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P29353 (SHC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SHC1
Synonyms:SHC, SHCA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length583 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 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. Ref.32

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 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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.32 Ref.33 Ref.34 Ref.36 Ref.40 Ref.41

Subcellular location

Cytoplasm Ref.35.

Isoform p46Shc: Mitochondrion matrix. 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. Ref.35

Isoform p66Shc: Mitochondrion By similarity. Note: In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation By similarity. Ref.35

Tissue specificity

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

Domain

In response to a variety of growth factors, isoform p46Shc and isoform p52Shc bind to phosphorylated Trk receptors through their phosphotyrosine binding (PID) and/or SH2 domains. The PID and SH2 domains bind to specific phosphorylated tyrosine residues in the Asn-Pro-Xaa-Tyr(P) motif of the Trk receptors. Isoform p46Shc and isoform p52Shc are in turn phosphorylated on three tyrosine residues within the extended proline-rich domain. These phosphotyrosines act as docking site for GRB2 and thereby are involved in Ras activation By similarity.

Post-translational modification

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. Ref.9 Ref.15 Ref.18 Ref.19 Ref.22 Ref.23 Ref.27 Ref.31 Ref.32 Ref.37 Ref.40

Sequence similarities

Contains 1 PID domain.

Contains 1 SH2 domain.

Sequence caution

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

Ontologies

Keywords
   Biological processAngiogenesis
Growth regulation
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DomainSH2 domain
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MAPK cascade

Inferred from direct assay PubMed 14676841. Source: UniProtKB

Ras protein signal transduction

Traceable author statement. Source: Reactome

actin cytoskeleton reorganization

Inferred from electronic annotation. Source: Ensembl

activation of MAPK activity

Inferred from direct assay PubMed 14676841. Source: UniProtKB

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

blood coagulation

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

heart development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

leukocyte migration

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-tyrosine phosphorylation

Traceable author statement. Source: GOC

platelet activation

Traceable author statement. Source: Reactome

positive regulation of DNA replication

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell proliferation

Non-traceable author statement PubMed 14676841. Source: UniProtKB

regulation of epidermal growth factor-activated receptor activity

Traceable author statement Ref.1. Source: ProtInc

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

single organismal cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentShc-EGFR complex

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 14676841. Source: UniProtKB

   Molecular_functionephrin receptor binding

Inferred from physical interaction Ref.29. Source: UniProtKB

epidermal growth factor receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

insulin receptor binding

Inferred from physical interaction Ref.13Ref.12. Source: UniProtKB

insulin-like growth factor receptor binding

Inferred from physical interaction Ref.11. Source: UniProtKB

neurotrophin TRKA receptor binding

Inferred from physical interaction Ref.30. Source: UniProtKB

phospholipid binding

Traceable author statement PubMed 14676841. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16520382Ref.11. Source: IntAct

protein tyrosine kinase activity

Traceable author statement. Source: Reactome

transmembrane receptor protein tyrosine kinase adaptor activity

Traceable author statement PubMed 14676841. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform p66Shc (identifier: P29353-1)

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.
Note: Regulated by epigenetic modifications of its promoter region.
Isoform p52Shc (identifier: P29353-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: Missing.
Isoform p46Shc (identifier: P29353-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-155: Missing.
Isoform 5 (identifier: P29353-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-214: Missing.
     215-221: PLSSILG → MSLCHRW
Note: Produced by alternative splicing.
Isoform 6 (identifier: P29353-6)

The sequence of this isoform differs from the canonical sequence as follows:
     417-417: P → PA
Note: Produced by alternative splicing.
Isoform 7 (identifier: P29353-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 583583SHC-transforming protein 1
PRO_0000097731

Regions

Domain156 – 339184PID
Domain488 – 57992SH2
Region340 – 487148CH1
Compositional bias411 – 47464Pro-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.48
Modified residue361Phosphoserine Ref.37
Modified residue1391Phosphoserine Ref.39 Ref.42 Ref.47
Modified residue1541N6-acetyllysine By similarity
Modified residue3491Phosphotyrosine Ref.15 Ref.19 Ref.23
Modified residue3501Phosphotyrosine Ref.15 Ref.19 Ref.23
Modified residue4261Phosphoserine
Modified residue4271Phosphotyrosine Ref.19 Ref.23 Ref.42 Ref.44

Natural variations

Alternative sequence1 – 214214Missing in isoform 5.
VSP_040090
Alternative sequence1 – 155155Missing in isoform p46Shc.
VSP_016107
Alternative sequence1 – 110110Missing in isoform p52Shc and isoform 7.
VSP_016108
Alternative sequence215 – 2217PLSSILG → MSLCHRW in isoform 5.
VSP_040091
Alternative sequence4171P → PA in isoform 7 and isoform 6.
VSP_040092
Natural variant2051A → V.
Corresponds to variant rs8191981 [ dbSNP | Ensembl ].
VAR_042428
Natural variant4101M → V.
Corresponds to variant rs8191979 [ dbSNP | Ensembl ].
VAR_051353

Experimental info

Mutagenesis3491Y → F: Alters interaction with GRB2; isoform p52Shc (in vitro). Ref.22
Mutagenesis4271Y → F: No effect on interaction with GRB2; isoform p52Shc (in vitro). Ref.22
Sequence conflict21D → N in CAA70977. Ref.3
Sequence conflict211L → M in CAA70977. Ref.3
Sequence conflict381S → P in CAA70977. Ref.3
Sequence conflict951V → D in AAB49972. Ref.2
Sequence conflict1011D → E in AAB49972. Ref.2
Sequence conflict4301V → A in BAG70069. Ref.5
Sequence conflict4301V → A in BAG70193. Ref.5

Secondary structure

........................................................................... 583
Helix Strand Turn

Details...

Sequences

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

Last modified April 8, 2008. Version 4.
Checksum: 7EFA5CB185A548D1

FASTA58362,822
        10         20         30         40         50         60 
MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP GDDSPTTLCS 

        70         80         90        100        110        120 
FFPRMSNLRL ANPAGGRPGS KGEPGRAADD GEGIVGAAMP DSGPLPLLQD 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 GAAPGAARPT APNAQTPSHL GATLPVGQPV GGDPEVRKQM PPPPPCPGRE 

       430        440        450        460        470        480 
LFDDPSYVNV QNLDKARQAV GGAGPPNPAI NGSAPRDLFD MKPFEDALRV PPPPQSVSMA 

       490        500        510        520        530        540 
EQLRGEPWFH GKLSRREAEA LLQLNGDFLV RESTTTPGQY VLTGLQSGQP KHLLLVDPEG 

       550        560        570        580 
VVRTKDHRFE SVSHLISYHM DNHLPIISAG SELCLQQPVE RKL 

« Hide

Isoform p52Shc [UniParc].

Checksum: 6DDC519E3F318B6D
Show »

FASTA47351,611
Isoform p46Shc [UniParc].

Checksum: 099FED4690662DD5
Show »

FASTA42846,668
Isoform 5 [UniParc].

Checksum: 46F34449B556DDD0
Show »

FASTA36940,415
Isoform 6 [UniParc].

Checksum: BDB2FF81953D4FF4
Show »

FASTA58462,893
Isoform 7 [UniParc].

Checksum: 43E1D98CBA87DB37
Show »

FASTA47451,682

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma."
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A., Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A., Mackay A.R.
Cancer Cell 6:347-360(2004) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND TYR-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[43]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Structure and ligand recognition of the phosphotyrosine binding domain of Shc."
Zhou M.-M., Ravichandran K.S., Olejniczak E.F., Petros A.M., Meadows R.P., Sattler M., Harlan J.E., Wade W.S., Burakoff S.J., Fesik S.W.
Nature 378:584-592(1995) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1076.1. [P29353-7]
CCDS30881.1. [P29353-1]
CCDS44233.1. [P29353-6]
CCDS44234.1. [P29353-2]
PIRS25776.
RefSeqNP_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]
UniGeneHs.433795.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00154.
ProteinModelPortalP29353.
SMRP29353. Positions 111-317, 482-583.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112361. 199 interactions.
DIPDIP-699N.
IntActP29353. 82 interactions.
MINTMINT-123530.

Chemistry

BindingDBP29353.
ChEMBLCHEMBL5626.

PTM databases

PhosphoSiteP29353.

Polymorphism databases

DMDM182676455.

Proteomic databases

MaxQBP29353.
PaxDbP29353.
PRIDEP29353.

Protocols and materials databases

DNASU6464.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368445; ENSP00000357430; ENSG00000160691. [P29353-1]
ENST00000368450; ENSP00000357435; ENSG00000160691. [P29353-2]
ENST00000368453; ENSP00000357438; ENSG00000160691. [P29353-7]
ENST00000448116; ENSP00000401303; ENSG00000160691. [P29353-6]
GeneID6464.
KEGGhsa:6464.
UCSCuc001ffv.3. human. [P29353-1]
uc001ffw.3. human. [P29353-6]
uc001ffx.3. human. [P29353-7]

Organism-specific databases

CTD6464.
GeneCardsGC01M154934.
HGNCHGNC:10840. SHC1.
HPACAB005374.
CAB016305.
HPA001844.
MIM600560. gene.
neXtProtNX_P29353.
PharmGKBPA35746.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315087.
HOVERGENHBG050121.
KOK06279.
OMAESPTTLC.
OrthoDBEOG7MD4QK.
PhylomeDBP29353.
TreeFamTF315807.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP29353.

Gene expression databases

ArrayExpressP29353.
BgeeP29353.
GenevestigatorP29353.

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. human.
EvolutionaryTraceP29353.
GeneWikiSHC1.
GenomeRNAi6464.
NextBio25115.
PROP29353.
SOURCESearch...

Entry information

Entry nameSHC1_HUMAN
AccessionPrimary (citable) accession number: P29353
Secondary accession number(s): B5BU19 expand/collapse secondary AC list , D3DV78, O15290, Q5T180, Q5T183, Q5T184, Q5T185, Q5T186, Q8N4K5, Q96CL1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: April 8, 2008
Last modified: July 9, 2014
This is version 174 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM