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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

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-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
  • endosome membrane Source: Ensembl
  • mitochondrial matrix Source: UniProtKB-SubCell
  • nucleus Source: Ensembl
  • plasma membrane Source: UniProtKB
  • Shc-EGFR complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi349 – 3491Y → F: Alters interaction with GRB2; isoform p52Shc (in vitro). 1 Publication
Mutagenesisi427 – 4271Y → F: No effect on interaction with GRB2; isoform p52Shc (in vitro). 1 Publication

Organism-specific databases

PharmGKBiPA35746.

Chemistry

ChEMBLiCHEMBL5626.

Polymorphism and mutation databases

BioMutaiSHC1.
DMDMi182676455.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 583583SHC-transforming protein 1PRO_0000097731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei36 – 361Phosphoserine1 Publication
Modified residuei139 – 1391PhosphoserineCombined sources
Modified residuei154 – 1541N6-acetyllysineBy similarity
Modified residuei349 – 3491Phosphotyrosine3 Publications
Modified residuei350 – 3501Phosphotyrosine3 Publications
Modified residuei427 – 4271PhosphotyrosineCombined sources2 Publications
Modified residuei453 – 4531PhosphoserineCombined sources
Isoform p52Shc (identifier: P29353-2)
Modified residuei1 – 11N-acetylmethionineCombined sources
Isoform 7 (identifier: P29353-7)
Modified residuei1 – 11N-acetylmethionineCombined sources

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.
PhosphoSiteiP29353.

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.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 interactions.
DIPiDIP-699N.
IntActiP29353. 93 interactions.
MINTiMINT-123530.
STRINGi9606.ENSP00000401303.

Chemistry

BindingDBiP29353.

Structurei

Secondary structure

1
583
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi113 – 1153Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi148 – 1503Combined sources
Helixi152 – 1565Combined sources
Beta strandi160 – 17213Combined sources
Helixi176 – 1783Combined sources
Helixi181 – 19818Combined sources
Helixi200 – 2023Combined sources
Beta strandi206 – 2083Combined sources
Turni215 – 2195Combined sources
Beta strandi220 – 2245Combined sources
Turni226 – 2294Combined sources
Beta strandi230 – 2367Combined sources
Beta strandi238 – 2458Combined sources
Turni246 – 2494Combined sources
Beta strandi251 – 2566Combined sources
Helixi257 – 2593Combined sources
Beta strandi262 – 2654Combined sources
Helixi268 – 2703Combined sources
Beta strandi273 – 2808Combined sources
Turni281 – 2833Combined sources
Beta strandi284 – 2918Combined sources
Beta strandi293 – 2953Combined sources
Helixi296 – 31015Combined sources
Beta strandi311 – 3144Combined sources
Beta strandi350 – 3523Combined sources
Turni483 – 4853Combined sources
Beta strandi487 – 4893Combined sources
Helixi495 – 4995Combined sources
Beta strandi507 – 5126Combined sources
Beta strandi514 – 5163Combined sources
Beta strandi518 – 5269Combined sources
Beta strandi529 – 5368Combined sources
Beta strandi540 – 5434Combined sources
Beta strandi548 – 5514Combined sources
Helixi552 – 56211Combined sources
Beta strandi566 – 5683Combined sources
Beta strandi571 – 5733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 111-317, 482-583.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29353.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini156 – 339184PIDPROSITE-ProRule annotationAdd
BLAST
Domaini488 – 57992SH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni340 – 487148CH1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi411 – 47464Pro-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21D → N in CAA70977 (PubMed:9192859).Curated
Sequence conflicti21 – 211L → M in CAA70977 (PubMed:9192859).Curated
Sequence conflicti38 – 381S → P in CAA70977 (PubMed:9192859).Curated
Sequence conflicti95 – 951V → D in AAB49972 (PubMed:9049300).Curated
Sequence conflicti101 – 1011D → E in AAB49972 (PubMed:9049300).Curated
Sequence conflicti430 – 4301V → A in BAG70069 (PubMed:19054851).Curated
Sequence conflicti430 – 4301V → A in BAG70193 (PubMed:19054851).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti205 – 2051A → V.
Corresponds to variant rs8191981 [ dbSNP | Ensembl ].
VAR_042428
Natural varianti410 – 4101M → V.
Corresponds to variant rs8191979 [ dbSNP | Ensembl ].
VAR_051353

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 214214Missing in isoform 5. CuratedVSP_040090Add
BLAST
Alternative sequencei1 – 155155Missing in isoform p46Shc. 1 PublicationVSP_016107Add
BLAST
Alternative sequencei1 – 110110Missing in isoform p52Shc and isoform 7. 3 PublicationsVSP_016108Add
BLAST
Alternative sequencei215 – 2217PLSSILG → MSLCHRW in isoform 5. CuratedVSP_040091
Alternative sequencei417 – 4171P → PA in isoform 7 and isoform 6. 2 PublicationsVSP_040092

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
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. Positions 111-317, 482-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP29353.
ChEMBLiCHEMBL5626.

PTM databases

iPTMnetiP29353.
PhosphoSiteiP29353.

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

Phylogenomic databases

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

Enzyme and pathway databases

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-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: September 7, 2016
This is version 198 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.