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Q14161 (GIT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 GIT2

Short name=ARF GAP GIT2
Alternative name(s):
Cool-interacting tyrosine-phosphorylated protein 2
Short name=CAT-2
Short name=CAT2
G protein-coupled receptor kinase-interactor 2
GRK-interacting protein 2
Gene names
Name:GIT2
Synonyms:KIAA0148
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase-activating protein for the ADP ribosylation factor family.

Subunit structure

Interacts with TGFB1I1 By similarity. Interacts with G protein-coupled receptor kinases. Associates with paxillin. Also interacts with PIX exchange factors. Identified in a complex with ARHGEF6 and BIN2. Ref.6 Ref.15

Sequence similarities

Contains 3 ANK repeats.

Contains 1 Arf-GAP domain.

Sequence caution

The sequence BAA09769.2 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q14161-1)

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: Q14161-2)

Also known as: GIT2-short;

The sequence of this isoform differs from the canonical sequence as follows:
     466-471: QTLQSE → LGKDAN
     472-759: Missing.
Isoform 3 (identifier: Q14161-3)

Also known as: C-;

The sequence of this isoform differs from the canonical sequence as follows:
     450-464: Missing.
Isoform 4 (identifier: Q14161-4)

Also known as: BC-;

The sequence of this isoform differs from the canonical sequence as follows:
     415-449: Missing.
     450-464: Missing.
Isoform 5 (identifier: Q14161-5)

Also known as: E-;

The sequence of this isoform differs from the canonical sequence as follows:
     548-577: Missing.
Isoform 6 (identifier: Q14161-6)

Also known as: CD-;

The sequence of this isoform differs from the canonical sequence as follows:
     450-464: Missing.
     465-547: Missing.
Isoform 7 (identifier: Q14161-7)

Also known as: DE-;

The sequence of this isoform differs from the canonical sequence as follows:
     465-547: Missing.
     548-577: Missing.
Isoform 8 (identifier: Q14161-8)

Also known as: BE-;

The sequence of this isoform differs from the canonical sequence as follows:
     415-449: Missing.
     548-577: Missing.
Isoform 9 (identifier: Q14161-9)

Also known as: AE-;

The sequence of this isoform differs from the canonical sequence as follows:
     334-414: Missing.
     548-577: Missing.
Isoform 10 (identifier: Q14161-10)

The sequence of this isoform differs from the canonical sequence as follows:
     255-255: S → RRL
     414-463: Missing.
     548-577: Missing.
Note: No experimental confirmation available.
Isoform 11 (identifier: Q14161-11)

The sequence of this isoform differs from the canonical sequence as follows:
     450-464: Missing.
     465-547: Missing.
     548-577: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759ARF GTPase-activating protein GIT2
PRO_0000074203

Regions

Domain1 – 124124Arf-GAP
Repeat132 – 16130ANK 1
Repeat166 – 19530ANK 2
Repeat199 – 22830ANK 3
Zinc finger11 – 3424C4-type

Amino acid modifications

Modified residue3941Phosphoserine Ref.11 Ref.12
Modified residue3971Phosphoserine Ref.11 Ref.12
Modified residue4011Phosphothreonine By similarity
Modified residue4151Phosphoserine Ref.9
Modified residue4181Phosphoserine Ref.9
Modified residue4211Phosphoserine Ref.9 Ref.13
Modified residue4841Phosphotyrosine Ref.8
Modified residue5591Phosphoserine Ref.12
Modified residue6141Phosphoserine Ref.10 Ref.12

Natural variations

Alternative sequence2551S → RRL in isoform 10.
VSP_026456
Alternative sequence334 – 41481Missing in isoform 9.
VSP_000305
Alternative sequence414 – 46350Missing in isoform 10.
VSP_008654
Alternative sequence415 – 44935Missing in isoform 4 and isoform 8.
VSP_000306
Alternative sequence450 – 46415Missing in isoform 3, isoform 4, isoform 6 and isoform 11.
VSP_000307
Alternative sequence465 – 54783Missing in isoform 6, isoform 7 and isoform 11.
VSP_000308
Alternative sequence466 – 4716QTLQSE → LGKDAN in isoform 2.
VSP_000303
Alternative sequence472 – 759288Missing in isoform 2.
VSP_000304
Alternative sequence548 – 57730Missing in isoform 5, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11.
VSP_000309
Natural variant3381N → S.
Corresponds to variant rs9804905 [ dbSNP | Ensembl ].
VAR_048324
Natural variant3871N → S.
Corresponds to variant rs925368 [ dbSNP | Ensembl ].
VAR_024368
Natural variant5521A → V.
Corresponds to variant rs11068997 [ dbSNP | Ensembl ].
VAR_048325

Experimental info

Sequence conflict2851V → M in AAP35976. Ref.4
Sequence conflict2851V → M in AAH01379. Ref.5

Sequences

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

Last modified October 18, 2001. Version 2.
Checksum: 07EFE266DB2F3258

FASTA75984,543
        10         20         30         40         50         60 
MSKRLRSSEV CADCSGPDPS WASVNRGTFL CDECCSVHRS LGRHISQVRH LKHTPWPPTL 

        70         80         90        100        110        120 
LQMVETLYNN GANSIWEHSL LDPASIMSGR RKANPQDKVH PNKAEFIRAK YQMLAFVHRL 

       130        140        150        160        170        180 
PCRDDDSVTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGNTP LHVASKAGQI 

       190        200        210        220        230        240 
LQAELLAVYG ADPGTQDSSG KTPVDYARQG GHHELAERLV EIQYELTDRL AFYLCGRKPD 

       250        260        270        280        290        300 
HKNGQHFIIP QMADSSLDLS ELAKAAKKKL QSLSNHLFEE LAMDVYDEVD RRETDAVWLA 

       310        320        330        340        350        360 
TQNHSALVTE TTVVPFLPVN PEYSSTRNQG RQKLARFNAH EFATLVIDIL SDAKRRQQGS 

       370        380        390        400        410        420 
SLSGSKDNVE LILKTINNQH SVESQDNDQP DYDSVASDED TDLETTASKT NRQKSLDSDL 

       430        440        450        460        470        480 
SDGPVTVQEF MEVKNALVAS EAKIQQLMKV NNNLSDELRI MQKKLQTLQS ENSNLRKQAT 

       490        500        510        520        530        540 
TNVYQVQTGS EYTDTSNHSS LKRRPSARGS RPMSMYETGS GQKPYLPMGE ASRPEESRMR 

       550        560        570        580        590        600 
LQPFPAHIGR SALVTSSSSL PSFPSTLSWS RDESARRASR LEKQNSTPES DYDNTPNDME 

       610        620        630        640        650        660 
PDGMGSSRKG RQRSMVWPGD GLVPDTAEPH VAPSPTLPST EDVIRKTEQI TKNIQELLRA 

       670        680        690        700        710        720 
AQENKHDSYI PCSERIHVAV TEMAALFPKK PKSDMVRTSL RLLTSSAYRL QSECKKTLPG 

       730        740        750 
DPGSPTDVQL VTQQVIQCAY DIAKAAKQLV TITTKENNN 

« Hide

Isoform 2 (GIT2-short) [UniParc].

Checksum: 4C82BB94EA3634DA
Show »

FASTA47152,577
Isoform 3 (C-) [UniParc].

Checksum: FE6EB7D7BA75DF1D
Show »

FASTA74482,759
Isoform 4 (BC-) [UniParc].

Checksum: 5D6679379A84F684
Show »

FASTA70978,954
Isoform 5 (E-) [UniParc].

Checksum: 6B3A644B9F357C11
Show »

FASTA72981,322
Isoform 6 (CD-) [UniParc].

Checksum: DD63B22D57DE9FAA
Show »

FASTA66173,403
Isoform 7 (DE-) [UniParc].

Checksum: 5A146DE59620E062
Show »

FASTA64671,967
Isoform 8 (BE-) [UniParc].

Checksum: 40D620FE62406931
Show »

FASTA69477,518
Isoform 9 (AE-) [UniParc].

Checksum: 3FE0E683427F3E09
Show »

FASTA64872,318
Isoform 10 [UniParc].

Checksum: DADC7AB863457F3D
Show »

FASTA68176,072
Isoform 11 [UniParc].

Checksum: C14DEB3FF1A577CD
Show »

FASTA63170,183

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] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 9), CHARACTERIZATION.
[2]"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
Tissue: Bone marrow.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"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 29-759 (ISOFORM 11).
Tissue: B-cell and Skin.
[6]"An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization."
Mazaki Y., Hashimoto S., Okawa K., Tsubouchi A., Nakamura K., Yagi R., Yano H., Kondo A., Iwamatsu A., Mizoguchi A., Sabe H.
Mol. Biol. Cell 12:645-662(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAXILLIN.
[7]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"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-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-415; SER-418 AND SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-394 AND SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-394; SER-397; SER-559 AND SER-614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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 SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Bin2 is a membrane sculpting N-BAR protein that influences leucocyte podosomes, motility and phagocytosis."
Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J., Veprintsev D.B., Evans P.R., McMahon H.T.
PLoS ONE 7:E52401-E52401(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH BIN2 AND ARHGEF6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF124491 mRNA. Translation: AAD28047.1.
D63482 mRNA. Translation: BAA09769.2. Different initiation.
BT007312 mRNA. Translation: AAP35976.1.
BC001379 mRNA. Translation: AAH01379.1.
BC014223 mRNA. Translation: AAH14223.2.
CCDSCCDS44968.1. [Q14161-5]
CCDS44969.1. [Q14161-11]
CCDS55884.1. [Q14161-10]
CCDS9138.1. [Q14161-1]
CCDS9139.1. [Q14161-2]
RefSeqNP_001128685.1. NM_001135213.1. [Q14161-10]
NP_001128686.1. NM_001135214.1. [Q14161-5]
NP_055591.2. NM_014776.3.
NP_476510.1. NM_057169.3. [Q14161-1]
NP_476511.1. NM_057170.3. [Q14161-11]
XP_006719770.1. XM_006719707.1. [Q14161-3]
XP_006719772.1. XM_006719709.1. [Q14161-4]
UniGeneHs.434996.

3D structure databases

ProteinModelPortalQ14161.
SMRQ14161. Positions 1-281, 420-477, 633-756.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115154. 44 interactions.
IntActQ14161. 45 interactions.
MINTMINT-1953372.
STRING9606.ENSP00000347464.

PTM databases

PhosphoSiteQ14161.

Polymorphism databases

DMDM17376322.

Proteomic databases

MaxQBQ14161.
PaxDbQ14161.
PRIDEQ14161.

Protocols and materials databases

DNASU9815.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338373; ENSP00000340342; ENSG00000139436. [Q14161-6]
ENST00000355312; ENSP00000347464; ENSG00000139436. [Q14161-1]
ENST00000356259; ENSP00000348595; ENSG00000139436. [Q14161-7]
ENST00000360185; ENSP00000353312; ENSG00000139436. [Q14161-4]
ENST00000361006; ENSP00000354282; ENSG00000139436. [Q14161-5]
ENST00000457474; ENSP00000391813; ENSG00000139436. [Q14161-10]
ENST00000547815; ENSP00000450348; ENSG00000139436. [Q14161-2]
ENST00000553118; ENSP00000447465; ENSG00000139436. [Q14161-11]
GeneID9815.
KEGGhsa:9815.
UCSCuc001tpq.2. human. [Q14161-5]
uc001tps.2. human. [Q14161-1]
uc001tpt.2. human. [Q14161-11]
uc001tpv.2. human. [Q14161-10]

Organism-specific databases

CTD9815.
GeneCardsGC12M110367.
HGNCHGNC:4273. GIT2.
HPACAB004681.
MIM608564. gene.
neXtProtNX_Q14161.
PharmGKBPA28684.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5347.
HOGENOMHOG000232135.
HOVERGENHBG012506.
InParanoidQ14161.
KOK12487.
OMANKAEFIR.
OrthoDBEOG7KQ212.
PhylomeDBQ14161.
TreeFamTF317762.

Gene expression databases

ArrayExpressQ14161.
BgeeQ14161.
CleanExHS_GIT2.
GenevestigatorQ14161.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR022018. GIT1_C.
IPR013724. GIT_SHD.
[Graphical view]
PfamPF00023. Ank. 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. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGIT2. human.
GeneWikiGIT2.
GenomeRNAi9815.
NextBio36954.
PROQ14161.
SOURCESearch...

Entry information

Entry nameGIT2_HUMAN
AccessionPrimary (citable) accession number: Q14161
Secondary accession number(s): Q86U59 expand/collapse secondary AC list , Q96CI2, Q9BV91, Q9Y5V2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 18, 2001
Last modified: July 9, 2014
This is version 151 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM