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P98083 (SHC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Shc1
Synonyms:Shc, ShcA
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 p52may 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. Ref.18 Ref.21

Subunit structure

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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.22

Subcellular location

Cytoplasm By similarity Ref.21.

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. Ref.21

Isoform p66Shc: Mitochondrion. Note: In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation. Ref.21

Tissue specificity

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

Domain

In response to a variety of growth factors, isoform p47Shc and isoform p52bind 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.

Post-translational modification

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. Ref.8 Ref.14 Ref.21

Sequence similarities

Contains 1 PID domain.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processAngiogenesis
Growth regulation
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityAlternative initiation
Alternative splicing
   DomainSH2 domain
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from mutant phenotype PubMed 10809671. Source: MGI

activation of MAPK activity

Inferred from sequence or structural similarity. Source: UniProtKB

angiogenesis

Inferred from mutant phenotype PubMed 10809671. Source: MGI

heart development

Inferred from mutant phenotype PubMed 10809671. Source: MGI

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

single organismal cell-cell adhesion

Inferred from mutant phenotype PubMed 10809671. Source: MGI

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionephrin receptor binding

Inferred from physical interaction Ref.17. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10748054PubMed 15102471PubMed 17673906PubMed 18273058PubMed 20075861PubMed 23452850PubMed 7529871PubMed 7535773PubMed 17673906PubMed 17673906. Source: IntAct

receptor tyrosine kinase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Note: In human, it is alternative promoter usage that produces such isoforms.
Isoform p66Shc (identifier: P98083-1)

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.
Isoform p52Shc (identifier: P98083-2)

Also known as: p52;

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: Missing.
Note: Produced by alternative splicing.
Isoform p47Shc (identifier: P98083-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579SHC-transforming protein 1
PRO_0000022339

Regions

Domain156 – 339184PID
Domain484 – 57592SH2
Region340 – 483144CH1
Compositional bias408 – 47063Pro-rich

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue361Phosphoserine; in isoform p66Shc Ref.8 Ref.21
Modified residue1391Phosphoserine Ref.23
Modified residue1541N6-acetyllysine Ref.24
Modified residue3491Phosphotyrosine
Modified residue3501Phosphotyrosine
Modified residue4221Phosphoserine By similarity
Modified residue4231Phosphotyrosine Ref.20 Ref.23

Natural variations

Alternative sequence1 – 155155Missing in isoform p47Shc.
VSP_018792
Alternative sequence1 – 110110Missing in isoform p52Shc.
VSP_018791

Sequences

Sequence LengthMass (Da)Tools
Isoform p66Shc (p66) [UniParc].

Last modified May 27, 2002. Version 3.
Checksum: 99C22E64412B6236

FASTA57962,608
        10         20         30         40         50         60 
MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP GDDSPTTLCS 

        70         80         90        100        110        120 
FFPRMSNLKL ANPAGGRLGP KGEPGKAAED GEGSAGAALR DSGLLPLLQD MNKLSGGGGR 

       130        140        150        160        170        180 
RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH PNDKVMGPGV SYLVRYMGCV EVLQSMRALD 

       190        200        210        220        230        240 
FNTRTQVTRE AISLVCEAVP GAKGATRRRK PCSRPLSSIL GRSNLKFAGM PITLTVSTSS 

       250        260        270        280        290        300 
LNLMAADCKQ IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL ECPEGLAQDV 

       310        320        330        340        350        360 
ISTIGQAFEL RFKQYLRNPP KLVTPHDRMA GFDGSAWDEE EEEPPDHQYY NDFPGKEPPL 

       370        380        390        400        410        420 
GGVVDMRLRE GAARPTLPSA QMSSHLGATL PIGQHAAGDH EVRKQMLPPP PCPGRELFDD 

       430        440        450        460        470        480 
PSYVNIQNLD KARQAGGGAG PPNPSLNGSA PRDLFDMKPF EDALRVPPPP QSMSMAEQLQ 

       490        500        510        520        530        540 
GEPWFHGKLS RREAEALLQL NGDFLVREST TTPGQYVLTG LQSGQPKHLL LVDPEGVVRT 

       550        560        570 
KDHRFESVSH LISYHMDNHL PIISAGSELC LQQPVDRKV 

« Hide

Isoform p52Shc (p52) [UniParc].

Checksum: DF33594E80107A3E
Show »

FASTA46951,409
Isoform p47Shc (p47) [UniParc].

Checksum: 5064FFF6CE5BD930
Show »

FASTA42446,467

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17508.1. [P98083-2]
CCDS50962.1. [P98083-1]
PIRA55484.
RefSeqNP_001106802.1. NM_001113331.2. [P98083-1]
NP_035498.2. NM_011368.5. [P98083-2]
UniGeneMm.86595.

3D structure databases

ProteinModelPortalP98083.
SMRP98083. Positions 111-317, 478-579.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203215. 21 interactions.
DIPDIP-271N.
DIP-29912N.
IntActP98083. 26 interactions.
MINTMINT-127650.

PTM databases

PhosphoSiteP98083.

Proteomic databases

MaxQBP98083.
PaxDbP98083.
PRIDEP98083.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000039110; ENSMUSP00000035361; ENSMUSG00000042626. [P98083-2]
ENSMUST00000094378; ENSMUSP00000091940; ENSMUSG00000042626. [P98083-1]
ENSMUST00000107417; ENSMUSP00000103040; ENSMUSG00000042626. [P98083-3]
GeneID20416.
KEGGmmu:20416.
UCSCuc008pzm.2. mouse. [P98083-1]

Organism-specific databases

CTD6464.
MGIMGI:98296. Shc1.

Phylogenomic databases

eggNOGNOG315087.
GeneTreeENSGT00390000018860.
HOGENOMHOG000231974.
HOVERGENHBG050121.
InParanoidP98083.
KOK06279.
OMAESPTTLC.
OrthoDBEOG7MD4QK.
PhylomeDBP98083.
TreeFamTF315807.

Gene expression databases

ArrayExpressP98083.
BgeeP98083.
GenevestigatorP98083.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR011993. PH_like_dom.
IPR006019. PID_Shc-like.
IPR006020. PTB/PI_dom.
IPR000980. SH2.
[Graphical view]
PfamPF00640. PID. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00629. SHCPIDOMAIN.
SMARTSM00462. PTB. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
PROSITEPS01179. PID. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSHC1. mouse.
NextBio298412.
PROP98083.
SOURCESearch...

Entry information

Entry nameSHC1_MOUSE
AccessionPrimary (citable) accession number: P98083
Secondary accession number(s): Q3U2Q7 expand/collapse secondary AC list , Q8BFY3, Q8K4C6, Q8K4C7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 27, 2002
Last modified: July 9, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot