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Q9Y2X7 (GIT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length761 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 761761ARF GTPase-activating protein GIT1
PRO_0000074200

Regions

Domain1 – 124124Arf-GAP
Repeat132 – 16130ANK 1
Repeat166 – 19530ANK 2
Repeat199 – 22830ANK 3
Zinc finger11 – 3424C4-type
Region251 – 415165PTK2/FAK1-binding By similarity
Region254 – 367114ARHGEF6-binding By similarity
Region637 – 761125Interaction with PXN and TGFB1I1 By similarity

Amino acid modifications

Modified residue2241Phosphotyrosine By similarity
Modified residue3621Phosphoserine Ref.13 Ref.16 Ref.19
Modified residue3641Phosphothreonine Ref.16 Ref.17
Modified residue3751Phosphoserine Ref.16
Modified residue3831Phosphotyrosine Ref.13 Ref.16
Modified residue3851Phosphoserine Ref.13 Ref.16 Ref.17
Modified residue3881Phosphoserine Ref.10 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19
Modified residue3921Phosphothreonine Ref.13 Ref.16
Modified residue4101Phosphoserine Ref.13 Ref.16 Ref.17
Modified residue5451Phosphotyrosine Ref.16
Modified residue5541Phosphotyrosine Ref.9
Modified residue5921Phosphoserine Ref.10 Ref.12 Ref.13 Ref.16
Modified residue5961Phosphoserine Ref.13 Ref.16
Modified residue6011Phosphothreonine Ref.16

Natural variations

Alternative sequence134 – 17643SKQLH…HVAAK → TGHRSWATPDINPHPNRATG TSALSAATLPGSQVPWCPPL SSP in isoform 2.
VSP_009666
Alternative sequence177 – 761585Missing in isoform 2.
VSP_009667
Alternative sequence2531D → DRSRQKCMSQ in isoform 3.
VSP_040984

Experimental info

Sequence conflict1211P → S in AAD28046. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: 702744942A796399

FASTA76184,341
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 2B5BB45555AB5201
Show »

FASTA17619,160
Isoform 3 [UniParc].

Checksum: 278AD8D706C32EE0
Show »

FASTA77085,446

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_001078923.1. NM_001085454.1.
NP_054749.2. NM_014030.3.
XP_005258024.1. XM_005257967.1.
UniGeneHs.514051.

3D structure databases

ProteinModelPortalQ9Y2X7.
SMRQ9Y2X7. Positions 3-285, 418-473, 631-761.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118789. 54 interactions.
IntActQ9Y2X7. 39 interactions.
MINTMINT-243639.
STRING9606.ENSP00000378338.

PTM databases

PhosphoSiteQ9Y2X7.

Polymorphism databases

DMDM45645212.

Proteomic databases

PaxDbQ9Y2X7.
PRIDEQ9Y2X7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225394; ENSP00000225394; ENSG00000108262. [Q9Y2X7-1]
ENST00000394869; ENSP00000378338; ENSG00000108262. [Q9Y2X7-3]
ENST00000581348; ENSP00000462775; ENSG00000108262.
GeneID28964.
KEGGhsa:28964.
UCSCuc002hef.2. human. [Q9Y2X7-1]
uc002heg.2. human. [Q9Y2X7-3]

Organism-specific databases

CTD28964.
GeneCardsGC17M027900.
H-InvDBHIX0013673.
HGNCHGNC:4272. GIT1.
HPAHPA004059.
HPA004186.
MIM608434. gene.
neXtProtNX_Q9Y2X7.
PharmGKBPA28683.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5347.
HOGENOMHOG000232135.
HOVERGENHBG012506.
KOK05737.
OMASARSQSD.
OrthoDBEOG7KQ212.
PhylomeDBQ9Y2X7.
TreeFamTF317762.

Enzyme and pathway databases

SignaLinkQ9Y2X7.

Gene expression databases

ArrayExpressQ9Y2X7.
BgeeQ9Y2X7.
CleanExHS_GIT1.
GenevestigatorQ9Y2X7.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR022018. GIT1_C.
IPR013724. GIT_SHD.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF12205. GIT1_C. 1 hit.
PF08518. GIT_SHD. 2 hits.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00555. GIT. 2 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 2 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGIT1. human.
GeneWikiGIT1.
GenomeRNAi28964.
NextBio51807.
PMAP-CutDBQ9Y2X7.
PROQ9Y2X7.
SOURCESearch...

Entry information

Entry nameGIT1_HUMAN
AccessionPrimary (citable) accession number: Q9Y2X7
Secondary accession number(s): B4DGU9 expand/collapse secondary AC list , B4DSV3, Q86SS0, Q9BRJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: March 15, 2004
Last modified: March 19, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM