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Protein

SHC-transforming protein 1

Gene

SHC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span (By similarity). Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis.By similarity1 Publication

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • epidermal growth factor binding Source: Ensembl
  • epidermal growth factor receptor binding Source: BHF-UCL
  • insulin-like growth factor receptor binding Source: UniProtKB
  • insulin receptor binding Source: UniProtKB
  • neurotrophin TRKA receptor binding Source: UniProtKB
  • phospholipid binding Source: UniProtKB
  • phosphotyrosine residue binding Source: CAFA
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: Ensembl
  • activation of MAPK activity Source: UniProtKB
  • angiogenesis Source: UniProtKB-KW
  • axon guidance Source: Reactome
  • cell-cell adhesion Source: Ensembl
  • cellular response to growth factor stimulus Source: UniProtKB
  • cytokine-mediated signaling pathway Source: Reactome
  • defense response to bacterium Source: CAFA
  • epidermal growth factor receptor signaling pathway Source: Reactome
  • ERBB2 signaling pathway Source: Reactome
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • heart development Source: Ensembl
  • insulin receptor signaling pathway Source: BHF-UCL
  • interleukin-15-mediated signaling pathway Source: Reactome
  • interleukin-2-mediated signaling pathway Source: Reactome
  • IRE1-mediated unfolded protein response Source: Reactome
  • leukocyte migration Source: Reactome
  • MAPK cascade Source: UniProtKB
  • negative regulation of angiogenesis Source: BHF-UCL
  • negative regulation of apoptotic process Source: CAFA
  • negative regulation of transcription, DNA-templated Source: CAFA
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of cell proliferation in bone marrow Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: CAFA
  • positive regulation of MAPK cascade Source: CAFA
  • positive regulation of transcription, DNA-templated Source: CAFA
  • Ras protein signal transduction Source: Reactome
  • regulation of epidermal growth factor-activated receptor activity Source: ProtInc
  • regulation of growth Source: UniProtKB-KW
  • regulation of superoxide metabolic process Source: BHF-UCL
  • viral process Source: UniProtKB-KW

Keywordsi

Biological processAngiogenesis, Growth regulation, Host-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1250196 SHC1 events in ERBB2 signaling
R-HSA-1250347 SHC1 events in ERBB4 signaling
R-HSA-167044 Signalling to RAS
R-HSA-180336 SHC1 events in EGFR signaling
R-HSA-210993 Tie2 Signaling
R-HSA-2424491 DAP12 signaling
R-HSA-2428933 SHC-related events triggered by IGF1R
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-354192 Integrin alphaIIb beta3 signaling
R-HSA-381038 XBP1(S) activates chaperone genes
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
R-HSA-512988 Interleukin-3, 5 and GM-CSF signaling
R-HSA-5637810 Constitutive Signaling by EGFRvIII
R-HSA-5654688 SHC-mediated cascade:FGFR1
R-HSA-5654699 SHC-mediated cascade:FGFR2
R-HSA-5654704 SHC-mediated cascade:FGFR3
R-HSA-5654719 SHC-mediated cascade:FGFR4
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-74749 Signal attenuation
R-HSA-74751 Insulin receptor signalling cascade
R-HSA-8851805 MET activates RAS signaling
R-HSA-8853659 RET signaling
R-HSA-8983432 Interleukin-15 signaling
R-HSA-9020558 Interleukin-2 signaling
R-HSA-9026519 Activated NTRK2 signals through RAS
R-HSA-912526 Interleukin receptor SHC signaling
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers
SignaLinkiP29353
SIGNORiP29353

Names & Taxonomyi

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

Organism-specific databases

EuPathDBiHostDB:ENSG00000160691.18
HGNCiHGNC:10840 SHC1
MIMi600560 gene
neXtProtiNX_P29353

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi349Y → F: Alters interaction with GRB2; isoform p52Shc (in vitro). 1 Publication1
Mutagenesisi427Y → F: No effect on interaction with GRB2; isoform p52Shc (in vitro). 1 Publication1

Organism-specific databases

DisGeNETi6464
OpenTargetsiENSG00000160691
PharmGKBiPA35746

Chemistry databases

ChEMBLiCHEMBL5626

Polymorphism and mutation databases

BioMutaiSHC1
DMDMi182676455

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000977311 – 583SHC-transforming protein 1Add BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei36Phosphoserine1 Publication1
Modified residuei139PhosphoserineCombined sources1
Modified residuei154N6-acetyllysineBy similarity1
Modified residuei349Phosphotyrosine3 Publications1
Modified residuei350Phosphotyrosine3 Publications1
Modified residuei427PhosphotyrosineCombined sources2 Publications1
Modified residuei453PhosphoserineCombined sources1
Isoform p52Shc (identifier: P29353-2)
Modified residuei1N-acetylmethionineCombined sources1
Isoform 7 (identifier: P29353-7)
Modified residuei1N-acetylmethionineCombined sources1

Post-translational modificationi

Phosphorylated by activated epidermal growth factor receptor. Phosphorylated in response to FLT4 and KIT signaling. Isoform p46Shc and isoform p52Shc are phosphorylated on tyrosine residues of the Pro-rich domain. Isoform p66Shc is phosphorylated on Ser-36 by PRKCB upon treatment with insulin, hydrogen peroxide or irradiation with ultraviolet light (By similarity). Tyrosine phosphorylated in response to FLT3 signaling (By similarity). Tyrosine phosphorylated by activated PTK2B/PYK2 (By similarity). Tyrosine phosphorylated by ligand-activated ALK. Tyrosine phosphorylated by ligand-activated PDGFRB. Tyrosine phosphorylated by TEK/TIE2. May be tyrosine phosphorylated by activated PTK2/FAK1; tyrosine phosphorylation was seen in an astrocytoma biopsy, where PTK2/FAK1 kinase activity is high, but not in normal brain tissue. Isoform p52Shc dephosphorylation by PTPN2 may regulate interaction with GRB2.By similarity11 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP29353
MaxQBiP29353
PaxDbiP29353
PeptideAtlasiP29353
PRIDEiP29353

PTM databases

iPTMnetiP29353
PhosphoSitePlusiP29353

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000160691
ExpressionAtlasiP29353 baseline and differential
GenevisibleiP29353 HS

Organism-specific databases

HPAiCAB005374
CAB016305
HPA001844

Interactioni

Subunit structurei

Interacts with CPNE3; this interaction may mediate the binding of CPNE3 with ERBB2 (PubMed:20010870). Interacts with the NPXY motif of tyrosine-phosphorylated IGF1R and INSR in vitro via the PID domain. Once activated, binds to GRB2. Interacts with tyrosine-phosphorylated CD3T and DDR2. Interacts with the N-terminal region of APS. Interacts with phosphorylated LRP1 and IRS4. Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with TRIM31. Interacts with PTPN6/SHP (tyrosine phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTT (By similarity). Interacts with ALK, GAB2, GRB7 and KIT. Interacts with FLT4 (tyrosine-phosphorylated). Interacts with EPHB1 and GRB2; activates the MAPK/ERK cascade to regulate cell migration. Interacts with PDGFRB (tyrosine-phosphorylated). Interacts with ERBB4. Interacts with TEK/TIE2 (tyrosine-phosphorylated). Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; in a phosphotyrosine-dependent manner. Interacts with PTK2/FAK1. Interacts with herpes simplex virus 1 UL46. Interacts with CEACAM1; this interaction is CEACAM1-phosphorylation-dependent and mediates interaction with EGFR or INSR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (By similarity).By similarity26 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • epidermal growth factor binding Source: Ensembl
  • epidermal growth factor receptor binding Source: BHF-UCL
  • insulin-like growth factor receptor binding Source: UniProtKB
  • insulin receptor binding Source: UniProtKB
  • neurotrophin TRKA receptor binding Source: UniProtKB
  • phosphotyrosine residue binding Source: CAFA
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: UniProtKB

Protein-protein interaction databases

BioGridi112361, 235 interactors
CORUMiP29353
DIPiDIP-699N
ELMiP29353
IntActiP29353, 97 interactors
MINTiP29353
STRINGi9606.ENSP00000401303

Chemistry databases

BindingDBiP29353

Structurei

Secondary structure

1583
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi113 – 115Combined sources3
Beta strandi142 – 145Combined sources4
Beta strandi148 – 150Combined sources3
Helixi152 – 156Combined sources5
Beta strandi160 – 172Combined sources13
Helixi176 – 178Combined sources3
Helixi181 – 198Combined sources18
Helixi200 – 202Combined sources3
Beta strandi206 – 208Combined sources3
Turni215 – 219Combined sources5
Beta strandi220 – 224Combined sources5
Turni226 – 229Combined sources4
Beta strandi230 – 236Combined sources7
Beta strandi238 – 245Combined sources8
Turni246 – 249Combined sources4
Beta strandi251 – 256Combined sources6
Helixi257 – 259Combined sources3
Beta strandi262 – 265Combined sources4
Helixi268 – 270Combined sources3
Beta strandi273 – 280Combined sources8
Turni281 – 283Combined sources3
Beta strandi284 – 291Combined sources8
Beta strandi293 – 295Combined sources3
Helixi296 – 310Combined sources15
Beta strandi311 – 314Combined sources4
Beta strandi350 – 352Combined sources3
Turni483 – 485Combined sources3
Beta strandi487 – 489Combined sources3
Helixi495 – 499Combined sources5
Beta strandi507 – 512Combined sources6
Beta strandi514 – 516Combined sources3
Beta strandi518 – 526Combined sources9
Beta strandi529 – 536Combined sources8
Beta strandi540 – 543Combined sources4
Beta strandi548 – 551Combined sources4
Helixi552 – 562Combined sources11
Beta strandi566 – 568Combined sources3
Beta strandi571 – 573Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XWXX-ray1.87A147-311[»]
5CZIX-ray2.60B345-353[»]
DisProtiDP00154
ProteinModelPortaliP29353
SMRiP29353
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29353

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini156 – 339PIDPROSITE-ProRule annotationAdd BLAST184
Domaini488 – 579SH2PROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni340 – 487CH1Add BLAST148

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi411 – 474Pro-richAdd BLAST64

Domaini

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

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiKOG3697 Eukaryota
ENOG410XTJN LUCA
GeneTreeiENSGT00390000018860
HOVERGENiHBG050121
InParanoidiP29353
KOiK06279
OMAiPHDRMAG
OrthoDBiEOG091G04DC
PhylomeDBiP29353
TreeFamiTF315807

Family and domain databases

CDDicd01209 PTB_Shc, 1 hit
cd09925 SH2_SHC, 1 hit
Gene3Di2.30.29.30, 1 hit
3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR011993 PH-like_dom_sf
IPR006019 PID_Shc-like
IPR006020 PTB/PI_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR029586 Shc1/ShcA
IPR035676 SHC_SH2
PANTHERiPTHR10337:SF2 PTHR10337:SF2, 1 hit
PfamiView protein in Pfam
PF00640 PID, 1 hit
PF00017 SH2, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00629 SHCPIDOMAIN
SMARTiView protein in SMART
SM00462 PTB, 1 hit
SM00252 SH2, 1 hit
SUPFAMiSSF55550 SSF55550, 1 hit
PROSITEiView protein in PROSITE
PS01179 PID, 1 hit
PS50001 SH2, 1 hit

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

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

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

« Hide

        10         20         30         40         50
MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP
60 70 80 90 100
GDDSPTTLCS FFPRMSNLRL ANPAGGRPGS KGEPGRAADD GEGIVGAAMP
110 120 130 140 150
DSGPLPLLQD MNKLSGGGGR RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH
160 170 180 190 200
PNDKVMGPGV SYLVRYMGCV EVLQSMRALD FNTRTQVTRE AISLVCEAVP
210 220 230 240 250
GAKGATRRRK PCSRPLSSIL GRSNLKFAGM PITLTVSTSS LNLMAADCKQ
260 270 280 290 300
IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL ECPEGLAQDV
310 320 330 340 350
ISTIGQAFEL RFKQYLRNPP KLVTPHDRMA GFDGSAWDEE EEEPPDHQYY
360 370 380 390 400
NDFPGKEPPL GGVVDMRLRE GAAPGAARPT APNAQTPSHL GATLPVGQPV
410 420 430 440 450
GGDPEVRKQM PPPPPCPGRE LFDDPSYVNV QNLDKARQAV GGAGPPNPAI
460 470 480 490 500
NGSAPRDLFD MKPFEDALRV PPPPQSVSMA EQLRGEPWFH GKLSRREAEA
510 520 530 540 550
LLQLNGDFLV RESTTTPGQY VLTGLQSGQP KHLLLVDPEG VVRTKDHRFE
560 570 580
SVSHLISYHM DNHLPIISAG SELCLQQPVE RKL
Note: Regulated by epigenetic modifications of its promoter region.
Length:583
Mass (Da):62,822
Last modified:April 8, 2008 - v4
Checksum:i7EFA5CB185A548D1
GO
Isoform p52Shc (identifier: P29353-2) [UniParc]FASTAAdd to basket

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

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

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

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

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

Note: Produced by alternative splicing.
Show »
Length:369
Mass (Da):40,415
Checksum:i46F34449B556DDD0
GO
Isoform 6 (identifier: P29353-6) [UniParc]FASTAAdd to basket

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

Note: Produced by alternative splicing.
Show »
Length:584
Mass (Da):62,893
Checksum:iBDB2FF81953D4FF4
GO
Isoform 7 (identifier: P29353-7) [UniParc]FASTAAdd to basket

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

Note: Produced by alternative splicing.Combined sources
Show »
Length:474
Mass (Da):51,682
Checksum:i43E1D98CBA87DB37
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2D → N in CAA70977 (PubMed:9192859).Curated1
Sequence conflicti21L → M in CAA70977 (PubMed:9192859).Curated1
Sequence conflicti38S → P in CAA70977 (PubMed:9192859).Curated1
Sequence conflicti95V → D in AAB49972 (PubMed:9049300).Curated1
Sequence conflicti101D → E in AAB49972 (PubMed:9049300).Curated1
Sequence conflicti430V → A in BAG70069 (PubMed:19054851).Curated1
Sequence conflicti430V → A in BAG70193 (PubMed:19054851).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042428205A → V. Corresponds to variant dbSNP:rs8191981Ensembl.1
Natural variantiVAR_051353410M → V. Corresponds to variant dbSNP:rs8191979Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0400901 – 214Missing in isoform 5. CuratedAdd BLAST214
Alternative sequenceiVSP_0161071 – 155Missing in isoform p46Shc. 1 PublicationAdd BLAST155
Alternative sequenceiVSP_0161081 – 110Missing in isoform p52Shc and isoform 7. 3 PublicationsAdd BLAST110
Alternative sequenceiVSP_040091215 – 221PLSSILG → MSLCHRW in isoform 5. Curated7
Alternative sequenceiVSP_040092417P → PA in isoform 7 and isoform 6. 2 Publications1

Sequence databases

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

Genome annotation databases

EnsembliENST00000368445; ENSP00000357430; ENSG00000160691 [P29353-1]
ENST00000368450; ENSP00000357435; ENSG00000160691 [P29353-2]
ENST00000368453; ENSP00000357438; ENSG00000160691 [P29353-7]
ENST00000448116; ENSP00000401303; ENSG00000160691 [P29353-6]
GeneIDi6464
KEGGihsa:6464
UCSCiuc001ffv.4 human [P29353-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSHC1_HUMAN
AccessioniPrimary (citable) accession number: P29353
Secondary accession number(s): B5BU19
, D3DV78, O15290, Q5T180, Q5T183, Q5T184, Q5T185, Q5T186, Q8N4K5, Q96CL1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: April 8, 2008
Last modified: May 23, 2018
This is version 217 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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