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P98083

- SHC1_MOUSE

UniProt

P98083 - SHC1_MOUSE

Protein

SHC-transforming protein 1

Gene

Shc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (27 May 2002)
      Previous versions | rss
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    Functioni

    Signaling adapter that couples activated growth factor receptors to signaling pathways. 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 similarity. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p47Shc and isoform p52Shc, once phosphorylated, couple activated receptor kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p47Shc and isoform p52 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 similarity2 Publications

    GO - Molecular functioni

    1. ephrin receptor binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. receptor tyrosine kinase binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: MGI
    2. activation of MAPK activity Source: UniProtKB
    3. angiogenesis Source: MGI
    4. heart development Source: MGI
    5. MAPK cascade Source: UniProtKB
    6. regulation of growth Source: UniProtKB-KW
    7. single organismal cell-cell adhesion Source: MGI

    Keywords - Biological processi

    Angiogenesis, Growth regulation

    Enzyme and pathway databases

    ReactomeiREACT_106572. XBP1(S) activates chaperone genes.
    REACT_188185. DAP12 signaling.
    REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188220. SHC-related events triggered by IGF1R.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_188574. SHC1 events in ERBB2 signaling.
    REACT_188580. SHC1 events in ERBB4 signaling.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_210793. Interleukin receptor SHC signaling.
    REACT_211860. Tie2 Signaling.
    REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_94437. SHC-mediated cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SHC-transforming protein 1
    Alternative name(s):
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:98296. Shc1.

    Subcellular locationi

    Cytoplasm By similarity
    Isoform p47Shc : Mitochondrion matrix By similarity
    Note: Targeting of isoform p47Shc 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 By similarity.By similarity
    Isoform p66Shc : Mitochondrion 1 Publication
    Note: In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 579579SHC-transforming protein 1PRO_0000022339Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei36 – 361Phosphoserine; in isoform p66Shc2 Publications
    Modified residuei139 – 1391Phosphoserine2 Publications
    Modified residuei154 – 1541N6-acetyllysine1 Publication
    Modified residuei349 – 3491Phosphotyrosine1 Publication
    Modified residuei350 – 3501Phosphotyrosine1 Publication
    Modified residuei422 – 4221PhosphoserineBy similarity
    Modified residuei423 – 4231Phosphotyrosine3 Publications

    Post-translational modificationi

    Phosphorylated in response to FLT4 signaling By similarity. Tyrosine phosphorylated by ligand-activated PDGFRB By similarity. May be tyrosine phosphorylated by activated PTK2/FAK1 By similarity. Tyrosine phosphorylated by TEK/TIE2 By similarity. Tyrosine phosphorylated by activated PTK2B/PYK2 By similarity. Dephosphorylation by PTPN2 may regulate interaction with GRB2 By similarity. Phosphorylated by activated epidermal growth factor receptor. Phosphorylated in response to KIT signaling. Isoform p47Shc 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. FLT3 signaling promotes tyrosine phosphorylation of isoform p47Shc and isoform p52Shc. Also tyrosine phosphorylated by ligand-activated ALK.By similarity4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP98083.
    PaxDbiP98083.
    PRIDEiP98083.

    PTM databases

    PhosphoSiteiP98083.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP98083.
    BgeeiP98083.
    GenevestigatoriP98083.

    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 DDR2 and CD3T. Interacts with the N-terminal region of APS. Interacts with GRB7 and KIT By similarity. Interacts with PTK2/FAK1 By similarity. Interacts with phosphorylated LRP1 and IRS4. Interacts with FLT4 (tyrosine-phosphorylated) By similarity. Interacts with PDGFRB (tyrosine-phosphorylated). Interacts with ERBB4 By similarity. Interacts with TEK/TIE2 (tyrosine-phosphorylated) By similarity. Interacts with ALK, GAB2, TRIM31, INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with PTPN6/SHP (tyrosine phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with EPHB1 and GRB2; activates the MAPK/ERK cascade to regulate cell migration. Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; in a phosphotyrosine-dependent manner.By similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Amd1P311547EBI-300201,EBI-644529
    Grb2Q606317EBI-300201,EBI-1688
    Iqgap1Q9JKF15EBI-300201,EBI-644633
    Ptpn12P358312EBI-300201,EBI-2642957
    Shcbp1Q9Z1795EBI-300201,EBI-644352
    Tgfbr1Q647293EBI-1019301,EBI-2899393
    Tgfbr2Q623123EBI-1019301,EBI-2899332

    Protein-protein interaction databases

    BioGridi203215. 21 interactions.
    DIPiDIP-271N.
    DIP-29912N.
    IntActiP98083. 26 interactions.
    MINTiMINT-127650.

    Structurei

    3D structure databases

    ProteinModelPortaliP98083.
    SMRiP98083. Positions 111-317, 478-579.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini156 – 339184PIDPROSITE-ProRule annotationAdd
    BLAST
    Domaini484 – 57592SH2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni340 – 483144CH1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi408 – 47063Pro-richAdd
    BLAST

    Domaini

    In response to a variety of growth factors, isoform p47Shc and isoform p52 bind to phosphorylated 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. Isoform p47Shc 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.

    Sequence similaritiesi

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

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG315087.
    GeneTreeiENSGT00390000018860.
    HOGENOMiHOG000231974.
    HOVERGENiHBG050121.
    InParanoidiP98083.
    KOiK06279.
    OMAiESPTTLC.
    OrthoDBiEOG7MD4QK.
    PhylomeDBiP98083.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. Align

    Note: In human, it is alternative promoter usage that produces such isoforms.

    Isoform p66Shc (identifier: P98083-1) [UniParc]FASTAAdd to Basket

    Also known as: p66

    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 FFPRMSNLKL ANPAGGRLGP KGEPGKAAED GEGSAGAALR 100
    DSGLLPLLQD 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 GAARPTLPSA QMSSHLGATL PIGQHAAGDH 400
    EVRKQMLPPP PCPGRELFDD PSYVNIQNLD KARQAGGGAG PPNPSLNGSA 450
    PRDLFDMKPF EDALRVPPPP QSMSMAEQLQ GEPWFHGKLS RREAEALLQL 500
    NGDFLVREST TTPGQYVLTG LQSGQPKHLL LVDPEGVVRT KDHRFESVSH 550
    LISYHMDNHL PIISAGSELC LQQPVDRKV 579
    Length:579
    Mass (Da):62,608
    Last modified:May 27, 2002 - v3
    Checksum:i99C22E64412B6236
    GO
    Isoform p52Shc (identifier: P98083-2) [UniParc]FASTAAdd to Basket

    Also known as: p52

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

    Note: Produced by alternative splicing.

    Show »
    Length:469
    Mass (Da):51,409
    Checksum:iDF33594E80107A3E
    GO
    Isoform p47Shc (identifier: P98083-3) [UniParc]FASTAAdd to Basket

    Also known as: p47

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

    Note: Produced by alternative initiation at Met-46 of isoform p52.

    Show »
    Length:424
    Mass (Da):46,467
    Checksum:i5064FFF6CE5BD930
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 155155Missing in isoform p47Shc. CuratedVSP_018792Add
    BLAST
    Alternative sequencei1 – 110110Missing in isoform p52Shc. 3 PublicationsVSP_018791Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46956 Genomic DNA. Translation: AAA91777.2.
    U15784 mRNA. Translation: AAC52146.1.
    AK049357 mRNA. Translation: BAC33706.1.
    AK155158 mRNA. Translation: BAE33083.1.
    BC036172 mRNA. Translation: AAH36172.1.
    AF455140 Genomic DNA. Translation: AAM61857.1.
    AF455140 Genomic DNA. Translation: AAM61858.1.
    CCDSiCCDS17508.1. [P98083-2]
    CCDS50962.1. [P98083-1]
    PIRiA55484.
    RefSeqiNP_001106802.1. NM_001113331.2. [P98083-1]
    NP_035498.2. NM_011368.5. [P98083-2]
    UniGeneiMm.86595.

    Genome annotation databases

    EnsembliENSMUST00000039110; ENSMUSP00000035361; ENSMUSG00000042626. [P98083-2]
    ENSMUST00000094378; ENSMUSP00000091940; ENSMUSG00000042626. [P98083-1]
    ENSMUST00000107417; ENSMUSP00000103040; ENSMUSG00000042626. [P98083-3]
    GeneIDi20416.
    KEGGimmu:20416.
    UCSCiuc008pzm.2. mouse. [P98083-1]

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46956 Genomic DNA. Translation: AAA91777.2 .
    U15784 mRNA. Translation: AAC52146.1 .
    AK049357 mRNA. Translation: BAC33706.1 .
    AK155158 mRNA. Translation: BAE33083.1 .
    BC036172 mRNA. Translation: AAH36172.1 .
    AF455140 Genomic DNA. Translation: AAM61857.1 .
    AF455140 Genomic DNA. Translation: AAM61858.1 .
    CCDSi CCDS17508.1. [P98083-2 ]
    CCDS50962.1. [P98083-1 ]
    PIRi A55484.
    RefSeqi NP_001106802.1. NM_001113331.2. [P98083-1 ]
    NP_035498.2. NM_011368.5. [P98083-2 ]
    UniGenei Mm.86595.

    3D structure databases

    ProteinModelPortali P98083.
    SMRi P98083. Positions 111-317, 478-579.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203215. 21 interactions.
    DIPi DIP-271N.
    DIP-29912N.
    IntActi P98083. 26 interactions.
    MINTi MINT-127650.

    PTM databases

    PhosphoSitei P98083.

    Proteomic databases

    MaxQBi P98083.
    PaxDbi P98083.
    PRIDEi P98083.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000039110 ; ENSMUSP00000035361 ; ENSMUSG00000042626 . [P98083-2 ]
    ENSMUST00000094378 ; ENSMUSP00000091940 ; ENSMUSG00000042626 . [P98083-1 ]
    ENSMUST00000107417 ; ENSMUSP00000103040 ; ENSMUSG00000042626 . [P98083-3 ]
    GeneIDi 20416.
    KEGGi mmu:20416.
    UCSCi uc008pzm.2. mouse. [P98083-1 ]

    Organism-specific databases

    CTDi 6464.
    MGIi MGI:98296. Shc1.

    Phylogenomic databases

    eggNOGi NOG315087.
    GeneTreei ENSGT00390000018860.
    HOGENOMi HOG000231974.
    HOVERGENi HBG050121.
    InParanoidi P98083.
    KOi K06279.
    OMAi ESPTTLC.
    OrthoDBi EOG7MD4QK.
    PhylomeDBi P98083.
    TreeFami TF315807.

    Enzyme and pathway databases

    Reactomei REACT_106572. XBP1(S) activates chaperone genes.
    REACT_188185. DAP12 signaling.
    REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188220. SHC-related events triggered by IGF1R.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_188574. SHC1 events in ERBB2 signaling.
    REACT_188580. SHC1 events in ERBB4 signaling.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_210793. Interleukin receptor SHC signaling.
    REACT_211860. Tie2 Signaling.
    REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_94437. SHC-mediated cascade.

    Miscellaneous databases

    ChiTaRSi SHC1. mouse.
    NextBioi 298412.
    PROi P98083.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P98083.
    Bgeei P98083.
    Genevestigatori P98083.

    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. Blaikie P.A., Yajnik V., Margolis B.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM P66SHC).
    2. "A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors."
      Blaikie P.A., Immanuel D., Wu J., Li N., Yajnik V., Margolis B.
      J. Biol. Chem. 269:32031-32034(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P52SHC).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P52SHC AND P66SHC).
      Strain: C57BL/6J and NOD.
    4. "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] (ISOFORM P52SHC).
      Strain: FVB/N.
      Tissue: Colon.
    5. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-165 (ISOFORMS P66SHC AND P52SHC).
      Strain: 129/SvJ.
    6. "p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity."
      Lioubin M.N., Algate P.A., Tsai S., Carlberg K., Aebersold A., Rohrschneider L.R.
      Genes Dev. 10:1084-1095(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    7. "The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase."
      Damen J.E., Liu L., Rosten P., Humphries R.K., Jefferson A.B., Majerus P.W., Krystal G.
      Proc. Natl. Acad. Sci. U.S.A. 93:1689-1693(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    8. "Insulin stimulates the phosphorylation of the 66- and 52-kilodalton Shc isoforms by distinct pathways."
      Kao A.W., Waters S.B., Okada S., Pessin J.E.
      Endocrinology 138:2474-2480(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-36.
    9. "The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis."
      Liu L., Damen J.E., Hughes M.R., Babic I., Jirik F.R., Krystal G.
      J. Biol. Chem. 272:8983-8988(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    10. "Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP."
      Lamkin T.D., Walk S.F., Liu L., Damen J.E., Krystal G., Ravichandran K.S.
      J. Biol. Chem. 272:10396-10401(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPPL1.
    11. "Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation."
      Gu H., Pratt J.C., Burakoff S.J., Neel B.G.
      Mol. Cell 2:729-740(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAB2.
    12. "Role of SHIP in FcgammaRIIb-mediated inhibition of Ras activation in B cells."
      Tridandapani S., Phee H., Shivakumar L., Kelley T.W., Coggeshall K.M.
      Mol. Immunol. 35:1135-1146(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    13. "A novel spliced form of SH2-containing inositol phosphatase is expressed during myeloid development."
      Lucas D.M., Rohrschneider L.R.
      Blood 93:1922-1933(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    14. "Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells."
      Zhang S., Mantel C., Broxmeyer H.E.
      J. Leukoc. Biol. 65:372-380(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING, INTERACTION WITH GRB2 AND PTPN6/SHP.
    15. "N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling."
      Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.
      Nat. Cell Biol. 3:650-657(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; SRC; SHC1; FGFR4 AND CTTN.
    16. "Mechanism of TrkB-mediated hippocampal long-term potentiation."
      Minichiello L., Calella A.M., Medina D.L., Bonhoeffer T., Klein R., Korte M.
      Neuron 36:121-137(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NTRK2.
    17. "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.
    18. "Deletion of the p66Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet."
      Napoli C., Martin-Padura I., de Nigris F., Giorgio M., Mansueto G., Somma P., Condorelli M., Sica G., De Rosa G., Pelicci P.-G.
      Proc. Natl. Acad. Sci. U.S.A. 100:2112-2116(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "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].
    20. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    21. "Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc."
      Pinton P., Rimessi A., Marchi S., Orsini F., Migliaccio E., Giorgio M., Contursi C., Minucci S., Mantovani F., Wieckowski M.R., Del Sal G., Pelicci P.G., Rizzuto R.
      Science 315:659-663(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORM P66SHC), PHOSPHORYLATION AT SER-36 (ISOFORM P66SHC).
    22. "TRIM31 interacts with p52(Shc) and inhibits Src-induced anchorage-independent growth."
      Watanabe M., Tsukiyama T., Hatakeyama S.
      Biochem. Biophys. Res. Commun. 388:422-427(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM31.
    23. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND TYR-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSHC1_MOUSE
    AccessioniPrimary (citable) accession number: P98083
    Secondary accession number(s): Q3U2Q7
    , Q8BFY3, Q8K4C6, Q8K4C7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: May 27, 2002
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3