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Q14161

- GIT2_HUMAN

UniProt

Q14161 - GIT2_HUMAN

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Protein
ARF GTPase-activating protein GIT2
Gene
GIT2, KIAA0148
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GTPase-activating protein for the ADP ribosylation factor family.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 3424C4-type
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. regulation of ARF GTPase activity Source: InterPro
  2. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GIT2
Synonyms:KIAA0148
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:4273. GIT2.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28684.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759ARF GTPase-activating protein GIT2
PRO_0000074203Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei394 – 3941Phosphoserine2 Publications
Modified residuei397 – 3971Phosphoserine2 Publications
Modified residuei401 – 4011Phosphothreonine By similarity
Modified residuei415 – 4151Phosphoserine1 Publication
Modified residuei418 – 4181Phosphoserine1 Publication
Modified residuei421 – 4211Phosphoserine2 Publications
Modified residuei484 – 4841Phosphotyrosine1 Publication
Modified residuei559 – 5591Phosphoserine1 Publication
Modified residuei614 – 6141Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14161.
PaxDbiQ14161.
PRIDEiQ14161.

PTM databases

PhosphoSiteiQ14161.

Expressioni

Gene expression databases

ArrayExpressiQ14161.
BgeeiQ14161.
CleanExiHS_GIT2.
GenevestigatoriQ14161.

Organism-specific databases

HPAiCAB004681.

Interactioni

Subunit structurei

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 BIN2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Arhgef7Q9ES282EBI-1046878,EBI-642580From a different organism.
IKBKGQ9Y6K96EBI-1046878,EBI-81279
PXNP490232EBI-1046878,EBI-702209
TNIP1Q150253EBI-1046878,EBI-357849
TRAF1Q130772EBI-1046878,EBI-359224
TSNQ156312EBI-1046878,EBI-1044160

Protein-protein interaction databases

BioGridi115154. 44 interactions.
IntActiQ14161. 45 interactions.
MINTiMINT-1953372.
STRINGi9606.ENSP00000347464.

Structurei

3D structure databases

ProteinModelPortaliQ14161.
SMRiQ14161. Positions 1-281, 420-477, 633-756.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 3 ANK repeats.
Contains 1 Arf-GAP domain.

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
HOGENOMiHOG000232135.
HOVERGENiHBG012506.
InParanoidiQ14161.
KOiK12487.
OMAiNKAEFIR.
OrthoDBiEOG7KQ212.
PhylomeDBiQ14161.
TreeFamiTF317762.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR022018. GIT1_C.
IPR013724. GIT_SHD.
[Graphical view]
PfamiPF00023. Ank. 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. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
[Graphical view]

Sequences (11)i

Sequence statusi: Complete.

This entry describes 11 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q14161-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSKRLRSSEV CADCSGPDPS WASVNRGTFL CDECCSVHRS LGRHISQVRH    50
LKHTPWPPTL LQMVETLYNN GANSIWEHSL LDPASIMSGR RKANPQDKVH 100
PNKAEFIRAK YQMLAFVHRL PCRDDDSVTA KDLSKQLHSS VRTGNLETCL 150
RLLSLGAQAN FFHPEKGNTP LHVASKAGQI LQAELLAVYG ADPGTQDSSG 200
KTPVDYARQG GHHELAERLV EIQYELTDRL AFYLCGRKPD HKNGQHFIIP 250
QMADSSLDLS ELAKAAKKKL QSLSNHLFEE LAMDVYDEVD RRETDAVWLA 300
TQNHSALVTE TTVVPFLPVN PEYSSTRNQG RQKLARFNAH EFATLVIDIL 350
SDAKRRQQGS SLSGSKDNVE LILKTINNQH SVESQDNDQP DYDSVASDED 400
TDLETTASKT NRQKSLDSDL SDGPVTVQEF MEVKNALVAS EAKIQQLMKV 450
NNNLSDELRI MQKKLQTLQS ENSNLRKQAT TNVYQVQTGS EYTDTSNHSS 500
LKRRPSARGS RPMSMYETGS GQKPYLPMGE ASRPEESRMR LQPFPAHIGR 550
SALVTSSSSL PSFPSTLSWS RDESARRASR LEKQNSTPES DYDNTPNDME 600
PDGMGSSRKG RQRSMVWPGD GLVPDTAEPH VAPSPTLPST EDVIRKTEQI 650
TKNIQELLRA AQENKHDSYI PCSERIHVAV TEMAALFPKK PKSDMVRTSL 700
RLLTSSAYRL QSECKKTLPG DPGSPTDVQL VTQQVIQCAY DIAKAAKQLV 750
TITTKENNN 759
Length:759
Mass (Da):84,543
Last modified:October 18, 2001 - v2
Checksum:i07EFE266DB2F3258
GO
Isoform 2 (identifier: Q14161-2) [UniParc]FASTAAdd to Basket

Also known as: GIT2-short

The sequence of this isoform differs from the canonical sequence as follows:
     466-471: QTLQSE → LGKDAN
     472-759: Missing.

Show »
Length:471
Mass (Da):52,577
Checksum:i4C82BB94EA3634DA
GO
Isoform 3 (identifier: Q14161-3) [UniParc]FASTAAdd to Basket

Also known as: C-

The sequence of this isoform differs from the canonical sequence as follows:
     450-464: Missing.

Show »
Length:744
Mass (Da):82,759
Checksum:iFE6EB7D7BA75DF1D
GO
Isoform 4 (identifier: Q14161-4) [UniParc]FASTAAdd to Basket

Also known as: BC-

The sequence of this isoform differs from the canonical sequence as follows:
     415-449: Missing.
     450-464: Missing.

Show »
Length:709
Mass (Da):78,954
Checksum:i5D6679379A84F684
GO
Isoform 5 (identifier: Q14161-5) [UniParc]FASTAAdd to Basket

Also known as: E-

The sequence of this isoform differs from the canonical sequence as follows:
     548-577: Missing.

Show »
Length:729
Mass (Da):81,322
Checksum:i6B3A644B9F357C11
GO
Isoform 6 (identifier: Q14161-6) [UniParc]FASTAAdd to Basket

Also known as: CD-

The sequence of this isoform differs from the canonical sequence as follows:
     450-464: Missing.
     465-547: Missing.

Show »
Length:661
Mass (Da):73,403
Checksum:iDD63B22D57DE9FAA
GO
Isoform 7 (identifier: Q14161-7) [UniParc]FASTAAdd to Basket

Also known as: DE-

The sequence of this isoform differs from the canonical sequence as follows:
     465-547: Missing.
     548-577: Missing.

Show »
Length:646
Mass (Da):71,967
Checksum:i5A146DE59620E062
GO
Isoform 8 (identifier: Q14161-8) [UniParc]FASTAAdd to Basket

Also known as: BE-

The sequence of this isoform differs from the canonical sequence as follows:
     415-449: Missing.
     548-577: Missing.

Show »
Length:694
Mass (Da):77,518
Checksum:i40D620FE62406931
GO
Isoform 9 (identifier: Q14161-9) [UniParc]FASTAAdd to Basket

Also known as: AE-

The sequence of this isoform differs from the canonical sequence as follows:
     334-414: Missing.
     548-577: Missing.

Show »
Length:648
Mass (Da):72,318
Checksum:i3FE0E683427F3E09
GO
Isoform 10 (identifier: Q14161-10) [UniParc]FASTAAdd to Basket

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.

Show »
Length:681
Mass (Da):76,072
Checksum:iDADC7AB863457F3D
GO
Isoform 11 (identifier: Q14161-11) [UniParc]FASTAAdd to Basket

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.

Show »
Length:631
Mass (Da):70,183
Checksum:iC14DEB3FF1A577CD
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti338 – 3381N → S.
Corresponds to variant rs9804905 [ dbSNP | Ensembl ].
VAR_048324
Natural varianti387 – 3871N → S.
Corresponds to variant rs925368 [ dbSNP | Ensembl ].
VAR_024368
Natural varianti552 – 5521A → V.
Corresponds to variant rs11068997 [ dbSNP | Ensembl ].
VAR_048325

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei255 – 2551S → RRL in isoform 10.
VSP_026456
Alternative sequencei334 – 41481Missing in isoform 9.
VSP_000305Add
BLAST
Alternative sequencei414 – 46350Missing in isoform 10.
VSP_008654Add
BLAST
Alternative sequencei415 – 44935Missing in isoform 4 and isoform 8.
VSP_000306Add
BLAST
Alternative sequencei450 – 46415Missing in isoform 3, isoform 4, isoform 6 and isoform 11.
VSP_000307Add
BLAST
Alternative sequencei465 – 54783Missing in isoform 6, isoform 7 and isoform 11.
VSP_000308Add
BLAST
Alternative sequencei466 – 4716QTLQSE → LGKDAN in isoform 2.
VSP_000303
Alternative sequencei472 – 759288Missing in isoform 2.
VSP_000304Add
BLAST
Alternative sequencei548 – 57730Missing in isoform 5, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11.
VSP_000309Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2851V → M in AAP35976. 1 Publication
Sequence conflicti285 – 2851V → M in AAH01379. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS44968.1. [Q14161-5]
CCDS44969.1. [Q14161-11]
CCDS55884.1. [Q14161-10]
CCDS9138.1. [Q14161-1]
CCDS9139.1. [Q14161-2]
RefSeqiNP_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]
UniGeneiHs.434996.

Genome annotation databases

EnsembliENST00000338373; 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]
GeneIDi9815.
KEGGihsa:9815.
UCSCiuc001tpq.2. human. [Q14161-5]
uc001tps.2. human. [Q14161-1]
uc001tpt.2. human. [Q14161-11]
uc001tpv.2. human. [Q14161-10]

Polymorphism databases

DMDMi17376322.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS44968.1. [Q14161-5 ]
CCDS44969.1. [Q14161-11 ]
CCDS55884.1. [Q14161-10 ]
CCDS9138.1. [Q14161-1 ]
CCDS9139.1. [Q14161-2 ]
RefSeqi NP_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 ]
UniGenei Hs.434996.

3D structure databases

ProteinModelPortali Q14161.
SMRi Q14161. Positions 1-281, 420-477, 633-756.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115154. 44 interactions.
IntActi Q14161. 45 interactions.
MINTi MINT-1953372.
STRINGi 9606.ENSP00000347464.

PTM databases

PhosphoSitei Q14161.

Polymorphism databases

DMDMi 17376322.

Proteomic databases

MaxQBi Q14161.
PaxDbi Q14161.
PRIDEi Q14161.

Protocols and materials databases

DNASUi 9815.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338373 ; 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 ]
GeneIDi 9815.
KEGGi hsa:9815.
UCSCi uc001tpq.2. human. [Q14161-5 ]
uc001tps.2. human. [Q14161-1 ]
uc001tpt.2. human. [Q14161-11 ]
uc001tpv.2. human. [Q14161-10 ]

Organism-specific databases

CTDi 9815.
GeneCardsi GC12M110367.
HGNCi HGNC:4273. GIT2.
HPAi CAB004681.
MIMi 608564. gene.
neXtProti NX_Q14161.
PharmGKBi PA28684.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5347.
HOGENOMi HOG000232135.
HOVERGENi HBG012506.
InParanoidi Q14161.
KOi K12487.
OMAi NKAEFIR.
OrthoDBi EOG7KQ212.
PhylomeDBi Q14161.
TreeFami TF317762.

Miscellaneous databases

ChiTaRSi GIT2. human.
GeneWikii GIT2.
GenomeRNAii 9815.
NextBioi 36954.
PROi Q14161.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14161.
Bgeei Q14161.
CleanExi HS_GIT2.
Genevestigatori Q14161.

Family and domain databases

Gene3Di 1.25.40.20. 2 hits.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR022018. GIT1_C.
IPR013724. GIT_SHD.
[Graphical view ]
Pfami PF00023. Ank. 1 hit.
PF01412. ArfGap. 1 hit.
PF12205. GIT1_C. 1 hit.
PF08518. GIT_SHD. 2 hits.
[Graphical view ]
PRINTSi PR00405. REVINTRACTNG.
SMARTi SM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00555. GIT. 2 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiGIT2_HUMAN
AccessioniPrimary (citable) accession number: Q14161
Secondary accession number(s): Q86U59
, Q96CI2, Q9BV91, Q9Y5V2
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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