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P29353

- SHC1_HUMAN

UniProt

P29353 - SHC1_HUMAN

Protein

SHC-transforming protein 1

Gene

SHC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 4 (08 Apr 2008)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    GO - Molecular functioni

    1. ephrin receptor binding Source: UniProtKB
    2. epidermal growth factor receptor binding Source: BHF-UCL
    3. insulin-like growth factor receptor binding Source: UniProtKB
    4. insulin receptor binding Source: UniProtKB
    5. neurotrophin TRKA receptor binding Source: UniProtKB
    6. phospholipid binding Source: UniProtKB
    7. protein binding Source: IntAct
    8. protein tyrosine kinase activity Source: Reactome
    9. transmembrane receptor protein tyrosine kinase adaptor activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: Ensembl
    2. activation of MAPK activity Source: UniProtKB
    3. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    4. angiogenesis Source: UniProtKB-KW
    5. blood coagulation Source: Reactome
    6. cellular protein metabolic process Source: Reactome
    7. endoplasmic reticulum unfolded protein response Source: Reactome
    8. epidermal growth factor receptor signaling pathway Source: Reactome
    9. Fc-epsilon receptor signaling pathway Source: Reactome
    10. fibroblast growth factor receptor signaling pathway Source: Reactome
    11. heart development Source: Ensembl
    12. innate immune response Source: Reactome
    13. insulin receptor signaling pathway Source: BHF-UCL
    14. leukocyte migration Source: Reactome
    15. MAPK cascade Source: UniProtKB
    16. neurotrophin TRK receptor signaling pathway Source: Reactome
    17. peptidyl-tyrosine phosphorylation Source: GOC
    18. platelet activation Source: Reactome
    19. positive regulation of cell proliferation Source: UniProtKB
    20. positive regulation of DNA replication Source: BHF-UCL
    21. Ras protein signal transduction Source: Reactome
    22. regulation of epidermal growth factor-activated receptor activity Source: ProtInc
    23. regulation of growth Source: UniProtKB-KW
    24. single organismal cell-cell adhesion Source: Ensembl

    Keywords - Biological processi

    Angiogenesis, Growth regulation

    Enzyme and pathway databases

    ReactomeiREACT_115852. Signaling by constitutively active EGFR.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116005. SHC1 events in ERBB4 signaling.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12033. Signalling to RAS.
    REACT_12579. SHC1 events in EGFR signaling.
    REACT_12621. Tie2 Signaling.
    REACT_147814. DAP12 signaling.
    REACT_150139. SHC-related events triggered by IGF1R.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_1661. SHC activation.
    REACT_18273. XBP1(S) activates chaperone genes.
    REACT_21374. SHC-mediated cascade.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_27283. Interleukin-2 signaling.
    REACT_508. Signal attenuation.
    REACT_661. SHC-mediated signalling.
    SignaLinkiP29353.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SHC-transforming protein 1
    Alternative name(s):
    SHC-transforming protein 3
    SHC-transforming protein A
    Src homology 2 domain-containing-transforming protein C1
    Short name:
    SH2 domain protein C1
    Gene namesi
    Name:SHC1
    Synonyms:SHC, SHCA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10840. SHC1.

    Subcellular locationi

    Isoform p46Shc : Mitochondrion matrix 1 Publication
    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.
    Isoform p66Shc : Mitochondrion By similarity
    Note: In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation.By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB
    4. Shc-EGFR complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi349 – 3491Y → F: Alters interaction with GRB2; isoform p52Shc (in vitro). 1 Publication
    Mutagenesisi427 – 4271Y → F: No effect on interaction with GRB2; isoform p52Shc (in vitro). 1 Publication

    Organism-specific databases

    PharmGKBiPA35746.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 583583SHC-transforming protein 1PRO_0000097731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei36 – 361Phosphoserine1 Publication
    Modified residuei139 – 1391Phosphoserine3 Publications
    Modified residuei154 – 1541N6-acetyllysineBy similarity
    Modified residuei349 – 3491Phosphotyrosine3 Publications
    Modified residuei350 – 3501Phosphotyrosine3 Publications
    Modified residuei426 – 4261Phosphoserine
    Modified residuei427 – 4271Phosphotyrosine4 Publications

    Post-translational modificationi

    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.By similarity15 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP29353.
    PaxDbiP29353.
    PRIDEiP29353.

    PTM databases

    PhosphoSiteiP29353.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in neural stem cells but absent in mature neurons.

    Gene expression databases

    ArrayExpressiP29353.
    BgeeiP29353.
    GenevestigatoriP29353.

    Organism-specific databases

    HPAiCAB005374.
    CAB016305.
    HPA001844.

    Interactioni

    Subunit structurei

    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.By similarity24 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APPP050675EBI-78835,EBI-77613
    ARP1027514EBI-78835,EBI-608057
    CRKP461083EBI-78835,EBI-886
    EGFRP0053326EBI-78835,EBI-297353
    ERBB2P046269EBI-78835,EBI-641062
    ERBB3P218605EBI-78835,EBI-720706
    ERBB4Q153032EBI-78835,EBI-80371
    ESR1P03372-42EBI-78835,EBI-4309277
    GAB1Q134809EBI-78835,EBI-517684
    GRB2P6299322EBI-78835,EBI-401755
    IGF1RP080692EBI-1000553,EBI-475981
    INSRP062132EBI-78835,EBI-475899
    Jak2Q621202EBI-78835,EBI-646604From a different organism.
    KITP107218EBI-78835,EBI-1379503
    METP085815EBI-78835,EBI-1039152
    NSP034952EBI-78835,EBI-2548993From a different organism.
    PIK3R1P279863EBI-78835,EBI-79464
    SOS1Q078892EBI-78835,EBI-297487

    Protein-protein interaction databases

    BioGridi112361. 199 interactions.
    DIPiDIP-699N.
    IntActiP29353. 83 interactions.
    MINTiMINT-123530.

    Structurei

    Secondary structure

    1
    583
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi113 – 1153
    Beta strandi142 – 1454
    Beta strandi148 – 1503
    Helixi152 – 1565
    Beta strandi160 – 1678
    Beta strandi169 – 1713
    Turni176 – 1783
    Beta strandi179 – 1813
    Helixi184 – 19815
    Helixi200 – 2023
    Beta strandi206 – 2083
    Beta strandi215 – 2184
    Beta strandi222 – 2243
    Beta strandi229 – 2379
    Beta strandi240 – 2456
    Turni246 – 2494
    Beta strandi251 – 2555
    Beta strandi256 – 2594
    Beta strandi261 – 2633
    Beta strandi265 – 2673
    Beta strandi270 – 2723
    Beta strandi274 – 2785
    Beta strandi281 – 2833
    Beta strandi286 – 2916
    Beta strandi293 – 2953
    Helixi297 – 3026
    Beta strandi311 – 3144
    Turni483 – 4853
    Beta strandi487 – 4893
    Helixi495 – 4995
    Beta strandi507 – 5126
    Beta strandi514 – 5163
    Beta strandi518 – 5269
    Beta strandi529 – 5368
    Beta strandi540 – 5434
    Beta strandi548 – 5514
    Helixi552 – 56211
    Beta strandi566 – 5683
    Beta strandi571 – 5733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MILX-ray2.70A482-583[»]
    1N3HNMR-A111-317[»]
    1OY2NMR-A111-317[»]
    1QG1NMR-I423-435[»]
    1SHCNMR-A127-317[»]
    1TCENMR-A480-583[»]
    1WCPmodel-A127-583[»]
    2L1CNMR-A127-317[»]
    4JMHX-ray2.41B344-356[»]
    DisProtiDP00154.
    ProteinModelPortaliP29353.
    SMRiP29353. Positions 111-317, 482-583.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29353.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini156 – 339184PIDPROSITE-ProRule annotationAdd
    BLAST
    Domaini488 – 57992SH2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni340 – 487148CH1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi411 – 47464Pro-richAdd
    BLAST

    Domaini

    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.By similarity

    Sequence similaritiesi

    Contains 1 PID domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG315087.
    HOVERGENiHBG050121.
    KOiK06279.
    OMAiESPTTLC.
    OrthoDBiEOG7MD4QK.
    PhylomeDBiP29353.
    TreeFamiTF315807.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR006019. PID_Shc-like.
    IPR006020. PTB/PI_dom.
    IPR000980. SH2.
    [Graphical view]
    PfamiPF00640. PID. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00629. SHCPIDOMAIN.
    SMARTiSM00462. PTB. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 1 hit.
    PROSITEiPS01179. PID. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform p66Shc (identifier: P29353-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP    50
    GDDSPTTLCS FFPRMSNLRL ANPAGGRPGS KGEPGRAADD GEGIVGAAMP 100
    DSGPLPLLQD MNKLSGGGGR RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH 150
    PNDKVMGPGV SYLVRYMGCV EVLQSMRALD FNTRTQVTRE AISLVCEAVP 200
    GAKGATRRRK PCSRPLSSIL GRSNLKFAGM PITLTVSTSS LNLMAADCKQ 250
    IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL ECPEGLAQDV 300
    ISTIGQAFEL RFKQYLRNPP KLVTPHDRMA GFDGSAWDEE EEEPPDHQYY 350
    NDFPGKEPPL GGVVDMRLRE GAAPGAARPT APNAQTPSHL GATLPVGQPV 400
    GGDPEVRKQM PPPPPCPGRE LFDDPSYVNV QNLDKARQAV GGAGPPNPAI 450
    NGSAPRDLFD MKPFEDALRV PPPPQSVSMA EQLRGEPWFH GKLSRREAEA 500
    LLQLNGDFLV RESTTTPGQY VLTGLQSGQP KHLLLVDPEG VVRTKDHRFE 550
    SVSHLISYHM DNHLPIISAG SELCLQQPVE RKL 583

    Note: Regulated by epigenetic modifications of its promoter region.

    Length:583
    Mass (Da):62,822
    Last modified:April 8, 2008 - v4
    Checksum:i7EFA5CB185A548D1
    GO
    Isoform p52Shc (identifier: P29353-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-110: Missing.

    Show »
    Length:473
    Mass (Da):51,611
    Checksum:i6DDC519E3F318B6D
    GO
    Isoform p46Shc (identifier: P29353-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-155: Missing.

    Show »
    Length:428
    Mass (Da):46,668
    Checksum:i099FED4690662DD5
    GO
    Isoform 5 (identifier: P29353-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-214: Missing.
         215-221: PLSSILG → MSLCHRW

    Note: Produced by alternative splicing.

    Show »
    Length:369
    Mass (Da):40,415
    Checksum:i46F34449B556DDD0
    GO
    Isoform 6 (identifier: P29353-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         417-417: P → PA

    Note: Produced by alternative splicing.

    Show »
    Length:584
    Mass (Da):62,893
    Checksum:iBDB2FF81953D4FF4
    GO
    Isoform 7 (identifier: P29353-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-110: Missing.
         417-417: P → PA

    Note: Produced by alternative splicing.

    Show »
    Length:474
    Mass (Da):51,682
    Checksum:i43E1D98CBA87DB37
    GO

    Sequence cautioni

    The sequence CAI13254.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21D → N in CAA70977. (PubMed:9192859)Curated
    Sequence conflicti21 – 211L → M in CAA70977. (PubMed:9192859)Curated
    Sequence conflicti38 – 381S → P in CAA70977. (PubMed:9192859)Curated
    Sequence conflicti95 – 951V → D in AAB49972. (PubMed:9049300)Curated
    Sequence conflicti101 – 1011D → E in AAB49972. (PubMed:9049300)Curated
    Sequence conflicti430 – 4301V → A in BAG70069. (PubMed:19054851)Curated
    Sequence conflicti430 – 4301V → A in BAG70193. (PubMed:19054851)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti205 – 2051A → V.
    Corresponds to variant rs8191981 [ dbSNP | Ensembl ].
    VAR_042428
    Natural varianti410 – 4101M → V.
    Corresponds to variant rs8191979 [ dbSNP | Ensembl ].
    VAR_051353

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 214214Missing in isoform 5. CuratedVSP_040090Add
    BLAST
    Alternative sequencei1 – 155155Missing in isoform p46Shc. 1 PublicationVSP_016107Add
    BLAST
    Alternative sequencei1 – 110110Missing in isoform p52Shc and isoform 7. 3 PublicationsVSP_016108Add
    BLAST
    Alternative sequencei215 – 2217PLSSILG → MSLCHRW in isoform 5. CuratedVSP_040091
    Alternative sequencei417 – 4171P → PA in isoform 7 and isoform 6. 2 PublicationsVSP_040092

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68148 mRNA. Translation: CAA48251.1.
    U73377 mRNA. Translation: AAB49972.1.
    Y09847 Genomic DNA. Translation: CAA70977.1.
    AK292143 mRNA. Translation: BAF84832.1.
    AK315842 mRNA. Translation: BAF98733.1.
    AB451255 mRNA. Translation: BAG70069.1.
    AB451379 mRNA. Translation: BAG70193.1.
    AL451085 Genomic DNA. Translation: CAI13248.1.
    AL451085 Genomic DNA. Translation: CAI13249.1.
    AL451085 Genomic DNA. Translation: CAI13250.1.
    AL451085 Genomic DNA. Translation: CAI13251.1.
    AL451085 Genomic DNA. Translation: CAI13254.1. Sequence problems.
    CH471121 Genomic DNA. Translation: EAW53168.1.
    CH471121 Genomic DNA. Translation: EAW53169.1.
    CH471121 Genomic DNA. Translation: EAW53170.1.
    CH471121 Genomic DNA. Translation: EAW53171.1.
    BC014158 mRNA. Translation: AAH14158.1.
    BC033925 mRNA. Translation: AAH33925.1.
    CCDSiCCDS1076.1. [P29353-7]
    CCDS30881.1. [P29353-1]
    CCDS44233.1. [P29353-6]
    CCDS44234.1. [P29353-2]
    PIRiS25776.
    RefSeqiNP_001123512.1. NM_001130040.1. [P29353-6]
    NP_001123513.1. NM_001130041.1. [P29353-2]
    NP_001189788.1. NM_001202859.1. [P29353-3]
    NP_003020.2. NM_003029.4. [P29353-7]
    NP_892113.4. NM_183001.4. [P29353-1]
    UniGeneiHs.433795.

    Genome annotation databases

    EnsembliENST00000368445; ENSP00000357430; ENSG00000160691. [P29353-1]
    ENST00000368450; ENSP00000357435; ENSG00000160691. [P29353-2]
    ENST00000368453; ENSP00000357438; ENSG00000160691. [P29353-7]
    ENST00000448116; ENSP00000401303; ENSG00000160691. [P29353-6]
    GeneIDi6464.
    KEGGihsa:6464.
    UCSCiuc001ffv.3. human. [P29353-1]
    uc001ffw.3. human. [P29353-6]
    uc001ffx.3. human. [P29353-7]

    Polymorphism databases

    DMDMi182676455.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68148 mRNA. Translation: CAA48251.1 .
    U73377 mRNA. Translation: AAB49972.1 .
    Y09847 Genomic DNA. Translation: CAA70977.1 .
    AK292143 mRNA. Translation: BAF84832.1 .
    AK315842 mRNA. Translation: BAF98733.1 .
    AB451255 mRNA. Translation: BAG70069.1 .
    AB451379 mRNA. Translation: BAG70193.1 .
    AL451085 Genomic DNA. Translation: CAI13248.1 .
    AL451085 Genomic DNA. Translation: CAI13249.1 .
    AL451085 Genomic DNA. Translation: CAI13250.1 .
    AL451085 Genomic DNA. Translation: CAI13251.1 .
    AL451085 Genomic DNA. Translation: CAI13254.1 . Sequence problems.
    CH471121 Genomic DNA. Translation: EAW53168.1 .
    CH471121 Genomic DNA. Translation: EAW53169.1 .
    CH471121 Genomic DNA. Translation: EAW53170.1 .
    CH471121 Genomic DNA. Translation: EAW53171.1 .
    BC014158 mRNA. Translation: AAH14158.1 .
    BC033925 mRNA. Translation: AAH33925.1 .
    CCDSi CCDS1076.1. [P29353-7 ]
    CCDS30881.1. [P29353-1 ]
    CCDS44233.1. [P29353-6 ]
    CCDS44234.1. [P29353-2 ]
    PIRi S25776.
    RefSeqi NP_001123512.1. NM_001130040.1. [P29353-6 ]
    NP_001123513.1. NM_001130041.1. [P29353-2 ]
    NP_001189788.1. NM_001202859.1. [P29353-3 ]
    NP_003020.2. NM_003029.4. [P29353-7 ]
    NP_892113.4. NM_183001.4. [P29353-1 ]
    UniGenei Hs.433795.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MIL X-ray 2.70 A 482-583 [» ]
    1N3H NMR - A 111-317 [» ]
    1OY2 NMR - A 111-317 [» ]
    1QG1 NMR - I 423-435 [» ]
    1SHC NMR - A 127-317 [» ]
    1TCE NMR - A 480-583 [» ]
    1WCP model - A 127-583 [» ]
    2L1C NMR - A 127-317 [» ]
    4JMH X-ray 2.41 B 344-356 [» ]
    DisProti DP00154.
    ProteinModelPortali P29353.
    SMRi P29353. Positions 111-317, 482-583.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112361. 199 interactions.
    DIPi DIP-699N.
    IntActi P29353. 83 interactions.
    MINTi MINT-123530.

    Chemistry

    BindingDBi P29353.
    ChEMBLi CHEMBL5626.

    PTM databases

    PhosphoSitei P29353.

    Polymorphism databases

    DMDMi 182676455.

    Proteomic databases

    MaxQBi P29353.
    PaxDbi P29353.
    PRIDEi P29353.

    Protocols and materials databases

    DNASUi 6464.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368445 ; ENSP00000357430 ; ENSG00000160691 . [P29353-1 ]
    ENST00000368450 ; ENSP00000357435 ; ENSG00000160691 . [P29353-2 ]
    ENST00000368453 ; ENSP00000357438 ; ENSG00000160691 . [P29353-7 ]
    ENST00000448116 ; ENSP00000401303 ; ENSG00000160691 . [P29353-6 ]
    GeneIDi 6464.
    KEGGi hsa:6464.
    UCSCi uc001ffv.3. human. [P29353-1 ]
    uc001ffw.3. human. [P29353-6 ]
    uc001ffx.3. human. [P29353-7 ]

    Organism-specific databases

    CTDi 6464.
    GeneCardsi GC01M154934.
    HGNCi HGNC:10840. SHC1.
    HPAi CAB005374.
    CAB016305.
    HPA001844.
    MIMi 600560. gene.
    neXtProti NX_P29353.
    PharmGKBi PA35746.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG315087.
    HOVERGENi HBG050121.
    KOi K06279.
    OMAi ESPTTLC.
    OrthoDBi EOG7MD4QK.
    PhylomeDBi P29353.
    TreeFami TF315807.

    Enzyme and pathway databases

    Reactomei REACT_115852. Signaling by constitutively active EGFR.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116005. SHC1 events in ERBB4 signaling.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12033. Signalling to RAS.
    REACT_12579. SHC1 events in EGFR signaling.
    REACT_12621. Tie2 Signaling.
    REACT_147814. DAP12 signaling.
    REACT_150139. SHC-related events triggered by IGF1R.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_1661. SHC activation.
    REACT_18273. XBP1(S) activates chaperone genes.
    REACT_21374. SHC-mediated cascade.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_27283. Interleukin-2 signaling.
    REACT_508. Signal attenuation.
    REACT_661. SHC-mediated signalling.
    SignaLinki P29353.

    Miscellaneous databases

    ChiTaRSi SHC1. human.
    EvolutionaryTracei P29353.
    GeneWikii SHC1.
    GenomeRNAii 6464.
    NextBioi 25115.
    PROi P29353.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29353.
    Bgeei P29353.
    Genevestigatori P29353.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR006019. PID_Shc-like.
    IPR006020. PTB/PI_dom.
    IPR000980. SH2.
    [Graphical view ]
    Pfami PF00640. PID. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00629. SHCPIDOMAIN.
    SMARTi SM00462. PTB. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 1 hit.
    PROSITEi PS01179. PID. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction."
      Pelicci G., Lanfrancone L., Grignani F., McGlade J., Cavallo F., Forni G., Nicoletti I., Grignani F., Pawson T., Pelicci P.-G.
      Cell 70:93-104(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P46SHC AND P52SHC).
    2. "Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on the EGF receptor-MAP kinase-fos signalling pathway."
      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.
      EMBO J. 16:706-716(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P66SHC).
    3. "Characterization of human SHC p66 cDNA and its processed pseudogene mapping to Xq12-q13.1."
      Harun R.B., Smith K.K., Leek J.P., Markham A.F., Norris A., Morrison J.F.
      Genomics 42:349-352(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Fibroblast.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P52SHC).
      Tissue: Mammary gland and Synovium.
    5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      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.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    6. "The DNA sequence and biological annotation of human chromosome 1."
      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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P52SHC AND 7).
      Tissue: Choriocarcinoma and Neuroblastoma.
    9. "Direct interaction between Shc and the platelet-derived growth factor beta-receptor."
      Yokote K., Mori S., Hansen K., McGlade J., Pawson T., Heldin C.H., Claesson-Welsh L.
      J. Biol. Chem. 269:15337-15343(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB AND GRB2, PHOSPHORYLATION.
    10. "Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses."
      Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A., Kaplan D.R.
      Neuron 12:691-705(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NTRK1.
    11. "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."
      Craparo A., O'Neill T.J., Gustafson T.A.
      J. Biol. Chem. 270:15639-15643(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGF1R.
    12. "Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via non-SH2 domains."
      He W., O'Neill T.J., Gustafson T.A.
      J. Biol. Chem. 270:23258-23262(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INSR.
    13. "Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain."
      Gustafson T.A., He W., Craparo A., Schaub C.D., O'Neill T.J.
      Mol. Cell. Biol. 15:2500-2508(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INSR.
    14. "Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation."
      Ware M.D., Rosten P., Damen J.E., Liu L., Humphries R.K., Krystal G.
      Blood 88:2833-2840(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    15. "The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions."
      van der Geer P., Wiley S., Gish G.D., Pawson T.
      Curr. Biol. 6:1435-1444(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-349 AND TYR-350.
    16. "Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors."
      Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.
      J. Biol. Chem. 271:30942-30949(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB7.
    17. "Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes."
      Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.
      J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIT.
    18. "Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src."
      Schlaepfer D.D., Hunter T.
      J. Biol. Chem. 272:13189-13195(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    19. "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."
      Gotoh N., Toyoda M., Shibuya M.
      Mol. Cell. Biol. 17:1824-1831(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-349; TYR-350 AND TYR-427.
    20. "Cloning and characterization of APS, an adaptor molecule containing PH and SH2 domains that is tyrosine phosphorylated upon B-cell receptor stimulation."
      Yokouchi M., Suzuki R., Masuhara M., Komiya S., Inoue A., Yoshimura A.
      Oncogene 15:7-15(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APS.
    21. "Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein."
      Habib T., Hejna J.A., Moses R.E., Decker S.J.
      J. Biol. Chem. 273:18605-18609(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D AND INPPL1.
    22. "Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase."
      Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.
      Mol. Cell. Biol. 18:1622-1634(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2, MUTAGENESIS OF TYR-349 AND TYR-427, INTERACTION WITH GRB2.
    23. "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."
      Schlaepfer D.D., Jones K.C., Hunter T.
      Mol. Cell. Biol. 18:2571-2585(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-349; TYR-350 AND TYR-427.
    24. "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."
      Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H., Geromanos S., Kavanaugh W.M., Tempst P., Clarkson B.
      Blood 93:2707-2720(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPPL1.
    25. "Ligand discrimination in signaling through an ErbB4 receptor homodimer."
      Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C., Carraway K.L. III
      J. Biol. Chem. 275:19803-19807(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB4.
    26. "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."
      Pesesse X., Dewaste V., De Smedt F., Laffargue M., Giuriato S., Moreau C., Payrastre B., Erneux C.
      J. Biol. Chem. 276:28348-28355(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPPL1.
    27. "Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples."
      Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr., Gladson C.L.
      Cancer Res. 62:2699-2707(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION.
    28. "The p66Shc longevity gene is silenced through epigenetic modifications of an alternative promoter."
      Ventura A., Luzi L., Pacini S., Baldari C.T., Pelicci P.-G.
      J. Biol. Chem. 277:22370-22376(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE.
    29. "EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis."
      Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.
      J. Cell Biol. 162:661-671(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPHB1 AND GRB2.
    30. Cited for: INTERACTION WITH NTRK1.
    31. "Signal transduction via the stem cell factor receptor/c-Kit."
      Ronnstrand L.
      Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN KIT SIGNALING, PHOSPHORYLATION.
    32. "Adaptor ShcA protein binds tyrosine kinase Tie2 receptor and regulates migration and sprouting but not survival of endothelial cells."
      Audero E., Cascone I., Maniero F., Napione L., Arese M., Lanfrancone L., Bussolino F.
      J. Biol. Chem. 279:13224-13233(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH TEK.
    33. "Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress."
      Wang J.F., Zhang X., Groopman J.E.
      J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT4.
    34. "Tyrosine phosphoproteomics of fibroblast growth factor signaling: a role for insulin receptor substrate-4."
      Hinsby A.M., Olsen J.V., Mann M.
      J. Biol. Chem. 279:46438-46447(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRS4.
    35. "A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria."
      Ventura A., Maccarana M., Raker V.A., Pelicci P.-G.
      J. Biol. Chem. 279:2299-2306(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORM P46SHC).
    36. "Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase Calpha regulates endocytosis and association with adaptor molecules."
      Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F., Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K.
      J. Biol. Chem. 279:40536-40544(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRP1.
    37. "Phosphorylation of p66Shc and forkhead proteins mediates Abeta toxicity."
      Smith W.W., Norton D.D., Gorospe M., Jiang H., Nemoto S., Holbrook N.J., Finkel T., Kusiak J.W.
      J. Cell Biol. 169:331-339(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-36.
    38. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      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.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    40. "ALK activation induces Shc and FRS2 recruitment: Signaling and phenotypic outcomes in PC12 cells differentiation."
      Degoutin J., Vigny M., Gouzi J.Y.
      FEBS Lett. 581:727-734(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALK, PHOSPHORYLATION.
    41. "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
      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.
      EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAB2.
    42. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND TYR-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    43. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    44. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    45. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    46. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    47. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    48. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    49. "Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide binding based on X-ray and NMR data."
      Mikol V., Baumann G., Zurini M.G.M., Hommel U.
      J. Mol. Biol. 254:86-95(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 482-583.
    50. Cited for: STRUCTURE BY NMR OF 127-317.
    51. "Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor."
      Zhou M.-M., Meadows R.P., Logan T.M., Yoon H.S., Wade W.S., Ravichandran K.S., Burakoff S.J., Fesik S.W.
      Proc. Natl. Acad. Sci. U.S.A. 92:7784-7788(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 480-583 IN COMPLEX WITH TYROSINE-PHOSPHORYLATED CD3Z.

    Entry informationi

    Entry nameiSHC1_HUMAN
    AccessioniPrimary (citable) accession number: P29353
    Secondary accession number(s): B5BU19
    , D3DV78, O15290, Q5T180, Q5T183, Q5T184, Q5T185, Q5T186, Q8N4K5, Q96CL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 176 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3