Q5M824 (SHC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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 process	Angiogenesis Growth regulation
Cellular component	Cytoplasm
Domain	SH2 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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 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 stimulus 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 nicotine Inferred from expression pattern PubMed 17068140. Source: RGD response to toxin Inferred from expression pattern PubMed 16699171. Source: RGD
Cellular_component	Shc-EGFR complex Inferred from direct assay PubMed 7513704. Source: BHF-UCL endosome membrane Inferred from direct assay PubMed 17363458. Source: RGD nucleus Inferred from direct assay PubMed 15375560. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 469	469	SHC-transforming protein 1		PRO_0000327222
Regions
	Domain	46 – 229	184	PID
	Domain	374 – 465	92	SH2
	Region	230 – 373	144	CH1
	Compositional bias	297 – 360	64	Pro-rich
Amino acid modifications
	Modified residue	29	1	Phosphoserine By similarity
	Modified residue	239	1	Phosphotyrosine By similarity
	Modified residue	240	1	Phosphotyrosine By similarity
	Modified residue	312	1	Phosphoserine By similarity
	Modified residue	313	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5M824 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: 9BFEE9D33E07B3F9	FASTA	469	51,503
	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

References

	« Hide 'large scale' referencesShow '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.
IPI	IPI00373231.
RefSeq	NP_445969.2. NM_053517.2.
UniGene	Rn.138818.
3D structure databases
HSSP	HSSP built from PDB template 1N3H based on UniProtKB P29353.
ProteinModelPortal	Q5M824.
SMR	Q5M824. Positions 1-207, 366-469.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000028038.
PTM databases
PhosphoSite	Q5M824.
Proteomic databases
PaxDb	Q5M824.
PRIDE	Q5M824.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	85385.
KEGG	rno:85385.
UCSC	RGD:620446. rat.
Organism-specific databases
CTD	6464.
RGD	620446. Shc1.
Phylogenomic databases
eggNOG	NOG315087.
HOGENOM	HOG000231974.
HOVERGEN	HBG050121.
InParanoid	Q5M824.
KO	K06279.
OrthoDB	EOG42NJ0D.
Gene expression databases
ArrayExpress	Q5M824.
Genevestigator	Q5M824.
Family and domain databases
Gene3D	2.30.29.30. 1 hit. 3.30.505.10. 1 hit.
InterPro	IPR011993. PH_like_dom. IPR006019. PID_domain. IPR006020. PTyr_interaction_dom. IPR000980. SH2. [Graphical view]
Pfam	PF00640. PID. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00629. SHCPIDOMAIN.
SMART	SM00462. PTB. 1 hit. SM00252. SH2. 1 hit. [Graphical view]
PROSITE	PS01179. PID. 1 hit. PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	617490.

Entry information

Entry name

SHC1_RAT

Accession

Primary (citable) accession number: Q5M824

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	February 1, 2005
Last modified:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program