Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q68FF6 (GIT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
G protein-coupled receptor kinase-interactor 1
GRK-interacting protein 1
Gene names
Name:Git1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length770 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 By similarity.

Subunit structure

Interacts with G protein-coupled receptor kinases: ADRBK1/GRK2, PPFIA1 and PPFIA4, with ARHGEF6/alpha-PIX, with ARHGEF7/beta-PIX, with PXN/paxillin and with PTK2/FAK1. Component of cytoplasmic complexes, which also contain PXN, ARHGEF6 and PAK1. Interacts with SCRIB By similarity. Interacts with TGFB1I1. Ref.3

Subcellular location

Cytoplasm By similarity. 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 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.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainANK repeat
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionGTPase activation
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of ARF GTPase activity

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionARF 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

Arhgef7Q9ES282EBI-645933,EBI-642580

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 770770ARF GTPase-activating protein GIT1
PRO_0000074201

Regions

Domain1 – 124124Arf-GAP
Repeat132 – 16130ANK 1
Repeat166 – 19530ANK 2
Repeat199 – 22830ANK 3
Zinc finger11 – 3424C4-type
Region253 – 424172PTK2/FAK1-binding By similarity
Region254 – 376123ARHGEF6-binding By similarity
Region646 – 770125Interaction with PXN and TGFB1I1 By similarity

Amino acid modifications

Modified residue2241Phosphotyrosine Ref.7
Modified residue3711Phosphoserine By similarity
Modified residue3731Phosphothreonine By similarity
Modified residue3841Phosphoserine By similarity
Modified residue3921Phosphotyrosine By similarity
Modified residue3941Phosphoserine By similarity
Modified residue3971Phosphoserine By similarity
Modified residue4011Phosphothreonine By similarity
Modified residue4191Phosphoserine By similarity
Modified residue5541Phosphotyrosine Ref.8
Modified residue5631Phosphotyrosine Ref.4
Modified residue6011Phosphoserine Ref.6
Modified residue6051Phosphoserine By similarity
Modified residue6101Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q68FF6 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C516E7A49578D0B4

FASTA77085,300
        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 SPTDNLELSA RSQSELDDQH DYDSVASDED TDQEPLPSAG ATRNNRARSM 

       430        440        450        460        470        480 
DSSDLSDGAV TLQEYLELKK ALATSEAKVQ QLMKVNSSLS DELRRLQREI HKLQAENLQL 

       490        500        510        520        530        540 
RQPPGPVPPP SLPSERAEHT LMGPGGSTHR RDRQAFSMYE PGSALKPFGG TPGDELATRL 

       550        560        570        580        590        600 
QPFHSTELED DAIYSVHVPA GLYRIRKGVS ASSVPFTPSS PLLSCSQEGS RHASKLSRHG 

       610        620        630        640        650        660 
SGADSDYENT QSGDPLLGLE GKRFLELSKE DELHPELESL DGDLDPGLPS TEDVILKTEQ 

       670        680        690        700        710        720 
VTKNIQELLR AAQEFKHDSF VPCSEKIHLA VTEMASLFPK RPALEPVRSS LRLLNASAYR 

       730        740        750        760        770 
LQSECRKTVP PEPGAPVDFQ LLTQQVIQCA YDIAKAAKQL VTITTREKKQ 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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].
Strain: C57BL/6.
Tissue: Brain.
[3]"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.
[4]"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-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL607072 Genomic DNA. Translation: CAI52039.1.
BC079870 mRNA. Translation: AAH79870.1.
RefSeqNP_001004144.1. NM_001004144.1.
UniGeneMm.290182.

3D structure databases

ProteinModelPortalQ68FF6.
SMRQ68FF6. Positions 3-286, 427-482, 640-770.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229822. 7 interactions.
IntActQ68FF6. 19 interactions.

PTM databases

PhosphoSiteQ68FF6.

Proteomic databases

PaxDbQ68FF6.
PRIDEQ68FF6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037285; ENSMUSP00000037210; ENSMUSG00000011877.
GeneID216963.
KEGGmmu:216963.
UCSCuc007kgy.1. mouse.

Organism-specific databases

CTD28964.
MGIMGI:1927140. Git1.

Phylogenomic databases

eggNOGCOG5347.
GeneTreeENSGT00730000110864.
HOGENOMHOG000232135.
HOVERGENHBG012506.
InParanoidQ68FF6.
KOK05737.
OMASARSQSD.
OrthoDBEOG7KQ212.
PhylomeDBQ68FF6.
TreeFamTF317762.

Gene expression databases

ArrayExpressQ68FF6.
BgeeQ68FF6.
CleanExMM_GIT1.
GenevestigatorQ68FF6.

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. mouse.
NextBio375468.
PROQ68FF6.
SOURCESearch...

Entry information

Entry nameGIT1_MOUSE
AccessionPrimary (citable) accession number: Q68FF6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot