Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ARF GTPase-activating protein GIT1

Gene

GIT1

Organism
Homo sapiens (Human)
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. Involved in the regulation of cytokinesis; the function may involve SDCCAG3 and PTPN13 (By similarity).By similarity1 Publication

Regions

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

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB-KW
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. axon guidance Source: Reactome
  2. ephrin receptor signaling pathway Source: Reactome
  3. regulation of cytokinesis Source: UniProtKB
  4. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_264047. Ephrin signaling.
SignaLinkiQ9Y2X7.

Names & Taxonomyi

Protein namesi
Recommended name:
ARF GTPase-activating protein GIT1
Short name:
ARF GAP GIT1
Alternative name(s):
Cool-associated and tyrosine-phosphorylated protein 1
Short name:
CAT-1
Short name:
CAT1
G protein-coupled receptor kinase-interactor 1
GRK-interacting protein 1
Gene namesi
Name:GIT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:4272. GIT1.

Subcellular locationi

  1. Cytoplasm 1 Publication

  2. 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.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28683.

Polymorphism and mutation databases

BioMutaiGIT1.
DMDMi45645212.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 761761ARF GTPase-activating protein GIT1PRO_0000074200Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei224 – 2241PhosphotyrosineBy similarity
Modified residuei362 – 3621Phosphoserine3 Publications
Modified residuei364 – 3641Phosphothreonine2 Publications
Modified residuei375 – 3751Phosphoserine1 Publication
Modified residuei383 – 3831Phosphotyrosine2 Publications
Modified residuei385 – 3851Phosphoserine3 Publications
Modified residuei388 – 3881Phosphoserine8 Publications
Modified residuei392 – 3921Phosphothreonine2 Publications
Modified residuei410 – 4101Phosphoserine3 Publications
Modified residuei480 – 4801Phosphothreonine1 Publication
Modified residuei545 – 5451Phosphotyrosine1 Publication
Modified residuei554 – 5541Phosphotyrosine1 Publication
Modified residuei592 – 5921Phosphoserine5 Publications
Modified residuei596 – 5961Phosphoserine2 Publications
Modified residuei601 – 6011Phosphothreonine1 Publication

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

MaxQBiQ9Y2X7.
PaxDbiQ9Y2X7.
PRIDEiQ9Y2X7.

PTM databases

PhosphoSiteiQ9Y2X7.

Miscellaneous databases

PMAP-CutDBQ9Y2X7.

Expressioni

Gene expression databases

BgeeiQ9Y2X7.
CleanExiHS_GIT1.
ExpressionAtlasiQ9Y2X7. baseline.
GenevestigatoriQ9Y2X7.

Organism-specific databases

HPAiHPA004059.
HPA004186.

Interactioni

Subunit structurei

Interacts with G protein-coupled receptor kinases: ADRBK1/GRK2, PPFIA1 and PPFIA4. Interacts with ARHGEF6/alpha-PIX, with ARHGEF7/beta-PIX, with PXN/paxillin and with PTK2/FAK1 (By similarity). Component of cytoplasmic complexes, which also contain PXN, ARHGEF6 and PAK1. Interacts with TGFB1I1. Interacts with SCRIB. Interacts with SDCCAG3 (PubMed:23108400).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRBK1P250985EBI-466061,EBI-3904795
ARHGEF7Q141554EBI-466061,EBI-717515
BARD1Q997282EBI-466061,EBI-473181
CHD3Q128732EBI-466061,EBI-523590
HTTP4285810EBI-466061,EBI-466029
KIAA1377Q9P2H02EBI-466061,EBI-473176
LRIF1Q5T3J32EBI-466061,EBI-473196
PAK1Q131532EBI-466061,EBI-1307
PXNP490243EBI-466061,EBI-2896280From a different organism.

Protein-protein interaction databases

BioGridi118789. 59 interactions.
IntActiQ9Y2X7. 39 interactions.
MINTiMINT-243639.
STRINGi9606.ENSP00000378338.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2X7.
SMRiQ9Y2X7. Positions 3-285, 418-473, 631-761.
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
Regioni251 – 415165PTK2/FAK1-bindingBy similarityAdd
BLAST
Regioni254 – 367114ARHGEF6-bindingBy similarityAdd
BLAST
Regioni637 – 761125Interaction with PXN and TGFB1I1By similarityAdd
BLAST

Domaini

The paxillin-binding domain is masked in the full-length protein and is regulated by ARHGEF6.By similarity

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.
InParanoidiQ9Y2X7.
KOiK05737.
OMAiSARSQSD.
OrthoDBiEOG7KQ212.
PhylomeDBiQ9Y2X7.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2X7-1) [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

        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
MADSLDLSEL AKAAKKKLQA LSNRLFEELA MDVYDEVDRR ENDAVWLATQ
310 320 330 340 350
NHSTLVTERS AVPFLPVNPE YSATRNQGRQ KLARFNAREF ATLIIDILSE
360 370 380 390 400
AKRRQQGKSL SSPTDNLELS LRSQSDLDDQ HDYDSVASDE DTDQEPLRST
410 420 430 440 450
GATRSNRARS MDSSDLSDGA VTLQEYLELK KALATSEAKV QQLMKVNSSL
460 470 480 490 500
SDELRRLQRE IHKLQAENLQ LRQPPGPVPT PPLPSERAEH TPMAPGGSTH
510 520 530 540 550
RRDRQAFSMY EPGSALKPFG GPPGDELTTR LQPFHSTELE DDAIYSVHVP
560 570 580 590 600
AGLYRIRKGV SASAVPFTPS SPLLSCSQEG SRHTSKLSRH GSGADSDYEN
610 620 630 640 650
TQSGDPLLGL EGKRFLELGK EEDFHPELES LDGDLDPGLP STEDVILKTE
660 670 680 690 700
QVTKNIQELL RAAQEFKHDS FVPCSEKIHL AVTEMASLFP KRPALEPVRS
710 720 730 740 750
SLRLLNASAY RLQSECRKTV PPEPGAPVDF QLLTQQVIQC AYDIAKAAKQ
760
LVTITTREKK Q
Length:761
Mass (Da):84,341
Last modified:March 15, 2004 - v2
Checksum:i702744942A796399
GO
Isoform 2 (identifier: Q9Y2X7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-176: SKQLHSSVRT...GTTPLHVAAK → TGHRSWATPD...VPWCPPLSSP
     177-761: Missing.

Note: No experimental confirmation available.

Show »
Length:176
Mass (Da):19,160
Checksum:i2B5BB45555AB5201
GO
Isoform 3 (identifier: Q9Y2X7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     253-253: D → DRSRQKCMSQ

Show »
Length:770
Mass (Da):85,446
Checksum:i278AD8D706C32EE0
GO

Sequence cautioni

The sequence AAH48196.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211P → S in AAD28046 (PubMed:10896954).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei134 – 17643SKQLH…HVAAK → TGHRSWATPDINPHPNRATG TSALSAATLPGSQVPWCPPL SSP in isoform 2. 1 PublicationVSP_009666Add
BLAST
Alternative sequencei177 – 761585Missing in isoform 2. 1 PublicationVSP_009667Add
BLAST
Alternative sequencei253 – 2531D → DRSRQKCMSQ in isoform 3. 1 PublicationVSP_040984

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124490 mRNA. Translation: AAD28046.1.
AK294785 mRNA. Translation: BAG57910.1.
AK299932 mRNA. Translation: BAG61765.1.
AC104564 Genomic DNA. No translation available.
BC006227 mRNA. Translation: AAH06227.2.
BC048196 mRNA. Translation: AAH48196.1. Different initiation.
CCDSiCCDS11250.1. [Q9Y2X7-1]
CCDS42290.1. [Q9Y2X7-3]
RefSeqiNP_001078923.1. NM_001085454.1. [Q9Y2X7-3]
NP_054749.2. NM_014030.3. [Q9Y2X7-1]
UniGeneiHs.514051.

Genome annotation databases

EnsembliENST00000225394; ENSP00000225394; ENSG00000108262. [Q9Y2X7-1]
ENST00000394869; ENSP00000378338; ENSG00000108262. [Q9Y2X7-3]
GeneIDi28964.
KEGGihsa:28964.
UCSCiuc002hef.2. human. [Q9Y2X7-1]
uc002heg.2. human. [Q9Y2X7-3]

Polymorphism and mutation databases

BioMutaiGIT1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124490 mRNA. Translation: AAD28046.1.
AK294785 mRNA. Translation: BAG57910.1.
AK299932 mRNA. Translation: BAG61765.1.
AC104564 Genomic DNA. No translation available.
BC006227 mRNA. Translation: AAH06227.2.
BC048196 mRNA. Translation: AAH48196.1. Different initiation.
CCDSiCCDS11250.1. [Q9Y2X7-1]
CCDS42290.1. [Q9Y2X7-3]
RefSeqiNP_001078923.1. NM_001085454.1. [Q9Y2X7-3]
NP_054749.2. NM_014030.3. [Q9Y2X7-1]
UniGeneiHs.514051.

3D structure databases

ProteinModelPortaliQ9Y2X7.
SMRiQ9Y2X7. Positions 3-285, 418-473, 631-761.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118789. 59 interactions.
IntActiQ9Y2X7. 39 interactions.
MINTiMINT-243639.
STRINGi9606.ENSP00000378338.

PTM databases

PhosphoSiteiQ9Y2X7.

Polymorphism and mutation databases

BioMutaiGIT1.
DMDMi45645212.

Proteomic databases

MaxQBiQ9Y2X7.
PaxDbiQ9Y2X7.
PRIDEiQ9Y2X7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225394; ENSP00000225394; ENSG00000108262. [Q9Y2X7-1]
ENST00000394869; ENSP00000378338; ENSG00000108262. [Q9Y2X7-3]
GeneIDi28964.
KEGGihsa:28964.
UCSCiuc002hef.2. human. [Q9Y2X7-1]
uc002heg.2. human. [Q9Y2X7-3]

Organism-specific databases

CTDi28964.
GeneCardsiGC17M027900.
H-InvDBHIX0013673.
HGNCiHGNC:4272. GIT1.
HPAiHPA004059.
HPA004186.
MIMi608434. gene.
neXtProtiNX_Q9Y2X7.
PharmGKBiPA28683.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00730000110864.
HOGENOMiHOG000232135.
HOVERGENiHBG012506.
InParanoidiQ9Y2X7.
KOiK05737.
OMAiSARSQSD.
OrthoDBiEOG7KQ212.
PhylomeDBiQ9Y2X7.
TreeFamiTF317762.

Enzyme and pathway databases

ReactomeiREACT_264047. Ephrin signaling.
SignaLinkiQ9Y2X7.

Miscellaneous databases

ChiTaRSiGIT1. human.
GeneWikiiGIT1.
GenomeRNAii28964.
NextBioi51807.
PMAP-CutDBQ9Y2X7.
PROiQ9Y2X7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2X7.
CleanExiHS_GIT1.
ExpressionAtlasiQ9Y2X7. baseline.
GenevestigatoriQ9Y2X7.

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. "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] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 585-761 (ISOFORM 1).
    Tissue: Lung and Melanoma.
  5. "Beta2-adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein."
    Premont R.T., Claing A., Vitale N., Freeman J.L.R., Pitcher J.A., Patton W.A., Moss J., Vaughan M., Lefkowitz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 95:14082-14087(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "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.
  7. "GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration."
    Manabe R., Kovalenko M., Webb D.J., Horwitz A.R.
    J. Cell Sci. 115:1497-1510(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION IN CELL MIGRATION.
  8. Cited for: INTERACTION WITH SCRIB.
  9. "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-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-388 AND SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Deregulation of scribble promotes mammary tumorigenesis and reveals a role for cell polarity in carcinoma."
    Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C., Muthuswamy S.K.
    Cell 135:865-878(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCRIB.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; TYR-383; SER-385; SER-388; THR-392; SER-410; SER-592 AND SER-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-362; THR-364; SER-375; TYR-383; SER-385; SER-388; THR-392; SER-410; TYR-545; SER-592; SER-596 AND THR-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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 THR-364; SER-385; SER-388 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362 AND SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SDCCAG3.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; THR-480 AND SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGIT1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2X7
Secondary accession number(s): B4DGU9
, B4DSV3, Q86SS0, Q9BRJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: March 15, 2004
Last modified: April 29, 2015
This is version 157 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.