Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q13480 (GAB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GRB2-associated-binding protein 1
Alternative name(s):
GRB2-associated binder 1
Growth factor receptor bound protein 2-associated protein 1
Gene names
Name:GAB1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR).

Subunit structure

Interacts with GRB2 and with other SH2-containing proteins. Interacts with phosphorylated LAT2. Interacts with PTPRJ. Identified in a complex containing FRS2, GRB2, GAB1, PIK3R1 and SOS1. Interacts (phosphorylated) with PTPN11. Interacts with HCK. Ref.7 Ref.8 Ref.10

Post-translational modification

Phosphorylated in response to FGFR1 activation. Phosphorylated on tyrosine residue(s) by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Tyrosine phosphorylation of GAB1 mediates interaction with several proteins that contain SH2 domains. Phosphorylated on tyrosine residues by HCK upon IL6 signaling. Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the GAB family.

Contains 1 PH domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTPN11Q061243EBI-517684,EBI-297779

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13480-1)

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: Q13480-2)

The sequence of this isoform differs from the canonical sequence as follows:
     528-528: K → KGQSPKILRLKPHGLERTDSQTIGDFATRRK
Note: Phosphorylated on Ser-547.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 694694GRB2-associated-binding protein 1
PRO_0000050282

Regions

Domain5 – 116112PH
Compositional bias449 – 54092Pro-rich

Amino acid modifications

Modified residue1831Phosphotyrosine Ref.15
Modified residue2591Phosphotyrosine Ref.9 Ref.15
Modified residue2661Phosphoserine Ref.9
Modified residue3731Phosphotyrosine Ref.13 Ref.15
Modified residue4061Phosphotyrosine Ref.12 Ref.13 Ref.15
Modified residue5031Phosphothreonine By similarity
Modified residue6271Phosphotyrosine Ref.12 Ref.13
Modified residue6591Phosphotyrosine Ref.12 Ref.13 Ref.14 Ref.15

Natural variations

Alternative sequence5281K → KGQSPKILRLKPHGLERTDS QTIGDFATRRK in isoform 2.
VSP_017137
Natural variant831Y → C in a breast cancer sample; somatic mutation. Ref.16
VAR_036132
Natural variant3111P → L. Ref.2
Corresponds to variant rs28925904 [ dbSNP | Ensembl ].
VAR_025261
Natural variant3771T → I.
Corresponds to variant rs2229879 [ dbSNP | Ensembl ].
VAR_053096
Natural variant3871T → N in a breast cancer sample; somatic mutation. Ref.16
VAR_036133

Experimental info

Sequence conflict2041A → G in AAC50380. Ref.1
Sequence conflict2131C → S in AAC50380. Ref.1

Sequences

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

Last modified February 7, 2006. Version 2.
Checksum: E0FAC78772B6677B

FASTA69476,616
        10         20         30         40         50         60 
MSGGEVVCSG WLRKSPPEKK LKRYAWKRRW FVLRSGRLTG DPDVLEYYKN DHAKKPIRII 

        70         80         90        100        110        120 
DLNLCQQVDA GLTFNKKEFE NSYIFDINTI DRIFYLVADS EEEMNKWVRC ICDICGFNPT 

       130        140        150        160        170        180 
EEDPVKPPGS SLQAPADLPL AINTAPPSTQ ADSSSATLPP PYQLINVPPH LETLGIQEDP 

       190        200        210        220        230        240 
QDYLLLINCQ SKKPEPTRTH ADSAKSTSSE TDCNDNVPSH KNPASSQSKH GMNGFFQQQM 

       250        260        270        280        290        300 
IYDSPPSRAP SASVDSSLYN LPRSYSHDVL PKVSPSSTEA DGELYVFNTP SGTSSVETQM 

       310        320        330        340        350        360 
RHVSISYDIP PTPGNTYQIP RTFPEGTLGQ TSKLDTIPDI PPPRPPKPHP AHDRSPVETC 

       370        380        390        400        410        420 
SIPRTASDTD SSYCIPTAGM SPSRSNTIST VDLNKLRKDA SSQDCYDIPR AFPSDRSSSL 

       430        440        450        460        470        480 
EGFHNHFKVK NVLTVGSVSS EELDENYVPM NPNSPPRQHS SSFTEPIQEA NYVPMTPGTF 

       490        500        510        520        530        540 
DFSSFGMQVP PPAHMGFRSS PKTPPRRPVP VADCEPPPVD RNLKPDRKVK PAPLEIKPLP 

       550        560        570        580        590        600 
EWEELQAPVR SPITRSFARD SSRFPMSPRP DSVHSTTSSS DSHDSEENYV PMNPNLSSED 

       610        620        630        640        650        660 
PNLFGSNSLD GGSSPMIKPK GDKQVEYLDL DLDSGKSTPP RKQKSSGSGS SVADERVDYV 

       670        680        690 
VVDQQKTLAL KSTREAWTDG RQSTESETPA KSVK 

« Hide

Isoform 2 [UniParc].

Checksum: EAA4573B9E5A25B9
Show »

FASTA72480,005

References

« Hide 'large scale' references
[1]"A Grb2-associated docking protein in EGF- and insulin-receptor signalling."
Holgado-Madruga M., Emlet D.R., Moscatello D.K., Godwin A.K., Wong A.J.
Nature 379:560-564(1996) [PubMed: 8596638] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]NIEHS SNPs program
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-311.
[3]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[7]"Non-T cell activation linker (NTAL): a transmembrane adaptor protein involved in immunoreceptor signaling."
Brdicka T., Imrich M., Angelisova P., Brdickova N., Horvath O., Spicka J., Hilgert I., Luskova P., Draber P., Novak P., Engels N., Wienands J., Simeoni L., Oesterreicher J., Aguado E., Malissen M., Schraven B., Horejsi V.
J. Exp. Med. 196:1617-1626(2002) [PubMed: 12486104] [Abstract]
Cited for: INTERACTION WITH LAT2.
[8]"Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1."
Palka H.L., Park M., Tonks N.K.
J. Biol. Chem. 278:5728-5735(2003) [PubMed: 12475979] [Abstract]
Cited for: INTERACTION WITH PTPRJ.
[9]"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-259 AND SER-266, MASS SPECTROMETRY.
[10]"Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation and survival of multiple myeloma cells."
Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T., Catley L.P., Hideshima T., Mulligan R.C., Chauhan D., Anderson K.C.
J. Biol. Chem. 279:21658-21665(2004) [PubMed: 15010462] [Abstract]
Cited for: PHOSPHORYLATION BY HCK, INTERACTION WITH HCK; CRKL PTPN11 AND GRB2.
[11]"Cellular signaling by fibroblast growth factor receptors."
Eswarakumar V.P., Lax I., Schlessinger J.
Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed: 15863030] [Abstract]
Cited for: REVIEW ON ROLE IN FGFR1 SIGNALING; SUBUNIT AND PHOSPHORYLATION.
[12]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-406; TYR-627 AND TYR-659, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[13]"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks."
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-373; TYR-406; TYR-627 AND TYR-659, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[14]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-659, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 (ISOFORM 2), MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-183; TYR-259; TYR-373; TYR-406 AND TYR-659, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-83 AND ASN-387.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43885 mRNA. Translation: AAC50380.1.
DQ021880 Genomic DNA. Translation: AAY26398.1.
AK289767 mRNA. Translation: BAF82456.1.
AC097658 Genomic DNA. No translation available.
AC104685 Genomic DNA. Translation: AAY40964.1.
CH471056 Genomic DNA. Translation: EAX05072.1.
BC064848 mRNA. Translation: AAH64848.1.
IPIIPI00031068.
IPI00410383.
PIRS68442.
RefSeqNP_002030.2. NM_002039.3.
NP_997006.1. NM_207123.2.
UniGeneHs.618456.
Hs.80720.

3D structure databases

ProteinModelPortalQ13480.
SMRQ13480. Positions 5-114.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13480. 14 interactions.
MINTMINT-140909.
STRINGQ13480.

PTM databases

PhosphoSiteQ13480.

Polymorphism databases

DMDM90180201.

Proteomic databases

PRIDEQ13480.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262994; ENSP00000262994; ENSG00000109458.
GeneID2549.
KEGGhsa:2549.
UCSCuc003ijd.1. human.
uc003ije.1. human.

Organism-specific databases

CTD2549.
GeneCardsGC04P144257.
H-InvDBHIX0004529.
HGNCHGNC:4066. GAB1.
MIM604439. gene.
neXtProtNX_Q13480.
PharmGKBPA28477.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09355.
GeneTreeENSGT00510000046662.
HOVERGENHBG051685.
OMAYLLLINC.

Enzyme and pathway databases

Pathway_Interaction_DBepopathway. EPO signaling pathway.
fgf_pathway. FGF signaling pathway.
il6_7pathway. IL6-mediated signaling events.
lysophospholipid_pathway. LPA receptor mediated events.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
pdgfrbpathway. PDGFR-beta signaling pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.
vegfr1_pathway. VEGFR1 specific signals.
ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ13480.
BgeeQ13480.
CleanExHS_GAB1.
GenevestigatorQ13480.
GermOnlineENSG00000109458. Homo sapiens.

Family and domain databases

InterProIPR011993. PH_type.
IPR001849. Pleckstrin_homology.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
KOK09593.
PfamPF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio10055.
SOURCESearch...

Entry information

Entry nameGAB1_HUMAN
AccessionPrimary (citable) accession number: Q13480
Secondary accession number(s): A8K152, Q4W5G2, Q6P1W2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 98 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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families