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Protein

Mothers against decapentaplegic homolog 7

Gene

SMAD7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity).By similarity5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi125ZincBy similarity1
Metal bindingi180ZincBy similarity1
Metal bindingi192ZincBy similarity1
Metal bindingi197ZincBy similarity1

GO - Molecular functioni

  • activin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • I-SMAD binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • transcription factor activity, sequence-specific DNA binding Source: InterPro
  • transcription regulatory region DNA binding Source: BHF-UCL
  • transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity Source: BHF-UCL
  • type I transforming growth factor beta receptor binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  • adherens junction assembly Source: BHF-UCL
  • artery morphogenesis Source: BHF-UCL
  • BMP signaling pathway Source: Reactome
  • cellular protein complex localization Source: BHF-UCL
  • cellular response to transforming growth factor beta stimulus Source: BHF-UCL
  • negative regulation of BMP signaling pathway Source: BHF-UCL
  • negative regulation of cell migration Source: BHF-UCL
  • negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • negative regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  • negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • negative regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
  • negative regulation of protein ubiquitination Source: BHF-UCL
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • negative regulation of transcription by competitive promoter binding Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • negative regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  • pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  • positive regulation of cell-cell adhesion Source: BHF-UCL
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • positive regulation of protein ubiquitination Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: Reactome
  • protein stabilization Source: BHF-UCL
  • regulation of activin receptor signaling pathway Source: BHF-UCL
  • regulation of cardiac muscle contraction Source: BHF-UCL
  • regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • regulation of ventricular cardiac muscle cell membrane depolarization Source: BHF-UCL
  • response to laminar fluid shear stress Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
  • transforming growth factor beta receptor signaling pathway Source: Ensembl
  • ureteric bud development Source: Ensembl
  • ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
  • ventricular septum morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101665-MONOMER.
ReactomeiR-HSA-201451. Signaling by BMP.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
SignaLinkiO15105.
SIGNORiO15105.

Names & Taxonomyi

Protein namesi
Recommended name:
Mothers against decapentaplegic homolog 7
Short name:
MAD homolog 7
Short name:
Mothers against DPP homolog 7
Alternative name(s):
Mothers against decapentaplegic homolog 8
Short name:
MAD homolog 8
Short name:
Mothers against DPP homolog 8
SMAD family member 7
Short name:
SMAD 7
Short name:
Smad7
Short name:
hSMAD7
Gene namesi
Name:SMAD7
Synonyms:MADH7, MADH8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:6773. SMAD7.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: HPA
  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • protein complex Source: MGI
  • transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Colorectal cancer 3 (CRCS3)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
See also OMIM:612229

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64K → A: Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-70. 1 Publication1
Mutagenesisi70K → A: Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-64. 1 Publication1
Mutagenesisi207 – 211Missing : Diminishes interaction with SMURF2. 1 Publication5
Mutagenesisi211Y → A: Diminishes interaction with SMURF2 and reduces inhibition of TGF-beta signaling. 1 Publication1
Mutagenesisi409 – 426Missing : 90% reduction in TGF-beta receptor binding. 1 PublicationAdd BLAST18

Organism-specific databases

DisGeNETi4092.
MalaCardsiSMAD7.
MIMi612229. phenotype.
OpenTargetsiENSG00000101665.
PharmGKBiPA134875286.

Polymorphism and mutation databases

BioMutaiSMAD7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000908721 – 426Mothers against decapentaplegic homolog 7Add BLAST426

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei64N6-acetyllysine; alternate1 Publication1
Cross-linki64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei70N6-acetyllysine; alternate1 Publication1
Cross-linki70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei249PhosphoserinePROSITE-ProRule annotationBy similarity1

Post-translational modificationi

Phosphorylation on Ser-249 does not affect its stability, nuclear localization or inhibitory function in TGFB signaling; however it affects its ability to regulate transcription (By similarity). Phosphorylated by PDPK1.By similarity1 Publication
Ubiquitinated by WWP1 (By similarity). Polyubiquitinated by RNF111, which is enhanced by AXIN1 and promotes proteasomal degradation. In response to TGF-beta, ubiquitinated by SMURF1; which promotes its degradation.By similarity
Acetylation prevents ubiquitination and degradation mediated by SMURF1.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO15105.
PRIDEiO15105.

PTM databases

iPTMnetiO15105.
PhosphoSitePlusiO15105.

Expressioni

Tissue specificityi

Ubiquitous with higher expression in the lung and vascular endothelium.

Inductioni

By TGFB1.

Gene expression databases

BgeeiENSG00000101665.
CleanExiHS_SMAD7.
ExpressionAtlasiO15105. baseline and differential.
GenevisibleiO15105. HS.

Organism-specific databases

HPAiCAB026212.
HPA028897.

Interactioni

Subunit structurei

Interacts with WWP1 (By similarity). Interacts with COPS5. Interacts with NEDD4L. Interacts with STAMBP. Interacts with RNF111, AXIN1 and AXIN2. Interacts with PPP1R15A. Interacts (via MH2 domain) with EP300. Interacts with ACVR1B, SMURF1, SMURF2 and TGFBR1; SMAD7 recruits SMURF1 and SMURF2 to the TGF-beta receptor and regulates its degradation. Interacts with PDPK1 (via PH domain).By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACVR1BP368962EBI-3861591,EBI-1384128
AXIN1O151698EBI-3861591,EBI-710484
COPS5Q9290510EBI-3861591,EBI-594661
FKBP1AP629423EBI-3861591,EBI-1027571
Rnf111Q99ML92EBI-3861591,EBI-646015From a different organism.
WWP2O003085EBI-3861591,EBI-743923
YAP1P469373EBI-3861591,EBI-1044059

GO - Molecular functioni

  • activin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • I-SMAD binding Source: BHF-UCL
  • type I transforming growth factor beta receptor binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110267. 88 interactors.
DIPiDIP-42252N.
IntActiO15105. 27 interactors.
MINTiMINT-1179821.
STRINGi9606.ENSP00000262158.

Structurei

Secondary structure

1426
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi204 – 206Combined sources3
Beta strandi212 – 214Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DJYNMR-B203-217[»]
2KXQNMR-B203-217[»]
2LTVNMR-B206-217[»]
2LTWNMR-B205-217[»]
2LTXNMR-B203-217[»]
2LTYNMR-B203-217[»]
2LTZNMR-B203-217[»]
ProteinModelPortaliO15105.
SMRiO15105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15105.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 207MH1PROSITE-ProRule annotationAdd BLAST144
Domaini261 – 426MH2PROSITE-ProRule annotationAdd BLAST166

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni208 – 217Important for interaction with SMURF210

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi208 – 211PY-motif4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi27 – 35Poly-Gly9
Compositional biasi49 – 56Poly-Gly8
Compositional biasi207 – 210Poly-Pro4

Sequence similaritiesi

Belongs to the dwarfin/SMAD family.Curated
Contains 1 MH1 (MAD homology 1) domain.PROSITE-ProRule annotation
Contains 1 MH2 (MAD homology 2) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3701. Eukaryota.
ENOG410XQKU. LUCA.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000060106.
HOVERGENiHBG053021.
InParanoidiO15105.
KOiK19631.
OMAiGQLCSEN.
OrthoDBiEOG091G0XBN.
PhylomeDBiO15105.
TreeFamiTF314923.

Family and domain databases

Gene3Di2.60.200.10. 1 hit.
3.90.520.10. 2 hits.
InterProiIPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR13703. PTHR13703. 2 hits.
PfamiPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTiSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 2 hits.
PROSITEiPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15105-1) [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
MFRTKRSALV RRLWRSRAPG GEDEEEGAGG GGGGGELRGE GATDSRAHGA
60 70 80 90 100
GGGGPGRAGC CLGKAVRGAK GHHHPHPPAA GAGAAGGAEA DLKALTHSVL
110 120 130 140 150
KKLKERQLEL LLQAVESRGG TRTACLLLPG RLDCRLGPGA PAGAQPAQPP
160 170 180 190 200
SSYSLPLLLC KVFRWPDLRH SSEVKRLCCC ESYGKINPEL VCCNPHHLSR
210 220 230 240 250
LCELESPPPP YSRYPMDFLK PTADCPDAVP SSAETGGTNY LAPGGLSDSQ
260 270 280 290 300
LLLEPGDRSH WCVVAYWEEK TRVGRLYCVQ EPSLDIFYDL PQGNGFCLGQ
310 320 330 340 350
LNSDNKSQLV QKVRSKIGCG IQLTREVDGV WVYNRSSYPI FIKSATLDNP
360 370 380 390 400
DSRTLLVHKV FPGFSIKAFD YEKAYSLQRP NDHEFMQQPW TGFTVQISFV
410 420
KGWGQCYTRQ FISSCPCWLE VIFNSR
Length:426
Mass (Da):46,426
Last modified:January 1, 1998 - v1
Checksum:i5B76EC986776C102
GO
Isoform 2 (identifier: O15105-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-215: Missing.

Note: No experimental confirmation available.
Show »
Length:211
Mass (Da):23,901
Checksum:i04F71C0D2D257D71
GO
Isoform 3 (identifier: O15105-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: Missing.

Note: No experimental confirmation available.
Show »
Length:425
Mass (Da):46,355
Checksum:i881EA3C25C342A91
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71G → C in AAB81354 (PubMed:9335507).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0451971 – 215Missing in isoform 2. 1 PublicationAdd BLAST215
Alternative sequenceiVSP_047540223Missing in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010193 mRNA. Translation: AAB81246.1.
AF015261 mRNA. Translation: AAB81354.1.
AF026559
, AF026556, AF026557, AF026558 Genomic DNA. Translation: AAL68977.1.
AK301535 mRNA. Translation: BAH13509.1.
DA882147 mRNA. No translation available.
AC114684 Genomic DNA. No translation available.
BC074818 mRNA. Translation: AAH74818.2.
BC074819 mRNA. Translation: AAH74819.2.
CCDSiCCDS11936.1. [O15105-1]
CCDS54186.1. [O15105-2]
CCDS59317.1. [O15105-3]
RefSeqiNP_001177750.1. NM_001190821.1. [O15105-3]
NP_001177751.1. NM_001190822.1. [O15105-2]
NP_001177752.1. NM_001190823.1.
NP_005895.1. NM_005904.3. [O15105-1]
UniGeneiHs.465087.

Genome annotation databases

EnsembliENST00000262158; ENSP00000262158; ENSG00000101665. [O15105-1]
ENST00000589634; ENSP00000467621; ENSG00000101665. [O15105-3]
ENST00000591805; ENSP00000466902; ENSG00000101665. [O15105-2]
GeneIDi4092.
KEGGihsa:4092.
UCSCiuc002ldg.3. human. [O15105-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010193 mRNA. Translation: AAB81246.1.
AF015261 mRNA. Translation: AAB81354.1.
AF026559
, AF026556, AF026557, AF026558 Genomic DNA. Translation: AAL68977.1.
AK301535 mRNA. Translation: BAH13509.1.
DA882147 mRNA. No translation available.
AC114684 Genomic DNA. No translation available.
BC074818 mRNA. Translation: AAH74818.2.
BC074819 mRNA. Translation: AAH74819.2.
CCDSiCCDS11936.1. [O15105-1]
CCDS54186.1. [O15105-2]
CCDS59317.1. [O15105-3]
RefSeqiNP_001177750.1. NM_001190821.1. [O15105-3]
NP_001177751.1. NM_001190822.1. [O15105-2]
NP_001177752.1. NM_001190823.1.
NP_005895.1. NM_005904.3. [O15105-1]
UniGeneiHs.465087.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DJYNMR-B203-217[»]
2KXQNMR-B203-217[»]
2LTVNMR-B206-217[»]
2LTWNMR-B205-217[»]
2LTXNMR-B203-217[»]
2LTYNMR-B203-217[»]
2LTZNMR-B203-217[»]
ProteinModelPortaliO15105.
SMRiO15105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110267. 88 interactors.
DIPiDIP-42252N.
IntActiO15105. 27 interactors.
MINTiMINT-1179821.
STRINGi9606.ENSP00000262158.

PTM databases

iPTMnetiO15105.
PhosphoSitePlusiO15105.

Polymorphism and mutation databases

BioMutaiSMAD7.

Proteomic databases

PaxDbiO15105.
PRIDEiO15105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262158; ENSP00000262158; ENSG00000101665. [O15105-1]
ENST00000589634; ENSP00000467621; ENSG00000101665. [O15105-3]
ENST00000591805; ENSP00000466902; ENSG00000101665. [O15105-2]
GeneIDi4092.
KEGGihsa:4092.
UCSCiuc002ldg.3. human. [O15105-1]

Organism-specific databases

CTDi4092.
DisGeNETi4092.
GeneCardsiSMAD7.
HGNCiHGNC:6773. SMAD7.
HPAiCAB026212.
HPA028897.
MalaCardsiSMAD7.
MIMi602932. gene.
612229. phenotype.
neXtProtiNX_O15105.
OpenTargetsiENSG00000101665.
PharmGKBiPA134875286.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3701. Eukaryota.
ENOG410XQKU. LUCA.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000060106.
HOVERGENiHBG053021.
InParanoidiO15105.
KOiK19631.
OMAiGQLCSEN.
OrthoDBiEOG091G0XBN.
PhylomeDBiO15105.
TreeFamiTF314923.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101665-MONOMER.
ReactomeiR-HSA-201451. Signaling by BMP.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
SignaLinkiO15105.
SIGNORiO15105.

Miscellaneous databases

ChiTaRSiSMAD7. human.
EvolutionaryTraceiO15105.
GeneWikiiMothers_against_decapentaplegic_homolog_7.
GenomeRNAii4092.
PROiO15105.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101665.
CleanExiHS_SMAD7.
ExpressionAtlasiO15105. baseline and differential.
GenevisibleiO15105. HS.

Family and domain databases

Gene3Di2.60.200.10. 1 hit.
3.90.520.10. 2 hits.
InterProiIPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR13703. PTHR13703. 2 hits.
PfamiPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTiSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 2 hits.
PROSITEiPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSMAD7_HUMAN
AccessioniPrimary (citable) accession number: O15105
Secondary accession number(s): B7Z773
, K7EQ10, O14740, Q6DK23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 172 of the entry and version 1 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 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.