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Q5M824 (SHC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SHC-transforming protein 1
Alternative name(s):
Src homology 2 domain-containing-transforming protein C1
Short name=SH2 domain protein C1
Gene names
Name:Shc1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis By similarity.

Subunit structure

Interacts with the NPXY motif of tyrosine-phosphorylated IGF1R and INSR in vitro via the PID domain. Once activated, binds to GRB2. Interacts with tyrosine-phosphorylated CD3T and DDR2. Interacts with the N-terminal region of APS. Interacts with phosphorylated LRP1 and IRS4. Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with ALK, GAB2, GRB7 and KIT. Interacts with PTPN6/SHP (tyrosine phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2A, SRC, SHC1, GAP43 and CTTN. Interacts with EPHB1 and GRB2; activates the MAPK/ERK cascade to regulate cell migration. Interacts with PDGFRB (tyrosine-phosphorylated). Interacts with ERBB4. Interacts with TEK/TIE2 (tyrosine-phosphorylated). Interacts with PTK2/FAK1 By similarity. Interacts with FLT4 (tyrosine-phosphorylated). Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; in a phosphotyrosine-dependent manner. Ref.3 Ref.4 Ref.5

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Phosphorylated by activated epidermal growth factor receptor. Phosphorylated in response to KIT signaling. Tyrosine phosphorylated in response to FLT3 signaling and by ligand-activated ALK. Tyrosine phosphorylated by TEK/TIE2 By similarity. Tyrosine phosphorylated by ligand-activated PDGFRB By similarity. May be tyrosine phosphorylated by activated PTK2/FAK1 By similarity. Dephosphorylation by PTPN2 may regulate interaction with GRB2 By similarity. Phosphorylated in response to FLT4 signaling. Tyrosine phosphorylated by activated PTK2B/PYK2. Ref.2 Ref.3

Sequence similarities

Contains 1 PID domain.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processAngiogenesis
Growth regulation
   Cellular componentCytoplasm
   DomainSH2 domain
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from mutant phenotype PubMed 15262993. Source: RGD

activation of MAPK activity

Inferred from mutant phenotype PubMed 15262993. Source: RGD

aging

Inferred from physical interaction PubMed 11954667. Source: RGD

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

insulin receptor signaling pathway

Inferred from direct assay PubMed 17925406. Source: BHF-UCL

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

neuron differentiation

Inferred from mutant phenotype PubMed 17274988. Source: RGD

neuron projection development

Inferred from mutant phenotype PubMed 15485499. Source: RGD

organ regeneration

Inferred from expression pattern PubMed 15067377. Source: RGD

positive regulation of DNA replication

Inferred from mutant phenotype PubMed 7513704. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from mutant phenotype PubMed 12837289. Source: RGD

positive regulation of vasoconstriction

Inferred from mutant phenotype PubMed 16242150. Source: RGD

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

response to glucocorticoid

Inferred from expression pattern PubMed 10612430. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern PubMed 16699171. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 16439820. Source: RGD

response to insulin

Inferred from expression pattern PubMed 11954667. Source: RGD

response to nicotine

Inferred from expression pattern PubMed 17068140. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 16699171. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 16699171. Source: RGD

   Cellular_componentShc-EGFR complex

Inferred from direct assay PubMed 7513704. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 15375560. Source: RGD

endosome membrane

Inferred from direct assay PubMed 17363458. Source: RGD

nucleus

Inferred from direct assay PubMed 15375560. Source: RGD

plasma membrane

Inferred from direct assay PubMed 12837289. Source: RGD

   Molecular_functionepidermal growth factor receptor binding

Inferred from physical interaction PubMed 7513704. Source: BHF-UCL

phosphoprotein binding

Inferred from physical interaction PubMed 8910399. Source: RGD

phosphotyrosine binding

Inferred from physical interaction PubMed 9271418. Source: RGD

protein binding

Inferred from physical interaction PubMed 12837289PubMed 12933696. Source: RGD

protein complex binding

Inferred from physical interaction PubMed 17274988. Source: RGD

receptor tyrosine kinase binding

Inferred from physical interaction Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469SHC-transforming protein 1
PRO_0000327222

Regions

Domain46 – 229184PID
Domain374 – 46592SH2
Region230 – 373144CH1
Compositional bias297 – 36064Pro-rich

Amino acid modifications

Modified residue291Phosphoserine By similarity
Modified residue441N6-acetyllysine By similarity
Modified residue2391Phosphotyrosine By similarity
Modified residue2401Phosphotyrosine By similarity
Modified residue3121Phosphoserine By similarity
Modified residue3131Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5M824 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 9BFEE9D33E07B3F9

FASTA46951,503
        10         20         30         40         50         60 
MNKLSGGGGR RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH PNDKVMGPGV SYLVRYMGCV 

        70         80         90        100        110        120 
EVLQSMRALD FNTRTQVTRE AISLVCEAVP GAKGAMRRRK PCSRPLSSIL GRSNLKFAGM 

       130        140        150        160        170        180 
PITLTVSTSS LNLMAADCKQ IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL 

       190        200        210        220        230        240 
ECPEGLAQDV ISTIGQAFEL RFKQYLRNPP KLVTPHDRMA GFDGSAWDEE EEELPDHQYY 

       250        260        270        280        290        300 
NDFPGKEPPL GGVVDMRLRE GAARPTLPST QMPSHLGATL PIGQHVTGDH EVRKQMLPPP 

       310        320        330        340        350        360 
PCPGRELFDD PSYVNIQNLD KARQAGGGAG PPNPSVNGSA PRDLFDMKPF EDALRVPPAP 

       370        380        390        400        410        420 
QSMSMAEQLQ GESWFHGKLS RREAEALLQL NGDFLVREST TTPGQYVLTG LQSGQPKHLL 

       430        440        450        460 
LVDPEGVVRT KDHRFESVSH LISYHMDNHL PIISAGSELC LQQPVDRKV 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Liver.
[2]"Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions."
Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., Schlessinger J.
Nature 376:737-745(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
Tissue: Brain.
[3]"Mutation at tyrosine residue 1337 abrogates ligand-dependent transforming capacity of the FLT4 receptor."
Fournier E., Dubreuil P., Birnbaum D., Borg J.P.
Oncogene 11:921-931(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH FLT4.
[4]"Activation loop tyrosines contribute varying roles to TrkB autophosphorylation and signal transduction."
McCarty J.H., Feinstein S.C.
Oncogene 16:1691-1700(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NTRK2.
[5]"Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src stimulates intramolecular autophosphorylation and Shc signaling complex formation."
Yang K., Kim J.H., Kim H.J., Park I.S., Kim I.Y., Yang B.S.
J. Biol. Chem. 280:39058-39066(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDR2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC088298 mRNA. Translation: AAH88298.1.
RefSeqNP_445969.2. NM_053517.2.
UniGeneRn.138818.

3D structure databases

ProteinModelPortalQ5M824.
SMRQ5M824. Positions 1-207, 366-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250090. 5 interactions.
IntActQ5M824. 4 interactions.
STRING10116.ENSRNOP00000028038.

PTM databases

PhosphoSiteQ5M824.

Proteomic databases

PaxDbQ5M824.
PRIDEQ5M824.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID85385.
KEGGrno:85385.
UCSCRGD:620446. rat.

Organism-specific databases

CTD6464.
RGD620446. Shc1.

Phylogenomic databases

eggNOGNOG315087.
HOGENOMHOG000231974.
HOVERGENHBG050121.
InParanoidQ5M824.
KOK06279.
PhylomeDBQ5M824.

Gene expression databases

GenevestigatorQ5M824.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR011993. PH_like_dom.
IPR006019. PID_Shc-like.
IPR006020. PTB/PI_dom.
IPR000980. SH2.
[Graphical view]
PfamPF00640. PID. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00629. SHCPIDOMAIN.
SMARTSM00462. PTB. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
PROSITEPS01179. PID. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio617490.
PROQ5M824.

Entry information

Entry nameSHC1_RAT
AccessionPrimary (citable) accession number: Q5M824
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: February 1, 2005
Last modified: June 11, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families