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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)DescriptionActionsGraphical viewLength
Zinc fingeri11 – 34C4-typePROSITE-ProRule annotationAdd BLAST24

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein complex binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3928664. 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
Proteomesi
  • UP000000589 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000742011 – 770ARF GTPase-activating protein GIT1Add BLAST770

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei224PhosphotyrosineCombined sources1
Modified residuei368PhosphoserineCombined sources1
Modified residuei371PhosphoserineCombined sources1
Modified residuei373PhosphothreonineBy similarity1
Modified residuei379PhosphoserineBy similarity1
Modified residuei384PhosphoserineBy similarity1
Modified residuei392PhosphotyrosineBy similarity1
Modified residuei394PhosphoserineCombined sources1
Modified residuei397PhosphoserineCombined sources1
Modified residuei401PhosphothreonineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei422PhosphoserineCombined sources1
Modified residuei426PhosphoserineCombined sources1
Modified residuei507PhosphoserineBy similarity1
Modified residuei545PhosphoserineCombined sources1
Modified residuei546PhosphothreonineCombined sources1
Modified residuei554PhosphotyrosineCombined sources1
Modified residuei563PhosphotyrosineCombined sources1
Modified residuei570PhosphoserineCombined sources1
Modified residuei580PhosphoserineBy similarity1
Modified residuei601PhosphoserineCombined sources1
Modified residuei605PhosphoserineCombined sources1
Modified residuei610PhosphothreonineCombined sources1
Modified residuei639PhosphoserineBy similarity1

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

EPDiQ68FF6.
MaxQBiQ68FF6.
PaxDbiQ68FF6.
PeptideAtlasiQ68FF6.
PRIDEiQ68FF6.

PTM databases

iPTMnetiQ68FF6.
PhosphoSitePlusiQ68FF6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000011877.
CleanExiMM_GIT1.
ExpressionAtlasiQ68FF6. baseline and differential.
GenevisibleiQ68FF6. MM.

Interactioni

Subunit structurei

Interacts with G protein-coupled receptor kinases: 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

GO - Molecular functioni

  • protein complex binding Source: MGI

Protein-protein interaction databases

BioGridi229822. 7 interactors.
IntActiQ68FF6. 20 interactors.
STRINGi10090.ENSMUSP00000037210.

Structurei

3D structure databases

ProteinModelPortaliQ68FF6.
SMRiQ68FF6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 124Arf-GAPPROSITE-ProRule annotationAdd BLAST124
Repeati132 – 161ANK 1Add BLAST30
Repeati166 – 195ANK 2Add BLAST30
Repeati199 – 228ANK 3Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni253 – 424PTK2/FAK1-bindingBy similarityAdd BLAST172
Regioni254 – 376ARHGEF6-bindingBy similarityAdd BLAST123
Regioni646 – 770Interaction with PXN and TGFB1I1By similarityAdd BLAST125

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri11 – 34C4-typePROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0818. Eukaryota.
ENOG410XR8U. LUCA.
GeneTreeiENSGT00860000133715.
HOGENOMiHOG000232135.
HOVERGENiHBG012506.
InParanoidiQ68FF6.
KOiK05737.
OMAiQKCMSQS.
OrthoDBiEOG091G03VD.
PhylomeDBiQ68FF6.
TreeFamiTF317762.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR032352. GIT1/2_CC.
IPR022018. GIT1_C.
IPR013724. GIT_SHD.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF12205. GIT1_C. 1 hit.
PF16559. GIT_CC. 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229822. 7 interactors.
IntActiQ68FF6. 20 interactors.
STRINGi10090.ENSMUSP00000037210.

PTM databases

iPTMnetiQ68FF6.
PhosphoSitePlusiQ68FF6.

Proteomic databases

EPDiQ68FF6.
MaxQBiQ68FF6.
PaxDbiQ68FF6.
PeptideAtlasiQ68FF6.
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

eggNOGiKOG0818. Eukaryota.
ENOG410XR8U. LUCA.
GeneTreeiENSGT00860000133715.
HOGENOMiHOG000232135.
HOVERGENiHBG012506.
InParanoidiQ68FF6.
KOiK05737.
OMAiQKCMSQS.
OrthoDBiEOG091G03VD.
PhylomeDBiQ68FF6.
TreeFamiTF317762.

Enzyme and pathway databases

ReactomeiR-MMU-3928664. Ephrin signaling.

Miscellaneous databases

ChiTaRSiGit1. mouse.
PROiQ68FF6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000011877.
CleanExiMM_GIT1.
ExpressionAtlasiQ68FF6. baseline and differential.
GenevisibleiQ68FF6. MM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR032352. GIT1/2_CC.
IPR022018. GIT1_C.
IPR013724. GIT_SHD.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF12205. GIT1_C. 1 hit.
PF16559. GIT_CC. 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...

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: November 30, 2016
This is version 130 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

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 one 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.