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Protein

SHC-transforming protein 1

Gene

SHC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 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
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Growth regulation, Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160691-MONOMER.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-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-451927. Interleukin-2 signaling.
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-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
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10840. SHC1.

Subcellular locationi

Isoform p46Shc :
  • Mitochondrion matrix 1 Publication

  • Note: Localized to the mitochondria matrix. Targeting of isoform p46Shc to mitochondria is mediated by its first 32 amino acids, which behave as a bona fide mitochondrial targeting sequence. Isoform p52Shc and isoform p66Shc, that contain the same sequence but more internally located, display a different subcellular localization.
Isoform p66Shc :
  • Mitochondrion By similarity

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

GO - Cellular componenti

  • cytosol Source: Reactome
  • mitochondrial matrix Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • Shc-EGFR complex Source: BHF-UCL
Complete GO annotation...

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

WithEntry#Exp.IntActNotes
APPP050675EBI-78835,EBI-77613
ARP1027514EBI-78835,EBI-608057
CRKP461083EBI-78835,EBI-886
EGFRP0053326EBI-78835,EBI-297353
ERBB2P046269EBI-78835,EBI-641062
ERBB3P218605EBI-78835,EBI-720706
ERBB4Q153032EBI-78835,EBI-80371
ESR1P03372-42EBI-78835,EBI-4309277
GAB1Q134809EBI-78835,EBI-517684
GRB2P6299323EBI-78835,EBI-401755
IGF1RP080692EBI-1000553,EBI-475981
INSRP062132EBI-78835,EBI-475899
Jak2Q621202EBI-78835,EBI-646604From a different organism.
KITP107218EBI-78835,EBI-1379503
METP085815EBI-78835,EBI-1039152
NSP034952EBI-78835,EBI-2548993From a different organism.
PIK3R1P279863EBI-78835,EBI-79464
PTPN12Q052094EBI-78835,EBI-2266035
SOS1Q078892EBI-78835,EBI-297487

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • 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
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: UniProtKB

Protein-protein interaction databases

BioGridi112361. 230 interactors.
DIPiDIP-699N.
IntActiP29353. 93 interactors.
MINTiMINT-123530.
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

Sequence similaritiesi

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

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiKOG3697. Eukaryota.
ENOG410XTJN. LUCA.
GeneTreeiENSGT00390000018860.
HOVERGENiHBG050121.
InParanoidiP29353.
KOiK06279.
OMAiPRMSNLK.
OrthoDBiEOG091G04DC.
PhylomeDBiP29353.
TreeFamiTF315807.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006019. PID_Shc-like.
IPR006020. PTB/PI_dom.
IPR000980. SH2.
IPR029586. Shc1/ShcA.
[Graphical view]
PANTHERiPTHR10337:SF2. PTHR10337:SF2. 1 hit.
PfamiPF00640. PID. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00629. SHCPIDOMAIN.
SMARTiSM00462. PTB. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS01179. PID. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. 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 rs8191981dbSNPEnsembl.1
Natural variantiVAR_051353410M → V.Corresponds to variant rs8191979dbSNPEnsembl.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

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

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...

Protein-protein interaction databases

BioGridi112361. 230 interactors.
DIPiDIP-699N.
IntActiP29353. 93 interactors.
MINTiMINT-123530.
STRINGi9606.ENSP00000401303.

Chemistry databases

BindingDBiP29353.
ChEMBLiCHEMBL5626.

PTM databases

iPTMnetiP29353.
PhosphoSitePlusiP29353.

Polymorphism and mutation databases

BioMutaiSHC1.
DMDMi182676455.

Proteomic databases

EPDiP29353.
MaxQBiP29353.
PaxDbiP29353.
PeptideAtlasiP29353.
PRIDEiP29353.

Protocols and materials databases

DNASUi6464.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi6464.
DisGeNETi6464.
GeneCardsiSHC1.
HGNCiHGNC:10840. SHC1.
HPAiCAB005374.
CAB016305.
HPA001844.
MIMi600560. gene.
neXtProtiNX_P29353.
OpenTargetsiENSG00000160691.
PharmGKBiPA35746.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3697. Eukaryota.
ENOG410XTJN. LUCA.
GeneTreeiENSGT00390000018860.
HOVERGENiHBG050121.
InParanoidiP29353.
KOiK06279.
OMAiPRMSNLK.
OrthoDBiEOG091G04DC.
PhylomeDBiP29353.
TreeFamiTF315807.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160691-MONOMER.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-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-451927. Interleukin-2 signaling.
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-912526. Interleukin receptor SHC signaling.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP29353.
SIGNORiP29353.

Miscellaneous databases

ChiTaRSiSHC1. human.
EvolutionaryTraceiP29353.
GeneWikiiSHC1.
GenomeRNAii6464.
PROiP29353.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000160691.
ExpressionAtlasiP29353. baseline and differential.
GenevisibleiP29353. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006019. PID_Shc-like.
IPR006020. PTB/PI_dom.
IPR000980. SH2.
IPR029586. Shc1/ShcA.
[Graphical view]
PANTHERiPTHR10337:SF2. PTHR10337:SF2. 1 hit.
PfamiPF00640. PID. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00629. SHCPIDOMAIN.
SMARTiSM00462. PTB. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS01179. PID. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSHC1_HUMAN
AccessioniPrimary (citable) accession number: P29353
Secondary accession number(s): B5BU19
, D3DV78, O15290, Q5T180, Q5T183, Q5T184, Q5T185, Q5T186, Q8N4K5, Q96CL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: April 8, 2008
Last modified: November 30, 2016
This is version 201 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.