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Protein

Segment polarity protein dishevelled homolog DVL-3

Gene

DVL3

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

Functioni

May play a role in the signal transduction pathway mediated by multiple Wnt genes.

GO - Molecular functioni

  • beta-catenin binding Source: BHF-UCL
  • frizzled binding Source: UniProtKB
  • protease binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL
  • Rac GTPase binding Source: ParkinsonsUK-UCL
  • receptor binding Source: BHF-UCL

GO - Biological processi

  • beta-catenin destruction complex disassembly Source: Reactome
  • canonical Wnt signaling pathway Source: BHF-UCL
  • cochlea morphogenesis Source: Ensembl
  • intracellular signal transduction Source: InterPro
  • negative regulation of canonical Wnt signaling pathway Source: Reactome
  • non-canonical Wnt signaling pathway Source: BHF-UCL
  • non-canonical Wnt signaling pathway via JNK cascade Source: BHF-UCL
  • outflow tract septum morphogenesis Source: Ensembl
  • planar cell polarity pathway involved in neural tube closure Source: GO_Central
  • positive regulation of GTPase activity Source: ParkinsonsUK-UCL
  • positive regulation of JUN kinase activity Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • protein stabilization Source: ParkinsonsUK-UCL
  • regulation of cellular protein localization Source: ParkinsonsUK-UCL
  • response to drug Source: Ensembl
  • Wnt signaling pathway Source: BHF-UCL
  • Wnt signaling pathway, planar cell polarity pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000161202-MONOMER.
ReactomeiR-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-201688. WNT mediated activation of DVL.
R-HSA-4086400. PCP/CE pathway.
R-HSA-4641258. Degradation of DVL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5368598. Negative regulation of TCF-dependent signaling by DVL-interacting proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
SignaLinkiQ92997.
SIGNORiQ92997.

Names & Taxonomyi

Protein namesi
Recommended name:
Segment polarity protein dishevelled homolog DVL-3
Short name:
Dishevelled-3
Alternative name(s):
DSH homolog 3
Gene namesi
Name:DVL3
Synonyms:KIAA0208
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3087. DVL3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: ParkinsonsUK-UCL
  • nuclear chromatin Source: ParkinsonsUK-UCL
  • Wnt signalosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Robinow syndrome, autosomal dominant 3 (DRS3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Robinow syndrome, a rare skeletal dysplasia syndrome characterized by dysmorphic features resembling a fetal face, mesomelic limb shortening, genital hypoplasia, renal anomalies, and costovertebral segmentation defects.
See also OMIM:616894

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi271R → K: Localizes to plasma membranes. 1 Publication1
Mutagenesisi342R → K: No effect on subcellular location. 1 Publication1
Mutagenesisi614R → K: Localizes to plasma membranes. 1 Publication1

Keywords - Diseasei

Dwarfism

Organism-specific databases

DisGeNETi1857.
MIMi616894. phenotype.
OpenTargetsiENSG00000161202.
PharmGKBiPA27543.

Chemistry databases

ChEMBLiCHEMBL6028.

Polymorphism and mutation databases

BioMutaiDVL3.
DMDMi6919875.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001457491 – 716Segment polarity protein dishevelled homolog DVL-3Add BLAST716

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27Omega-N-methylarginine1 Publication1
Modified residuei48PhosphoserineCombined sources1
Modified residuei125PhosphoserineCombined sources1
Modified residuei192PhosphoserineCombined sources1 Publication1
Modified residuei212Omega-N-methylarginine1 Publication1
Modified residuei271Asymmetric dimethylarginine; by PRMT1; alternate1 Publication1
Modified residuei271Symmetric dimethylarginine; by PRMT7; alternate1 Publication1
Modified residuei342Omega-N-methylarginine; alternate2 Publications1
Modified residuei342Symmetric dimethylarginine; by PRMT7; alternate2 Publications1
Modified residuei346Phosphothreonine1 Publication1
Modified residuei614Symmetric dimethylarginine; by PRMT71 Publication1
Modified residuei697PhosphoserineCombined sources1
Modified residuei698Dimethylated arginine; alternate1 Publication1
Modified residuei698Omega-N-methylarginine; alternate1 Publication1
Modified residuei700Phosphoserine1 Publication1

Post-translational modificationi

Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains.1 Publication
Phosphorylated by CSNK1D.2 Publications
Arginine methylation may function as a switch in regulation of function in Wnt signaling.2 Publications

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ92997.
PaxDbiQ92997.
PeptideAtlasiQ92997.
PRIDEiQ92997.

PTM databases

iPTMnetiQ92997.
PhosphoSitePlusiQ92997.

Expressioni

Gene expression databases

BgeeiENSG00000161202.
CleanExiHS_DVL3.
ExpressionAtlasiQ92997. baseline and differential.
GenevisibleiQ92997. HS.

Organism-specific databases

HPAiCAB046486.
HPA058265.

Interactioni

Subunit structurei

Interacts (via the PDZ domain) with the C-terminal regions of VANGL1 and VANGL2 (By similarity). Interacts (via the region containing both the PDZ and DEP domains) with LRRFIP2; the DIX domain may inhibit this interaction. Interacts with CYLD, CEP164 and DAB2. Interacts with DCDC2. Interacts with FOXK1 and FOXK2 (PubMed:25805136).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAP1O756893EBI-739789,EBI-714732
BAHD1Q8TBE03EBI-739789,EBI-742750
CEP164Q9UPV05EBI-739789,EBI-3937015
CSNK1DP487304EBI-739789,EBI-751621
CSNK1EP496743EBI-739789,EBI-749343
Dab2P980782EBI-739789,EBI-1391846From a different organism.
DPPA2Q7Z7J53EBI-739789,EBI-741400
DVL1A0A087WWA74EBI-739789,EBI-11995868
DVL1O146405EBI-739789,EBI-723489
FAM13CQ8NE313EBI-739789,EBI-751248
KCTD7Q96MP8-24EBI-739789,EBI-11954971
KLF3P576823EBI-739789,EBI-8472267
KLHL12Q53G593EBI-739789,EBI-740929
LRRFIP2Q9Y6082EBI-739789,EBI-1023718
LRRK2Q5S0074EBI-739789,EBI-5323863
NOL12Q9UGY13EBI-739789,EBI-716098
NXF1Q9UBU93EBI-739789,EBI-398874
PITX1P783373EBI-739789,EBI-748265
PRICKLE1Q96MT33EBI-739789,EBI-2348662
PRPF3O433952EBI-739789,EBI-744322
RWDD2BP570603EBI-739789,EBI-724442
STOMP271053EBI-739789,EBI-1211440
SYT6Q5T7P8-25EBI-739789,EBI-10246152
TNFAIP8L1Q8WVP53EBI-739789,EBI-752102
UTP3Q9NQZ23EBI-739789,EBI-714067
YTHDC1Q96MU75EBI-739789,EBI-2849854
ZBTB48P100743EBI-739789,EBI-744864
ZNF264Q14C613EBI-739789,EBI-2826570
ZNF697Q8N5083EBI-739789,EBI-10265733

GO - Molecular functioni

  • beta-catenin binding Source: BHF-UCL
  • frizzled binding Source: UniProtKB
  • protease binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL
  • Rac GTPase binding Source: ParkinsonsUK-UCL
  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108190. 88 interactors.
DIPiDIP-34509N.
IntActiQ92997. 158 interactors.
MINTiMINT-1186858.
STRINGi9606.ENSP00000316054.

Chemistry databases

BindingDBiQ92997.

Structurei

3D structure databases

ProteinModelPortaliQ92997.
SMRiQ92997.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 82DIXPROSITE-ProRule annotationAdd BLAST82
Domaini249 – 321PDZPROSITE-ProRule annotationAdd BLAST73
Domaini422 – 496DEPPROSITE-ProRule annotationAdd BLAST75

Sequence similaritiesi

Belongs to the DSH family.Curated
Contains 1 DEP domain.PROSITE-ProRule annotation
Contains 1 DIX domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3571. Eukaryota.
ENOG410Y5G4. LUCA.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiQ92997.
KOiK02353.
OMAiGPEHTTR.
OrthoDBiEOG091G041O.
PhylomeDBiQ92997.
TreeFamiTF318198.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR008342. DVL3.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF6. PTHR10878:SF6. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR01760. DISHEVELLED.
PR01763. DISHEVELLED3.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92997-1) [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
MGETKIIYHL DGQETPYLVK LPLPAERVTL ADFKGVLQRP SYKFFFKSMD
60 70 80 90 100
DDFGVVKEEI SDDNAKLPCF NGRVVSWLVS AEGSHPDPAP FCADNPSELP
110 120 130 140 150
PPMERTGGIG DSRPPSFHPH AGGGSQENLD NDTETDSLVS AQRERPRRRD
160 170 180 190 200
GPEHATRLNG TAKGERRREP GGYDSSSTLM SSELETTSFF DSDEDDSTSR
210 220 230 240 250
FSSSTEQSSA SRLMRRHKRR RRKQKVSRIE RSSSFSSITD STMSLNIITV
260 270 280 290 300
TLNMEKYNFL GISIVGQSNE RGDGGIYIGS IMKGGAVAAD GRIEPGDMLL
310 320 330 340 350
QVNEINFENM SNDDAVRVLR EIVHKPGPIT LTVAKCWDPS PRGCFTLPRS
360 370 380 390 400
EPIRPIDPAA WVSHTAAMTG TFPAYGMSPS LSTITSTSSS ITSSIPDTER
410 420 430 440 450
LDDFHLSIHS DMAAIVKAMA SPESGLEVRD RMWLKITIPN AFIGSDVVDW
460 470 480 490 500
LYHNVEGFTD RREARKYASN LLKAGFIRHT VNKITFSEQC YYIFGDLCGN
510 520 530 540 550
MANLSLHDHD GSSGASDQDT LAPLPHPGAA PWPMAFPYQY PPPPHPYNPH
560 570 580 590 600
PGFPELGYSY GGGSASSQHS EGSRSSGSNR SGSDRRKEKD PKAGDSKSGG
610 620 630 640 650
SGSESDHTTR SSLRGPRERA PSERSGPAAS EHSHRSHHSL ASSLRSHHTH
660 670 680 690 700
PSYGPPGVPP LYGPPMLMMP PPPAAMGPPG APPGRDLASV PPELTASRQS
710
FRMAMGNPSE FFVDVM
Length:716
Mass (Da):78,055
Last modified:May 30, 2000 - v2
Checksum:iB1A55EBF9507D06E
GO
Isoform 2 (identifier: Q92997-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     350-367: SEPIRPIDPAAWVSHTAA → T

Note: No experimental confirmation available.
Show »
Length:699
Mass (Da):76,256
Checksum:iAD4CB18FDB88AA63
GO

Sequence cautioni

The sequence BAA13199 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2G → D in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti76S → Y in AAB84228 (PubMed:9344861).Curated1
Sequence conflicti102P → S in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti151G → W in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti182S → R in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti218K → N in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti222R → W in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti230E → D in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti233S → C in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti236S → T in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti239T → S in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti242T → A in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti303N → K in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti431R → C in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti450W → C in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti465R → P in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti472L → V in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti543P → R in AAB65244 (PubMed:9192851).Curated1
Sequence conflicti553 – 554FP → LG in AAB65244 (PubMed:9192851).Curated2
Sequence conflicti629A → T in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti633S → I in AAB47447 (PubMed:8817329).Curated1
Sequence conflicti682 – 716PPGRD…FVDVM → LRAATWPQCPRN in BAA13199 (PubMed:9039502).CuratedAdd BLAST35

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036116216R → T in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_025519433W → L.1 PublicationCorresponds to variant rs17853048dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_053371350 – 367SEPIR…SHTAA → T in isoform 2. 1 PublicationAdd BLAST18

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49262 mRNA. Translation: AAB47447.1.
U75651 mRNA. Translation: AAB84228.1.
AF006013 mRNA. Translation: AAB65244.1.
D86963 mRNA. Translation: BAA13199.2. Different initiation.
AK304686 mRNA. Translation: BAG65457.1.
AC131235 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78295.1.
CH471052 Genomic DNA. Translation: EAW78296.1.
BC032459 mRNA. Translation: AAH32459.1.
CCDSiCCDS3253.1. [Q92997-1]
PIRiJC5763.
RefSeqiNP_004414.3. NM_004423.3. [Q92997-1]
UniGeneiHs.388116.

Genome annotation databases

EnsembliENST00000313143; ENSP00000316054; ENSG00000161202. [Q92997-1]
ENST00000431765; ENSP00000405885; ENSG00000161202. [Q92997-2]
GeneIDi1857.
KEGGihsa:1857.
UCSCiuc003fms.4. human. [Q92997-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49262 mRNA. Translation: AAB47447.1.
U75651 mRNA. Translation: AAB84228.1.
AF006013 mRNA. Translation: AAB65244.1.
D86963 mRNA. Translation: BAA13199.2. Different initiation.
AK304686 mRNA. Translation: BAG65457.1.
AC131235 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78295.1.
CH471052 Genomic DNA. Translation: EAW78296.1.
BC032459 mRNA. Translation: AAH32459.1.
CCDSiCCDS3253.1. [Q92997-1]
PIRiJC5763.
RefSeqiNP_004414.3. NM_004423.3. [Q92997-1]
UniGeneiHs.388116.

3D structure databases

ProteinModelPortaliQ92997.
SMRiQ92997.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108190. 88 interactors.
DIPiDIP-34509N.
IntActiQ92997. 158 interactors.
MINTiMINT-1186858.
STRINGi9606.ENSP00000316054.

Chemistry databases

BindingDBiQ92997.
ChEMBLiCHEMBL6028.

PTM databases

iPTMnetiQ92997.
PhosphoSitePlusiQ92997.

Polymorphism and mutation databases

BioMutaiDVL3.
DMDMi6919875.

Proteomic databases

MaxQBiQ92997.
PaxDbiQ92997.
PeptideAtlasiQ92997.
PRIDEiQ92997.

Protocols and materials databases

DNASUi1857.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313143; ENSP00000316054; ENSG00000161202. [Q92997-1]
ENST00000431765; ENSP00000405885; ENSG00000161202. [Q92997-2]
GeneIDi1857.
KEGGihsa:1857.
UCSCiuc003fms.4. human. [Q92997-1]

Organism-specific databases

CTDi1857.
DisGeNETi1857.
GeneCardsiDVL3.
HGNCiHGNC:3087. DVL3.
HPAiCAB046486.
HPA058265.
MIMi601368. gene.
616894. phenotype.
neXtProtiNX_Q92997.
OpenTargetsiENSG00000161202.
PharmGKBiPA27543.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3571. Eukaryota.
ENOG410Y5G4. LUCA.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiQ92997.
KOiK02353.
OMAiGPEHTTR.
OrthoDBiEOG091G041O.
PhylomeDBiQ92997.
TreeFamiTF318198.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000161202-MONOMER.
ReactomeiR-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-201688. WNT mediated activation of DVL.
R-HSA-4086400. PCP/CE pathway.
R-HSA-4641258. Degradation of DVL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5368598. Negative regulation of TCF-dependent signaling by DVL-interacting proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
SignaLinkiQ92997.
SIGNORiQ92997.

Miscellaneous databases

ChiTaRSiDVL3. human.
GeneWikiiDVL3.
GenomeRNAii1857.
PROiQ92997.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000161202.
CleanExiHS_DVL3.
ExpressionAtlasiQ92997. baseline and differential.
GenevisibleiQ92997. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR008342. DVL3.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF6. PTHR10878:SF6. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR01760. DISHEVELLED.
PR01763. DISHEVELLED3.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDVL3_HUMAN
AccessioniPrimary (citable) accession number: Q92997
Secondary accession number(s): B4E3E5
, D3DNT0, O14642, Q13531, Q8N5E9, Q92607
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 30, 2016
This is version 169 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. 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.