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SHC1_HUMAN
ID   SHC1_HUMAN              Reviewed;         583 AA.
AC   P29353; B5BU19; D3DV78; O15290; Q5T180; Q5T183; Q5T184; Q5T185; Q5T186;
AC   Q8N4K5; Q96CL1;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 4.
DT   03-AUG-2022, entry version 246.
DE   RecName: Full=SHC-transforming protein 1;
DE   AltName: Full=SHC-transforming protein 3;
DE   AltName: Full=SHC-transforming protein A;
DE   AltName: Full=Src homology 2 domain-containing-transforming protein C1;
DE            Short=SH2 domain protein C1;
GN   Name=SHC1; Synonyms=SHC, SHCA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P46SHC AND P52SHC).
RX   PubMed=1623525; DOI=10.1016/0092-8674(92)90536-l;
RA   Pelicci G., Lanfrancone L., Grignani F., McGlade J., Cavallo F., Forni G.,
RA   Nicoletti I., Grignani F., Pawson T., Pelicci P.-G.;
RT   "A novel transforming protein (SHC) with an SH2 domain is implicated in
RT   mitogenic signal transduction.";
RL   Cell 70:93-104(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P66SHC).
RX   PubMed=9049300; DOI=10.1093/emboj/16.4.706;
RA   Migliaccio E., Mele S., Salcini A.E., Pelicci G., Lai K.M.,
RA   Superti-Furga G., Pawson T., Di Fiore P.P., Lanfrancone L., Pelicci P.-G.;
RT   "Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on the
RT   EGF receptor-MAP kinase-fos signalling pathway.";
RL   EMBO J. 16:706-716(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Fibroblast;
RX   PubMed=9192859; DOI=10.1006/geno.1997.4728;
RA   Harun R.B., Smith K.K., Leek J.P., Markham A.F., Norris A., Morrison J.F.;
RT   "Characterization of human SHC p66 cDNA and its processed pseudogene
RT   mapping to Xq12-q13.1.";
RL   Genomics 42:349-352(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P52SHC).
RC   TISSUE=Mammary gland, and Synovium;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA   Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA   Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA   Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA   Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA   Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA   Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in vitro-
RT   expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P52SHC AND 7).
RC   TISSUE=Choriocarcinoma, and Neuroblastoma;
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   [9]
RP   INTERACTION WITH PDGFRB AND GRB2, AND PHOSPHORYLATION.
RX   PubMed=8195171; DOI=10.1016/s0021-9258(17)36611-5;
RA   Yokote K., Mori S., Hansen K., McGlade J., Pawson T., Heldin C.H.,
RA   Claesson-Welsh L.;
RT   "Direct interaction between Shc and the platelet-derived growth factor
RT   beta-receptor.";
RL   J. Biol. Chem. 269:15337-15343(1994).
RN   [10]
RP   INTERACTION WITH NTRK1.
RX   PubMed=8155326; DOI=10.1016/0896-6273(94)90223-2;
RA   Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A.,
RA   Kaplan D.R.;
RT   "Trk receptors use redundant signal transduction pathways involving SHC and
RT   PLC-gamma 1 to mediate NGF responses.";
RL   Neuron 12:691-705(1994).
RN   [11]
RP   INTERACTION WITH IGF1R.
RX   PubMed=7541045; DOI=10.1074/jbc.270.26.15639;
RA   Craparo A., O'Neill T.J., Gustafson T.A.;
RT   "Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their
RT   phosphotyrosine-dependent interaction with the NPEY motif of the insulin-
RT   like growth factor I receptor.";
RL   J. Biol. Chem. 270:15639-15643(1995).
RN   [12]
RP   INTERACTION WITH INSR.
RX   PubMed=7559478; DOI=10.1074/jbc.270.40.23258;
RA   He W., O'Neill T.J., Gustafson T.A.;
RT   "Distinct modes of interaction of SHC and insulin receptor substrate-1 with
RT   the insulin receptor NPEY region via non-SH2 domains.";
RL   J. Biol. Chem. 270:23258-23262(1995).
RN   [13]
RP   INTERACTION WITH INSR.
RX   PubMed=7537849; DOI=10.1128/mcb.15.5.2500;
RA   Gustafson T.A., He W., Craparo A., Schaub C.D., O'Neill T.J.;
RT   "Phosphotyrosine-dependent interaction of SHC and insulin receptor
RT   substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2
RT   domain.";
RL   Mol. Cell. Biol. 15:2500-2508(1995).
RN   [14]
RP   INTERACTION WITH INPP5D.
RX   PubMed=8874179;
RA   Ware M.D., Rosten P., Damen J.E., Liu L., Humphries R.K., Krystal G.;
RT   "Cloning and characterization of human SHIP, the 145-kD inositol 5-
RT   phosphatase that associates with SHC after cytokine stimulation.";
RL   Blood 88:2833-2840(1996).
RN   [15]
RP   PHOSPHORYLATION AT TYR-349 AND TYR-350.
RX   PubMed=8939605; DOI=10.1016/s0960-9822(96)00748-8;
RA   van der Geer P., Wiley S., Gish G.D., Pawson T.;
RT   "The Shc adaptor protein is highly phosphorylated at conserved, twin
RT   tyrosine residues (Y239/240) that mediate protein-protein interactions.";
RL   Curr. Biol. 6:1435-1444(1996).
RN   [16]
RP   INTERACTION WITH GRB7.
RX   PubMed=8940081; DOI=10.1074/jbc.271.48.30942;
RA   Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.;
RT   "Grb7 is a downstream signaling component of platelet-derived growth factor
RT   alpha- and beta-receptors.";
RL   J. Biol. Chem. 271:30942-30949(1996).
RN   [17]
RP   INTERACTION WITH KIT.
RX   PubMed=9038210; DOI=10.1074/jbc.272.9.5915;
RA   Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.;
RT   "Direct association of Csk homologous kinase (CHK) with the
RT   diphosphorylated site Tyr568/570 of the activated c-KIT in
RT   megakaryocytes.";
RL   J. Biol. Chem. 272:5915-5920(1997).
RN   [18]
RP   PHOSPHORYLATION.
RX   PubMed=9148935; DOI=10.1074/jbc.272.20.13189;
RA   Schlaepfer D.D., Hunter T.;
RT   "Focal adhesion kinase overexpression enhances ras-dependent integrin
RT   signaling to ERK2/mitogen-activated protein kinase through interactions
RT   with and activation of c-Src.";
RL   J. Biol. Chem. 272:13189-13195(1997).
RN   [19]
RP   PHOSPHORYLATION AT TYR-349; TYR-350 AND TYR-427.
RX   PubMed=9121430; DOI=10.1128/mcb.17.4.1824;
RA   Gotoh N., Toyoda M., Shibuya M.;
RT   "Tyrosine phosphorylation sites at amino acids 239 and 240 of Shc are
RT   involved in epidermal growth factor-induced mitogenic signaling that is
RT   distinct from Ras/mitogen-activated protein kinase activation.";
RL   Mol. Cell. Biol. 17:1824-1831(1997).
RN   [20]
RP   INTERACTION WITH SH2B2.
RX   PubMed=9233773; DOI=10.1038/sj.onc.1201163;
RA   Yokouchi M., Suzuki R., Masuhara M., Komiya S., Inoue A., Yoshimura A.;
RT   "Cloning and characterization of APS, an adaptor molecule containing PH and
RT   SH2 domains that is tyrosine phosphorylated upon B-cell receptor
RT   stimulation.";
RL   Oncogene 15:7-15(1997).
RN   [21]
RP   INTERACTION WITH INPP5D AND INPPL1.
RX   PubMed=9660833; DOI=10.1074/jbc.273.29.18605;
RA   Habib T., Hejna J.A., Moses R.E., Decker S.J.;
RT   "Growth factors and insulin stimulate tyrosine phosphorylation of the
RT   51C/SHIP2 protein.";
RL   J. Biol. Chem. 273:18605-18609(1998).
RN   [22]
RP   PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2, MUTAGENESIS OF TYR-349 AND
RP   TYR-427, AND INTERACTION WITH GRB2.
RX   PubMed=9488479; DOI=10.1128/mcb.18.3.1622;
RA   Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.;
RT   "Epidermal growth factor receptor and the adaptor protein p52Shc are
RT   specific substrates of T-cell protein tyrosine phosphatase.";
RL   Mol. Cell. Biol. 18:1622-1634(1998).
RN   [23]
RP   PHOSPHORYLATION AT TYR-349; TYR-350 AND TYR-427.
RX   PubMed=9566877; DOI=10.1128/mcb.18.5.2571;
RA   Schlaepfer D.D., Jones K.C., Hunter T.;
RT   "Multiple Grb2-mediated integrin-stimulated signaling pathways to
RT   ERK2/mitogen-activated protein kinase: summation of both c-Src- and focal
RT   adhesion kinase-initiated tyrosine phosphorylation events.";
RL   Mol. Cell. Biol. 18:2571-2585(1998).
RN   [24]
RP   INTERACTION WITH INPPL1.
RX   PubMed=10194451;
RA   Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H., Geromanos S.,
RA   Kavanaugh W.M., Tempst P., Clarkson B.;
RT   "A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-
RT   phosphatase (SHIP2) is constitutively tyrosine phosphorylated and
RT   associated with src homologous and collagen gene (SHC) in chronic
RT   myelogenous leukemia progenitor cells.";
RL   Blood 93:2707-2720(1999).
RN   [25]
RP   INTERACTION WITH ERBB4.
RX   PubMed=10867024; DOI=10.1074/jbc.c901015199;
RA   Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C.,
RA   Carraway K.L. III;
RT   "Ligand discrimination in signaling through an ErbB4 receptor homodimer.";
RL   J. Biol. Chem. 275:19803-19807(2000).
RN   [26]
RP   INTERACTION WITH INPPL1.
RX   PubMed=11349134; DOI=10.1074/jbc.m103537200;
RA   Pesesse X., Dewaste V., De Smedt F., Laffargue M., Giuriato S., Moreau C.,
RA   Payrastre B., Erneux C.;
RT   "The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is
RT   recruited to the epidermal growth factor (EGF) receptor and
RT   dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated
RT   COS-7 cells.";
RL   J. Biol. Chem. 276:28348-28355(2001).
RN   [27]
RP   INTERACTION WITH PTK2/FAK1, AND PHOSPHORYLATION.
RX   PubMed=11980671;
RA   Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr., Gladson C.L.;
RT   "Focal adhesion kinase enhances signaling through the Shc/extracellular
RT   signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy
RT   samples.";
RL   Cancer Res. 62:2699-2707(2002).
RN   [28]
RP   ALTERNATIVE PROMOTER USAGE.
RX   PubMed=11948181; DOI=10.1074/jbc.m200280200;
RA   Ventura A., Luzi L., Pacini S., Baldari C.T., Pelicci P.-G.;
RT   "The p66Shc longevity gene is silenced through epigenetic modifications of
RT   an alternative promoter.";
RL   J. Biol. Chem. 277:22370-22376(2002).
RN   [29]
RP   INTERACTION WITH EPHB1 AND GRB2.
RX   PubMed=12925710; DOI=10.1083/jcb.200302073;
RA   Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.;
RT   "EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote
RT   chemotaxis.";
RL   J. Cell Biol. 162:661-671(2003).
RN   [30]
RP   INTERACTION WITH NTRK1.
RX   PubMed=15488758; DOI=10.1016/j.ccr.2004.09.011;
RA   Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A.,
RA   Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A.,
RA   Mackay A.R.;
RT   "TrkA alternative splicing: a regulated tumor-promoting switch in human
RT   neuroblastoma.";
RL   Cancer Cell 6:347-360(2004).
RN   [31]
RP   REVIEW ON ROLE IN KIT SIGNALING, AND PHOSPHORYLATION.
RX   PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
RA   Ronnstrand L.;
RT   "Signal transduction via the stem cell factor receptor/c-Kit.";
RL   Cell. Mol. Life Sci. 61:2535-2548(2004).
RN   [32]
RP   FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH TEK.
RX   PubMed=14665640; DOI=10.1074/jbc.m307456200;
RA   Audero E., Cascone I., Maniero F., Napione L., Arese M., Lanfrancone L.,
RA   Bussolino F.;
RT   "Adaptor ShcA protein binds tyrosine kinase Tie2 receptor and regulates
RT   migration and sprouting but not survival of endothelial cells.";
RL   J. Biol. Chem. 279:13224-13233(2004).
RN   [33]
RP   INTERACTION WITH FLT4.
RX   PubMed=15102829; DOI=10.1074/jbc.m314015200;
RA   Wang J.F., Zhang X., Groopman J.E.;
RT   "Activation of vascular endothelial growth factor receptor-3 and its
RT   downstream signaling promote cell survival under oxidative stress.";
RL   J. Biol. Chem. 279:27088-27097(2004).
RN   [34]
RP   INTERACTION WITH IRS4.
RX   PubMed=15316024; DOI=10.1074/jbc.m404537200;
RA   Hinsby A.M., Olsen J.V., Mann M.;
RT   "Tyrosine phosphoproteomics of fibroblast growth factor signaling: a role
RT   for insulin receptor substrate-4.";
RL   J. Biol. Chem. 279:46438-46447(2004).
RN   [35]
RP   SUBCELLULAR LOCATION (ISOFORM P46SHC).
RX   PubMed=14573619; DOI=10.1074/jbc.m307655200;
RA   Ventura A., Maccarana M., Raker V.A., Pelicci P.-G.;
RT   "A cryptic targeting signal induces isoform-specific localization of p46Shc
RT   to mitochondria.";
RL   J. Biol. Chem. 279:2299-2306(2004).
RN   [36]
RP   INTERACTION WITH LRP1.
RX   PubMed=15272003; DOI=10.1074/jbc.m407592200;
RA   Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F., Peltan I.D.,
RA   Mikhailenko I., Hyman B.T., Strickland D.K.;
RT   "Serine and threonine phosphorylation of the low density lipoprotein
RT   receptor-related protein by protein kinase Calpha regulates endocytosis and
RT   association with adaptor molecules.";
RL   J. Biol. Chem. 279:40536-40544(2004).
RN   [37]
RP   PHOSPHORYLATION AT SER-36.
RX   PubMed=15837797; DOI=10.1083/jcb.200410041;
RA   Smith W.W., Norton D.D., Gorospe M., Jiang H., Nemoto S., Holbrook N.J.,
RA   Finkel T., Kusiak J.W.;
RT   "Phosphorylation of p66Shc and forkhead proteins mediates Abeta toxicity.";
RL   J. Cell Biol. 169:331-339(2005).
RN   [38]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [39]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [40]
RP   INTERACTION WITH ALK, AND PHOSPHORYLATION.
RX   PubMed=17274988; DOI=10.1016/j.febslet.2007.01.039;
RA   Degoutin J., Vigny M., Gouzi J.Y.;
RT   "ALK activation induces Shc and FRS2 recruitment: Signaling and phenotypic
RT   outcomes in PC12 cells differentiation.";
RL   FEBS Lett. 581:727-734(2007).
RN   [41]
RP   INTERACTION WITH GAB2.
RX   PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA   Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA   Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M.,
RA   James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the
RT   Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [42]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND TYR-427, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [43]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [44]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-427, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [45]
RP   INTERACTION WITH CPNE3.
RX   PubMed=20010870; DOI=10.1038/onc.2009.456;
RA   Heinrich C., Keller C., Boulay A., Vecchi M., Bianchi M., Sack R.,
RA   Lienhard S., Duss S., Hofsteenge J., Hynes N.E.;
RT   "Copine-III interacts with ErbB2 and promotes tumor cell migration.";
RL   Oncogene 29:1598-1610(2010).
RN   [46]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [47]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [48]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [49]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, ACETYLATION [LARGE SCALE
RP   ANALYSIS] AT MET-1 (ISOFORMS 7 AND P52SHC), AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [50]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139; TYR-427 AND SER-453, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [51]
RP   INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL46 (MICROBIAL INFECTION).
RX   PubMed=23946459; DOI=10.1128/jvi.01702-13;
RA   Strunk U., Saffran H.A., Wu F.W., Smiley J.R.;
RT   "Role of herpes simplex virus VP11/12 tyrosine-based motifs in binding and
RT   activation of the Src family kinase Lck and recruitment of p85, Grb2, and
RT   Shc.";
RL   J. Virol. 87:11276-11286(2013).
RN   [52]
RP   INTERACTION WITH PEAK1, INTERACTION WITH PPP1CA, PPP1CC AND PEAK1, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23846654; DOI=10.1038/nature12308;
RA   Zheng Y., Zhang C., Croucher D.R., Soliman M.A., St-Denis N.,
RA   Pasculescu A., Taylor L., Tate S.A., Hardy W.R., Colwill K., Dai A.Y.,
RA   Bagshaw R., Dennis J.W., Gingras A.C., Daly R.J., Pawson T.;
RT   "Temporal regulation of EGF signalling networks by the scaffold protein
RT   Shc1.";
RL   Nature 499:166-171(2013).
RN   [53]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [54]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 482-583.
RX   PubMed=7473762; DOI=10.1006/jmbi.1995.0601;
RA   Mikol V., Baumann G., Zurini M.G.M., Hommel U.;
RT   "Crystal structure of the SH2 domain from the adaptor protein SHC: a model
RT   for peptide binding based on X-ray and NMR data.";
RL   J. Mol. Biol. 254:86-95(1995).
RN   [55]
RP   STRUCTURE BY NMR OF 127-317.
RX   PubMed=8524391; DOI=10.1038/378584a0;
RA   Zhou M.-M., Ravichandran K.S., Olejniczak E.F., Petros A.M., Meadows R.P.,
RA   Sattler M., Harlan J.E., Wade W.S., Burakoff S.J., Fesik S.W.;
RT   "Structure and ligand recognition of the phosphotyrosine binding domain of
RT   Shc.";
RL   Nature 378:584-592(1995).
RN   [56]
RP   STRUCTURE BY NMR OF 480-583 IN COMPLEX WITH TYROSINE-PHOSPHORYLATED CD3Z.
RX   PubMed=7544002; DOI=10.1073/pnas.92.17.7784;
RA   Zhou M.-M., Meadows R.P., Logan T.M., Yoon H.S., Wade W.S.,
RA   Ravichandran K.S., Burakoff S.J., Fesik S.W.;
RT   "Solution structure of the Shc SH2 domain complexed with a tyrosine-
RT   phosphorylated peptide from the T-cell receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7784-7788(1995).
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. Isoform p46Shc and isoform
CC       p52Shc, once phosphorylated, couple activated receptor tyrosine kinases
CC       to Ras via the recruitment of the GRB2/SOS complex and are implicated
CC       in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and
CC       isoform p52Shc may thus function as initiators of the Ras signaling
CC       cascade in various non-neuronal systems. Isoform p66Shc does not
CC       mediate Ras activation, but is involved in signal transduction pathways
CC       that regulate the cellular response to oxidative stress and life span.
CC       Isoform p66Shc acts as a downstream target of the tumor suppressor p53
CC       and is indispensable for the ability of stress-activated p53 to induce
CC       elevation of intracellular oxidants, cytochrome c release and
CC       apoptosis. The expression of isoform p66Shc has been correlated with
CC       life span (By similarity). Participates in signaling downstream of the
CC       angiopoietin receptor TEK/TIE2, and plays a role in the regulation of
CC       endothelial cell migration and sprouting angiogenesis. {ECO:0000250,
CC       ECO:0000269|PubMed:14665640}.
CC   -!- SUBUNIT: Interacts with CPNE3; this interaction may mediate the binding
CC       of CPNE3 with ERBB2 (PubMed:20010870). Interacts with the NPXY motif of
CC       tyrosine-phosphorylated IGF1R and INSR in vitro via the PID domain.
CC       Once activated, binds to GRB2. Interacts with tyrosine-phosphorylated
CC       CD3T and DDR2. Interacts with the N-terminal region of SH2B2. Interacts
CC       with phosphorylated LRP1 and IRS4. Interacts with INPP5D/SHIP1 and
CC       INPPL1/SHIP2. Interacts with TRIM31. Interacts with PTPN6/SHP (tyrosine
CC       phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2,
CC       PLCG1, FRS2, SRC, SHC1, GAP43 and CTT (By similarity). Interacts with
CC       ALK, GAB2, GRB7 and KIT. Interacts with FLT4 (tyrosine-phosphorylated).
CC       Interacts with EPHB1 and GRB2; activates the MAPK/ERK cascade to
CC       regulate cell migration. Interacts with PDGFRB (tyrosine-
CC       phosphorylated). Interacts with ERBB4. Interacts with TEK/TIE2
CC       (tyrosine-phosphorylated). Interacts with the Trk receptors NTRK1,
CC       NTRK2 and NTRK3; in a phosphotyrosine-dependent manner. Interacts with
CC       PTK2/FAK1. Interacts with CEACAM1; this interaction is CEACAM1-
CC       phosphorylation-dependent and mediates interaction with EGFR or INSR
CC       resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2
CC       pathway (By similarity). Interacts (via PID domain) with PEAK1 (when
CC       phosphorylated at 'Tyr-1188') (PubMed:23846654). Found in a complex
CC       with PPP1CA, PPP1CC, SHC1 and PEAK1 (PubMed:23846654).
CC       {ECO:0000250|UniProtKB:P98083, ECO:0000250|UniProtKB:Q5M824,
CC       ECO:0000269|PubMed:10194451, ECO:0000269|PubMed:10867024,
CC       ECO:0000269|PubMed:11349134, ECO:0000269|PubMed:11980671,
CC       ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:14665640,
CC       ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:15272003,
CC       ECO:0000269|PubMed:15316024, ECO:0000269|PubMed:15488758,
CC       ECO:0000269|PubMed:17274988, ECO:0000269|PubMed:19172738,
CC       ECO:0000269|PubMed:20010870, ECO:0000269|PubMed:23846654,
CC       ECO:0000269|PubMed:7537849, ECO:0000269|PubMed:7541045,
CC       ECO:0000269|PubMed:7544002, ECO:0000269|PubMed:7559478,
CC       ECO:0000269|PubMed:8155326, ECO:0000269|PubMed:8195171,
CC       ECO:0000269|PubMed:8874179, ECO:0000269|PubMed:8940081,
CC       ECO:0000269|PubMed:9038210, ECO:0000269|PubMed:9233773,
CC       ECO:0000269|PubMed:9488479, ECO:0000269|PubMed:9660833}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1
CC       UL46. {ECO:0000269|PubMed:23946459}.
CC   -!- INTERACTION:
CC       P29353; P05067: APP; NbExp=5; IntAct=EBI-78835, EBI-77613;
CC       P29353; P10275: AR; NbExp=14; IntAct=EBI-78835, EBI-608057;
CC       P29353; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-78835, EBI-739580;
CC       P29353; P00533: EGFR; NbExp=34; IntAct=EBI-78835, EBI-297353;
CC       P29353; P04626: ERBB2; NbExp=10; IntAct=EBI-78835, EBI-641062;
CC       P29353; P21860: ERBB3; NbExp=5; IntAct=EBI-78835, EBI-720706;
CC       P29353; Q15303: ERBB4; NbExp=2; IntAct=EBI-78835, EBI-80371;
CC       P29353; P03372-4: ESR1; NbExp=2; IntAct=EBI-78835, EBI-4309277;
CC       P29353; Q13480: GAB1; NbExp=9; IntAct=EBI-78835, EBI-517684;
CC       P29353; P62993: GRB2; NbExp=28; IntAct=EBI-78835, EBI-401755;
CC       P29353; P06213: INSR; NbExp=2; IntAct=EBI-78835, EBI-475899;
CC       P29353; P10721: KIT; NbExp=8; IntAct=EBI-78835, EBI-1379503;
CC       P29353; P08581: MET; NbExp=5; IntAct=EBI-78835, EBI-1039152;
CC       P29353; Q05209: PTPN12; NbExp=8; IntAct=EBI-78835, EBI-2266035;
CC       P29353; Q07889: SOS1; NbExp=2; IntAct=EBI-78835, EBI-297487;
CC       P29353; Q62120: Jak2; Xeno; NbExp=2; IntAct=EBI-78835, EBI-646604;
CC       P29353; P03495: NS; Xeno; NbExp=2; IntAct=EBI-78835, EBI-2548993;
CC       P29353-1; P62993: GRB2; NbExp=3; IntAct=EBI-8160716, EBI-401755;
CC       P29353-2; P08069: IGF1R; NbExp=2; IntAct=EBI-1000553, EBI-475981;
CC       P29353-2; P28482: MAPK1; NbExp=4; IntAct=EBI-1000553, EBI-959949;
CC       P29353-7; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-9691288, EBI-1383687;
CC       P29353-7; P00533: EGFR; NbExp=4; IntAct=EBI-9691288, EBI-297353;
CC       P29353-7; P43405-2: SYK; NbExp=3; IntAct=EBI-9691288, EBI-25892332;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform p46Shc]: Mitochondrion matrix
CC       {ECO:0000269|PubMed:14573619}. Note=Localized to the mitochondria
CC       matrix. Targeting of isoform p46Shc to mitochondria is mediated by its
CC       first 32 amino acids, which behave as a bona fide mitochondrial
CC       targeting sequence. Isoform p52Shc and isoform p66Shc, that contain the
CC       same sequence but more internally located, display a different
CC       subcellular localization.
CC   -!- SUBCELLULAR LOCATION: [Isoform p66Shc]: Mitochondrion {ECO:0000250}.
CC       Note=In case of oxidative conditions, phosphorylation at 'Ser-36' of
CC       isoform p66Shc, leads to mitochondrial accumulation. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC       Name=p66Shc;
CC         IsoId=P29353-1; Sequence=Displayed;
CC       Name=p52Shc;
CC         IsoId=P29353-2; Sequence=VSP_016108;
CC       Name=p46Shc;
CC         IsoId=P29353-3; Sequence=VSP_016107;
CC       Name=5;
CC         IsoId=P29353-5; Sequence=VSP_040090, VSP_040091;
CC       Name=6;
CC         IsoId=P29353-6; Sequence=VSP_040092;
CC       Name=7;
CC         IsoId=P29353-7; Sequence=VSP_016108, VSP_040092;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in neural stem cells
CC       but absent in mature neurons.
CC   -!- DOMAIN: In response to a variety of growth factors, isoform p46Shc and
CC       isoform p52Shc bind to phosphorylated Trk receptors through their
CC       phosphotyrosine binding (PID) and/or SH2 domains. The PID and SH2
CC       domains bind to specific phosphorylated tyrosine residues in the Asn-
CC       Pro-Xaa-Tyr(P) motif of the Trk receptors. Isoform p46Shc and isoform
CC       p52Shc are in turn phosphorylated on three tyrosine residues within the
CC       extended proline-rich domain. These phosphotyrosines act as docking
CC       site for GRB2 and thereby are involved in Ras activation (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated by activated epidermal growth factor receptor.
CC       Phosphorylated in response to FLT4 and KIT signaling. Isoform p46Shc
CC       and isoform p52Shc are phosphorylated on tyrosine residues of the Pro-
CC       rich domain. Isoform p66Shc is phosphorylated on Ser-36 by PRKCB upon
CC       treatment with insulin, hydrogen peroxide or irradiation with
CC       ultraviolet light (By similarity). Tyrosine phosphorylated in response
CC       to FLT3 signaling (By similarity). Tyrosine phosphorylated by activated
CC       PTK2B/PYK2 (By similarity). Tyrosine phosphorylated by ligand-activated
CC       ALK. Tyrosine phosphorylated by ligand-activated PDGFRB. Tyrosine
CC       phosphorylated by TEK/TIE2. May be tyrosine phosphorylated by activated
CC       PTK2/FAK1; tyrosine phosphorylation was seen in an astrocytoma biopsy,
CC       where PTK2/FAK1 kinase activity is high, but not in normal brain
CC       tissue. Isoform p52Shc dephosphorylation by PTPN2 may regulate
CC       interaction with GRB2. {ECO:0000250, ECO:0000269|PubMed:11980671,
CC       ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:15526160,
CC       ECO:0000269|PubMed:15837797, ECO:0000269|PubMed:17274988,
CC       ECO:0000269|PubMed:8195171, ECO:0000269|PubMed:8939605,
CC       ECO:0000269|PubMed:9121430, ECO:0000269|PubMed:9148935,
CC       ECO:0000269|PubMed:9488479, ECO:0000269|PubMed:9566877}.
CC   -!- MISCELLANEOUS: [Isoform p66Shc]: Regulated by epigenetic modifications
CC       of its promoter region.
CC   -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SHC1ID42287ch1q21.html";
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DR   EMBL; X68148; CAA48251.1; -; mRNA.
DR   EMBL; U73377; AAB49972.1; -; mRNA.
DR   EMBL; Y09847; CAA70977.1; -; Genomic_DNA.
DR   EMBL; AK292143; BAF84832.1; -; mRNA.
DR   EMBL; AK315842; BAF98733.1; -; mRNA.
DR   EMBL; AB451255; BAG70069.1; -; mRNA.
DR   EMBL; AB451379; BAG70193.1; -; mRNA.
DR   EMBL; AL451085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53168.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53169.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53170.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53171.1; -; Genomic_DNA.
DR   EMBL; BC014158; AAH14158.1; -; mRNA.
DR   EMBL; BC033925; AAH33925.1; -; mRNA.
DR   CCDS; CCDS1076.1; -. [P29353-7]
DR   CCDS; CCDS30881.1; -. [P29353-1]
DR   CCDS; CCDS44233.1; -. [P29353-6]
DR   CCDS; CCDS44234.1; -. [P29353-2]
DR   PIR; S25776; S25776.
DR   RefSeq; NP_001123512.1; NM_001130040.1. [P29353-6]
DR   RefSeq; NP_001123513.1; NM_001130041.1. [P29353-2]
DR   RefSeq; NP_001189788.1; NM_001202859.1. [P29353-3]
DR   RefSeq; NP_003020.2; NM_003029.4. [P29353-7]
DR   RefSeq; NP_892113.4; NM_183001.4. [P29353-1]
DR   PDB; 1MIL; X-ray; 2.70 A; A=482-583.
DR   PDB; 1N3H; NMR; -; A=111-317.
DR   PDB; 1OY2; NMR; -; A=111-317.
DR   PDB; 1QG1; NMR; -; I=423-435.
DR   PDB; 1SHC; NMR; -; A=127-317.
DR   PDB; 1TCE; NMR; -; A=480-583.
DR   PDB; 2L1C; NMR; -; A=127-317.
DR   PDB; 4JMH; X-ray; 2.41 A; B=344-356.
DR   PDB; 4XWX; X-ray; 1.87 A; A=147-311.
DR   PDB; 5CZI; X-ray; 2.60 A; B=345-353.
DR   PDB; 6DM4; X-ray; 1.90 A; E/G/H=425-431.
DR   PDBsum; 1MIL; -.
DR   PDBsum; 1N3H; -.
DR   PDBsum; 1OY2; -.
DR   PDBsum; 1QG1; -.
DR   PDBsum; 1SHC; -.
DR   PDBsum; 1TCE; -.
DR   PDBsum; 2L1C; -.
DR   PDBsum; 4JMH; -.
DR   PDBsum; 4XWX; -.
DR   PDBsum; 5CZI; -.
DR   PDBsum; 6DM4; -.
DR   AlphaFoldDB; P29353; -.
DR   BMRB; P29353; -.
DR   SMR; P29353; -.
DR   BioGRID; 112361; 333.
DR   CORUM; P29353; -.
DR   DIP; DIP-699N; -.
DR   ELM; P29353; -.
DR   IntAct; P29353; 160.
DR   MINT; P29353; -.
DR   STRING; 9606.ENSP00000401303; -.
DR   BindingDB; P29353; -.
DR   ChEMBL; CHEMBL5626; -.
DR   GlyGen; P29353; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P29353; -.
DR   PhosphoSitePlus; P29353; -.
DR   BioMuta; SHC1; -.
DR   DMDM; 182676455; -.
DR   CPTAC; CPTAC-1366; -.
DR   CPTAC; CPTAC-1559; -.
DR   EPD; P29353; -.
DR   jPOST; P29353; -.
DR   MassIVE; P29353; -.
DR   MaxQB; P29353; -.
DR   PaxDb; P29353; -.
DR   PeptideAtlas; P29353; -.
DR   PRIDE; P29353; -.
DR   ProteomicsDB; 54546; -. [P29353-1]
DR   ProteomicsDB; 54547; -. [P29353-2]
DR   ProteomicsDB; 54548; -. [P29353-3]
DR   ProteomicsDB; 54549; -. [P29353-5]
DR   ProteomicsDB; 54550; -. [P29353-6]
DR   ProteomicsDB; 54551; -. [P29353-7]
DR   ABCD; P29353; 9 sequenced antibodies.
DR   Antibodypedia; 731; 1210 antibodies from 45 providers.
DR   DNASU; 6464; -.
DR   Ensembl; ENST00000368445.9; ENSP00000357430.5; ENSG00000160691.19. [P29353-1]
DR   Ensembl; ENST00000368450.5; ENSP00000357435.1; ENSG00000160691.19. [P29353-2]
DR   Ensembl; ENST00000368453.8; ENSP00000357438.4; ENSG00000160691.19. [P29353-7]
DR   Ensembl; ENST00000448116.7; ENSP00000401303.3; ENSG00000160691.19. [P29353-6]
DR   GeneID; 6464; -.
DR   KEGG; hsa:6464; -.
DR   MANE-Select; ENST00000448116.7; ENSP00000401303.3; NM_001130040.2; NP_001123512.1. [P29353-6]
DR   UCSC; uc001ffv.4; human. [P29353-1]
DR   CTD; 6464; -.
DR   DisGeNET; 6464; -.
DR   GeneCards; SHC1; -.
DR   HGNC; HGNC:10840; SHC1.
DR   HPA; ENSG00000160691; Low tissue specificity.
DR   MIM; 600560; gene.
DR   neXtProt; NX_P29353; -.
DR   OpenTargets; ENSG00000160691; -.
DR   PharmGKB; PA35746; -.
DR   VEuPathDB; HostDB:ENSG00000160691; -.
DR   eggNOG; KOG3697; Eukaryota.
DR   GeneTree; ENSGT00950000182870; -.
DR   HOGENOM; CLU_029532_2_0_1; -.
DR   InParanoid; P29353; -.
DR   OMA; FFPRMSS; -.
DR   OrthoDB; 1351843at2759; -.
DR   PhylomeDB; P29353; -.
DR   TreeFam; TF315807; -.
DR   PathwayCommons; P29353; -.
DR   Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
DR   Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
DR   Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
DR   Reactome; R-HSA-167044; Signalling to RAS.
DR   Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
DR   Reactome; R-HSA-201556; Signaling by ALK.
DR   Reactome; R-HSA-210993; Tie2 Signaling.
DR   Reactome; R-HSA-2424491; DAP12 signaling. [P29353-2]
DR   Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
DR   Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization. [P29353-2]
DR   Reactome; R-HSA-2871796; FCERI mediated MAPK activation. [P29353-2]
DR   Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization. [P29353-2]
DR   Reactome; R-HSA-354192; Integrin signaling.
DR   Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR   Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR   Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
DR   Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
DR   Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
DR   Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
DR   Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-74749; Signal attenuation.
DR   Reactome; R-HSA-74751; Insulin receptor signalling cascade.
DR   Reactome; R-HSA-8851805; MET activates RAS signaling. [P29353-2]
DR   Reactome; R-HSA-8853659; RET signaling.
DR   Reactome; R-HSA-8983432; Interleukin-15 signaling.
DR   Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-HSA-9020558; Interleukin-2 signaling.
DR   Reactome; R-HSA-9026519; Activated NTRK2 signals through RAS.
DR   Reactome; R-HSA-9027284; Erythropoietin activates RAS.
DR   Reactome; R-HSA-9034864; Activated NTRK3 signals through RAS.
DR   Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR   Reactome; R-HSA-9634285; Constitutive Signaling by Overexpressed ERBB2.
DR   Reactome; R-HSA-9634597; GPER1 signaling.
DR   Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR   Reactome; R-HSA-9665348; Signaling by ERBB2 ECD mutants.
DR   Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR   Reactome; R-HSA-9674555; Signaling by CSF3 (G-CSF).
DR   Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR   SignaLink; P29353; -.
DR   SIGNOR; P29353; -.
DR   BioGRID-ORCS; 6464; 49 hits in 1074 CRISPR screens.
DR   ChiTaRS; SHC1; human.
DR   EvolutionaryTrace; P29353; -.
DR   GeneWiki; SHC1; -.
DR   GenomeRNAi; 6464; -.
DR   Pharos; P29353; Tchem.
DR   PRO; PR:P29353; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P29353; protein.
DR   Bgee; ENSG00000160691; Expressed in stromal cell of endometrium and 204 other tissues.
DR   ExpressionAtlas; P29353; baseline and differential.
DR   Genevisible; P29353; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0070435; C:Shc-EGFR complex; ISS:BHF-UCL.
DR   GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR   GO; GO:0048408; F:epidermal growth factor binding; IEA:Ensembl.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:BHF-UCL.
DR   GO; GO:0005158; F:insulin receptor binding; IPI:UniProtKB.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:UniProtKB.
DR   GO; GO:0005168; F:neurotrophin TRKA receptor binding; IPI:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; TAS:UniProtKB.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
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:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; TAS:UniProtKB.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:CAFA.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IGI:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CAFA.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CAFA.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:BHF-UCL.
DR   GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IGI:BHF-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:CAFA.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
DR   GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; TAS:ProtInc.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0090322; P:regulation of superoxide metabolic process; IGI:BHF-UCL.
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   DisProt; DP00154; -.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   IDEAL; IID00511; -.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative promoter usage;
KW   Alternative splicing; Angiogenesis; Cytoplasm; Growth regulation;
KW   Host-virus interaction; Mitochondrion; Phosphoprotein; Reference proteome;
KW   SH2 domain.
FT   CHAIN           1..583
FT                   /note="SHC-transforming protein 1"
FT                   /id="PRO_0000097731"
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          340..487
FT                   /note="CH1"
FT   REGION          372..415
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:0007744|PubMed:22814378"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:15837797"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         154
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P98083"
FT   MOD_RES         349
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:8939605,
FT                   ECO:0000269|PubMed:9121430, ECO:0000269|PubMed:9566877"
FT   MOD_RES         350
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:8939605,
FT                   ECO:0000269|PubMed:9121430, ECO:0000269|PubMed:9566877"
FT   MOD_RES         427
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:9121430,
FT                   ECO:0000269|PubMed:9566877, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..214
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_040090"
FT   VAR_SEQ         1..155
FT                   /note="Missing (in isoform p46Shc)"
FT                   /evidence="ECO:0000303|PubMed:1623525"
FT                   /id="VSP_016107"
FT   VAR_SEQ         1..110
FT                   /note="Missing (in isoform p52Shc and isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1623525"
FT                   /id="VSP_016108"
FT   VAR_SEQ         215..221
FT                   /note="PLSSILG -> MSLCHRW (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_040091"
FT   VAR_SEQ         417
FT                   /note="P -> PA (in isoform 7 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:19054851"
FT                   /id="VSP_040092"
FT   VARIANT         205
FT                   /note="A -> V (in dbSNP:rs8191981)"
FT                   /id="VAR_042428"
FT   VARIANT         410
FT                   /note="M -> V (in dbSNP:rs8191979)"
FT                   /id="VAR_051353"
FT   MUTAGEN         349
FT                   /note="Y->F: Alters interaction with GRB2; isoform p52Shc
FT                   (in vitro)."
FT                   /evidence="ECO:0000269|PubMed:9488479"
FT   MUTAGEN         427
FT                   /note="Y->F: No effect on interaction with GRB2; isoform
FT                   p52Shc (in vitro)."
FT                   /evidence="ECO:0000269|PubMed:9488479"
FT   CONFLICT        2
FT                   /note="D -> N (in Ref. 3; CAA70977)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="L -> M (in Ref. 3; CAA70977)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        38
FT                   /note="S -> P (in Ref. 3; CAA70977)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="V -> D (in Ref. 2; AAB49972)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="D -> E (in Ref. 2; AAB49972)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        430
FT                   /note="V -> A (in Ref. 5; BAG70069/BAG70193)"
FT                   /evidence="ECO:0000305"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:1N3H"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:1SHC"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:1N3H"
FT   HELIX           152..156
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   STRAND          160..172
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   HELIX           181..198
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:1OY2"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:1SHC"
FT   TURN            215..219
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   TURN            226..229
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   STRAND          230..236
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   STRAND          238..245
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   TURN            246..249
FT                   /evidence="ECO:0007829|PDB:1N3H"
FT   STRAND          251..256
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   STRAND          262..265
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   HELIX           268..270
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   STRAND          273..280
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   TURN            281..283
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   STRAND          284..291
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:1N3H"
FT   HELIX           296..310
FT                   /evidence="ECO:0007829|PDB:4XWX"
FT   STRAND          311..314
FT                   /evidence="ECO:0007829|PDB:1N3H"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:5CZI"
FT   TURN            483..485
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   STRAND          487..489
FT                   /evidence="ECO:0007829|PDB:1TCE"
FT   HELIX           495..499
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   STRAND          507..512
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   STRAND          514..516
FT                   /evidence="ECO:0007829|PDB:1TCE"
FT   STRAND          518..526
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   STRAND          529..536
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   STRAND          540..543
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   STRAND          548..551
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   HELIX           552..562
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   STRAND          566..568
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   STRAND          571..573
FT                   /evidence="ECO:0007829|PDB:1MIL"
FT   MOD_RES         P29353-2:1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         P29353-7:1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   583 AA;  62822 MW;  7EFA5CB185A548D1 CRC64;
     MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP GDDSPTTLCS
     FFPRMSNLRL ANPAGGRPGS KGEPGRAADD GEGIVGAAMP DSGPLPLLQD 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 GAAPGAARPT APNAQTPSHL GATLPVGQPV GGDPEVRKQM PPPPPCPGRE
     LFDDPSYVNV QNLDKARQAV GGAGPPNPAI NGSAPRDLFD MKPFEDALRV PPPPQSVSMA
     EQLRGEPWFH GKLSRREAEA LLQLNGDFLV RESTTTPGQY VLTGLQSGQP KHLLLVDPEG
     VVRTKDHRFE SVSHLISYHM DNHLPIISAG SELCLQQPVE RKL
 
 
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