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Q13480 (GAB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. 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
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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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.9

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

Sequence similarities

Belongs to the GAB family.

Contains 1 PH domain.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of JUN kinase activity

Inferred from electronic annotation. Source: Compara

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

epidermis development

Inferred from electronic annotation. Source: Compara

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

heart development

Inferred from electronic annotation. Source: Compara

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

interleukin-6-mediated signaling pathway

Inferred from electronic annotation. Source: Compara

labyrinthine layer development

Inferred from electronic annotation. Source: Compara

platelet-derived growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Compara

regulation of cell migration

Inferred from electronic annotation. Source: Compara

response to oxidative stress

Inferred from electronic annotation. Source: Compara

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionSH3/SH2 adaptor activity

Traceable author statement Ref.1. Source: ProtInc

phospholipid binding

Inferred from electronic annotation. Source: InterPro

signal transducer activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

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: Contains a phosphoserine at position 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 residue2661Phosphoserine By similarity
Modified residue5031Phosphothreonine By similarity
Modified residue6271Phosphotyrosine Ref.12
Modified residue6591Phosphotyrosine Ref.11

Natural variations

Alternative sequence5281K → KGQSPKILRLKPHGLERTDS QTIGDFATRRK in isoform 2.
VSP_017137
Natural variant831Y → C in a breast cancer sample; somatic mutation. Ref.13
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.13
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRJ.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY HCK, INTERACTION WITH HCK; CRKL PTPN11 AND GRB2.
[10]"Cellular signaling by fibroblast growth factor receptors."
Eswarakumar V.P., Lax I., Schlessinger J.
Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN FGFR1 SIGNALING; SUBUNIT AND PHOSPHORYLATION.
[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 TYR-659, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 (ISOFORM 2), MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"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 TYR-627, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-83 AND ASN-387.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13480. 13 interactions.
MINTMINT-140909.
STRING9606.ENSP00000262995.

PTM databases

PhosphoSiteQ13480.

Polymorphism databases

DMDM90180201.

Proteomic databases

PaxDbQ13480.
PRIDEQ13480.

Protocols and materials databases

DNASU2549.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262994; ENSP00000262994; ENSG00000109458.
ENST00000262995; ENSP00000262995; ENSG00000109458.
GeneID2549.
KEGGhsa:2549.
UCSCuc003ijd.3. human.
uc003ije.3. human.

Organism-specific databases

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

Phylogenomic databases

eggNOGNOG80382.
HOGENOMHOG000236270.
HOVERGENHBG051685.
KOK09593.
OMAETDCNDN.

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.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

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

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi2549.
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: May 1, 2013
This is version 113 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

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents