ARF GTPase-activating protein GIT1 - Mus musculus (Mouse)

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Q68FF6 (GIT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

Git1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	770 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 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 component	Cytoplasm
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
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from electronic annotation. Source: Compara
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	Q9ES28	2	EBI-645933,EBI-642580

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 770

770

ARF GTPase-activating protein GIT1

PRO_0000074201

Regions

Domain

1 – 124

124

Arf-GAP

Repeat

132 – 161

ANK 1

Repeat

166 – 195

ANK 2

Repeat

199 – 228

ANK 3

Zinc finger

11 – 34

C4-type

Region

253 – 424

172

PTK2/FAK1-binding By similarity

Region

254 – 376

123

ARHGEF6-binding By similarity

Region

646 – 770

125

Interaction with PXN and TGFB1I1 By similarity

Amino acid modifications

Modified residue

224

Phosphotyrosine Ref.4

Modified residue

370

Phosphoserine Ref.5

Modified residue

371

Phosphoserine Ref.5

Modified residue

373

Phosphothreonine By similarity

Modified residue

384

Phosphoserine By similarity

Modified residue

392

Phosphotyrosine By similarity

Modified residue

394

Phosphoserine Ref.5

Modified residue

397

Phosphoserine Ref.6

Modified residue

401

Phosphothreonine By similarity

Modified residue

419

Phosphoserine By similarity

Modified residue

517

Phosphoserine Ref.6

Modified residue

554

Phosphotyrosine Ref.7

Modified residue

563

Phosphotyrosine By similarity

Modified residue

601

Phosphoserine Ref.6

Modified residue

605

Phosphoserine By similarity

Modified residue

610

Phosphothreonine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q68FF6 [UniParc].

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

770

85,300

        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' referencesShow '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. 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]	"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, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 AND SER-394, MASS SPECTROMETRY. Tissue: Brain cortex.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-517 AND SER-601, MASS SPECTROMETRY. Tissue: Melanoma.
[7]	"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, MASS SPECTROMETRY. 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.
IPI	IPI00470095.
RefSeq	NP_001004144.1. NM_001004144.1.
UniGene	Mm.290182.
3D structure databases
ProteinModelPortal	Q68FF6.
SMR	Q68FF6. Positions 3-280, 427-482, 640-770.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q68FF6. 18 interactions.
PTM databases
PhosphoSite	Q68FF6.
Proteomic databases
PaxDb	Q68FF6.
PRIDE	Q68FF6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000037285; ENSMUSP00000037210; ENSMUSG00000011877.
GeneID	216963.
KEGG	mmu:216963.
UCSC	uc007kgy.1. mouse.
Organism-specific databases
CTD	28964.
MGI	MGI:1927140. Git1.
Phylogenomic databases
eggNOG	COG5347.
GeneTree	ENSGT00700000104126.
HOGENOM	HOG000232135.
HOVERGEN	HBG012506.
InParanoid	Q68FF6.
KO	K05737.
OMA	RAEHTPM.
OrthoDB	EOG4GTKCB.
Gene expression databases
ArrayExpress	Q68FF6.
Bgee	Q68FF6.
CleanEx	MM_GIT1.
Genevestigator	Q68FF6.
GermOnline	ENSMUSG00000011877. Mus musculus.
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. mouse.
NextBio	375468.
SOURCE	Search...

Entry information

Entry name

GIT1_MOUSE

Accession

Primary (citable) accession number: Q68FF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents