GIT2

From Wikipedia, the free encyclopedia

G protein-coupled receptor kinase interactor 2

Identifiers

GIT2; CAT-2; DKFZp686G01261; KIAA0148; MGC760

External IDs

OMIM: 608564 MGI: 1347053 HomoloGene: 41336

Gene ontology
Molecular Function:	• GTPase activator activity • zinc ion binding • metal ion binding
Cellular Component:	• nucleoplasm
Biological Process:	• regulation of G-protein coupled receptor protein signaling pathway • regulation of GTPase activity

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_014776 (mRNA)
NP_055591 (protein)

NM_001077359 (mRNA)
NP_001070827 (protein)

Location

Chr 12: 108.85 - 108.92 Mb

Chr 5: 114.99 - 115.03 Mb

Pubmed search

[1]

[2]

G protein-coupled receptor kinase interactor 2, also known as GIT2, is a human gene.^[1]

This gene encodes a member of the GIT protein family. GIT proteins interact with G protein-coupled receptor kinases and possess ADP-ribosylation factor (ARF) GTPase-activating protein (GAP) activity. This gene undergoes extensive alternative splicing; although ten transcript variants have been described, the full length sequence has been determined for only four variants. The various isoforms have functional differences, with respect to ARF GAP activity and to G protein-coupled receptor kinase 2 binding.^[1]

[edit] References

^ ^a ^b Entrez Gene: GIT2 G protein-coupled receptor kinase interactor 2.

[edit] Further reading

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. PMID 12168954.
Hoefen RJ, Berk BC (2006). "The multifunctional GIT family of proteins.". J. Cell. Sci. 119 (Pt 8): 1469–75. doi:10.1242/jcs.02925. PMID 16598076.
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. PMID 8125298.
Nagase T, Seki N, Tanaka A, et al. (1996). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 2 (4): 167–74, 199–210. PMID 8590280.
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. PMID 9373149.
Premont RT, Claing A, Vitale N, et al. (1998). "beta2-Adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein.". Proc. Natl. Acad. Sci. U.S.A. 95 (24): 14082–7. PMID 9826657.
Turner CE, Brown MC, Perrotta JA, et al. (1999). "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling.". J. Cell Biol. 145 (4): 851–63. PMID 10330411.
Bagrodia S, Bailey D, Lenard Z, et al. (1999). "A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins.". J. Biol. Chem. 274 (32): 22393–400. PMID 10428811.
Vitale N, Patton WA, Moss J, et al. (2000). "GIT proteins, A novel family of phosphatidylinositol 3,4, 5-trisphosphate-stimulated GTPase-activating proteins for ARF6.". J. Biol. Chem. 275 (18): 13901–6. PMID 10788515.
Premont RT, Claing A, Vitale N, et al. (2000). "The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing.". J. Biol. Chem. 275 (29): 22373–80. PMID 10896954.
Hoja MR, Wahlestedt C, Höög C (2000). "A visual intracellular classification strategy for uncharacterized human proteins.". Exp. Cell Res. 259 (1): 239–46. doi:10.1006/excr.2000.4948. PMID 10942595.
Ku GM, Yablonski D, Manser E, et al. (2001). "A PAK1-PIX-PKL complex is activated by the T-cell receptor independent of Nck, Slp-76 and LAT.". EMBO J. 20 (3): 457–65. doi:10.1093/emboj/20.3.457. PMID 11157752.
Mazaki Y, Hashimoto S, Okawa K, et al. (2001). "An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization.". Mol. Biol. Cell 12 (3): 645–62. PMID 11251077.
Kim S, Ko J, Shin H, et al. (2003). "The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo.". J. Biol. Chem. 278 (8): 6291–300. doi:10.1074/jbc.M212287200. PMID 12473661.
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. PMID 12477932.
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.
Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
Premont RT, Perry SJ, Schmalzigaug R, et al. (2005). "The GIT/PIX complex: an oligomeric assembly of GIT family ARF GTPase-activating proteins and PIX family Rac1/Cdc42 guanine nucleotide exchange factors.". Cell. Signal. 16 (9): 1001–11. doi:10.1016/j.cellsig.2004.02.002. PMID 15212761.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.