CAP1

CAP1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1K8F
Identifiers
Aliases	CAP1 , CAP, CAP1-PEN, CAP, adenylate cyclase-associated protein 1 (yeast), adenylate cyclase associated protein 1
External IDs	OMIM: 617801; MGI: 88262; HomoloGene: 74572; GeneCards: CAP1; OMA:CAP1 - orthologs
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	122,779,849 bp
RNA expression pattern
	n/a
	Top expressed in
	granulocyte; ; lateral septal nucleus; ; dentate gyrus of hippocampal formation granule cell; ; superior frontal gyrus; ; transitional epithelium of urinary bladder; ; tibiofemoral joint; ; cervix; ; yolk sac; ; decidua; ; lip;
	; ;
	More reference expression data
Gene ontology
Molecular function	adenylate cyclase binding ; actin binding ;
Cellular component	cytoplasm ; plasma membrane ; extracellular exosome ; membrane ; focal adhesion ; cortical actin cytoskeleton ; extracellular region ; extracellular space ; azurophil granule lumen ;
Biological process	establishment or maintenance of cell polarity ; ameboidal-type cell migration ; receptor-mediated endocytosis ; actin cytoskeleton organization ; cytoskeleton organization ; signal transduction ; activation of adenylate cyclase activity ; cell morphogenesis ; actin polymerization or depolymerization ; neutrophil degranulation ; regulation of adenylate cyclase activity ;
	Sources:Amigo / QuickGO
Orthologs
	10487
	12331
	ENSG00000131236
	ENSMUSG00000028656
	Q01518 ; Q5T0R9
	P40124
	NM_001105530 ; NM_006367 ; NM_001330502
	NM_001301067 ; NM_007598 ; NM_001358035 ; NM_001358036
NP_001099000 ; NP_001317431 ; NP_006358 ; NP_001337404 ; NP_001337405 ;
	NP_001337406 ; NP_001337407 ; NP_001337408 ; NP_001337409 ; NP_001337410 ; NP_001337411 ; NP_001337412 ; NP_001337413 ; NP_001337414 Contents Interactions ; See also ; References ; External links ; Further reading ;
	NP_001287996 ; NP_031624 ; NP_001344964 ; NP_001344965
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated November 18, 2024

Adenylyl cyclase-associated protein 1 is an enzyme that in humans is encoded by the CAP1 gene.^[4]^[5]^[6] Hahfak

The protein encoded by this gene is related to the Saccharomyces 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.^[6]

Interactions

CAP1 has been shown to interact with ACTG1 ^[7] and CAP2.^[5]

Related Research Articles

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Adenylyl cyclase type 5 is an enzyme that in humans is encoded by the ADCY5 gene.

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Dynamin-3 is a protein that in humans is encoded by the DNM3 gene. The protein encoded by this gene is a member of the dynamin family which possess mechanochemical properties involved in actin-membrane processes, predominantly in membrane budding. DNM3 is upregulated in Sézary's syndrome.

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Adenylyl cyclase type 2 is an enzyme typically expressed in the brain of humans, that is encoded by the ADCY2 gene. It belongs to the adenylyl cyclase class-3 or guanylyl cyclase family because it contains two guanylate cyclase domains. ADCY2 is one of ten different mammalian isoforms of adenylyl cyclases. ADCY2 can be found on chromosome 5 and the "MIR2113-POU3F2" region of chromosome 6, with a length of 1091 amino-acids. An essential cofactor for ADCY2 is magnesium; two ions bind per subunit.

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<span class="mw-page-title-main">ADCY9</span> Protein-coding gene in the species Homo sapiens

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RNA 3'-terminal phosphate cyclase-like protein is an enzyme that in humans is encoded by the RCL1 gene.

Coronin-1C is a protein that in humans is encoded by the CORO1C gene.

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Adenylyl cyclase-associated protein 2 is an enzyme that in humans is encoded by the CAP2 gene.

Cofilin 2 (muscle) also known as CFL2 is a protein which in humans is encoded by the CFL2 gene.

In molecular biology, the cyclase-associated protein family (CAP) is a family of highly conserved actin-binding proteins present in a wide range of organisms including yeast, flies, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways. In Drosophila, CAP functions in Hedgehog-mediated eye development and in establishing oocyte polarity. In Dictyostelium discoideum, CAP is involved in microfilament reorganisation near the plasma membrane in a PIP2-regulated manner and is required to perpetuate the cAMP relay signal to organise fruitbody formation. In plants, CAP is involved in plant signalling pathways required for co-ordinated organ expansion. In yeast, CAP is involved in adenylate cyclase activation, as well as in vesicle trafficking and endocytosis. In both yeast and mammals, CAPs appear to be involved in recycling G-actin monomers from ADF/cofilins for subsequent rounds of filament assembly. In mammals, there are two different CAPs that share 64% amino acid identity.

References

1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028656 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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. doi:10.1128/mcb.12.11.5033. PMC 360436 . PMID 1406678.
1 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. S2CID 46076387.
1 2 "Entrez Gene: CAP1 CAP, adenylate cyclase-associated protein 1 (yeast)".
↑ Hubberstey, A; Yu G; Loewith R; Lakusta C; Young D (Jun 1996). "Mammalian CAP interacts with CAP, CAP2, and actin". J. Cell. Biochem. 61 (3). UNITED STATES: 459–66. doi:10.1002/(SICI)1097-4644(19960601)61:3<459::AID-JCB13>3.0.CO;2-E. ISSN 0730-2312. PMID 8761950. S2CID 46076387.

External links

Human CAP1 genome location and CAP1 gene details page in the UCSC Genome Browser .

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. doi:10.1242/jcs.107.6.1671. 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. doi:10.1242/jcs.115.8.1591. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 23783563.
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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
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. S2CID 69278.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. 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. S2CID 10789246.
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. S2CID 46630115.

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[refGRCm38Ensembl-1] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028656 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1406678-4] 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. doi:10.1128/mcb.12.11.5033. PMC 360436 . PMID 1406678.

[pmid8761950-5] 1 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. S2CID 46076387.

[entrez-6] 1 2 "Entrez Gene: CAP1 CAP, adenylate cyclase-associated protein 1 (yeast)".

[autogenerated1-7] Hubberstey, A; Yu G; Loewith R; Lakusta C; Young D (Jun 1996). "Mammalian CAP interacts with CAP, CAP2, and actin". J. Cell. Biochem. 61 (3). UNITED STATES: 459–66. doi:10.1002/(SICI)1097-4644(19960601)61:3<459::AID-JCB13>3.0.CO;2-E. ISSN 0730-2312. PMID 8761950. S2CID 46076387.

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CAP1

Contents

Interactions

See also

Related Research Articles

References

External links

Further reading