU23ASP [dbSNP:rs36068296]

In a 31-year-old man of Portuguese origin who had suffered from diabetes mellitus since the age of 15 years, Wajcman et al. (1994) found an abnormal hemoglobin during measurement of Hb A1c by an isoelectrofocusing study. There were no abnormal hematologic features.

.0189 HEMOGLOBIN ROANNE

HBA1, ASP94GLU [dbSNP:rs34814612]

Kister et al. (1995) described a new hemoglobin variant in a 73-year-old woman from Roanne in central France. She suffered from mild chronic hemolytic anemia. An asp94-to-glu substitution was found in the alpha-1 chain. Aspartate-94 is involved in several contacts, both in the deoxy- and oxy-structures of the hemoglobin.

.0190 HEMOGLOBIN MALHACEN

HBA1, ALA123SER [dbSNP:rs28928881]

Kazanetz et al. (1995) observed this variant hemoglobin in an adult male in Granada, Spain, who was evaluated because of severe iron deficiency anemia. Sequencing of the HBA1 gene showed 2 nucleotide changes. One was a simple polymorphism, as both GCG and GCT code for alanine (at codon 120). The second mutation was a GCC-to-TCC change at codon 123 resulting in replacement of alanine by serine. The replacement caused slight differences in the IEF and reversed-phase HPLC experiments, but the stability of the hemoglobin was normal. Family studies were not performed; thus, whether the 2 mutations were in coupling or repulsion was not known.

.0191 HEMOGLOBIN TUNIS-BIZERTE

HBA1, LEU129PRO [dbSNP:rs35993655]

In 3 members of a Tunisian family, Darbellay et al. (1995) identified a leu129-to-pro substitution in the HBA1 gene by sequencing the entirety of the HBA2 and HBA1 genes. In the heterozygous state, the variant was manifested by microcytosis, whereas the homozygous state showed moderate anemia with marked microcytosis.

.0192 MOVED TO 141850.0068

.0193 HEMOGLOBIN BOIS GUILLAUME

HBA1, ALA65VAL [dbSNP:rs34733452]

By tiny abnormalities observed during isoelectrofocusing, Wajcman et al. (1995) identified this electrophoretically silent variant in 3 members of a Caucasian-French family. This hemoglobin was the first alpha-chain variant that involved position 64. In the beta chain, the corresponding position, E14, is also occupied by an alanine residue; in Hb Seattle (141900.0256), it is replaced by aspartic acid (ala70-to-asp).

.0194 HEMOGLOBIN MANTES-LA-JOLIE

HBA1, ALA79THR [dbSNP:rs34586189]

Wajcman et al. (1995) found this variant hemoglobin during a systematic study of the iron status in a 6-month-old baby and his mother who originated from Chad in North Central Africa.

.0195 HEMOGLOBIN MOSELLA

HBA1, ALA111THR [dbSNP:rs34863047] [dbSNP:rs63749808]

Wajcman et al. (1995) found this variant in a 35-year-old pregnant woman of Caucasian origin who lived in Luxembourg. The abnormal Hb was also found in one of her daughters.

.0196 HEMOGLOBIN FUCHU-I

HBA1, HIS72TYR [dbSNP:rs36104787]

At the Fuchu Municipal Medical Center in Tokyo, Harano et al. (1995) identified 2 Hb variants in the course of assaying glycated hemoglobin, Hb A(1c), of the peripheral blood by cation exchange HPLC. Structural analyses demonstrated that 1 patient had a his72-to-tyr substitution and the other an asn97-to-his substitution (141800.0197) of the alpha-globin chain. These were named Hb Fuchu-I and Hb Fuchu-II, respectively. Both were healthy adults.

.0197 HEMOGLOBIN FUCHU-II

HBA1, ASN97HIS [dbSNP:rs41322954]

See 141800.0196.

.0198 HEMOGLOBIN GOUDA

HBA1, HIS72GLN [dbSNP:rs28928882]

In a 54-year-old Dutch woman under treatment for diabetes mellitus, Giordano et al. (1996) incidentally found a silent alpha-chain variant on testing for glycated hemoglobin. A CAC-to-CAA transversion was predicted to result in substitution of glutamine for histidine at residue 72 in the HBA1 gene.

.0199 HEMOGLOBIN J (BISKRA)

HBA1, 24-BP DEL [dbSNP:rs63750122]

Wajcman et al. (1998) described Hb J-Biskra, a variant hemoglobin consisting of deletion of 24 nucleotides from the HBA1 gene and 8 amino acid residues from the alpha-globin chain: residues 50-57, 51-58, or 52-59. This variant was mildly unstable in vitro only, and there was no hematologic or biochemical evidence of hemolysis in affected family members. Wajcman et al. (1998) stated that this was the largest deletion reported to that time in a hemoglobin molecule that is expressed at an almost normal level in the red blood cell.

.0200 HEMOGLOBIN GODAVARI

HBA1, PRO95THR [dbSNP:rs33984621]

Hb Godavari is the fourth example of a substitution involving neutral residues at position 95 of the alpha-1 chain. In all of these variants, the electrophoretic pattern suggested that the structural modification unmasks a charged residue in the alpha-1/beta-2 contact area. The other examples are Hb Denmark Hill, pro95 to ala (141800.0027); Hb G (Georgia), and pro95 to leu (141800.0038). Hb Godavari shared the same electrophoretic properties as these variants, but displayed minimal alterations of the oxygen-binding properties. Wajcman et al. (1998) identified Hb Godavari in 2 families of different ethnic origin. The first case, found in the Netherlands, involved an Indian patient. The second case was identified a few months later in an African family from Mali, living in France.

.0201 HEMOGLOBIN OITA

HBA1, HIS45PRO [dbSNP:rs28928883]

Hamaguchi et al. (1998) reported a neutral (silent) hemoglobin variant, designated Hb Oita, in which a change from CAC to CCC caused a his45-to-pro substitution. In Hb Bari (141800.0009), his45 is replaced by gln. In Hb Fort de France (141800.0034), his45 is replaced by arg. In Hb Portiers (141800.0176), his45 is replaced by asp.

.0202 HEMOGLOBIN AGHIA SOPHIA

HEMOGLOBIN H DISEASE, NONDELETIONAL, INCLUDED

HBA1, VAL62DEL [dbSNP:rs35672478]

In a Greek child with Hb H disease (613978), Traeger-Synodinos et al. (1999) found deletion of codon 62 of the alpha-1 gene, leading to alpha-plus-thalassemia. Codon 62 encodes a valine residue at the E11 alpha helix, which is located in the interior of the heme pocket. Substitutions of this valine with other amino acid residues in the alpha as well as beta polypeptide chains lead, in the heterozygous carrier, either to Hb M disease or to congenital nonspherocytic hemolytic anemia. Traeger-Synodinos et al. (1999) assumed that deletion of val at position 62 disrupted the conformation of the alpha chain to such an extent that the mutated subunit was rapidly removed by proteolysis. The final result was an alpha-thalassemia phenotype rather than an unstable hemoglobin syndrome. This conclusion was supported by the apparent absence of an abnormal alpha chain in the peripheral blood of the patient. Hb Evans (141850.0006) is a val62-to-met mutation of the HBA2 gene and was found in a patient with mild hemolytic anemia. Four amino acid substitutions at position 67(E11)val of the beta chain lead to instability of the Hb tetramer and an anemia of variable degrees in the heterozygotes. One of these substitutions, val67 to glu (141900.0163), results in the stable Hb M-Milwaukee-I.

.0203 HEMOGLOBIN CHAROLLES

HBA1, HIS103TYR [dbSNP:rs28928884]

Lacan et al. (1999) detected Hb Charolles in a 46-year-old patient who presented with microcytosis and hypochromia. It was easily detected by isoelectrofocusing and high performance liquid chromatography. It accounted for 11% of the total hemoglobin. The amino acid change resulted from a CAC-to-TAC change in codon 103.

.0204 HEMOGLOBIN ROUBAIX

HBA1, VAL55LEU [dbSNP:rs34068598]

In a French family from the north of France, Prehu et al. (1999) found a new HBA1 variant in 5 members. The variant was initially detected during measurement of glycated hemoglobin in a woman originating from Roubaix. Codon 55 in exon 2 was found to have a heterozygous change from GTT (val) to CTT (leu). This was a neutral variant.

.0205 HEMOGLOBIN DOUALA

HBA1, SER3PHE [dbSNP:rs35850071]

In a woman from Cameroon, Prehu et al. (2001) identified a new hemoglobin variant, designated Hb Douala, with a C-to-T transition (TCT-TTT) in the HBA1 gene, resulting in a ser3-to-phe (S3F) amino acid substitution. The patient was also heterozygous for Hb S (141900.0243) and for a 3.7-kb deletional alpha-thalassemia.

.0206 THALASSEMIA, ALPHA-PLUS

HBA1, 21-BP INS-DUP

In a patient of Iranian descent with the hematologic profile of alpha-plus-thalassemia characterized by mild microcytosis, Waye et al. (2001) found a 21-bp insertion/duplication that gave rise to a predicted alpha-globin chain containing a duplication of amino acid residues 93-99.

.0207 THALASSEMIA, ALPHA-PLUS

HBA1, 33-BP DEL

In a patient of Greek descent with the hematologic profile of alpha-plus-thalassemia characterized by mild microcytosis, Waye et al. (2001) found a 33-bp deletion in the HBA1 gene resulting in a predicted alpha-globin chain missing amino acid residues 64-74.

.0208 HEMOGLOBIN DELFZICHT

HBA1, ASN9LYS [dbSNP:rs28928885]

Harteveld et al. (2002) reported a 69-year-old Dutch woman monitored for diabetes mellitus in whom Hb A(L1c) analysis revealed a clinically silent hemoglobin variant, asn9 to lys (N9K), due to an AAC-to-AAG transversion in heterozygous state. The mutation was identical to that found at the same position in the HBA2 gene that leads to a variant named Hb Park Ridge (141850.0048).

.0209 HEMOGLOBIN SARATOGA SPRINGS

HBA1, LYS40ASN [dbSNP:rs28928886]

In a 34-year-old Caucasian male of Swedish ancestry who lived in Saratoga Springs, New York, Hoyer et al. (2003) identified a hemoglobin variant with abnormal oxygen affinity, designated Hb Saratoga Springs. There was no family history of erythrocytosis. The patient had no smoking history. A change of codon 40 of the HBA1 gene from AAG to AAC resulted in a lys40-to-asn (K40N) change. Lys40 is replaced by glu in Hb Kariya (141800.0081), and by met in Hb Kanagawa (141800.0169). Both of these hemoglobins had been shown to have increased oxygen affinity, but neither was associated with erythrocytosis.

.0210 HEMOGLOBIN DIE

HBA1, VAL93ALA [dbSNP:rs34769782]

In a 7-year-old girl living near the town of Die in southeast France, Lacan et al. (2004) identified a val93-to-ala (V93A) mutation in the HBA1 gene. The family was of French Caucasian origin.

.0211 HEMOGLOBIN BEZIERS

HBA1, LYS99ASN [dbSNP:rs34273731]

In a 72-year-old woman of French Caucasian origin living in the city of Beziers in the south of France, Lacan et al. (2004) identified a lys99-to-asn (K99N) mutation in the HBA1 gene. The variant was found during the determination of Hb A(1c) by high performance liquid chromatography (HPLC) in this diabetic patient. Hematologic data were normal, without hepatomegaly or splenomegaly.

.0212 HEMOGLOBIN BUFFALO

HBA1, HIS89GLN [dbSNP:rs1061009]

In a 32-year-old Somali male living in the Netherlands who was being monitored for diabetes mellitus, Harteveld et al. (2004) identified Hb S (141900.0243) in heterozygous state and a heterozygous C-to-G transversion in the HBA1 gene, resulting in a his89-to-gln (H89Q) substitution. The H89Q mutation had previously been described in a Yemenite woman and 2 apparently unrelated Somali males (Hoyer et al., 2002), and had been designated Hb Buffalo. No hematologic abnormality had been associated with the allelic variant in this or other cases. In addition to Hb Buffalo, 4 amino acid substitutions had been reported at codon 89: Hb Luton (his89 to leu; 141800.0172), Hb Villeurbanne (his89 to tyr; 141800.0213), Hb Tokyo (his89 to pro; 141800.0214), and Hb Tamano (his89 to arg; 141800.0215).

.0213 HEMOGLOBIN VILLEURBANNE

HBA1, HIS89TYR [dbSNP:rs34988734]

Deon et al. (1997) identified a his89-to-tyr (H89Y) mutation in the HBA1 gene as the defect in Hb Villeurbanne.

.0214 HEMOGLOBIN TOKYO

HBA1, HIS89PRO [dbSNP:rs33944813]

Harteveld et al. (2004) stated that Hb Tokyo carries a his89-to-pro (H89P) mutation in the HBA1 gene.

.0215 HEMOGLOBIN TAMANO

HBA1, HIS89ARG [dbSNP:rs33944813]

Harteveld et al. (2004) stated that Hb Tamano carries a his89-to-arg (H89R) mutation in the HBA1 gene.

.0216 HEMOGLOBIN RICCARTON

HBA1, GLY51SER [dbSNP:rs33960522]

In a 4-year-old Caucasian boy investigated for fatigue and microcytosis, Brennan et al. (2005) found a GGC-to-AGC transition at codon 51 in the HBA1 gene, resulting in a gly51-to-ser substitution (G51S). The mutation was thought not to be the cause of the microcytosis as it was detected also in the boy's father who had normal red cell indices.

.0217 HEMOGLOBIN OEGSTGEEST

HBA1, CYS104SER [dbSNP:rs35059618]

In an 8-year-old black female of Surinamese origin with a mild alpha-thalassemia phenotype, Harteveld et al. (2005) identified homozygosity for a TGC-to-AGC transversion in the HBA1 gene, resulting in a cys104-to-ser substitution. Cysteine-104 is involved in alpha/beta globin contact and had been described as a critical amino acid of the HBA2 chain when substituted by a tyrosine (cys104 to tyr) in Hb Sallanches (141850.0031).

.0218 HEMOGLOBIN LAMEN ISLAND

HBA1, 149709T-C

De Gobbi et al. (2006) studied 148 individuals from Melanesia with alpha-thalassemia, including 5 with HbH disease, in whom none of the theretofore described molecular defects could be found. The pattern of inheritance suggested that individuals with HbH disease were homozygous for a codominant defect, referred to as (alpha-alpha)T, causing alpha-thalassemia with a predicted genotype of (alpha-alpha)T/(alpha-alpha)T. In situ RNA hybridization in erythroid cells from an affected individual from Lamen Island (Vanuatu) detected substantially fewer nuclear transcripts from the alpha-globin genes than from the beta-globin genes. DNA FISH in 2 affected individuals showed that the alpha-globin cluster was present at its normal location of chromosome 16, and no deletions or chromosomal rearrangements were detected in any of these individuals. Linkage analysis showed that the disease phenotype in individuals was derived from telomeric chromosome 16 T. Only the C allele of SNP195 (C or T, located at coordinate 149709) segregated with thalassemia in the affected families and showed complete association with the (alpha-alpha)T haplotype. This allele was not found in a separate analysis of 131 nonthalassemic Melanesian individuals. SNP195 changes the sequence 5-prime-TAATAA-3-prime (T allele) to 5-prime-TGATAA-3-prime (C allele), potentially creating a new binding site for the key erythroid transcription factor GATA1. GATA1 binds at the C allele of SNP195 in vivo. SNP195 creates a new promoter-like element between the upstream regulatory elements and their cognate promoters. This element, when activated, causes significant downregulation of the alpha-D, alpha-2, and alpha-1 genes that lie downstream, thereby causing alpha-thalassemia.

.0219 ALPHA-THALASSEMIA

HBA1, 1-BP DEL, 354C

In a newborn of mixed black and Chinese descent who carried the Southeast Asian alpha-0-thal deletion, Eng et al. (2006) also found a 1-bp deletion of cysteine from codon 78 in exon 2 of the HBA1 gene, resulting in a frameshift and premature termination at codon 83.

.0220 HEMOGLOBIN AUCKLAND

HBA1, HIS87ASN [dbSNP:rs28928876]

In a 27-year-old woman with mild compensated hemolytic anemia, Brennan and Matthews (1997) identified Hb Auckland, a his87-to-asn substitution in the HBA1 gene.

.9999 HEMOGLOBIN ALPHA VARIANTS, MOLECULAR DEFECT UNKNOWN

HEMOGLOBIN J (INDIA). See Raper (1957).

HEMOGLOBIN J (MALAYA). See Lehmann (1962).

HEMOGLOBIN K (CALCUTTA). Fast hemoglobin. See Lehmann (1962).

HEMOGLOBIN K (MADRAS). See Ager and Lehmann (1957).

HEMOGLOBIN KARAMOJO. See Allbrook et al. (1965).

HEMOGLOBIN L (BOMBAY). See Sukumaran and Pik (1965).

HEMOGLOBIN M (RESERVE). Reduced oxygen affinity and decreased reversible oxygen-binding capacity (Overly et al., 1967).

HEMOGLOBIN N, ALPHA TYPE. An alpha chain anomaly was deduced from molecular hybridization experiments with canine hemoglobin (Silvestroni et al., 1963). Other hemoglobin N variants have a beta change.

HEMOGLOBIN NICOSIA. See Fessas et al. (1965).

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422.	Yodsowan, B., Svasti, J., Srisomsap, C., Winichagoon, P., Fucharoen, S. Hb Siam [alpha-15(A13)gly-arg] is a GGT-CGT mutation in the alpha-1-globin gene. Hemoglobin 24: 71-75, 2000. [PubMed: 10722119, related citations] [Full Text: Pubget]

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424.	Zeng, F.-Y., Fucharoen, S., Huang, S.-Z., Rodgers, G. P. Hb Q-Thailand (alpha74 (EF3) asp-to-his): gene organization, molecular structure, and DNA diagnosis. Hemoglobin 16: 481-491, 1992. [PubMed: 1487419, related citations] [Full Text: Pubget]

425.	Zeng, Y., Huang, S., Liang, X., Long, G., Lam, H., Wilson, J. B., Huisman, T. H. J. Hb Wuming or alpha11 (A9) lys-to-gln. Hemoglobin 5: 679-687, 1981. [PubMed: 7338470, related citations] [Full Text: Pubget]

426.	Zeng, Y., Huang, S., Qiu, X., Cheng, G., Ren, Z., Jin, Q., Chen, C., Jiao, C., Tang, Z., Liu, R., Bao, X., Zeng, L., Duan, Y., Zhang, G. Hemoglobin Chongqing (alpha2 (NA2) leu-to-arg) and hemoglobin Harbin (alpha16 (A14) lys-to-met) found in China. Hemoglobin 8: 569-581, 1984. [PubMed: 6526652, related citations] [Full Text: Pubget]

427.	Zeng, Y., Huang, S., Zhou, X., Qiu, X., Dong, Q., Li, M., Bai, J. Hb Shenyang (alpha26 (B7) ala-to-glu): a new unstable variant found in China. Hemoglobin 6: 625-628, 1982. [PubMed: 7161109, related citations] [Full Text: Pubget]

428.	Zhao, W., Wilson, J. B., Webber, B. B., Kutlar, A., Tamagnini, G. P., Kuam, B., Huisman, T. H. J. Hb Hekinan observed in three Chinese from Macau: identification of the GAG-to-GAT mutation in the alpha-1-globin gene. Hemoglobin 14: 627-635, 1990. [PubMed: 1983218, related citations] [Full Text: Pubget]

429.	Zhou, Z., Chen, L., Chen, P., Zhang, K., Wang, Y. Hemoglobin Hangzhou alpha64 (E13) asp-to-gly: a new variant found in China. Hemoglobin 11: 31-33, 1987. [PubMed: 3583763, related citations] [Full Text: Pubget]

430.	Zimmer, E. A., Martin, S. L., Beverley, S. M., Kan, Y. W., Wilson, A. C. Rapid duplication and loss of genes coding for the alpha chains of hemoglobin. Proc. Nat. Acad. Sci. 77: 2158-2162, 1980. [PubMed: 6929543, related citations] [Full Text: Pubget]

431.	Zwerdling, T., Williams, S., Nasr, S. A., Rucknagel, D. L. Hb Port Huron (alpha56(E5)lys-to-arg): a new alpha chain variant. Hemoglobin 15: 381-391, 1991. [PubMed: 1802882, related citations] [Full Text: Pubget]

Contributors:	Patricia A. Hartz - updated : 1/28/2010
	Carol A. Bocchini - updated : 5/22/2009 Victor A. McKusick - updated : 9/19/2006 Ada Hamosh - updated : 7/21/2006 Victor A. McKusick - updated : 3/29/2006 Victor A. McKusick - updated : 10/11/2005 Victor A. McKusick - updated : 8/11/2005 Victor A. McKusick - updated : 5/11/2005 Victor A. McKusick - updated : 12/6/2004 Victor A. McKusick - updated : 8/6/2004 Victor A. McKusick - updated : 6/2/2004 Victor A. McKusick - updated : 1/20/2004 Victor A. McKusick - updated : 1/15/2004 Victor A. McKusick - updated : 9/2/2003 Victor A. McKusick - updated : 3/5/2003 Victor A. McKusick - updated : 10/2/2002 Victor A. McKusick - updated : 6/3/2002 Victor A. McKusick - updated : 5/23/2002 Victor A. McKusick - updated : 2/27/2002 Victor A. McKusick - updated : 11/1/2001 Victor A. McKusick - updated : 10/11/2001 Victor A. McKusick - updated : 5/1/2000 Victor A. McKusick - updated : 1/19/2000 Victor A. McKusick - updated : 7/14/1999 Ada Hamosh - updated : 4/21/1999 Victor A. McKusick - updated : 2/24/1999 Victor A. McKusick - updated : 2/9/1999 Ada Hamosh - updated : 6/12/1998 Victor A. McKusick - updated : 4/30/1998 Victor A. McKusick - updated : 2/6/1998 Victor A. McKusick - updated : 8/27/1997
Creation Date:	Victor A. McKusick : 6/23/1986
Edit History:	alopez : 07/25/2011
	carol : 6/9/2011 alopez : 5/13/2011 alopez : 1/28/2010 terry : 6/3/2009 carol : 5/22/2009 terry : 1/15/2009 terry : 1/15/2009 terry : 1/14/2009 wwang : 10/4/2007 wwang : 10/3/2006 terry : 9/19/2006 alopez : 7/25/2006 terry : 7/21/2006 terry : 6/23/2006 terry : 3/29/2006 carol : 10/21/2005 wwang : 10/21/2005 terry : 10/11/2005 carol : 10/3/2005 terry : 8/11/2005 wwang : 6/7/2005 terry : 5/17/2005 terry : 5/17/2005 wwang : 5/13/2005 terry : 5/11/2005 terry : 2/7/2005 tkritzer : 1/25/2005 terry : 12/6/2004 tkritzer : 8/10/2004 terry : 8/6/2004 tkritzer : 6/8/2004 terry : 6/2/2004 carol : 3/17/2004 tkritzer : 1/21/2004 terry : 1/20/2004 terry : 1/15/2004 cwells : 9/3/2003 terry : 9/2/2003 carol : 8/29/2003 carol : 8/25/2003 carol : 5/13/2003 terry : 4/17/2003 terry : 3/5/2003 terry : 3/3/2003 tkritzer : 12/10/2002 tkritzer : 10/7/2002 tkritzer : 10/3/2002 tkritzer : 10/2/2002 carol : 6/3/2002 terry : 6/3/2002 terry : 5/23/2002 cwells : 3/22/2002 cwells : 3/20/2002 terry : 2/27/2002 mcapotos : 11/1/2001 mcapotos : 10/26/2001 mcapotos : 10/11/2001 cwells : 5/31/2001 mcapotos : 2/19/2001 mcapotos : 2/15/2001 terry : 2/14/2001 mcapotos : 5/26/2000 mcapotos : 5/24/2000 terry : 5/1/2000 mcapotos : 2/7/2000 mcapotos : 2/4/2000 carol : 1/28/2000 mcapotos : 1/28/2000 mcapotos : 1/24/2000 terry : 1/19/2000 carol : 12/8/1999 mgross : 7/16/1999 terry : 7/14/1999 carol : 6/27/1999 terry : 4/30/1999 alopez : 4/21/1999 terry : 3/24/1999 carol : 3/9/1999 terry : 2/24/1999 mgross : 2/16/1999 mgross : 2/11/1999 terry : 2/9/1999 dkim : 7/21/1998 dkim : 7/21/1998 carol : 7/2/1998 alopez : 6/12/1998 terry : 6/5/1998 terry : 6/5/1998 alopez : 5/14/1998 carol : 5/4/1998 terry : 4/30/1998 mark : 2/16/1998 terry : 2/6/1998 terry : 2/6/1998 mark : 10/19/1997 jenny : 9/5/1997 terry : 8/27/1997 alopez : 7/31/1997 alopez : 7/29/1997 terry : 7/10/1997 mark : 7/10/1997 alopez : 7/10/1997 terry : 7/9/1997 terry : 7/7/1997 mark : 6/14/1997 terry : 11/15/1996 terry : 11/13/1996 mark : 4/12/1996 terry : 4/9/1996 mark : 2/13/1996 terry : 2/5/1996 mark : 11/17/1995 terry : 11/18/1994 jason : 7/29/1994 pfoster : 4/25/1994 mimadm : 4/17/1994 warfield : 4/8/1994

Table of Contents - +141800

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