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Protein

Growth factor receptor-bound protein 14

Gene

Grb14

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

Functioni

Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal (By similarity).By similarity

GO - Molecular functioni

  • phosphoprotein binding Source: RGD

GO - Biological processi

  • insulin receptor signaling pathway Source: RGD
  • intracellular signal transduction Source: RGD
  • negative regulation of insulin receptor signaling pathway Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Growth factor receptor-bound protein 14
Alternative name(s):
GRB14 adapter protein
Gene namesi
Name:Grb14
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61869. Grb14.

Subcellular locationi

  • Cytoplasm By similarity
  • Endosome membrane By similarity; Peripheral membrane protein By similarity

  • Note: Upon insulin stimulation, translocates to the plasma membrane.By similarity

GO - Cellular componenti

  • cytoplasm Source: RGD
  • endosome Source: RGD
  • endosome membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 538537Growth factor receptor-bound protein 14PRO_0000150350Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei370 – 3701PhosphoserineCombined sources
Modified residuei373 – 3731PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on serine residues. Phosphorylated on tyrosine residues by TEK/TIE2 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO88900.
PRIDEiO88900.

PTM databases

PhosphoSiteiO88900.

Interactioni

Subunit structurei

Interacts with the cytoplasmic domain of the autophosphorylated insulin receptor, through the SH2 domain. Interacts with GRB14 (via BPS domain); this interaction protects the tyrosines in the activation loop on INSR from dephosphorylation (By similarity). Binds to the ankyrin repeat region of TNKS2 via its N-terminus. Interacts with activated NRAS. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FGFR1P113623EBI-7639197,EBI-1028277From a different organism.

GO - Molecular functioni

  • phosphoprotein binding Source: RGD

Protein-protein interaction databases

BioGridi248645. 2 interactions.
IntActiO88900. 3 interactions.
MINTiMINT-1347978.
STRINGi10116.ENSRNOP00000046233.

Structurei

3D structure databases

DisProtiDP00490.
ProteinModelPortaliO88900.
SMRiO88900. Positions 371-407, 431-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 19087Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini232 – 340109PHPROSITE-ProRule annotationAdd
BLAST
Domaini437 – 53397SH2PROSITE-ProRule annotationAdd
BLAST

Domaini

The PH domain binds relatively non-specifically and with low affinity to several phosphoinositides, the best binder being PI(3,4,5)P3.

Sequence similaritiesi

Belongs to the GRB7/10/14 family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Ras-associating domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiKOG3751. Eukaryota.
ENOG410XXC8. LUCA.
HOGENOMiHOG000231904.
HOVERGENiHBG000468.
InParanoidiO88900.
PhylomeDBiO88900.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR015042. BPS-dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
IPR000980. SH2.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF08947. BPS. 1 hit.
PF00169. PH. 1 hit.
PF00788. RA. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O88900-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSLQDGQS AAGRAGAQDS PLAVQVCRVA QGKGDAQDPA QVPGLHALSP
60 70 80 90 100
ASDATRRGAM DRRKAKDLEV QETPSIPNPF PELCCSPLTS VLSAGLFPRS
110 120 130 140 150
NSRKKQVIKV YSEDETSRAL EVPSDVTARD VCQLLILKNH YVDDNSWTLF
160 170 180 190 200
EHLSHTGVER TVEDHELLTE VLSHWVMEED NKLYLRKNYA KYEFFKNPMY
210 220 230 240 250
FFPEHMVSFA TEMNGDRSLT QIPQVFLSSN TYPEIHGFLH AKEQGKKSWK
260 270 280 290 300
KAYFFLRRSG LYFSTKGTSK EPRHLQFFSE FSTSNVYMSL AGKKKHGAPT
310 320 330 340 350
PYGFCFKPTK AGGPRDLKML CAEEDQSRMC WVTAIRLLKY GMQLYQNYMH
360 370 380 390 400
PSQARSACSS QSVSPMRSVS ENSLVAMDFS GQKTRVIDNP TEALSVAVEE
410 420 430 440 450
GLAWRKKGCL RLGNHGSPTA PSQSSAVNMA LHRSQPWFHH RISRDEAQQL
460 470 480 490 500
ITRQGPVDGV FLVRDSQSNP RTFVLSMSHG QKIKHFQIIP VEDDGEVFHT
510 520 530
LDDGHTKFTD LIQLVEFYQL NKGVLPCKLK HYCARMAV
Length:538
Mass (Da):60,593
Last modified:November 1, 1998 - v1
Checksum:iCEBC9037E7868EEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076619 mRNA. Translation: AAC61478.1.
RefSeqiNP_113811.1. NM_031623.1.
UniGeneiRn.30028.

Genome annotation databases

GeneIDi58844.
KEGGirno:58844.
UCSCiRGD:61869. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076619 mRNA. Translation: AAC61478.1.
RefSeqiNP_113811.1. NM_031623.1.
UniGeneiRn.30028.

3D structure databases

DisProtiDP00490.
ProteinModelPortaliO88900.
SMRiO88900. Positions 371-407, 431-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248645. 2 interactions.
IntActiO88900. 3 interactions.
MINTiMINT-1347978.
STRINGi10116.ENSRNOP00000046233.

PTM databases

PhosphoSiteiO88900.

Proteomic databases

PaxDbiO88900.
PRIDEiO88900.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi58844.
KEGGirno:58844.
UCSCiRGD:61869. rat.

Organism-specific databases

CTDi2888.
RGDi61869. Grb14.

Phylogenomic databases

eggNOGiKOG3751. Eukaryota.
ENOG410XXC8. LUCA.
HOGENOMiHOG000231904.
HOVERGENiHBG000468.
InParanoidiO88900.
PhylomeDBiO88900.

Miscellaneous databases

NextBioi611417.
PROiO88900.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR015042. BPS-dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
IPR000980. SH2.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF08947. BPS. 1 hit.
PF00169. PH. 1 hit.
PF00788. RA. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGRB14_RAT
AccessioniPrimary (citable) accession number: O88900
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 118 of the entry and version 1 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

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 one 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.