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

GRB2-associated-binding protein 2

Gene

Gab2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis (By similarity).By similarity

GO - Molecular functioni

  1. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  2. phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
  3. protein domain specific binding Source: RGD
  4. transmembrane receptor protein tyrosine kinase adaptor activity Source: UniProtKB

GO - Biological processi

  1. intracellular signal transduction Source: RGD
  2. osteoclast differentiation Source: UniProtKB
  3. phosphatidylinositol-mediated signaling Source: UniProtKB
  4. positive regulation of cell proliferation Source: UniProtKB
  5. positive regulation of mast cell degranulation Source: UniProtKB
  6. transmembrane receptor protein tyrosine kinase signaling pathway Source: GOC
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
GRB2-associated-binding protein 2
Alternative name(s):
GRB2-associated binder 2
Growth factor receptor bound protein 2-associated protein 2
Gene namesi
Name:Gab2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621367. Gab2.

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. plasma membrane Source: UniProtKB
  3. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 665665GRB2-associated-binding protein 2PRO_0000050287Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei135 – 1351PhosphoserineBy similarity
Modified residuei142 – 1421PhosphoserineBy similarity
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei149 – 1491PhosphoserineBy similarity
Modified residuei150 – 1501PhosphoserineBy similarity
Modified residuei160 – 1601PhosphoserineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei220 – 2201PhosphoserineBy similarity
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei262 – 2621PhosphothreonineBy similarity
Modified residuei263 – 2631PhosphotyrosineBy similarity
Modified residuei275 – 2751PhosphothreonineBy similarity
Modified residuei278 – 2781PhosphoserineBy similarity
Modified residuei284 – 2841PhosphothreonineBy similarity
Modified residuei290 – 2901PhosphotyrosineBy similarity
Modified residuei328 – 3281PhosphothreonineBy similarity
Modified residuei382 – 3821PhosphothreonineBy similarity
Modified residuei388 – 3881PhosphothreonineBy similarity
Modified residuei402 – 4021PhosphoserineBy similarity
Modified residuei441 – 4411PhosphotyrosineBy similarity
Modified residuei532 – 5321PhosphoserineBy similarity
Modified residuei612 – 6121PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated upon EGF stimulation. Phosphorylated on tyrosine residues by HCK upon IL6 signaling (By similarity). Phosphorylated on tyrosine residue(s) by the thrombopoietin receptor (TPOR), stem cell factor receptor (SCFR), and T-cell and B-cell antigen receptors, gp130, IL-2R and IL-3R (By similarity). Phosphorylated upon stimulation of TNFRSF11A/RANK by TNFSF11/RANKL (By similarity).By similarity
Dephosphorylated by PTPN11.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9EQH1.
PRIDEiQ9EQH1.

PTM databases

PhosphoSiteiQ9EQH1.

Expressioni

Gene expression databases

GenevestigatoriQ9EQH1.

Interactioni

Subunit structurei

Interacts with HCK. Interacts with SHC1; may mediate interaction with receptors (By similarity). Interacts with SYK (By similarity). Interacts with PI-3 kinase (By similarity). Interacts with GRB2 (via SH3 2 domain) (By similarity). Interacts (phosphorylated) with PTPN11 (By similarity). Interacts with TNFRSF11A (via cytoplasmic domain) (By similarity). Interacts (phosphorylated) with 14-3-3 family proteins SFN, YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ and YWHAZ; prevents interaction with GRB2 and attenuates GAB2 signaling (By similarity).By similarity

Protein-protein interaction databases

BioGridi249977. 1 interaction.
IntActiQ9EQH1. 1 interaction.
MINTiMINT-7138417.
STRINGi10116.ENSRNOP00000016361.

Structurei

3D structure databases

ProteinModelPortaliQ9EQH1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 119112PHPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi348 – 3558SH3-bindingBy similarity
Motifi499 – 50810SH3-bindingBy similarity

Domaini

The SH3-binding motifs mediate interaction with SHC1 and GRB2.By similarity
The PH domain mediates phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate binding.By similarity

Sequence similaritiesi

Belongs to the GAB family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG83177.
HOGENOMiHOG000236270.
HOVERGENiHBG051685.
InParanoidiQ9EQH1.
KOiK08091.
PhylomeDBiQ9EQH1.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EQH1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGGGGDDVV CTGWLRKSPP EKKLRRYAWK KRWFILRSGR MSGDPDVLEY
60 70 80 90 100
YKNEHSKKPL RIINLNFCEQ VDAGLTFNKK ELQDSFVFDI KTSERTFYLV
110 120 130 140 150
AETEADMNKW VQSICQICGF NQAEESTDSL RNLSSASHGP RSSPAEFSSS
160 170 180 190 200
QHLLRERKSS APSHSSQPTL FTFEPPMTSH MQPALSTSAP QEYLYLHQCI
210 220 230 240 250
SRRTENSRSA SFSQGTRQKS DTAVQKLAQS NGHCINGVSN QVHGFYSLPK
260 270 280 290 300
PSRHNTEFKD STYDLPRSLA SHGHTKSSLT GSETDNEDVY TFKMPSNTLC
310 320 330 340 350
REFGDLLVDN MDVPTTPLSA YQIPRTFTLD KNHNAMTVAT SGDSAIAPPP
360 370 380 390 400
RPPKPSQAET PRWGSPQQKP PIGENSRSVA ATIPRRNTLP AMDNSRLHRA
410 420 430 440 450
SSCETYEYPT RGSGESASWS AESPGKTAVG RSDSASSDEN YVPMNPGSST
460 470 480 490 500
LLAMERAGDN SQSAYIPMGP GPHHFDPLGY PSTALPIHRG PSRGSEIQPP
510 520 530 540 550
PVNRNLKPDR KAKPTPLDLR NNTVIDELPF KSPVTKSWSR INHTFNSSSS
560 570 580 590 600
QYCRPISTQS ITSTDSGDSE ENYVPMQNPV SASPVPSGTN SPAPRKSTGS
610 620 630 640 650
VDYLALDFQP GSPSPHRKPS TSSVTSDEKV DYVQVDKEKT QALQNTMQEW
660
TDVRQSSEPS KGAKL
Length:665
Mass (Da):73,328
Last modified:October 1, 2001 - v2
Checksum:iBEB170B69406063E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230367 mRNA. Translation: AAG44268.2.
RefSeqiNP_445869.1. NM_053417.1.
UniGeneiRn.211990.

Genome annotation databases

GeneIDi84477.
KEGGirno:84477.
UCSCiRGD:621367. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230367 mRNA. Translation: AAG44268.2.
RefSeqiNP_445869.1. NM_053417.1.
UniGeneiRn.211990.

3D structure databases

ProteinModelPortaliQ9EQH1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249977. 1 interaction.
IntActiQ9EQH1. 1 interaction.
MINTiMINT-7138417.
STRINGi10116.ENSRNOP00000016361.

PTM databases

PhosphoSiteiQ9EQH1.

Proteomic databases

PaxDbiQ9EQH1.
PRIDEiQ9EQH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84477.
KEGGirno:84477.
UCSCiRGD:621367. rat.

Organism-specific databases

CTDi9846.
RGDi621367. Gab2.

Phylogenomic databases

eggNOGiNOG83177.
HOGENOMiHOG000236270.
HOVERGENiHBG051685.
InParanoidiQ9EQH1.
KOiK08091.
PhylomeDBiQ9EQH1.

Miscellaneous databases

NextBioi616982.
PROiQ9EQH1.

Gene expression databases

GenevestigatoriQ9EQH1.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of Gab2 as the major molecule responsible for EGF-induced PI3-kinase activation and DNA synthesis in rat hepatocytes."
    Kong M., Mounier C., Wu J., Posner B.I.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiGAB2_RAT
AccessioniPrimary (citable) accession number: Q9EQH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2001
Last modified: January 7, 2015
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.