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SHC3_MOUSE
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   03-AUG-2022, entry version 155.
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; Q61120; -.
DR   PeptideAtlas; Q61120; -.
DR   PRIDE; Q61120; -.
DR   ProteomicsDB; 255404; -.
DR   Antibodypedia; 27964; 225 antibodies from 29 providers.
DR   DNASU; 20418; -.
DR   Ensembl; ENSMUST00000021898; ENSMUSP00000021898; ENSMUSG00000021448.
DR   GeneID; 20418; -.
DR   KEGG; mmu:20418; -.
DR   UCSC; uc007qmg.1; mouse.
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; 1351843at2759; -.
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 59 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 73 other 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:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR   GO; GO:0007417; P:central nervous system development; IEA:InterPro.
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; -; 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; IPR029593; Shc3/ShcC/N-Shc.
DR   InterPro; IPR035676; SHC_SH2.
DR   PANTHER; PTHR10337:SF4; PTHR10337:SF4; 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   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
 
 
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