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SHC-transforming protein 1 (SHC-transforming protein 3) (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)

 SHC1_HUMAN              Reviewed;         583 AA.
P29353; B5BU19; D3DV78; O15290; Q5T180; Q5T183; Q5T184; Q5T185;
Q5T186; Q8N4K5; Q96CL1;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
08-APR-2008, sequence version 4.
30-AUG-2017, entry version 209.
RecName: Full=SHC-transforming protein 1;
AltName: Full=SHC-transforming protein 3;
AltName: Full=SHC-transforming protein A;
AltName: Full=Src homology 2 domain-containing-transforming protein C1;
Short=SH2 domain protein C1;
Name=SHC1; Synonyms=SHC, SHCA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P46SHC AND P52SHC).
PubMed=1623525; DOI=10.1016/0092-8674(92)90536-L;
Pelicci G., Lanfrancone L., Grignani F., McGlade J., Cavallo F.,
Forni G., Nicoletti I., Grignani F., Pawson T., Pelicci P.-G.;
"A novel transforming protein (SHC) with an SH2 domain is implicated
in mitogenic signal transduction.";
Cell 70:93-104(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P66SHC).
PubMed=9049300; DOI=10.1093/emboj/16.4.706;
Migliaccio E., Mele S., Salcini A.E., Pelicci G., Lai K.M.,
Superti-Furga G., Pawson T., Di Fiore P.P., Lanfrancone L.,
Pelicci P.-G.;
"Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on
the EGF receptor-MAP kinase-fos signalling pathway.";
EMBO J. 16:706-716(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Fibroblast;
PubMed=9192859; DOI=10.1006/geno.1997.4728;
Harun R.B., Smith K.K., Leek J.P., Markham A.F., Norris A.,
Morrison J.F.;
"Characterization of human SHC p66 cDNA and its processed pseudogene
mapping to Xq12-q13.1.";
Genomics 42:349-352(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P52SHC).
TISSUE=Mammary gland, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P52SHC AND 7).
TISSUE=Choriocarcinoma, and Neuroblastoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH PDGFRB AND GRB2, AND PHOSPHORYLATION.
PubMed=8195171;
Yokote K., Mori S., Hansen K., McGlade J., Pawson T., Heldin C.H.,
Claesson-Welsh L.;
"Direct interaction between Shc and the platelet-derived growth factor
beta-receptor.";
J. Biol. Chem. 269:15337-15343(1994).
[10]
INTERACTION WITH NTRK1.
PubMed=8155326; DOI=10.1016/0896-6273(94)90223-2;
Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A.,
Kaplan D.R.;
"Trk receptors use redundant signal transduction pathways involving
SHC and PLC-gamma 1 to mediate NGF responses.";
Neuron 12:691-705(1994).
[11]
INTERACTION WITH IGF1R.
PubMed=7541045; DOI=10.1074/jbc.270.26.15639;
Craparo A., O'Neill T.J., Gustafson T.A.;
"Non-SH2 domains within insulin receptor substrate-1 and SHC mediate
their phosphotyrosine-dependent interaction with the NPEY motif of the
insulin-like growth factor I receptor.";
J. Biol. Chem. 270:15639-15643(1995).
[12]
INTERACTION WITH INSR.
PubMed=7559478; DOI=10.1074/jbc.270.40.23258;
He W., O'Neill T.J., Gustafson T.A.;
"Distinct modes of interaction of SHC and insulin receptor substrate-1
with the insulin receptor NPEY region via non-SH2 domains.";
J. Biol. Chem. 270:23258-23262(1995).
[13]
INTERACTION WITH INSR.
PubMed=7537849; DOI=10.1128/MCB.15.5.2500;
Gustafson T.A., He W., Craparo A., Schaub C.D., O'Neill T.J.;
"Phosphotyrosine-dependent interaction of SHC and insulin receptor
substrate 1 with the NPEY motif of the insulin receptor via a novel
non-SH2 domain.";
Mol. Cell. Biol. 15:2500-2508(1995).
[14]
INTERACTION WITH INPP5D.
PubMed=8874179;
Ware M.D., Rosten P., Damen J.E., Liu L., Humphries R.K., Krystal G.;
"Cloning and characterization of human SHIP, the 145-kD inositol 5-
phosphatase that associates with SHC after cytokine stimulation.";
Blood 88:2833-2840(1996).
[15]
PHOSPHORYLATION AT TYR-349 AND TYR-350.
PubMed=8939605; DOI=10.1016/S0960-9822(96)00748-8;
van der Geer P., Wiley S., Gish G.D., Pawson T.;
"The Shc adaptor protein is highly phosphorylated at conserved, twin
tyrosine residues (Y239/240) that mediate protein-protein
interactions.";
Curr. Biol. 6:1435-1444(1996).
[16]
INTERACTION WITH GRB7.
PubMed=8940081; DOI=10.1074/jbc.271.48.30942;
Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.;
"Grb7 is a downstream signaling component of platelet-derived growth
factor alpha- and beta-receptors.";
J. Biol. Chem. 271:30942-30949(1996).
[17]
INTERACTION WITH KIT.
PubMed=9038210; DOI=10.1074/jbc.272.9.5915;
Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.;
"Direct association of Csk homologous kinase (CHK) with the
diphosphorylated site Tyr568/570 of the activated c-KIT in
megakaryocytes.";
J. Biol. Chem. 272:5915-5920(1997).
[18]
PHOSPHORYLATION.
PubMed=9148935; DOI=10.1074/jbc.272.20.13189;
Schlaepfer D.D., Hunter T.;
"Focal adhesion kinase overexpression enhances ras-dependent integrin
signaling to ERK2/mitogen-activated protein kinase through
interactions with and activation of c-Src.";
J. Biol. Chem. 272:13189-13195(1997).
[19]
PHOSPHORYLATION AT TYR-349; TYR-350 AND TYR-427.
PubMed=9121430; DOI=10.1128/MCB.17.4.1824;
Gotoh N., Toyoda M., Shibuya M.;
"Tyrosine phosphorylation sites at amino acids 239 and 240 of Shc are
involved in epidermal growth factor-induced mitogenic signaling that
is distinct from Ras/mitogen-activated protein kinase activation.";
Mol. Cell. Biol. 17:1824-1831(1997).
[20]
INTERACTION WITH APS.
PubMed=9233773; DOI=10.1038/sj.onc.1201163;
Yokouchi M., Suzuki R., Masuhara M., Komiya S., Inoue A.,
Yoshimura A.;
"Cloning and characterization of APS, an adaptor molecule containing
PH and SH2 domains that is tyrosine phosphorylated upon B-cell
receptor stimulation.";
Oncogene 15:7-15(1997).
[21]
INTERACTION WITH INPP5D AND INPPL1.
PubMed=9660833; DOI=10.1074/jbc.273.29.18605;
Habib T., Hejna J.A., Moses R.E., Decker S.J.;
"Growth factors and insulin stimulate tyrosine phosphorylation of the
51C/SHIP2 protein.";
J. Biol. Chem. 273:18605-18609(1998).
[22]
PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2, MUTAGENESIS OF TYR-349
AND TYR-427, AND INTERACTION WITH GRB2.
PubMed=9488479; DOI=10.1128/MCB.18.3.1622;
Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.;
"Epidermal growth factor receptor and the adaptor protein p52Shc are
specific substrates of T-cell protein tyrosine phosphatase.";
Mol. Cell. Biol. 18:1622-1634(1998).
[23]
PHOSPHORYLATION AT TYR-349; TYR-350 AND TYR-427.
PubMed=9566877; DOI=10.1128/MCB.18.5.2571;
Schlaepfer D.D., Jones K.C., Hunter T.;
"Multiple Grb2-mediated integrin-stimulated signaling pathways to
ERK2/mitogen-activated protein kinase: summation of both c-Src- and
focal adhesion kinase-initiated tyrosine phosphorylation events.";
Mol. Cell. Biol. 18:2571-2585(1998).
[24]
INTERACTION WITH INPPL1.
PubMed=10194451;
Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H.,
Geromanos S., Kavanaugh W.M., Tempst P., Clarkson B.;
"A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-
phosphatase (SHIP2) is constitutively tyrosine phosphorylated and
associated with src homologous and collagen gene (SHC) in chronic
myelogenous leukemia progenitor cells.";
Blood 93:2707-2720(1999).
[25]
INTERACTION WITH ERBB4.
PubMed=10867024; DOI=10.1074/jbc.C901015199;
Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C.,
Carraway K.L. III;
"Ligand discrimination in signaling through an ErbB4 receptor
homodimer.";
J. Biol. Chem. 275:19803-19807(2000).
[26]
INTERACTION WITH INPPL1.
PubMed=11349134; DOI=10.1074/jbc.M103537200;
Pesesse X., Dewaste V., De Smedt F., Laffargue M., Giuriato S.,
Moreau C., Payrastre B., Erneux C.;
"The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is
recruited to the epidermal growth factor (EGF) receptor and
dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-
stimulated COS-7 cells.";
J. Biol. Chem. 276:28348-28355(2001).
[27]
INTERACTION WITH PTK2/FAK1, AND PHOSPHORYLATION.
PubMed=11980671;
Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr.,
Gladson C.L.;
"Focal adhesion kinase enhances signaling through the
Shc/extracellular signal-regulated kinase pathway in anaplastic
astrocytoma tumor biopsy samples.";
Cancer Res. 62:2699-2707(2002).
[28]
ALTERNATIVE PROMOTER USAGE.
PubMed=11948181; DOI=10.1074/jbc.M200280200;
Ventura A., Luzi L., Pacini S., Baldari C.T., Pelicci P.-G.;
"The p66Shc longevity gene is silenced through epigenetic
modifications of an alternative promoter.";
J. Biol. Chem. 277:22370-22376(2002).
[29]
INTERACTION WITH EPHB1 AND GRB2.
PubMed=12925710; DOI=10.1083/jcb.200302073;
Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.;
"EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote
chemotaxis.";
J. Cell Biol. 162:661-671(2003).
[30]
INTERACTION WITH NTRK1.
PubMed=15488758; DOI=10.1016/j.ccr.2004.09.011;
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A.,
Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A.,
Mackay A.R.;
"TrkA alternative splicing: a regulated tumor-promoting switch in
human neuroblastoma.";
Cancer Cell 6:347-360(2004).
[31]
REVIEW ON ROLE IN KIT SIGNALING, AND PHOSPHORYLATION.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[32]
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH TEK.
PubMed=14665640; DOI=10.1074/jbc.M307456200;
Audero E., Cascone I., Maniero F., Napione L., Arese M.,
Lanfrancone L., Bussolino F.;
"Adaptor ShcA protein binds tyrosine kinase Tie2 receptor and
regulates migration and sprouting but not survival of endothelial
cells.";
J. Biol. Chem. 279:13224-13233(2004).
[33]
INTERACTION WITH FLT4.
PubMed=15102829; DOI=10.1074/jbc.M314015200;
Wang J.F., Zhang X., Groopman J.E.;
"Activation of vascular endothelial growth factor receptor-3 and its
downstream signaling promote cell survival under oxidative stress.";
J. Biol. Chem. 279:27088-27097(2004).
[34]
INTERACTION WITH IRS4.
PubMed=15316024; DOI=10.1074/jbc.M404537200;
Hinsby A.M., Olsen J.V., Mann M.;
"Tyrosine phosphoproteomics of fibroblast growth factor signaling: a
role for insulin receptor substrate-4.";
J. Biol. Chem. 279:46438-46447(2004).
[35]
SUBCELLULAR LOCATION (ISOFORM P46SHC).
PubMed=14573619; DOI=10.1074/jbc.M307655200;
Ventura A., Maccarana M., Raker V.A., Pelicci P.-G.;
"A cryptic targeting signal induces isoform-specific localization of
p46Shc to mitochondria.";
J. Biol. Chem. 279:2299-2306(2004).
[36]
INTERACTION WITH LRP1.
PubMed=15272003; DOI=10.1074/jbc.M407592200;
Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F.,
Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K.;
"Serine and threonine phosphorylation of the low density lipoprotein
receptor-related protein by protein kinase Calpha regulates
endocytosis and association with adaptor molecules.";
J. Biol. Chem. 279:40536-40544(2004).
[37]
PHOSPHORYLATION AT SER-36.
PubMed=15837797; DOI=10.1083/jcb.200410041;
Smith W.W., Norton D.D., Gorospe M., Jiang H., Nemoto S.,
Holbrook N.J., Finkel T., Kusiak J.W.;
"Phosphorylation of p66Shc and forkhead proteins mediates Abeta
toxicity.";
J. Cell Biol. 169:331-339(2005).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[40]
INTERACTION WITH ALK, AND PHOSPHORYLATION.
PubMed=17274988; DOI=10.1016/j.febslet.2007.01.039;
Degoutin J., Vigny M., Gouzi J.Y.;
"ALK activation induces Shc and FRS2 recruitment: Signaling and
phenotypic outcomes in PC12 cells differentiation.";
FEBS Lett. 581:727-734(2007).
[41]
INTERACTION WITH GAB2.
PubMed=19172738; DOI=10.1038/emboj.2008.159;
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
Guilhaus M., James D.E., Daly R.J.;
"Phosphorylation-dependent binding of 14-3-3 terminates signalling by
the Gab2 docking protein.";
EMBO J. 27:2305-2316(2008).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND TYR-427, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-427, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[45]
INTERACTION WITH CPNE3.
PubMed=20010870; DOI=10.1038/onc.2009.456;
Heinrich C., Keller C., Boulay A., Vecchi M., Bianchi M., Sack R.,
Lienhard S., Duss S., Hofsteenge J., Hynes N.E.;
"Copine-III interacts with ErbB2 and promotes tumor cell migration.";
Oncogene 29:1598-1610(2010).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[47]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[49]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, ACETYLATION [LARGE SCALE
ANALYSIS] AT MET-1 (ISOFORMS 7 AND P52SHC), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139; TYR-427 AND
SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[51]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL46.
PubMed=23946459; DOI=10.1128/JVI.01702-13;
Strunk U., Saffran H.A., Wu F.W., Smiley J.R.;
"Role of herpes simplex virus VP11/12 tyrosine-based motifs in binding
and activation of the Src family kinase Lck and recruitment of p85,
Grb2, and Shc.";
J. Virol. 87:11276-11286(2013).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[53]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 482-583.
PubMed=7473762; DOI=10.1006/jmbi.1995.0601;
Mikol V., Baumann G., Zurini M.G.M., Hommel U.;
"Crystal structure of the SH2 domain from the adaptor protein SHC: a
model for peptide binding based on X-ray and NMR data.";
J. Mol. Biol. 254:86-95(1995).
[54]
STRUCTURE BY NMR OF 127-317.
PubMed=8524391; DOI=10.1038/378584a0;
Zhou M.-M., Ravichandran K.S., Olejniczak E.F., Petros A.M.,
Meadows R.P., Sattler M., Harlan J.E., Wade W.S., Burakoff S.J.,
Fesik S.W.;
"Structure and ligand recognition of the phosphotyrosine binding
domain of Shc.";
Nature 378:584-592(1995).
[55]
STRUCTURE BY NMR OF 480-583 IN COMPLEX WITH TYROSINE-PHOSPHORYLATED
CD3Z.
PubMed=7544002; DOI=10.1073/pnas.92.17.7784;
Zhou M.-M., Meadows R.P., Logan T.M., Yoon H.S., Wade W.S.,
Ravichandran K.S., Burakoff S.J., Fesik S.W.;
"Solution structure of the Shc SH2 domain complexed with a tyrosine-
phosphorylated peptide from the T-cell receptor.";
Proc. Natl. Acad. Sci. U.S.A. 92:7784-7788(1995).
-!- FUNCTION: Signaling adapter that couples activated growth factor
receptors to signaling pathways. Participates in a signaling
cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc
and isoform p52Shc, once phosphorylated, couple activated receptor
tyrosine kinases to Ras via the recruitment of the GRB2/SOS
complex and are implicated in the cytoplasmic propagation of
mitogenic signals. Isoform p46Shc and isoform p52Shc may thus
function as initiators of the Ras signaling cascade in various
non-neuronal systems. Isoform p66Shc does not mediate Ras
activation, but is involved in signal transduction pathways that
regulate the cellular response to oxidative stress and life span.
Isoform p66Shc acts as a downstream target of the tumor suppressor
p53 and is indispensable for the ability of stress-activated p53
to induce elevation of intracellular oxidants, cytochrome c
release and apoptosis. The expression of isoform p66Shc has been
correlated with life span (By similarity). Participates in
signaling downstream of the angiopoietin receptor TEK/TIE2, and
plays a role in the regulation of endothelial cell migration and
sprouting angiogenesis. {ECO:0000250,
ECO:0000269|PubMed:14665640}.
-!- SUBUNIT: Interacts with CPNE3; this interaction may mediate the
binding of CPNE3 with ERBB2 (PubMed:20010870). Interacts with the
NPXY motif of tyrosine-phosphorylated IGF1R and INSR in vitro via
the PID domain. Once activated, binds to GRB2. Interacts with
tyrosine-phosphorylated CD3T and DDR2. Interacts with the N-
terminal region of APS. Interacts with phosphorylated LRP1 and
IRS4. Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with
TRIM31. Interacts with PTPN6/SHP (tyrosine phosphorylated).
Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1,
FRS2, SRC, SHC1, GAP43 and CTT (By similarity). Interacts with
ALK, GAB2, GRB7 and KIT. Interacts with FLT4 (tyrosine-
phosphorylated). Interacts with EPHB1 and GRB2; activates the
MAPK/ERK cascade to regulate cell migration. Interacts with PDGFRB
(tyrosine-phosphorylated). Interacts with ERBB4. Interacts with
TEK/TIE2 (tyrosine-phosphorylated). Interacts with the Trk
receptors NTRK1, NTRK2 and NTRK3; in a phosphotyrosine-dependent
manner. Interacts with PTK2/FAK1. Interacts with herpes simplex
virus 1 UL46. Interacts with CEACAM1; this interaction is CEACAM1-
phosphorylation-dependent and mediates interaction with EGFR or
INSR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-
MAPK1/ERK2 pathway (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P98083, ECO:0000250|UniProtKB:Q5M824,
ECO:0000269|PubMed:10194451, ECO:0000269|PubMed:10867024,
ECO:0000269|PubMed:11349134, ECO:0000269|PubMed:11980671,
ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:14665640,
ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:15272003,
ECO:0000269|PubMed:15316024, ECO:0000269|PubMed:15488758,
ECO:0000269|PubMed:17274988, ECO:0000269|PubMed:19172738,
ECO:0000269|PubMed:20010870, ECO:0000269|PubMed:23946459,
ECO:0000269|PubMed:7537849, ECO:0000269|PubMed:7541045,
ECO:0000269|PubMed:7544002, ECO:0000269|PubMed:7559478,
ECO:0000269|PubMed:8155326, ECO:0000269|PubMed:8195171,
ECO:0000269|PubMed:8874179, ECO:0000269|PubMed:8940081,
ECO:0000269|PubMed:9038210, ECO:0000269|PubMed:9233773,
ECO:0000269|PubMed:9488479, ECO:0000269|PubMed:9660833}.
-!- INTERACTION:
P05067:APP; NbExp=5; IntAct=EBI-78835, EBI-77613;
P10275:AR; NbExp=14; IntAct=EBI-78835, EBI-608057;
P46108:CRK; NbExp=3; IntAct=EBI-78835, EBI-886;
P00533:EGFR; NbExp=26; IntAct=EBI-78835, EBI-297353;
P04626:ERBB2; NbExp=9; IntAct=EBI-78835, EBI-641062;
P21860:ERBB3; NbExp=5; IntAct=EBI-78835, EBI-720706;
Q15303:ERBB4; NbExp=2; IntAct=EBI-78835, EBI-80371;
P03372-4:ESR1; NbExp=2; IntAct=EBI-78835, EBI-4309277;
Q13480:GAB1; NbExp=9; IntAct=EBI-78835, EBI-517684;
P62993:GRB2; NbExp=23; IntAct=EBI-78835, EBI-401755;
P08069:IGF1R; NbExp=2; IntAct=EBI-1000553, EBI-475981;
P06213:INSR; NbExp=2; IntAct=EBI-78835, EBI-475899;
Q62120:Jak2 (xeno); NbExp=2; IntAct=EBI-78835, EBI-646604;
P10721:KIT; NbExp=8; IntAct=EBI-78835, EBI-1379503;
P08581:MET; NbExp=5; IntAct=EBI-78835, EBI-1039152;
P03495:NS (xeno); NbExp=2; IntAct=EBI-78835, EBI-2548993;
P27986:PIK3R1; NbExp=3; IntAct=EBI-78835, EBI-79464;
Q05209:PTPN12; NbExp=4; IntAct=EBI-78835, EBI-2266035;
Q07889:SOS1; NbExp=2; IntAct=EBI-78835, EBI-297487;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform p46Shc: Mitochondrion matrix
{ECO:0000269|PubMed:14573619}. Note=Localized to the mitochondria
matrix. Targeting of isoform p46Shc to mitochondria is mediated by
its first 32 amino acids, which behave as a bona fide
mitochondrial targeting sequence. Isoform p52Shc and isoform
p66Shc, that contain the same sequence but more internally
located, display a different subcellular localization.
-!- SUBCELLULAR LOCATION: Isoform p66Shc: Mitochondrion {ECO:0000250}.
Note=In case of oxidative conditions, phosphorylation at 'Ser-36'
of isoform p66Shc, leads to mitochondrial accumulation.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
Name=p66Shc;
IsoId=P29353-1; Sequence=Displayed;
Note=Regulated by epigenetic modifications of its promoter
region.;
Name=p52Shc;
IsoId=P29353-2; Sequence=VSP_016108;
Note=Contains a N-acetylmethionine at position 1.
{ECO:0000244|PubMed:22814378};
Name=p46Shc;
IsoId=P29353-3; Sequence=VSP_016107;
Name=5;
IsoId=P29353-5; Sequence=VSP_040090, VSP_040091;
Note=Produced by alternative splicing.;
Name=6;
IsoId=P29353-6; Sequence=VSP_040092;
Note=Produced by alternative splicing.;
Name=7;
IsoId=P29353-7; Sequence=VSP_016108, VSP_040092;
Note=Produced by alternative splicing. Contains a
N-acetylmethionine at position 1. {ECO:0000244|PubMed:22814378};
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in neural stem
cells but absent in mature neurons.
-!- DOMAIN: In response to a variety of growth factors, isoform p46Shc
and isoform p52Shc bind to phosphorylated Trk receptors through
their phosphotyrosine binding (PID) and/or SH2 domains. The PID
and SH2 domains bind to specific phosphorylated tyrosine residues
in the Asn-Pro-Xaa-Tyr(P) motif of the Trk receptors. Isoform
p46Shc and isoform p52Shc are in turn phosphorylated on three
tyrosine residues within the extended proline-rich domain. These
phosphotyrosines act as docking site for GRB2 and thereby are
involved in Ras activation (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by activated epidermal growth factor receptor.
Phosphorylated in response to FLT4 and KIT signaling. Isoform
p46Shc and isoform p52Shc are phosphorylated on tyrosine residues
of the Pro-rich domain. Isoform p66Shc is phosphorylated on Ser-36
by PRKCB upon treatment with insulin, hydrogen peroxide or
irradiation with ultraviolet light (By similarity). Tyrosine
phosphorylated in response to FLT3 signaling (By similarity).
Tyrosine phosphorylated by activated PTK2B/PYK2 (By similarity).
Tyrosine phosphorylated by ligand-activated ALK. Tyrosine
phosphorylated by ligand-activated PDGFRB. Tyrosine phosphorylated
by TEK/TIE2. May be tyrosine phosphorylated by activated
PTK2/FAK1; tyrosine phosphorylation was seen in an astrocytoma
biopsy, where PTK2/FAK1 kinase activity is high, but not in normal
brain tissue. Isoform p52Shc dephosphorylation by PTPN2 may
regulate interaction with GRB2. {ECO:0000250,
ECO:0000269|PubMed:11980671, ECO:0000269|PubMed:14665640,
ECO:0000269|PubMed:15526160, ECO:0000269|PubMed:15837797,
ECO:0000269|PubMed:17274988, ECO:0000269|PubMed:8195171,
ECO:0000269|PubMed:8939605, ECO:0000269|PubMed:9121430,
ECO:0000269|PubMed:9148935, ECO:0000269|PubMed:9488479,
ECO:0000269|PubMed:9566877}.
-!- SEQUENCE CAUTION:
Sequence=CAI13254.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SHC1ID42287ch1q21.html";
-----------------------------------------------------------------------
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EMBL; X68148; CAA48251.1; -; mRNA.
EMBL; U73377; AAB49972.1; -; mRNA.
EMBL; Y09847; CAA70977.1; -; Genomic_DNA.
EMBL; AK292143; BAF84832.1; -; mRNA.
EMBL; AK315842; BAF98733.1; -; mRNA.
EMBL; AB451255; BAG70069.1; -; mRNA.
EMBL; AB451379; BAG70193.1; -; mRNA.
EMBL; AL451085; CAI13248.1; -; Genomic_DNA.
EMBL; AL451085; CAI13249.1; -; Genomic_DNA.
EMBL; AL451085; CAI13250.1; -; Genomic_DNA.
EMBL; AL451085; CAI13251.1; -; Genomic_DNA.
EMBL; AL451085; CAI13254.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471121; EAW53168.1; -; Genomic_DNA.
EMBL; CH471121; EAW53169.1; -; Genomic_DNA.
EMBL; CH471121; EAW53170.1; -; Genomic_DNA.
EMBL; CH471121; EAW53171.1; -; Genomic_DNA.
EMBL; BC014158; AAH14158.1; -; mRNA.
EMBL; BC033925; AAH33925.1; -; mRNA.
CCDS; CCDS1076.1; -. [P29353-7]
CCDS; CCDS30881.1; -. [P29353-1]
CCDS; CCDS44233.1; -. [P29353-6]
CCDS; CCDS44234.1; -. [P29353-2]
PIR; S25776; S25776.
RefSeq; NP_001123512.1; NM_001130040.1. [P29353-6]
RefSeq; NP_001123513.1; NM_001130041.1. [P29353-2]
RefSeq; NP_001189788.1; NM_001202859.1. [P29353-3]
RefSeq; NP_003020.2; NM_003029.4. [P29353-7]
RefSeq; NP_892113.4; NM_183001.4. [P29353-1]
UniGene; Hs.433795; -.
PDB; 1MIL; X-ray; 2.70 A; A=482-583.
PDB; 1N3H; NMR; -; A=111-317.
PDB; 1OY2; NMR; -; A=111-317.
PDB; 1QG1; NMR; -; I=423-435.
PDB; 1SHC; NMR; -; A=127-317.
PDB; 1TCE; NMR; -; A=480-583.
PDB; 1WCP; Model; -; A=127-583.
PDB; 2L1C; NMR; -; A=127-317.
PDB; 4JMH; X-ray; 2.41 A; B=344-356.
PDB; 4XWX; X-ray; 1.87 A; A=147-311.
PDB; 5CZI; X-ray; 2.60 A; B=345-353.
PDBsum; 1MIL; -.
PDBsum; 1N3H; -.
PDBsum; 1OY2; -.
PDBsum; 1QG1; -.
PDBsum; 1SHC; -.
PDBsum; 1TCE; -.
PDBsum; 1WCP; -.
PDBsum; 2L1C; -.
PDBsum; 4JMH; -.
PDBsum; 4XWX; -.
PDBsum; 5CZI; -.
DisProt; DP00154; -.
ProteinModelPortal; P29353; -.
SMR; P29353; -.
BioGrid; 112361; 234.
DIP; DIP-699N; -.
ELM; P29353; -.
IntAct; P29353; 93.
MINT; MINT-123530; -.
STRING; 9606.ENSP00000401303; -.
BindingDB; P29353; -.
ChEMBL; CHEMBL5626; -.
iPTMnet; P29353; -.
PhosphoSitePlus; P29353; -.
BioMuta; SHC1; -.
DMDM; 182676455; -.
EPD; P29353; -.
MaxQB; P29353; -.
PaxDb; P29353; -.
PeptideAtlas; P29353; -.
PRIDE; P29353; -.
DNASU; 6464; -.
Ensembl; ENST00000368445; ENSP00000357430; ENSG00000160691. [P29353-1]
Ensembl; ENST00000368450; ENSP00000357435; ENSG00000160691. [P29353-2]
Ensembl; ENST00000368453; ENSP00000357438; ENSG00000160691. [P29353-7]
Ensembl; ENST00000448116; ENSP00000401303; ENSG00000160691. [P29353-6]
GeneID; 6464; -.
KEGG; hsa:6464; -.
UCSC; uc001ffv.4; human. [P29353-1]
CTD; 6464; -.
DisGeNET; 6464; -.
GeneCards; SHC1; -.
HGNC; HGNC:10840; SHC1.
HPA; CAB005374; -.
HPA; CAB016305; -.
HPA; HPA001844; -.
MIM; 600560; gene.
neXtProt; NX_P29353; -.
OpenTargets; ENSG00000160691; -.
PharmGKB; PA35746; -.
eggNOG; KOG3697; Eukaryota.
eggNOG; ENOG410XTJN; LUCA.
GeneTree; ENSGT00390000018860; -.
HOVERGEN; HBG050121; -.
InParanoid; P29353; -.
KO; K06279; -.
OMA; PHDRMAG; -.
OrthoDB; EOG091G04DC; -.
PhylomeDB; P29353; -.
TreeFam; TF315807; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-HSA-167044; Signalling to RAS.
Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-451927; Interleukin-2 signaling.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-74749; Signal attenuation.
Reactome; R-HSA-74751; Insulin receptor signalling cascade.
Reactome; R-HSA-8851805; MET activates RAS signaling.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P29353; -.
SIGNOR; P29353; -.
ChiTaRS; SHC1; human.
EvolutionaryTrace; P29353; -.
GeneWiki; SHC1; -.
GenomeRNAi; 6464; -.
PRO; PR:P29353; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160691; -.
ExpressionAtlas; P29353; baseline and differential.
Genevisible; P29353; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0070435; C:Shc-EGFR complex; ISS:BHF-UCL.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0048408; F:epidermal growth factor binding; IEA:Ensembl.
GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:BHF-UCL.
GO; GO:0005158; F:insulin receptor binding; IPI:UniProtKB.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:UniProtKB.
GO; GO:0005168; F:neurotrophin TRKA receptor binding; IPI:UniProtKB.
GO; GO:0005543; F:phospholipid binding; TAS:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; TAS:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IMP:CAFA.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CAFA.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CAFA.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0045740; P:positive regulation of DNA replication; ISS:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:CAFA.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; TAS:ProtInc.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0016337; P:single organismal cell-cell adhesion; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd01209; PTB_Shc; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR006019; PID_Shc-like.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR000980; SH2.
InterPro; IPR029586; Shc1/ShcA.
PANTHER; PTHR10337:SF18; PTHR10337:SF18; 1.
Pfam; PF00640; PID; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00629; SHCPIDOMAIN.
SMART; SM00462; PTB; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS01179; PID; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative promoter usage;
Alternative splicing; Angiogenesis; Complete proteome; Cytoplasm;
Growth regulation; Host-virus interaction; Mitochondrion;
Phosphoprotein; Polymorphism; Reference proteome; SH2 domain.
CHAIN 1 583 SHC-transforming protein 1.
/FTId=PRO_0000097731.
DOMAIN 156 339 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
DOMAIN 488 579 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 340 487 CH1.
COMPBIAS 411 474 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000269|PubMed:15837797}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 154 154 N6-acetyllysine.
{ECO:0000250|UniProtKB:P98083}.
MOD_RES 349 349 Phosphotyrosine.
{ECO:0000269|PubMed:8939605,
ECO:0000269|PubMed:9121430,
ECO:0000269|PubMed:9566877}.
MOD_RES 350 350 Phosphotyrosine.
{ECO:0000269|PubMed:8939605,
ECO:0000269|PubMed:9121430,
ECO:0000269|PubMed:9566877}.
MOD_RES 427 427 Phosphotyrosine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:9121430,
ECO:0000269|PubMed:9566877}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 214 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_040090.
VAR_SEQ 1 155 Missing (in isoform p46Shc).
{ECO:0000303|PubMed:1623525}.
/FTId=VSP_016107.
VAR_SEQ 1 110 Missing (in isoform p52Shc and isoform
7). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1623525}.
/FTId=VSP_016108.
VAR_SEQ 215 221 PLSSILG -> MSLCHRW (in isoform 5).
{ECO:0000305}.
/FTId=VSP_040091.
VAR_SEQ 417 417 P -> PA (in isoform 7 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:19054851}.
/FTId=VSP_040092.
VARIANT 205 205 A -> V (in dbSNP:rs8191981).
/FTId=VAR_042428.
VARIANT 410 410 M -> V (in dbSNP:rs8191979).
/FTId=VAR_051353.
MUTAGEN 349 349 Y->F: Alters interaction with GRB2;
isoform p52Shc (in vitro).
{ECO:0000269|PubMed:9488479}.
MUTAGEN 427 427 Y->F: No effect on interaction with GRB2;
isoform p52Shc (in vitro).
{ECO:0000269|PubMed:9488479}.
CONFLICT 2 2 D -> N (in Ref. 3; CAA70977).
{ECO:0000305}.
CONFLICT 21 21 L -> M (in Ref. 3; CAA70977).
{ECO:0000305}.
CONFLICT 38 38 S -> P (in Ref. 3; CAA70977).
{ECO:0000305}.
CONFLICT 95 95 V -> D (in Ref. 2; AAB49972).
{ECO:0000305}.
CONFLICT 101 101 D -> E (in Ref. 2; AAB49972).
{ECO:0000305}.
CONFLICT 430 430 V -> A (in Ref. 5; BAG70069/BAG70193).
{ECO:0000305}.
STRAND 113 115 {ECO:0000244|PDB:1N3H}.
STRAND 142 145 {ECO:0000244|PDB:1SHC}.
STRAND 148 150 {ECO:0000244|PDB:1N3H}.
HELIX 152 156 {ECO:0000244|PDB:4XWX}.
STRAND 160 172 {ECO:0000244|PDB:4XWX}.
HELIX 176 178 {ECO:0000244|PDB:4XWX}.
HELIX 181 198 {ECO:0000244|PDB:4XWX}.
HELIX 200 202 {ECO:0000244|PDB:1OY2}.
STRAND 206 208 {ECO:0000244|PDB:1SHC}.
TURN 215 219 {ECO:0000244|PDB:4XWX}.
STRAND 220 224 {ECO:0000244|PDB:4XWX}.
TURN 226 229 {ECO:0000244|PDB:4XWX}.
STRAND 230 236 {ECO:0000244|PDB:4XWX}.
STRAND 238 245 {ECO:0000244|PDB:4XWX}.
TURN 246 249 {ECO:0000244|PDB:1N3H}.
STRAND 251 256 {ECO:0000244|PDB:4XWX}.
HELIX 257 259 {ECO:0000244|PDB:4XWX}.
STRAND 262 265 {ECO:0000244|PDB:4XWX}.
HELIX 268 270 {ECO:0000244|PDB:4XWX}.
STRAND 273 280 {ECO:0000244|PDB:4XWX}.
TURN 281 283 {ECO:0000244|PDB:4XWX}.
STRAND 284 291 {ECO:0000244|PDB:4XWX}.
STRAND 293 295 {ECO:0000244|PDB:1N3H}.
HELIX 296 310 {ECO:0000244|PDB:4XWX}.
STRAND 311 314 {ECO:0000244|PDB:1N3H}.
STRAND 350 352 {ECO:0000244|PDB:5CZI}.
TURN 483 485 {ECO:0000244|PDB:1MIL}.
STRAND 487 489 {ECO:0000244|PDB:1TCE}.
HELIX 495 499 {ECO:0000244|PDB:1MIL}.
STRAND 507 512 {ECO:0000244|PDB:1MIL}.
STRAND 514 516 {ECO:0000244|PDB:1TCE}.
STRAND 518 526 {ECO:0000244|PDB:1MIL}.
STRAND 529 536 {ECO:0000244|PDB:1MIL}.
STRAND 540 543 {ECO:0000244|PDB:1MIL}.
STRAND 548 551 {ECO:0000244|PDB:1MIL}.
HELIX 552 562 {ECO:0000244|PDB:1MIL}.
STRAND 566 568 {ECO:0000244|PDB:1MIL}.
STRAND 571 573 {ECO:0000244|PDB:1MIL}.
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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