CAP1

CAP, adenylate cyclase-associated protein 1 (yeast)
PDB rendering based on 1k8f.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1K8F​
Identifiers
Symbols	CAP1 ; CAP; CAP1-PEN
External IDs	MGI: 88262 HomoloGene: 74572 GeneCards: CAP1 Gene
Gene ontology Molecular function • actin binding Cellular component • plasma membrane • focal adhesion • cortical actin cytoskeleton • extracellular exosome Biological process • ameboidal-type cell migration • platelet degranulation • receptor-mediated endocytosis • establishment or maintenance of cell polarity • signal transduction • activation of adenylate cyclase activity • axon guidance • blood coagulation • actin cytoskeleton organization • platelet activation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10487	12331
Ensembl	ENSG00000131236	ENSMUSG00000028656
UniProt	Q01518	P40124
RefSeq (mRNA)	NM_001105530	NM_001301067
RefSeq (protein)	NP_001099000	NP_001287996
Location (UCSC)	Chr 1: 40.04 – 40.07 Mb	Chr 4: 122.86 – 122.89 Mb
PubMed search

Adenylyl cyclase-associated protein 1 is an enzyme that in humans is encoded by the CAP1 gene.^[1][2][3]

The protein encoded by this gene is related to the S. cerevisiae CAP protein, which is involved in the cyclic AMP pathway. The human protein is able to interact with other molecules of the same protein, as well as with CAP2 and actin.^[3]

Interactions

CAP1 has been shown to interact with ACTG1^[4] and CAP2.^[2]

References

1. Matviw H, Yu G, Young D (Nov 1992). "Identification of a human cDNA encoding a protein that is structurally and functionally related to the yeast adenylyl cyclase-associated CAP proteins". Mol Cell Biol 12 (11): 5033–40. PMC 360436. PMID 1406678.
2. Hubberstey A, Yu G, Loewith R, Lakusta C, Young D (Apr 1997). "Mammalian CAP interacts with CAP, CAP2, and actin". J Cell Biochem 61 (3): 459–66. doi:10.1002/(SICI)1097-4644(19960601)61:3<459::AID-JCB13>3.0.CO;2-E. PMID 8761950.
3. "Entrez Gene: CAP1 CAP, adenylate cyclase-associated protein 1 (yeast)".
4. Hubberstey, A; Yu G; Loewith R; Lakusta C; Young D (Jun 1996). "Mammalian CAP interacts with CAP, CAP2, and actin". J. Cell. Biochem. (UNITED STATES) 61 (3): 459–66. doi:10.1002/(SICI)1097-4644(19960601)61:3<459::AID-JCB13>3.0.CO;2-E. ISSN 0730-2312. PMID 8761950.

Further reading

• Yu G, Swiston J, Young D (1994). "Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins". J. Cell. Sci. 107 (6): 1671–8. PMID 7962207.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Moriyama K, Yahara I (2003). "Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover". J. Cell. Sci. 115 (Pt 8): 1591–601. PMID 11950878.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gevaert K, Goethals M, Martens L; et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Dodatko T, Fedorov AA, Grynberg M; et al. (2004). "Crystal structure of the actin binding domain of the cyclase-associated protein". Biochemistry 43 (33): 10628–41. doi:10.1021/bi049071r. PMID 15311924.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Fautsch MP, Vrabel AM, Johnson DH (2006). "The identification of myocilin-associated proteins in the human trabecular meshwork". Exp. Eye Res. 82 (6): 1046–52. doi:10.1016/j.exer.2005.09.016. PMID 16289162.
• Oh JH, Yang JO, Hahn Y; et al. (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.
• Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
• Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F (2006). "Phosphoproteomic analysis of the human pituitary". Pituitary 9 (2): 109–20. doi:10.1007/s11102-006-8916-x. PMID 16807684.
• Garewal G, Das R, Awasthi A; et al. (2007). "The clinical significance of the spectrum of interactions of CAP+1 (A-->C), a silent beta-globin gene mutation, with other beta-thalassemia mutations and globin gene modifiers in north Indians". Eur. J. Haematol. 79 (5): 417–21. doi:10.1111/j.1600-0609.2007.00958.x. PMID 17900295.