ID SHC3_MOUSE Reviewed; 474 AA.
AC Q61120; Q3ZAX2;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 24-JAN-2024, entry version 163.
DE RecName: Full=SHC-transforming protein 3;
DE AltName: Full=Neuronal Shc;
DE Short=N-Shc;
DE AltName: Full=SHC-transforming protein C;
DE AltName: Full=Src homology 2 domain-containing-transforming protein C3;
DE Short=SH2 domain protein C3;
GN Name=Shc3; Synonyms=Nshc, ShcC;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8610109; DOI=10.1073/pnas.93.7.2729;
RA O'Bryan J.P., Songyang Z., Cantley L., Der C.J., Pawson T.;
RT "A mammalian adaptor protein with conserved Src homology 2 and
RT phosphotyrosine-binding domains is related to Shc and is specifically
RT expressed in the brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2729-2734(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Signaling adapter that couples activated growth factor
CC receptors to signaling pathway in neurons. Involved in the signal
CC transduction pathways of neurotrophin-activated Trk receptors in
CC cortical neurons (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the Trk receptors in a phosphotyrosine-
CC dependent manner. Once activated, binds to GRB2. Interacts with
CC activated EGF receptors (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q61120; P12023: App; NbExp=2; IntAct=EBI-79107, EBI-78814;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the adult brain.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250}.
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DR EMBL; U46854; AAC52508.1; -; mRNA.
DR EMBL; BC103612; AAI03613.1; -; mRNA.
DR EMBL; BC105644; AAI05645.1; -; mRNA.
DR EMBL; BC105645; AAI05646.1; -; mRNA.
DR RefSeq; NP_033193.2; NM_009167.3.
DR AlphaFoldDB; Q61120; -.
DR SMR; Q61120; -.
DR BioGRID; 203216; 9.
DR IntAct; Q61120; 1.
DR MINT; Q61120; -.
DR STRING; 10090.ENSMUSP00000021898; -.
DR iPTMnet; Q61120; -.
DR PhosphoSitePlus; Q61120; -.
DR jPOST; Q61120; -.
DR MaxQB; Q61120; -.
DR PaxDb; 10090-ENSMUSP00000021898; -.
DR PeptideAtlas; Q61120; -.
DR ProteomicsDB; 255404; -.
DR Antibodypedia; 27964; 250 antibodies from 29 providers.
DR DNASU; 20418; -.
DR Ensembl; ENSMUST00000021898.6; ENSMUSP00000021898.6; ENSMUSG00000021448.9.
DR GeneID; 20418; -.
DR KEGG; mmu:20418; -.
DR UCSC; uc007qmg.1; mouse.
DR AGR; MGI:106179; -.
DR CTD; 53358; -.
DR MGI; MGI:106179; Shc3.
DR VEuPathDB; HostDB:ENSMUSG00000021448; -.
DR eggNOG; KOG3697; Eukaryota.
DR GeneTree; ENSGT00950000182870; -.
DR HOGENOM; CLU_029532_0_0_1; -.
DR InParanoid; Q61120; -.
DR OrthoDB; 2903566at2759; -.
DR PhylomeDB; Q61120; -.
DR TreeFam; TF315807; -.
DR Reactome; R-MMU-167044; Signalling to RAS.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-8853659; RET signaling.
DR BioGRID-ORCS; 20418; 3 hits in 62 CRISPR screens.
DR ChiTaRS; Shc3; mouse.
DR PRO; PR:Q61120; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61120; Protein.
DR Bgee; ENSMUSG00000021448; Expressed in dentate gyrus of hippocampal formation granule cell and 75 other cell types or tissues.
DR ExpressionAtlas; Q61120; baseline and differential.
DR Genevisible; Q61120; MM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
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; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 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; IPR035676; SHC_SH2.
DR PANTHER; PTHR10337; SHC TRANSFORMING PROTEIN; 1.
DR PANTHER; PTHR10337:SF4; SHC-TRANSFORMING PROTEIN 3; 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; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..474
FT /note="SHC-transforming protein 3"
FT /id="PRO_0000097735"
FT DOMAIN 29..214
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 379..470
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..378
FT /note="CH1"
FT REGION 308..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 71
FT /note="A -> R (in Ref. 1; AAC52508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 52121 MW; 18550FB1C5F0F270 CRC64;
MSATRKSRAG DEPLPRPPRG APHTSDQVLG PGVTYVVKYL GCIEVLRSMR SLDFSTRTQV
TREAISRVCE AVPGAKGALK KRKPPSKMLS SILGKSNLQF AGMSISLTIS TASLNLRTPD
SKQIIANHHM RSISFASGGD PDTTDYVAYV AKDPVNRRAC HILECCDGLA QDVIGSIGQA
FELRFKQYLQ CPSKVPALQD RMQSLDEPWT EEEGDGPDHP YYNSVPTKMP PPGGFLDARL
KGRPHAPEAA QFAGKEQTYY QGRHLGDTFG EDWQRAPTRQ GSLDIYSTAE GKTHMVPVGE
TPTYVNTQPV PPQVWPAATS STESSPRKDL FDMKPFEDAL RNQPLGPMLS KAASVECISP
VTPRAPDARM LEELNAEPWY QGEMSRKEAE ALLREDGDFL VRKSTTNPGS FVLTGMHNGQ
AKHLLLVDPE GTIRTKDRVF DSISHLINYH LESSLPIVSA GSELCLQQPV ERKP
//
