CENTD2

ARAP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4X1V
Identifiers
Aliases	ARAP1, CENTD2, ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 1, cnt-d2
External IDs	OMIM: 606646 MGI: 1916960 HomoloGene: 12326 GeneCards: ARAP1
Gene location (Human) Chr. Chromosome 11 (human) Band 11q13.4 Start 72,685,069 bp End 72,793,599 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 E2 Start 100,997,274 bp End 101,061,793 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte right uterine tube upper lobe of left lung right lung spleen anterior pituitary right lobe of thyroid gland left lobe of thyroid gland gallbladder sural nerve Top expressed in lip thymus uterus spleen vas deferens esophagus dermis carotid body duodenum stomach More reference expression data BioGPS n/a
Gene ontology Molecular function metal ion binding protein binding GTPase activator activity phosphatidylinositol-3,4,5-trisphosphate binding type 1 angiotensin receptor binding Cellular component cytoplasm Golgi apparatus membrane Golgi cisterna membrane trans-Golgi network cytoplasmic vesicle nucleoplasm cytosol plasma membrane intracellular membrane-bounded organelle Biological process actin filament reorganization involved in cell cycle regulation of cell shape negative regulation of stress fiber assembly regulation of small GTPase mediated signal transduction positive regulation of filopodium assembly signal transduction positive regulation of receptor recycling positive regulation of epidermal growth factor receptor signaling pathway positive regulation of GTPase activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 116985 69710 Ensembl ENSG00000186635 ENSMUSG00000032812 UniProt Q96P48 Q4LDD4 RefSeq (mRNA) NM_015242 NM_001040118 NM_001135190 NM_001369489 NM_001040111 NM_001040112 NM_027180 NM_198096 RefSeq (protein) NP_001035207 NP_001128662 NP_056057 NP_001356418 NP_001035200 NP_001035201 NP_081456 NP_932764 NP_001394730 NP_001394732 Location (UCSC) Chr 11: 72.69 – 72.79 Mb Chr 7: 101 – 101.06 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 is a protein that in humans is encoded by the ARAP1 gene.

Function

The protein encoded by this gene contains ARF-GAP, RHO-GAP, ankyrin repeat, RAS-associating, and pleckstrin homology domains. In vitro, this protein displays RHO-GAP and phosphatidylinositol (3,4,5) trisphosphate (PIP3)-dependent ARF-GAP activity. The encoded protein associates with the Golgi, and the ARF-GAP activity mediates changes in the Golgi and the formation of filopodia. The RHO-GAP activity may mediate cell rounding and loss of stress fibers. At least three transcript variants encoding different isoforms have been found for this gene, but the full-length natures of all variants have not been determined.

External links

• Human ARAP1 genome location and ARAP1 gene details page in the UCSC Genome Browser.

Further reading

• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (June 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research. 9 (3): 99–106. CiteSeerX 10.1.1.500.923. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (October 1998). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.
• Krugmann S, Anderson KE, Ridley SH, Risso N, McGregor A, Coadwell J, Davidson K, Eguinoa A, Ellson CD, Lipp P, Manifava M, Ktistakis N, Painter G, Thuring JW, Cooper MA, Lim ZY, Holmes AB, Dove SK, Michell RH, Grewal A, Nazarian A, Erdjument-Bromage H, Tempst P, Stephens LR, Hawkins PT (January 2002). "Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices". Molecular Cell. 9 (1): 95–108. doi:10.1016/S1097-2765(02)00434-3. PMID 11804589.
• Miura K, Jacques KM, Stauffer S, Kubosaki A, Zhu K, Hirsch DS, Resau J, Zheng Y, Randazzo PA (January 2002). "ARAP1: a point of convergence for Arf and Rho signaling". Molecular Cell. 9 (1): 109–19. doi:10.1016/S1097-2765(02)00428-8. PMID 11804590.
• Ahn J, Chung KS, Kim DU, Won M, Kim L, Kim KS, Nam M, Choi SJ, Kim HC, Yoon M, Chae SK, Hoe KL (November 2004). "Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus". Journal of Biochemistry and Molecular Biology. 37 (6): 741–8. doi:10.5483/bmbrep.2004.37.6.741. PMID 15607035.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.