SHC2_MOUSE
ID SHC2_MOUSE Reviewed; 573 AA.
AC Q8BMC3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=SHC-transforming protein 2;
DE AltName: Full=Protein Sck;
DE AltName: Full=Protein Sli;
DE AltName: Full=SHC-transforming protein B;
DE AltName: Full=Src homology 2 domain-containing-transforming protein C2;
DE Short=SH2 domain protein C2;
GN Name=Shc2; Synonyms=Sck, ShcB;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-573.
RC STRAIN=C57BL/6J; TISSUE=Mesonephros;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION AT TYR-316; TYR-317 AND TYR-395, AND INTERACTION WITH THE
RP TRK RECEPTORS.
RX PubMed=12006576; DOI=10.1074/jbc.m111659200;
RA Liu H.Y., Meakin S.O.;
RT "ShcB and ShcC activation by the Trk family of receptor tyrosine kinases.";
RL J. Biol. Chem. 277:26046-26056(2002).
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.
CC -!- SUBUNIT: Interacts with the Trk receptors in a phosphotyrosine-
CC dependent manner and MEGF12. Once activated, binds to GRB2 (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Expressed at high level in the
CC hypothalamus and at low level in the caudate nucleus.
CC -!- DOMAIN: The PID domain mediates binding to the TrkA receptor.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine by the Trk receptors.
CC {ECO:0000269|PubMed:12006576}.
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DR EMBL; AC132265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK032878; BAC28066.1; -; mRNA.
DR CCDS; CCDS48620.1; -.
DR RefSeq; NP_001019710.1; NM_001024539.1.
DR AlphaFoldDB; Q8BMC3; -.
DR SMR; Q8BMC3; -.
DR BioGRID; 229705; 4.
DR IntAct; Q8BMC3; 1.
DR MINT; Q8BMC3; -.
DR STRING; 10090.ENSMUSP00000129491; -.
DR iPTMnet; Q8BMC3; -.
DR PhosphoSitePlus; Q8BMC3; -.
DR MaxQB; Q8BMC3; -.
DR PaxDb; Q8BMC3; -.
DR PRIDE; Q8BMC3; -.
DR ProteomicsDB; 261397; -.
DR Ensembl; ENSMUST00000020564; ENSMUSP00000020564; ENSMUSG00000020312.
DR GeneID; 216148; -.
DR KEGG; mmu:216148; -.
DR UCSC; uc007fzd.2; mouse.
DR CTD; 25759; -.
DR MGI; MGI:106180; Shc2.
DR VEuPathDB; HostDB:ENSMUSG00000020312; -.
DR eggNOG; KOG3697; Eukaryota.
DR GeneTree; ENSGT00950000182870; -.
DR HOGENOM; CLU_029532_2_0_1; -.
DR InParanoid; Q8BMC3; -.
DR OMA; HGGQPKH; -.
DR OrthoDB; 1351843at2759; -.
DR PhylomeDB; Q8BMC3; -.
DR TreeFam; TF315807; -.
DR Reactome; R-MMU-167044; Signalling to RAS.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR BioGRID-ORCS; 216148; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Shc2; mouse.
DR PRO; PR:Q8BMC3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BMC3; protein.
DR Bgee; ENSMUSG00000020312; Expressed in superior cervical ganglion and 129 other tissues.
DR Genevisible; Q8BMC3; MM.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:InterPro.
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; IPR029591; SHC2.
DR InterPro; IPR035676; SHC_SH2.
DR PANTHER; PTHR10337:SF5; PTHR10337:SF5; 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..573
FT /note="SHC-transforming protein 2"
FT /id="PRO_0000097733"
FT DOMAIN 125..309
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 478..569
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 310..477
FT /note="CH1"
FT MOD_RES 316
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12006576"
FT MOD_RES 317
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12006576"
FT MOD_RES 395
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12006576"
FT CONFLICT 84..93
FT /note="RCRGSGTRGA -> PGSAGAPRRP (in Ref. 2; BAC28066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 61771 MW; 7663705836A902C8 CRC64;
MTQGPGGRAA PEPEAPTTFC ALLPRMPQWK FAAPGSFLGR GPAATRVAGV AEAQPEPGVP
ALAAVLGACE PRCAAPCPLP ALGRCRGSGT RGARVTPDVA DEWVRKGGFI HKPAHGWLHP
DARVLGPGVS YIVRYMGCIE VLRSMRSLDF NTRTQVTREA INRLHEAVPG VRGSWKKKAP
NKALASILGK SNLRFAGMSI SVNISVDGLN LSVPATRQII ANHHMQSISF ASGGDTDMTD
YVAYVAKDPI NQRACHILEC CEGLAQSVIS TVGQAFELRF KQYLHSPPKA VVPPERLTGL
EELAWGDDDA AADHNYYNSI PGKEPPLGGL VDSRLAVTQP CALATLGGLG QGMTPVWRDA
RGLPWDMGPS GAAPPGDGYV QADARGPHDY EEHLYVNTQG LDAVELEDTA EAPLQFEDSP
KKDLFDMRPF EDALKLHACS VAAGITAASP PLEDQWPSPP TRRAPIAPTE EQLRQEPWYH
GRMSRRAAEK LLRADGDFLV RDSVTNPGQY VLTGMHAGQP KHLLLVDPEG VVRTKDVLFE
SISHLIDYHL KNGLPIVAAE SELHLRGVVS REP
