Q9Y2X7 (GIT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ARF GTPase-activating protein GIT1
Short name=ARF GAP GIT1

Alternative name(s):
Cool-associated and tyrosine-phosphorylated protein 1
Short name=CAT-1
Short name=CAT1
G protein-coupled receptor kinase-interactor 1
GRK-interacting protein 1

Gene names

Name:

GIT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	761 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes. Ref.7
Subunit structure	Interacts with G protein-coupled receptor kinases: ADRBK1/GRK2, PPFIA1 and PPFIA4. Interacts with ARHGEF6/alpha-PIX, with ARHGEF7/beta-PIX, with PXN/paxillin and with PTK2/FAK1 By similarity. Component of cytoplasmic complexes, which also contain PXN, ARHGEF6 and PAK1. Interacts with TGFB1I1. Interacts with SCRIB. Ref.6 Ref.8 Ref.11
Subcellular location	Cytoplasm. Note: Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytoplasmic complexes and membrane protrusions. During cell migration, when cells detach, moves from the adhesions into the cytoplasmic complexes towards the leading edge, while, when cells adhere, it is found in vinculin-containing adhesions. Recruitment to adhesions may be mediated by active tyrosine-phosphorylated paxillin. Ref.7
Domain	The paxillin-binding domain is masked in the full-length protein and is regulated by ARHGEF6 By similarity.
Post-translational modification	Phosphorylated on tyrosine residues by PTK2/FAK1 and SRC in growing fibroblasts. Tyrosine-phosphorylation is increased following cell spreading on fibronectin, decreased in cells arrested in mitosis and increased in the ensuing G1 phase By similarity.
Sequence similarities	Contains 3 ANK repeats. Contains 1 Arf-GAP domain.
Sequence caution	The sequence AAH48196.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC regulation of ARF GTPase activity Inferred from electronic annotation. Source: InterPro regulation of G-protein coupled receptor protein signaling pathway Traceable author statement Ref.5. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA focal adhesion Inferred from direct assay. Source: HPA
Molecular_function	ARF GTPase activator activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARHGEF7	Q14155	2	EBI-466061,EBI-717515
BARD1	Q99728	2	EBI-466061,EBI-473181
CHD3	Q12873	2	EBI-466061,EBI-523590
HTT	P42858	10	EBI-466061,EBI-466029
KIAA1377	Q9P2H0	2	EBI-466061,EBI-473176
LRIF1	Q5T3J3	2	EBI-466061,EBI-473196

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y2X7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9Y2X7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     134-176: SKQLHSSVRT...GTTPLHVAAK → TGHRSWATPD...VPWCPPLSSP
     177-761: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9Y2X7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     253-253: D → DRSRQKCMSQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 761	761	ARF GTPase-activating protein GIT1		PRO_0000074200
Regions
	Domain	1 – 124	124	Arf-GAP
	Repeat	132 – 161	30	ANK 1
	Repeat	166 – 195	30	ANK 2
	Repeat	199 – 228	30	ANK 3
	Zinc finger	11 – 34	24	C4-type
	Region	251 – 415	165	PTK2/FAK1-binding By similarity
	Region	254 – 367	114	ARHGEF6-binding By similarity
	Region	637 – 761	125	Interaction with PXN and TGFB1I1 By similarity
Amino acid modifications
	Modified residue	224	1	Phosphotyrosine By similarity
	Modified residue	361	1	Phosphoserine By similarity
	Modified residue	362	1	Phosphoserine Ref.13 Ref.15 Ref.18
	Modified residue	364	1	Phosphothreonine Ref.15 Ref.16
	Modified residue	375	1	Phosphoserine Ref.15
	Modified residue	383	1	Phosphotyrosine Ref.13 Ref.15
	Modified residue	385	1	Phosphoserine Ref.13 Ref.15 Ref.16
	Modified residue	388	1	Phosphoserine Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18
	Modified residue	392	1	Phosphothreonine Ref.13 Ref.15
	Modified residue	410	1	Phosphoserine Ref.13 Ref.15 Ref.16
	Modified residue	508	1	Phosphoserine By similarity
	Modified residue	545	1	Phosphotyrosine Ref.15
	Modified residue	554	1	Phosphotyrosine Ref.9
	Modified residue	592	1	Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15
	Modified residue	596	1	Phosphoserine Ref.13 Ref.15
	Modified residue	601	1	Phosphothreonine Ref.15
Natural variations
	Alternative sequence	134 – 176	43	SKQLH…HVAAK → TGHRSWATPDINPHPNRATG TSALSAATLPGSQVPWCPPL SSP in isoform 2.		VSP_009666
	Alternative sequence	177 – 761	585	Missing in isoform 2.		VSP_009667
	Alternative sequence	253	1	D → DRSRQKCMSQ in isoform 3.		VSP_040984
Experimental info
	Sequence conflict	121	1	P → S in AAD28046. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 15, 2004. Version 2. Checksum: 702744942A796399	FASTA	761	84,341
	10 20 30 40 50 60 MSRKGPRAEV CADCSAPDPG WASISRGVLV CDECCSVHRS LGRHISIVKH LRHSAWPPTL 70 80 90 100 110 120 LQMVHTLASN GANSIWEHSL LDPAQVQSGR RKANPQDKVH PIKSEFIRAK YQMLAFVHKL 130 140 150 160 170 180 PCRDDDGVTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGTTP LHVAAKAGQT 190 200 210 220 230 240 LQAELLVVYG ADPGSPDVNG RTPIDYARQA GHHELAERLV ECQYELTDRL AFYLCGRKPD 250 260 270 280 290 300 HKNGHYIIPQ MADSLDLSEL AKAAKKKLQA LSNRLFEELA MDVYDEVDRR ENDAVWLATQ 310 320 330 340 350 360 NHSTLVTERS AVPFLPVNPE YSATRNQGRQ KLARFNAREF ATLIIDILSE AKRRQQGKSL 370 380 390 400 410 420 SSPTDNLELS LRSQSDLDDQ HDYDSVASDE DTDQEPLRST GATRSNRARS MDSSDLSDGA 430 440 450 460 470 480 VTLQEYLELK KALATSEAKV QQLMKVNSSL SDELRRLQRE IHKLQAENLQ LRQPPGPVPT 490 500 510 520 530 540 PPLPSERAEH TPMAPGGSTH RRDRQAFSMY EPGSALKPFG GPPGDELTTR LQPFHSTELE 550 560 570 580 590 600 DDAIYSVHVP AGLYRIRKGV SASAVPFTPS SPLLSCSQEG SRHTSKLSRH GSGADSDYEN 610 620 630 640 650 660 TQSGDPLLGL EGKRFLELGK EEDFHPELES LDGDLDPGLP STEDVILKTE QVTKNIQELL 670 680 690 700 710 720 RAAQEFKHDS FVPCSEKIHL AVTEMASLFP KRPALEPVRS SLRLLNASAY RLQSECRKTV 730 740 750 760 PPEPGAPVDF QLLTQQVIQC AYDIAKAAKQ LVTITTREKK Q
	Isoform 2 [UniParc]. Checksum: 2B5BB45555AB5201	FASTA	176	19,160
	10 20 30 40 50 60 MSRKGPRAEV CADCSAPDPG WASISRGVLV CDECCSVHRS LGRHISIVKH LRHSAWPPTL 70 80 90 100 110 120 LQMVHTLASN GANSIWEHSL LDPAQVQSGR RKANPQDKVH PIKSEFIRAK YQMLAFVHKL 130 140 150 160 170 PCRDDDGVTA KDLTGHRSWA TPDINPHPNR ATGTSALSAA TLPGSQVPWC PPLSSP
	Isoform 3 [UniParc]. Checksum: 278AD8D706C32EE0	FASTA	770	85,446
	10 20 30 40 50 60 MSRKGPRAEV CADCSAPDPG WASISRGVLV CDECCSVHRS LGRHISIVKH LRHSAWPPTL 70 80 90 100 110 120 LQMVHTLASN GANSIWEHSL LDPAQVQSGR RKANPQDKVH PIKSEFIRAK YQMLAFVHKL 130 140 150 160 170 180 PCRDDDGVTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGTTP LHVAAKAGQT 190 200 210 220 230 240 LQAELLVVYG ADPGSPDVNG RTPIDYARQA GHHELAERLV ECQYELTDRL AFYLCGRKPD 250 260 270 280 290 300 HKNGHYIIPQ MADRSRQKCM SQSLDLSELA KAAKKKLQAL SNRLFEELAM DVYDEVDRRE 310 320 330 340 350 360 NDAVWLATQN HSTLVTERSA VPFLPVNPEY SATRNQGRQK LARFNAREFA TLIIDILSEA 370 380 390 400 410 420 KRRQQGKSLS SPTDNLELSL RSQSDLDDQH DYDSVASDED TDQEPLRSTG ATRSNRARSM 430 440 450 460 470 480 DSSDLSDGAV TLQEYLELKK ALATSEAKVQ QLMKVNSSLS DELRRLQREI HKLQAENLQL 490 500 510 520 530 540 RQPPGPVPTP PLPSERAEHT PMAPGGSTHR RDRQAFSMYE PGSALKPFGG PPGDELTTRL 550 560 570 580 590 600 QPFHSTELED DAIYSVHVPA GLYRIRKGVS ASAVPFTPSS PLLSCSQEGS RHTSKLSRHG 610 620 630 640 650 660 SGADSDYENT QSGDPLLGLE GKRFLELGKE EDFHPELESL DGDLDPGLPS TEDVILKTEQ 670 680 690 700 710 720 VTKNIQELLR AAQEFKHDSF VPCSEKIHLA VTEMASLFPK RPALEPVRSS LRLLNASAYR 730 740 750 760 770 LQSECRKTVP PEPGAPVDFQ LLTQQVIQCA YDIAKAAKQL VTITTREKKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing." Premont R.T., Claing A., Vitale N., Perry S.J., Lefkowitz R.J. J. Biol. Chem. 275:22373-22380(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 585-761 (ISOFORM 1). Tissue: Lung and Melanoma.
[5]	"Beta2-adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein." Premont R.T., Claing A., Vitale N., Freeman J.L.R., Pitcher J.A., Patton W.A., Moss J., Vaughan M., Lefkowitz R.J. Proc. Natl. Acad. Sci. U.S.A. 95:14082-14087(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Hic-5 interacts with GIT1 with a different binding mode from paxillin." Nishiya N., Shirai T., Suzuki W., Nose K. J. Biochem. 132:279-289(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[7]	"GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration." Manabe R., Kovalenko M., Webb D.J., Horwitz A.R. J. Cell Sci. 115:1497-1510(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION IN CELL MIGRATION.
[8]	"Mammalian Scribble forms a tight complex with the betaPIX exchange factor." Audebert S., Navarro C., Nourry C., Chasserot-Golaz S., Lecine P., Bellaiche Y., Dupont J.-L., Premont R.T., Sempere C., Strub J.-M., Van Dorsselaer A., Vitale N., Borg J.-P. Curr. Biol. 14:987-995(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCRIB.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, MASS SPECTROMETRY.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-592, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Deregulation of scribble promotes mammary tumorigenesis and reveals a role for cell polarity in carcinoma." Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C., Muthuswamy S.K. Cell 135:865-878(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCRIB.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-592, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; TYR-383; SER-385; SER-388; THR-392; SER-410; SER-592 AND SER-596, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, MASS SPECTROMETRY. Tissue: Liver.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; THR-364; SER-375; TYR-383; SER-385; SER-388; THR-392; SER-410; TYR-545; SER-592; SER-596 AND THR-601, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-364; SER-385; SER-388 AND SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362 AND SER-388, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF124490 mRNA. Translation: AAD28046.1. AK294785 mRNA. Translation: BAG57910.1. AK299932 mRNA. Translation: BAG61765.1. AC104564 Genomic DNA. No translation available. BC006227 mRNA. Translation: AAH06227.2. BC048196 mRNA. Translation: AAH48196.1. Different initiation.
IPI	IPI00383987. IPI00384861. IPI00795611.
RefSeq	NP_001078923.1. NM_001085454.1. NP_054749.2. NM_014030.3.
UniGene	Hs.514051.
3D structure databases
ProteinModelPortal	Q9Y2X7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y2X7. 29 interactions.
MINT	MINT-243639.
STRING	9606.ENSP00000378338.
PTM databases
PhosphoSite	Q9Y2X7.
Polymorphism databases
DMDM	45645212.
Proteomic databases
PaxDb	Q9Y2X7.
PRIDE	Q9Y2X7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000225394; ENSP00000225394; ENSG00000108262. ENST00000394869; ENSP00000378338; ENSG00000108262. ENST00000581348; ENSP00000462775; ENSG00000108262.
GeneID	28964.
KEGG	hsa:28964.
UCSC	uc002hef.2. human.
Organism-specific databases
CTD	28964.
GeneCards	GC17M027900.
H-InvDB	HIX0013673.
HGNC	HGNC:4272. GIT1.
HPA	HPA004059. HPA004186.
MIM	608434. gene.
neXtProt	NX_Q9Y2X7.
PharmGKB	PA28683.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5347.
HOGENOM	HOG000232135.
HOVERGEN	HBG012506.
KO	K05737.
OMA	RAEHTPM.
OrthoDB	EOG4GTKCB.
PhylomeDB	Q9Y2X7.
Enzyme and pathway databases
Pathway_Interaction_DB	arf6cyclingpathway. Arf6 signaling events. aurora_a_pathway. Aurora A signaling. a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1. a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.
Gene expression databases
ArrayExpress	Q9Y2X7.
Bgee	Q9Y2X7.
CleanEx	HS_GIT1.
Genevestigator	Q9Y2X7.
GermOnline	ENSG00000108262. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.20. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR001164. ArfGAP. IPR022018. GIT1_C. IPR013724. GIT_SHD. [Graphical view]
Pfam	PF12796. Ank_2. 1 hit. PF01412. ArfGap. 1 hit. PF12205. GIT1_C. 1 hit. PF08518. GIT_SHD. 2 hits. [Graphical view]
PRINTS	PR00405. REVINTRACTNG.
SMART	SM00248. ANK. 3 hits. SM00105. ArfGap. 1 hit. SM00555. GIT. 2 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 1 hit. PS50115. ARFGAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GIT1. human.
GenomeRNAi	28964.
NextBio	51807.
PMAP-CutDB	Q9Y2X7.
SOURCE	Search...

Entry information

Entry name

GIT1_HUMAN

Accession

Primary (citable) accession number: Q9Y2X7
Secondary accession number(s): B4DGU9 , B4DSV3, Q86SS0, Q9BRJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	March 15, 2004
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.