Entry - *608721 - CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II INHIBITOR 2; CAMK2N2 - OMIM
 
* 608721

CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II INHIBITOR 2; CAMK2N2


Alternative titles; symbols

CAMKII INHIBITORY PROTEIN; CAMKIIN
CAMKIIN-BETA


HGNC Approved Gene Symbol: CAMK2N2

Cytogenetic location: 3q27.1   Genomic coordinates (GRCh38) : 3:184,259,213-184,261,553 (from NCBI)


TEXT

Cloning and Expression

By sequencing clones obtained from a dendritic cell (DC) cDNA library, Zhang et al. (2001) cloned CAMKIIN. The deduced 79-amino acid protein has a calculated molecular mass of 8.7 kD. CAMKIIN shares 98% amino acid identity with rat Camkiin-beta and 65% identity with rat Camkiin-alpha. Northern blot analysis detected robust expression of a 5.2-kb transcript in kidney and liver, with moderate expression in heart, skeletal muscle, and placenta, low expression in small intestine, and no expression in colon, thymus, spleen, lung, peripheral blood leukocytes (PBLs), or brain. A 1.65-kb CAMKIIN transcript was expressed in brain at a high level. Expression was also detected in cancer cell lines of diverse tissue origin. RT-PCR detected strong expression in stimulated DCs derived from PBLs and lower expression in unstimulated mature and immature DCs. No expression was detected in monocytes, T cells, or B cells.


Gene Function

Chang et al. (1998) determined that rat brain Camkiin bound the catalytic domain of Camk2a (114078) and Camk2b (607707) and potently inhibited kinase activity. The full-length 79-amino acid protein and a 28-amino acid peptide derived from it were highly selective for inhibition of Camk2. Camkiin interacted with activated Camk2 (i.e., in the presence of Ca(2+)/calmodulin (see 114180) or after autophosphorylation) both in vivo and in vitro. In COS-7 cells, phosphorylation of a test substrate by Camk2 was blocked upon cotransfection with Camkiin.

Zhang et al. (2001) found that overexpression of CAMKIIN in a colon adenocarcinoma cell line altered cell morphology, inhibited cell proliferation, and decreased the viable cell number. CAMKIIN had no effect following overexpression in HeLa cells.


Mapping

Hartz (2004) mapped the CAMK2N2 gene to chromosome 3q27.1 based on an alignment of the CAMK2N2 sequence (GenBank AY037149) with the genomic sequence.


REFERENCES

  1. Chang, B. H., Mukherji, S., Soderling, T. R. Characterization of a calmodulin kinase II inhibitor protein in brain. Proc. Nat. Acad. Sci. 95: 10890-10895, 1998. [PubMed: 9724800, images, related citations] [Full Text]

  2. Hartz, P. A. Personal Communication. Baltimore, Md. 6/9/2004.

  3. Zhang, J., Li, N., Yu, J., Zhang, W., Cao, X. Molecular cloning and characterization of a novel calcium/calmodulin-dependent protein kinase II inhibitor from human dendritic cells. Biochem. Biophys. Res. Commun. 285: 229-234, 2001. [PubMed: 11444830, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 6/9/2004
mgross : 12/17/2012
alopez : 1/28/2008
mgross : 6/9/2004

* 608721

CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II INHIBITOR 2; CAMK2N2


Alternative titles; symbols

CAMKII INHIBITORY PROTEIN; CAMKIIN
CAMKIIN-BETA


HGNC Approved Gene Symbol: CAMK2N2

Cytogenetic location: 3q27.1   Genomic coordinates (GRCh38) : 3:184,259,213-184,261,553 (from NCBI)


TEXT

Cloning and Expression

By sequencing clones obtained from a dendritic cell (DC) cDNA library, Zhang et al. (2001) cloned CAMKIIN. The deduced 79-amino acid protein has a calculated molecular mass of 8.7 kD. CAMKIIN shares 98% amino acid identity with rat Camkiin-beta and 65% identity with rat Camkiin-alpha. Northern blot analysis detected robust expression of a 5.2-kb transcript in kidney and liver, with moderate expression in heart, skeletal muscle, and placenta, low expression in small intestine, and no expression in colon, thymus, spleen, lung, peripheral blood leukocytes (PBLs), or brain. A 1.65-kb CAMKIIN transcript was expressed in brain at a high level. Expression was also detected in cancer cell lines of diverse tissue origin. RT-PCR detected strong expression in stimulated DCs derived from PBLs and lower expression in unstimulated mature and immature DCs. No expression was detected in monocytes, T cells, or B cells.


Gene Function

Chang et al. (1998) determined that rat brain Camkiin bound the catalytic domain of Camk2a (114078) and Camk2b (607707) and potently inhibited kinase activity. The full-length 79-amino acid protein and a 28-amino acid peptide derived from it were highly selective for inhibition of Camk2. Camkiin interacted with activated Camk2 (i.e., in the presence of Ca(2+)/calmodulin (see 114180) or after autophosphorylation) both in vivo and in vitro. In COS-7 cells, phosphorylation of a test substrate by Camk2 was blocked upon cotransfection with Camkiin.

Zhang et al. (2001) found that overexpression of CAMKIIN in a colon adenocarcinoma cell line altered cell morphology, inhibited cell proliferation, and decreased the viable cell number. CAMKIIN had no effect following overexpression in HeLa cells.


Mapping

Hartz (2004) mapped the CAMK2N2 gene to chromosome 3q27.1 based on an alignment of the CAMK2N2 sequence (GenBank AY037149) with the genomic sequence.


REFERENCES

  1. Chang, B. H., Mukherji, S., Soderling, T. R. Characterization of a calmodulin kinase II inhibitor protein in brain. Proc. Nat. Acad. Sci. 95: 10890-10895, 1998. [PubMed: 9724800] [Full Text: https://doi.org/10.1073/pnas.95.18.10890]

  2. Hartz, P. A. Personal Communication. Baltimore, Md. 6/9/2004.

  3. Zhang, J., Li, N., Yu, J., Zhang, W., Cao, X. Molecular cloning and characterization of a novel calcium/calmodulin-dependent protein kinase II inhibitor from human dendritic cells. Biochem. Biophys. Res. Commun. 285: 229-234, 2001. [PubMed: 11444830] [Full Text: https://doi.org/10.1006/bbrc.2001.5175]


Creation Date:
Patricia A. Hartz : 6/9/2004

Edit History:
mgross : 12/17/2012
alopez : 1/28/2008
mgross : 6/9/2004