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Protein

ARF GTPase-activating protein GIT1

Gene

Git1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). Involved in the regulation of cytokinesis; the function may involve SDCCAG3 and PTPN13 (PubMed:23108400).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 3424C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ARF GTPase activator activity Source: InterPro
  2. protein complex binding Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. dendritic spine development Source: MGI
  2. ephrin receptor signaling pathway Source: MGI
  3. immunological synapse formation Source: MGI
  4. regulation of ARF GTPase activity Source: InterPro
  5. regulation of cytokinesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_278281. Ephrin signaling.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Git1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1927140. Git1.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. aggresome Source: MGI
  2. cytoplasm Source: MGI
  3. cytosol Source: Reactome
  4. focal adhesion Source: MGI
  5. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 770770ARF GTPase-activating protein GIT1PRO_0000074201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei224 – 2241Phosphotyrosine1 Publication
Modified residuei371 – 3711PhosphoserineBy similarity
Modified residuei373 – 3731PhosphothreonineBy similarity
Modified residuei384 – 3841PhosphoserineBy similarity
Modified residuei392 – 3921PhosphotyrosineBy similarity
Modified residuei394 – 3941PhosphoserineBy similarity
Modified residuei397 – 3971PhosphoserineBy similarity
Modified residuei401 – 4011PhosphothreonineBy similarity
Modified residuei419 – 4191PhosphoserineBy similarity
Modified residuei554 – 5541Phosphotyrosine1 Publication
Modified residuei563 – 5631Phosphotyrosine1 Publication
Modified residuei601 – 6011Phosphoserine1 Publication
Modified residuei605 – 6051PhosphoserineBy similarity
Modified residuei610 – 6101PhosphothreonineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ68FF6.
PaxDbiQ68FF6.
PRIDEiQ68FF6.

PTM databases

PhosphoSiteiQ68FF6.

Expressioni

Gene expression databases

BgeeiQ68FF6.
CleanExiMM_GIT1.
ExpressionAtlasiQ68FF6. baseline and differential.
GenevestigatoriQ68FF6.

Interactioni

Subunit structurei

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. Interacts with SDCCAG3 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Arhgef7Q9ES282EBI-645933,EBI-642580

Protein-protein interaction databases

BioGridi229822. 7 interactions.
IntActiQ68FF6. 19 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ68FF6.
SMRiQ68FF6. Positions 3-221, 427-482, 640-770.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 124124Arf-GAPPROSITE-ProRule annotationAdd
BLAST
Repeati132 – 16130ANK 1Add
BLAST
Repeati166 – 19530ANK 2Add
BLAST
Repeati199 – 22830ANK 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni253 – 424172PTK2/FAK1-bindingBy similarityAdd
BLAST
Regioni254 – 376123ARHGEF6-bindingBy similarityAdd
BLAST
Regioni646 – 770125Interaction with PXN and TGFB1I1By similarityAdd
BLAST

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation
Contains 1 Arf-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 3424C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00730000110864.
HOGENOMiHOG000232135.
HOVERGENiHBG012506.
InParanoidiQ68FF6.
KOiK05737.
OMAiSARSQSD.
OrthoDBiEOG7KQ212.
PhylomeDBiQ68FF6.
TreeFamiTF317762.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR022018. GIT1_C.
IPR013724. GIT_SHD.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF12205. GIT1_C. 1 hit.
PF08518. GIT_SHD. 2 hits.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00555. GIT. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q68FF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRKGPRAEV CADCSAPDPG WASISRGVLV CDECCSVHRS LGRHISIVKH
60 70 80 90 100
LRHSAWPPTL LQMVHTLASN GANSIWEHSL LDPAQVQSGR RKANPQDKVH
110 120 130 140 150
PIKSEFIRAK YQMLAFVHKL PCRDDDGVTA KDLSKQLHSS VRTGNLETCL
160 170 180 190 200
RLLSLGAQAN FFHPEKGTTP LHVAAKAGQT LQAELLVVYG ADPGSPDVNG
210 220 230 240 250
RTPIDYARQA GHHELAERLV ECQYELTDRL AFYLCGRKPD HKNGHYIIPQ
260 270 280 290 300
MADRSRQKCM SQSLDLSELA KAAKKKLQAL SNRLFEELAM DVYDEVDRRE
310 320 330 340 350
NDAVWLATQN HSTLVTERSA VPFLPVNPEY SATRNQGRQK LARFNAREFA
360 370 380 390 400
TLIIDILSEA KRRQQGKSLS SPTDNLELSA RSQSELDDQH DYDSVASDED
410 420 430 440 450
TDQEPLPSAG ATRNNRARSM DSSDLSDGAV TLQEYLELKK ALATSEAKVQ
460 470 480 490 500
QLMKVNSSLS DELRRLQREI HKLQAENLQL RQPPGPVPPP SLPSERAEHT
510 520 530 540 550
LMGPGGSTHR RDRQAFSMYE PGSALKPFGG TPGDELATRL QPFHSTELED
560 570 580 590 600
DAIYSVHVPA GLYRIRKGVS ASSVPFTPSS PLLSCSQEGS RHASKLSRHG
610 620 630 640 650
SGADSDYENT QSGDPLLGLE GKRFLELSKE DELHPELESL DGDLDPGLPS
660 670 680 690 700
TEDVILKTEQ VTKNIQELLR AAQEFKHDSF VPCSEKIHLA VTEMASLFPK
710 720 730 740 750
RPALEPVRSS LRLLNASAYR LQSECRKTVP PEPGAPVDFQ LLTQQVIQCA
760 770
YDIAKAAKQL VTITTREKKQ
Length:770
Mass (Da):85,300
Last modified:October 11, 2004 - v1
Checksum:iC516E7A49578D0B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL607072 Genomic DNA. Translation: CAI52039.1.
BC079870 mRNA. Translation: AAH79870.1.
CCDSiCCDS25080.1.
RefSeqiNP_001004144.1. NM_001004144.1.
UniGeneiMm.290182.

Genome annotation databases

EnsembliENSMUST00000037285; ENSMUSP00000037210; ENSMUSG00000011877.
GeneIDi216963.
KEGGimmu:216963.
UCSCiuc007kgy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL607072 Genomic DNA. Translation: CAI52039.1.
BC079870 mRNA. Translation: AAH79870.1.
CCDSiCCDS25080.1.
RefSeqiNP_001004144.1. NM_001004144.1.
UniGeneiMm.290182.

3D structure databases

ProteinModelPortaliQ68FF6.
SMRiQ68FF6. Positions 3-221, 427-482, 640-770.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229822. 7 interactions.
IntActiQ68FF6. 19 interactions.

PTM databases

PhosphoSiteiQ68FF6.

Proteomic databases

MaxQBiQ68FF6.
PaxDbiQ68FF6.
PRIDEiQ68FF6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037285; ENSMUSP00000037210; ENSMUSG00000011877.
GeneIDi216963.
KEGGimmu:216963.
UCSCiuc007kgy.1. mouse.

Organism-specific databases

CTDi28964.
MGIiMGI:1927140. Git1.

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00730000110864.
HOGENOMiHOG000232135.
HOVERGENiHBG012506.
InParanoidiQ68FF6.
KOiK05737.
OMAiSARSQSD.
OrthoDBiEOG7KQ212.
PhylomeDBiQ68FF6.
TreeFamiTF317762.

Enzyme and pathway databases

ReactomeiREACT_278281. Ephrin signaling.

Miscellaneous databases

ChiTaRSiGit1. mouse.
NextBioi375468.
PROiQ68FF6.
SOURCEiSearch...

Gene expression databases

BgeeiQ68FF6.
CleanExiMM_GIT1.
ExpressionAtlasiQ68FF6. baseline and differential.
GenevestigatoriQ68FF6.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR022018. GIT1_C.
IPR013724. GIT_SHD.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF12205. GIT1_C. 1 hit.
PF08518. GIT_SHD. 2 hits.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00555. GIT. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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(2003) [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(2001) [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(2004) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. 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(2007) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. "The serologically defined colon cancer antigen-3 interacts with the protein tyrosine phosphatase PTPN13 and is involved in the regulation of cytokinesis."
    Hagemann N., Ackermann N., Christmann J., Brier S., Yu F., Erdmann K.S.
    Oncogene 32:4602-4613(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGIT1_MOUSE
AccessioniPrimary (citable) accession number: Q68FF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 11, 2004
Last modified: April 1, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.