CENTG2

ArfGAP with GTPase domain, ankyrin repeat and PH domain 1

Identifiers

AGAP1 ; AGAP-1; CENTG2; GGAP1; cnt-g2

External IDs

OMIM: 608651 MGI: 2653690 HomoloGene: 56689 GeneCards: AGAP1 Gene

Gene ontology
Molecular function	• GTP binding • phospholipid binding • ARF GTPase activator activity • zinc ion binding
Cellular component	• cytoplasm
Biological process	• small GTPase mediated signal transduction • protein transport • regulation of ARF GTPase activity • positive regulation of GTPase activity
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

ENSG00000157985

ENSMUSG00000055013

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
236.4 – 237.04 Mb

Chr 1:
89.45 – 89.9 Mb

PubMed search

Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1 is an enzyme that in humans is encoded by the AGAP1 gene.^[1]

CENTG2 belongs to an ADP-ribosylation factor GTPase-activating (ARF-GAP) protein family involved in membrane traffic and actin cytoskeleton dynamics (Nie et al., 2002).[supplied by OMIM]^[1]

HACNS1

HACNS1 is located in an intron of the gene CENTG2 (also known as Human Accelerated Region 2). HACNS1 is hypothesized to be a gene enhancer "that may have contributed to the evolution of the uniquely opposable human thumb, and possibly also modifications in the ankle or foot that allow humans to walk on two legs". Evidence to date shows that of the 110,000 gene enhancer sequences identified in the human genome, HACNS1 has undergone the most change during the evolution of humans following the split with the ancestors of chimpanzees.^[2]

References

Further reading

Kikuno R, Nagase T, Ishikawa K et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197–205. doi:10.1093/dnares/6.3.197. PMID 10470851.
Nie Z, Stanley KT, Stauffer S et al. (2003). "AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton". J. Biol. Chem. 277 (50): 48965–75. doi:10.1074/jbc.M202969200. PMID 12388557.
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.
Xia C, Ma W, Stafford LJ et al. (2003). "GGAPs, a New Family of Bifunctional GTP-Binding and GTPase-Activating Proteins". Mol. Cell. Biol. 23 (7): 2476–88. doi:10.1128/MCB.23.7.2476-2488.2003. PMC 150724. PMID 12640130.
Nie Z, Boehm M, Boja ES et al. (2003). "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Dev. Cell 5 (3): 513–21. doi:10.1016/S1534-5807(03)00234-X. PMID 12967569.
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.
Meurer S, Pioch S, Wagner K et al. (2005). "AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl cyclase". J. Biol. Chem. 279 (47): 49346–54. doi:10.1074/jbc.M410565200. PMID 15381706.
Wassink TH, Piven J, Vieland VJ et al. (2005). "Evaluation of the chromosome 2q37.3 gene CENTG2 as an autism susceptibility gene". Am. J. Med. Genet. B Neuropsychiatr. Genet. 136 (1): 36–44. doi:10.1002/ajmg.b.30180. PMID 15892143.
Nie Z, Fei J, Premont RT, Randazzo PA (2005). "The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3". J. Cell. Sci. 118 (Pt 15): 3555–66. doi:10.1242/jcs.02486. PMID 16079295.
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.