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ARF GTPase-activating protein GIT2 (ARF GAP GIT2) (Cool-interacting tyrosine-phosphorylated protein 2) (CAT-2) (CAT2) (G protein-coupled receptor kinase-interactor 2) (GRK-interacting protein 2)

 GIT2_HUMAN              Reviewed;         759 AA.
Q14161; Q86U59; Q96CI2; Q9BV91; Q9Y5V2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
22-NOV-2017, entry version 182.
RecName: Full=ARF GTPase-activating protein GIT2;
Short=ARF GAP GIT2;
AltName: Full=Cool-interacting tyrosine-phosphorylated protein 2;
Short=CAT-2;
Short=CAT2;
AltName: Full=G protein-coupled receptor kinase-interactor 2;
AltName: Full=GRK-interacting protein 2;
Name=GIT2; Synonyms=KIAA0148;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 9),
AND CHARACTERIZATION.
PubMed=10896954; DOI=10.1074/jbc.275.29.22373;
Premont R.T., Claing A., Vitale N., Perry S.J., Lefkowitz R.J.;
"The GIT family of ADP-ribosylation factor GTPase-activating proteins.
Functional diversity of GIT2 through alternative splicing.";
J. Biol. Chem. 275:22373-22380(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
TISSUE=Bone marrow;
PubMed=8590280; DOI=10.1093/dnares/2.4.167;
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
"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.";
DNA Res. 2:167-174(1995).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 29-759 (ISOFORM 11).
TISSUE=B-cell, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH PAXILLIN.
PubMed=11251077; DOI=10.1091/mbc.12.3.645;
Mazaki Y., Hashimoto S., Okawa K., Tsubouchi A., Nakamura K., Yagi R.,
Yano H., Kondo A., Iwamatsu A., Mizoguchi A., Sabe H.;
"An ADP-ribosylation factor GTPase-activating protein Git2-
short/KIAA0148 is involved in subcellular localization of paxillin and
actin cytoskeletal organization.";
Mol. Biol. Cell 12:645-662(2001).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-418 AND
SER-421, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-397, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-397; SER-559
AND SER-614, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
IDENTIFICATION IN A COMPLEX WITH BIN2 AND ARHGEF6.
PubMed=23285027; DOI=10.1371/journal.pone.0052401;
Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
Veprintsev D.B., Evans P.R., McMahon H.T.;
"Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
podosomes, motility and phagocytosis.";
PLoS ONE 7:E52401-E52401(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: GTPase-activating protein for the ADP ribosylation
factor family.
-!- SUBUNIT: 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. {ECO:0000250, ECO:0000269|PubMed:11251077,
ECO:0000269|PubMed:23285027}.
-!- INTERACTION:
Q15052:ARHGEF6; NbExp=4; IntAct=EBI-12028686, EBI-1642523;
Q9ES28:Arhgef7 (xeno); NbExp=2; IntAct=EBI-1046878, EBI-642580;
Q9Y6K9:IKBKG; NbExp=6; IntAct=EBI-1046878, EBI-81279;
P49023:PXN; NbExp=2; IntAct=EBI-1046878, EBI-702209;
Q15025:TNIP1; NbExp=3; IntAct=EBI-1046878, EBI-357849;
Q13077:TRAF1; NbExp=2; IntAct=EBI-1046878, EBI-359224;
Q15631:TSN; NbExp=2; IntAct=EBI-1046878, EBI-1044160;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q14161-1; Sequence=Displayed;
Name=2; Synonyms=GIT2-short;
IsoId=Q14161-2; Sequence=VSP_000303, VSP_000304;
Name=3; Synonyms=C-;
IsoId=Q14161-3; Sequence=VSP_000307;
Name=4; Synonyms=BC-;
IsoId=Q14161-4; Sequence=VSP_000306, VSP_000307;
Name=5; Synonyms=E-;
IsoId=Q14161-5; Sequence=VSP_000309;
Name=6; Synonyms=CD-;
IsoId=Q14161-6; Sequence=VSP_000307, VSP_000308;
Name=7; Synonyms=DE-;
IsoId=Q14161-7; Sequence=VSP_000308, VSP_000309;
Name=8; Synonyms=BE-;
IsoId=Q14161-8; Sequence=VSP_000306, VSP_000309;
Name=9; Synonyms=AE-;
IsoId=Q14161-9; Sequence=VSP_000305, VSP_000309;
Name=10;
IsoId=Q14161-10; Sequence=VSP_026456, VSP_008654, VSP_000309;
Note=No experimental confirmation available.;
Name=11;
IsoId=Q14161-11; Sequence=VSP_000307, VSP_000308, VSP_000309;
Note=No experimental confirmation available.;
-!- SEQUENCE CAUTION:
Sequence=BAA09769.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF124491; AAD28047.1; -; mRNA.
EMBL; D63482; BAA09769.2; ALT_INIT; mRNA.
EMBL; BT007312; AAP35976.1; -; mRNA.
EMBL; BC001379; AAH01379.1; -; mRNA.
EMBL; BC014223; AAH14223.2; -; mRNA.
CCDS; CCDS44968.1; -. [Q14161-5]
CCDS; CCDS44969.1; -. [Q14161-11]
CCDS; CCDS55884.1; -. [Q14161-10]
CCDS; CCDS9138.1; -. [Q14161-1]
CCDS; CCDS9139.1; -. [Q14161-2]
RefSeq; NP_001128685.1; NM_001135213.2. [Q14161-10]
RefSeq; NP_001128686.1; NM_001135214.2. [Q14161-5]
RefSeq; NP_001317082.1; NM_001330153.1.
RefSeq; NP_055591.2; NM_014776.4.
RefSeq; NP_476510.1; NM_057169.4. [Q14161-1]
RefSeq; NP_476511.1; NM_057170.4. [Q14161-11]
RefSeq; XP_006719770.1; XM_006719707.3. [Q14161-3]
RefSeq; XP_006719772.1; XM_006719709.3. [Q14161-4]
UniGene; Hs.434996; -.
ProteinModelPortal; Q14161; -.
SMR; Q14161; -.
BioGrid; 115154; 95.
IntAct; Q14161; 48.
MINT; MINT-1953372; -.
STRING; 9606.ENSP00000347464; -.
iPTMnet; Q14161; -.
PhosphoSitePlus; Q14161; -.
BioMuta; GIT2; -.
DMDM; 17376322; -.
EPD; Q14161; -.
MaxQB; Q14161; -.
PaxDb; Q14161; -.
PeptideAtlas; Q14161; -.
PRIDE; Q14161; -.
DNASU; 9815; -.
Ensembl; ENST00000355312; ENSP00000347464; ENSG00000139436. [Q14161-1]
Ensembl; ENST00000361006; ENSP00000354282; ENSG00000139436. [Q14161-5]
Ensembl; ENST00000457474; ENSP00000391813; ENSG00000139436. [Q14161-10]
Ensembl; ENST00000547815; ENSP00000450348; ENSG00000139436. [Q14161-2]
Ensembl; ENST00000553118; ENSP00000447465; ENSG00000139436. [Q14161-11]
GeneID; 9815; -.
KEGG; hsa:9815; -.
UCSC; uc001tpq.3; human. [Q14161-1]
CTD; 9815; -.
DisGeNET; 9815; -.
EuPathDB; HostDB:ENSG00000139436.20; -.
GeneCards; GIT2; -.
HGNC; HGNC:4273; GIT2.
HPA; CAB004681; -.
MIM; 608564; gene.
neXtProt; NX_Q14161; -.
OpenTargets; ENSG00000139436; -.
PharmGKB; PA28684; -.
eggNOG; KOG0818; Eukaryota.
eggNOG; ENOG410XR8U; LUCA.
GeneTree; ENSGT00900000140990; -.
HOGENOM; HOG000232135; -.
HOVERGEN; HBG012506; -.
InParanoid; Q14161; -.
KO; K12487; -.
OMA; RQGGHHE; -.
OrthoDB; EOG091G03VD; -.
PhylomeDB; Q14161; -.
TreeFam; TF317762; -.
SIGNOR; Q14161; -.
ChiTaRS; GIT2; human.
GeneWiki; GIT2; -.
GenomeRNAi; 9815; -.
PRO; PR:Q14161; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139436; -.
CleanEx; HS_GIT2; -.
ExpressionAtlas; Q14161; baseline and differential.
Genevisible; Q14161; HS.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; TAS:ProtInc.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR001164; ArfGAP.
InterPro; IPR037278; ARFGAP/RecO.
InterPro; IPR032352; GIT1/2_CC.
InterPro; IPR022018; GIT1_C.
InterPro; IPR013724; GIT_SHD.
Pfam; PF12796; Ank_2; 1.
Pfam; PF01412; ArfGap; 1.
Pfam; PF12205; GIT1_C; 1.
Pfam; PF16559; GIT_CC; 1.
Pfam; PF08518; GIT_SHD; 2.
PRINTS; PR00405; REVINTRACTNG.
SMART; SM00248; ANK; 3.
SMART; SM00105; ArfGap; 1.
SMART; SM00555; GIT; 2.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF57863; SSF57863; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 1.
PROSITE; PS50115; ARFGAP; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Complete proteome;
GTPase activation; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Zinc; Zinc-finger.
CHAIN 1 759 ARF GTPase-activating protein GIT2.
/FTId=PRO_0000074203.
DOMAIN 1 124 Arf-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
REPEAT 132 161 ANK 1.
REPEAT 166 195 ANK 2.
REPEAT 199 228 ANK 3.
ZN_FING 11 34 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 401 401 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JLQ2}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:24275569}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
MOD_RES 484 484 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JLQ2}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JLQ2}.
MOD_RES 587 587 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JLQ2}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332}.
VAR_SEQ 255 255 S -> RRL (in isoform 10).
{ECO:0000303|PubMed:8590280}.
/FTId=VSP_026456.
VAR_SEQ 334 414 Missing (in isoform 9).
{ECO:0000303|PubMed:10896954}.
/FTId=VSP_000305.
VAR_SEQ 414 463 Missing (in isoform 10).
{ECO:0000303|PubMed:8590280}.
/FTId=VSP_008654.
VAR_SEQ 415 449 Missing (in isoform 4 and isoform 8).
{ECO:0000303|PubMed:10896954}.
/FTId=VSP_000306.
VAR_SEQ 450 464 Missing (in isoform 3, isoform 4, isoform
6 and isoform 11).
{ECO:0000303|PubMed:10896954,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_000307.
VAR_SEQ 465 547 Missing (in isoform 6, isoform 7 and
isoform 11).
{ECO:0000303|PubMed:10896954,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_000308.
VAR_SEQ 466 471 QTLQSE -> LGKDAN (in isoform 2).
{ECO:0000303|PubMed:10896954,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_000303.
VAR_SEQ 472 759 Missing (in isoform 2).
{ECO:0000303|PubMed:10896954,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_000304.
VAR_SEQ 548 577 Missing (in isoform 5, isoform 7, isoform
8, isoform 9, isoform 10 and isoform 11).
{ECO:0000303|PubMed:10896954,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8590280}.
/FTId=VSP_000309.
VARIANT 338 338 N -> S (in dbSNP:rs9804905).
/FTId=VAR_048324.
VARIANT 387 387 N -> S (in dbSNP:rs925368).
/FTId=VAR_024368.
VARIANT 552 552 A -> V (in dbSNP:rs11068997).
/FTId=VAR_048325.
CONFLICT 285 285 V -> M (in Ref. 4; AAP35976 and 5;
AAH01379). {ECO:0000305}.
SEQUENCE 759 AA; 84543 MW; 07EFE266DB2F3258 CRC64;
MSKRLRSSEV CADCSGPDPS WASVNRGTFL CDECCSVHRS LGRHISQVRH LKHTPWPPTL
LQMVETLYNN GANSIWEHSL LDPASIMSGR RKANPQDKVH PNKAEFIRAK YQMLAFVHRL
PCRDDDSVTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGNTP LHVASKAGQI
LQAELLAVYG ADPGTQDSSG KTPVDYARQG GHHELAERLV EIQYELTDRL AFYLCGRKPD
HKNGQHFIIP QMADSSLDLS ELAKAAKKKL QSLSNHLFEE LAMDVYDEVD RRETDAVWLA
TQNHSALVTE TTVVPFLPVN PEYSSTRNQG RQKLARFNAH EFATLVIDIL SDAKRRQQGS
SLSGSKDNVE LILKTINNQH SVESQDNDQP DYDSVASDED TDLETTASKT NRQKSLDSDL
SDGPVTVQEF MEVKNALVAS EAKIQQLMKV NNNLSDELRI MQKKLQTLQS ENSNLRKQAT
TNVYQVQTGS EYTDTSNHSS LKRRPSARGS RPMSMYETGS GQKPYLPMGE ASRPEESRMR
LQPFPAHIGR SALVTSSSSL PSFPSTLSWS RDESARRASR LEKQNSTPES DYDNTPNDME
PDGMGSSRKG RQRSMVWPGD GLVPDTAEPH VAPSPTLPST EDVIRKTEQI TKNIQELLRA
AQENKHDSYI PCSERIHVAV TEMAALFPKK PKSDMVRTSL RLLTSSAYRL QSECKKTLPG
DPGSPTDVQL VTQQVIQCAY DIAKAAKQLV TITTKENNN


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EIAAB34716 ARHGAP32,Brain-specific Rho GTPase-activating protein,GAB-associated Cdc42_Rac GTPase-activating protein,GC-GAP,GRIT,GTPase regulator interacting with TrkA,Homo sapiens,Human,KIAA0712,p200RhoGAP,p250G
15-288-21470 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.05 mg
15-288-21471 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.05 mg
15-288-21471 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.1 mg
15-288-21470 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.1 mg
EIAAB34871 Homocysteine respondent protein HCYP2,Rat,Rattus norvegicus,Receptor-interacting protein 3,Receptor-interacting serine_threonine-protein kinase 3,Rip3,RIP-3,Ripk3,RIP-like protein kinase 3
EIAAB47949 HNF-4a coactivator,Homo sapiens,Human,Thyroid hormone receptor interactor 3,Thyroid receptor-interacting protein 3,TR-interacting protein 3,TRIP3,TRIP-3,Zinc finger HIT domain-containing protein 3,ZNH
EIAAB47947 Mouse,Mus musculus,Thyroid hormone receptor interactor 3,Thyroid receptor-interacting protein 3,TR-interacting protein 3,Trip3,TRIP-3,Zinc finger HIT domain-containing protein 3,Znhit3
EIAAB30151 Mouse,Mus musculus,Pachytene checkpoint protein 2 homolog,Pch2,Thyroid hormone receptor interactor 13,Thyroid receptor-interacting protein 13,TR-interacting protein 13,Trip13,TRIP-13
EIAAB30147 Pachytene checkpoint protein 2 homolog,Pch2,Rat,Rattus norvegicus,Thyroid hormone receptor interactor 13,Thyroid receptor-interacting protein 13,TR-interacting protein 13,Trip13,TRIP-13
EIAAB07420 Cdc42-interacting protein 4,CIP4,Homo sapiens,hSTP,Human,Protein Felic,Salt tolerant protein,STOT,STP,Thyroid receptor-interacting protein 10,TR-interacting protein 10,TRIP10,TRIP-10
EIAAB30150 Pachytene checkpoint protein 2 homolog,PCH2,Pig,Sus scrofa,Thyroid hormone receptor interactor 13,Thyroid receptor-interacting protein 13,TR-interacting protein 13,TRIP13,TRIP-13
EIAAB34733 ARHGAP44,Homo sapiens,Human,KIAA0672,NPC-A-10,Rho GTPase-activating protein 44,RhoGAP interacting with CIP4 homologs protein 2,Rho-type GTPase-activating protein RICH2,RICH2,RICH-2
EIAAB34734 Arhgap44,Mouse,Mus musculus,Rho GTPase-activating protein 44,RhoGAP interacting with CIP4 homologs protein 2,Rho-type GTPase-activating protein RICH2,Rich2,RICH-2


 

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