SHC1_PONAB
ID SHC1_PONAB Reviewed; 583 AA.
AC Q5R7W7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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|UniProtKB:P29353,
CC ECO:0000250|UniProtKB:P98083, 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; CR859992; CAH92143.1; -; mRNA.
DR RefSeq; NP_001126253.1; NM_001132781.1.
DR AlphaFoldDB; Q5R7W7; -.
DR BMRB; Q5R7W7; -.
DR SMR; Q5R7W7; -.
DR STRING; 9601.ENSPPYP00000000893; -.
DR PRIDE; Q5R7W7; -.
DR GeneID; 100173225; -.
DR KEGG; pon:100173225; -.
DR CTD; 6464; -.
DR eggNOG; KOG3697; Eukaryota.
DR InParanoid; Q5R7W7; -.
DR OrthoDB; 1351843at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:InterPro.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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..583
FT /note="SHC-transforming protein 1"
FT /id="PRO_0000327221"
FT DOMAIN 156..339
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 488..579
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..487
FT /note="CH1"
FT REGION 372..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P98083"
FT MOD_RES 349
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 350
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 427
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29353"
SQ SEQUENCE 583 AA; 62797 MW; 69FB6553B510EA2E CRC64;
MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP GDDSPTTLCS
FFPRMSNLRL ANPAGGRPGS KGEPGRAADD GEGIVGAAMP DSGPLPLLRD MNKLSGGGGR
RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH PNDKVMGPGV SYLVRYMGCV EVLQSMRALD
FNTRTQVTRE AISLVCEAVP GAKGATRRRK PCSRPLSSIL GRSNLKFAGM PITLTVSTSS
LNLMAADCKQ IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL ECPEGLAQDV
ISTIGQAFEL RFKQYLRNPP KLVTPHDRMA GFDGSAWDEE EEEPPDHQYY NDFPGKEPPL
GGVVDMRLRE GAAPGAARST APSAQTPSHL GATLPVGQPV GGDPEVRKQM PPPPPCPGRE
LFDDPSYVNV QNLDKARQAV GGAGPPNPAV NGSAPRDLFD MRPFEDALRV PPPPQSVSMA
EQLRGEPWFH GKLSRREAEA LLQLNGDFLV RESTTTPGQY VLTGLQSGQP KHLLLVDPEG
VVRTKDHRFE SVSHLIGYHM DNHLPIISAG SELCLQQPVE RKL
