SHC1_BOVIN
ID SHC1_BOVIN Reviewed; 473 AA.
AC Q0IIE2; Q45KX9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=SHC-transforming protein 1;
DE AltName: Full=Src homology 2 domain-containing-transforming protein C1;
DE Short=SH2 domain protein C1;
GN Name=SHC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-151.
RC TISSUE=Peripheral blood monocyte;
RA Ozer D., Herzig C.T.A., Telfer J., Baldwin C.L.;
RT "Comparison of gene expression of intracellular signaling molecules in
RT WC1.1+ vs. WC1.2+ gamma/delta T lymphocytes.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Signaling adapter that couples activated growth factor
CC receptors to signaling pathways. Participates in a signaling cascade
CC initiated by activated KIT and KITLG/SCF. Participates in signaling
CC downstream of the angiopoietin receptor TEK/TIE2, and plays a role in
CC the regulation of endothelial cell migration and sprouting angiogenesis
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CPNE3; this interaction may mediate the binding
CC of CPNE3 with ERBB2 (By similarity). Interacts with the Trk receptors
CC NTRK1, NTRK2 and NTRK3; in a phosphotyrosine-dependent manner.
CC Interacts with the NPXY motif of tyrosine-phosphorylated IGF1R and INSR
CC in vitro via the PID domain. Once activated, binds to GRB2. Interacts
CC with tyrosine-phosphorylated CD3T and DDR2. Interacts with the N-
CC terminal region of APS. Interacts with phosphorylated LRP1 and IRS4.
CC Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with ALK, GAB2,
CC GRB7 and KIT. Interacts with PTPN6/SHP (tyrosine phosphorylated).
CC Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2,
CC SRC, SHC1, GAP43 and CTTN. Interacts with FLT4 (tyrosine-
CC phosphorylated). Interacts with EPHB1 and GRB2; activates the MAPK/ERK
CC cascade to regulate cell migration. Interacts with PDGFRB (tyrosine-
CC phosphorylated). Interacts with ERBB4. Interacts with TEK/TIE2
CC (tyrosine-phosphorylated). Interacts with PTK2/FAK1 (By similarity).
CC Interacts with CEACAM1; this interaction is CEACAM1-phosphorylation-
CC dependent and mediates interaction with EGFR or INSR resulting in
CC decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (By
CC similarity). Interacts (via PID domain) with PEAK1 (when
CC phosphorylated) (By similarity). Found in a complex with PPP1CA,
CC PPP1CC, SHC1 and PEAK1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P29353, ECO:0000250|UniProtKB:P98083,
CC ECO:0000250|UniProtKB:Q5M824}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated by activated epidermal growth factor receptor.
CC Phosphorylated in response to KIT signaling. Tyrosine phosphorylated in
CC response to FLT3 and FLT4 signaling and by ligand-activated ALK.
CC Tyrosine phosphorylated by ligand-activated PDGFRB. Tyrosine
CC phosphorylated by TEK/TIE2. May be tyrosine phosphorylated by activated
CC PTK2/FAK1. Tyrosine phosphorylated by activated PTK2B/PYK2.
CC Dephosphorylation by PTPN2 may regulate interaction with GRB2 (By
CC similarity). {ECO:0000250}.
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DR EMBL; BC122688; AAI22689.1; -; mRNA.
DR EMBL; DQ125497; AAZ38953.1; -; mRNA.
DR RefSeq; NP_001068773.1; NM_001075305.2.
DR RefSeq; NP_001157533.1; NM_001164061.1.
DR AlphaFoldDB; Q0IIE2; -.
DR BMRB; Q0IIE2; -.
DR SMR; Q0IIE2; -.
DR STRING; 9913.ENSBTAP00000026432; -.
DR PaxDb; Q0IIE2; -.
DR PRIDE; Q0IIE2; -.
DR Ensembl; ENSBTAT00000040264; ENSBTAP00000040041; ENSBTAG00000019838.
DR Ensembl; ENSBTAT00000075224; ENSBTAP00000062285; ENSBTAG00000019838.
DR GeneID; 507196; -.
DR KEGG; bta:507196; -.
DR CTD; 6464; -.
DR VEuPathDB; HostDB:ENSBTAG00000019838; -.
DR VGNC; VGNC:34590; SHC1.
DR eggNOG; KOG3697; Eukaryota.
DR GeneTree; ENSGT00950000182870; -.
DR HOGENOM; CLU_029532_2_0_1; -.
DR InParanoid; Q0IIE2; -.
DR OrthoDB; 1351843at2759; -.
DR Reactome; R-BTA-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-BTA-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-BTA-167044; Signalling to RAS.
DR Reactome; R-BTA-180336; SHC1 events in EGFR signaling.
DR Reactome; R-BTA-201556; Signaling by ALK.
DR Reactome; R-BTA-2424491; DAP12 signaling.
DR Reactome; R-BTA-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-BTA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-BTA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-BTA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-BTA-354192; Integrin signaling.
DR Reactome; R-BTA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-BTA-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-BTA-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-BTA-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-BTA-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-BTA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-BTA-74749; Signal attenuation.
DR Reactome; R-BTA-74751; Insulin receptor signalling cascade.
DR Reactome; R-BTA-8853659; RET signaling.
DR Reactome; R-BTA-8983432; Interleukin-15 signaling.
DR Reactome; R-BTA-912526; Interleukin receptor SHC signaling.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000019838; Expressed in pigment epithelium of eye and 105 other tissues.
DR ExpressionAtlas; Q0IIE2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd01209; PTB_Shc; 1.
DR CDD; cd09925; SH2_SHC; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006019; PID_Shc-like.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR029586; Shc1/ShcA.
DR InterPro; IPR035676; SHC_SH2.
DR PANTHER; PTHR10337:SF2; PTHR10337:SF2; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00629; SHCPIDOMAIN.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Angiogenesis; Cytoplasm; Growth regulation; Phosphoprotein;
KW Reference proteome; SH2 domain.
FT CHAIN 1..473
FT /note="SHC-transforming protein 1"
FT /id="PRO_0000327220"
FT DOMAIN 46..229
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 378..469
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..377
FT /note="CH1"
FT REGION 328..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P98083"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 240
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 317
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT CONFLICT 2..3
FT /note="NK -> HN (in Ref. 2; AAZ38953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 51631 MW; D2B0277087268CDF CRC64;
MNKLSGGGGR RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH PNDKVMGPGV SYLVRYMGCV
EVLQSMRALD FNTRTQVTRE AISLVCEAVP GAKGATRRRK PCSRPLSSIL GRSNLKFAGM
PITLTVSTSS LNLMAADCKQ IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL
ECPEGLAQDV ISTIGQAFEL RFKQYLRNPP RLVTPHDRMA GFDGSAWDEE EEEPPDHQYY
NDFPGKEPPL GGVVDMRLRE GALPGAARPT PPSAQTPSHL GATLPVGQPA GGDPEARRQM
PPPPPSSGRE LFDDPSYVNV QNLDKARQAG AGAGPPNPTI NGSAPRDLFD MKPFEDALRM
PPPPQSTAMA EQLRGEPWFH GKLSRREAEA LLQVNGDFLV RESTTTPGQY VLTGLQSGQP
KHLLLVDPEG VVRTKDHRFE SVSHLISYHM DNHLPIISAG SELCLQQPVE RKL
