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Protein

Protein Wnt-3a

Gene

WNT3A

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

Functioni

Ligand for members of the frizzled family of seven transmembrane receptors. Wnt-3 and Wnt-3a play distinct roles in cell-cell signaling during morphogenesis of the developing neural tube.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei26 – 272Cleavage; by TIKI1 and TIKI2By similarity

GO - Molecular functioni

  • frizzled binding Source: GO_Central
  • receptor agonist activity Source: BHF-UCL
  • transcription coactivator activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.
REACT_18372. Class B/2 (Secretin family receptors).
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264378. RNF mutants show enhanced WNT signaling and proliferation.
REACT_264383. negative regulation of TCF-dependent signaling by WNT ligand antagonists.
REACT_264580. regulation of FZD by ubiquitination.
REACT_264596. TCF dependent signaling in response to WNT.
SignaLinkiP56704.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Wnt-3a
Gene namesi
Name:WNT3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:15983. WNT3A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 871N → Q: Strongly reduced ability to stimulate Wnt-responsive reporters; when associated with Q-298. 1 Publication
Mutagenesisi209 – 2091S → A: Abrogates WLS binding. 3 Publications
Mutagenesisi209 – 2091S → A: Complete loss of palmitoleylation. 3 Publications
Mutagenesisi209 – 2091S → T: No effect on palmitoleylation and secretion; the threonine can functionally replace the serine. 3 Publications
Mutagenesisi298 – 2981N → Q: Strongly reduced ability to stimulate Wnt-responsive reporters; when associated with Q-87. 1 Publication
Mutagenesisi334 – 3341C → A: No signaling activity despite the presence of significant amounts of secreted monomeric Wnt3a exhibit dominant negative properties; when associated with A-335. 1 Publication
Mutagenesisi335 – 3351C → A: No signaling activity despite the presence of significant amounts of secreted monomeric Wnt3a, exhibit dominant negative properties; when associated with A-334. 1 Publication

Organism-specific databases

Orphaneti85193. Idiopathic juvenile osteoporosis.
PharmGKBiPA38074.

Polymorphism and mutation databases

BioMutaiWNT3A.
DMDMi20532424.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 352334Protein Wnt-3aPRO_0000041418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi77 ↔ 881 Publication
Glycosylationi87 – 871N-linked (GlcNAc...)1 Publication
Disulfide bondi128 ↔ 136By similarity
Disulfide bondi138 ↔ 155By similarity
Disulfide bondi203 ↔ 217By similarity
Disulfide bondi205 ↔ 212By similarity
Lipidationi209 – 2091O-palmitoleyl serine; by PORCN4 Publications
Disulfide bondi297 ↔ 312By similarity
Glycosylationi298 – 2981N-linked (GlcNAc...)1 Publication
Disulfide bondi327 ↔ 342By similarity
Disulfide bondi329 ↔ 339By similarity
Disulfide bondi334 ↔ 335By similarity

Post-translational modificationi

Palmitoleylation by PORCN is required for efficient binding to frizzled receptors. Palmitoleylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoleylated WNT3A from WLS in secretory vesicles (PubMed:20826466, PubMed:21244856, PubMed:24292069). Depalmitoleylated by NOTUM, leading to inhibit Wnt signaling pathway, possibly by promoting disulfide bond formation and oligomerization (PubMed:25731175).4 Publications
Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT3A.By similarity
Disulfide bonds have critical and distinct roles in secretion and activity. Loss of each conserved cysteine in WNT3A results in high molecular weight oxidized Wnt oligomers, which are formed through inter-Wnt disulfide bonding.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein

Proteomic databases

PaxDbiP56704.
PRIDEiP56704.

PTM databases

PhosphoSiteiP56704.

Expressioni

Tissue specificityi

Moderately expressed in placenta and at low levels in adult lung, spleen, and prostate.

Gene expression databases

BgeeiP56704.
CleanExiHS_WNT3A.

Organism-specific databases

HPAiHPA050514.

Interactioni

Subunit structurei

Homooligomer; disulfide-linked, leading to inactivation (By similarity). Interacts with PORCN. Interacts with APCDD1 and WLS. Component of the Wnt-Fzd-LRP5-LRP6 signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts directly in the complex with LRP6.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FZD8Q9H4612EBI-6173037,EBI-6254212

Protein-protein interaction databases

BioGridi124599. 14 interactions.
DIPiDIP-58592N.
IntActiP56704. 3 interactions.
STRINGi9606.ENSP00000284523.

Structurei

3D structure databases

ProteinModelPortaliP56704.
SMRiP56704. Positions 57-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Wnt family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG284879.
GeneTreeiENSGT00760000118943.
HOGENOMiHOG000039529.
HOVERGENiHBG001595.
InParanoidiP56704.
KOiK00312.
OMAiFLKCKCH.
OrthoDBiEOG7C8GJ8.
PhylomeDBiP56704.
TreeFamiTF105310.

Family and domain databases

InterProiIPR005817. Wnt.
IPR009141. Wnt3.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01843. WNT3PROTEIN.
PR01349. WNTPROTEIN.
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]
PROSITEiPS00246. WNT1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: P56704-1) [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
MAPLGYFLLL CSLKQALGSY PIWWSLAVGP QYSSLGSQPI LCASIPGLVP
60 70 80 90 100
KQLRFCRNYV EIMPSVAEGI KIGIQECQHQ FRGRRWNCTT VHDSLAIFGP
110 120 130 140 150
VLDKATRESA FVHAIASAGV AFAVTRSCAE GTAAICGCSS RHQGSPGKGW
160 170 180 190 200
KWGGCSEDIE FGGMVSREFA DARENRPDAR SAMNRHNNEA GRQAIASHMH
210 220 230 240 250
LKCKCHGLSG SCEVKTCWWS QPDFRAIGDF LKDKYDSASE MVVEKHRESR
260 270 280 290 300
GWVETLRPRY TYFKVPTERD LVYYEASPNF CEPNPETGSF GTRDRTCNVS
310 320 330 340 350
SHGIDGCDLL CCGRGHNARA ERRREKCRCV FHWCCYVSCQ ECTRVYDVHT

CK
Length:352
Mass (Da):39,365
Last modified:May 10, 2002 - v2
Checksum:iA317BD6D4A73920B
GO
Isoform 2 (identifier: P56704-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     352-352: K → KNPGSRAGNSAHQPPHPQPPVRFHPPLRRAGKVP

Show »
Length:385
Mass (Da):42,905
Checksum:iB2BBBFD1C7CA7E56
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei352 – 3521K → KNPGSRAGNSAHQPPHPQPP VRFHPPLRRAGKVP in isoform 2. 1 PublicationVSP_046558

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB060284 mRNA. Translation: BAB61052.1.
AK056278 mRNA. Translation: BAB71136.1.
AL136379 Genomic DNA. Translation: CAI23122.1.
BC103921 mRNA. Translation: AAI03922.1.
BC103922 mRNA. Translation: AAI03923.1.
BC103923 mRNA. Translation: AAI03924.1.
CCDSiCCDS1564.1. [P56704-1]
RefSeqiNP_149122.1. NM_033131.3. [P56704-1]
UniGeneiHs.336930.

Genome annotation databases

EnsembliENST00000284523; ENSP00000284523; ENSG00000154342.
GeneIDi89780.
KEGGihsa:89780.
UCSCiuc001hrp.2. human.
uc001hrq.2. human. [P56704-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB060284 mRNA. Translation: BAB61052.1.
AK056278 mRNA. Translation: BAB71136.1.
AL136379 Genomic DNA. Translation: CAI23122.1.
BC103921 mRNA. Translation: AAI03922.1.
BC103922 mRNA. Translation: AAI03923.1.
BC103923 mRNA. Translation: AAI03924.1.
CCDSiCCDS1564.1. [P56704-1]
RefSeqiNP_149122.1. NM_033131.3. [P56704-1]
UniGeneiHs.336930.

3D structure databases

ProteinModelPortaliP56704.
SMRiP56704. Positions 57-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124599. 14 interactions.
DIPiDIP-58592N.
IntActiP56704. 3 interactions.
STRINGi9606.ENSP00000284523.

Chemistry

BindingDBiP56704.
ChEMBLiCHEMBL1255137.

PTM databases

PhosphoSiteiP56704.

Polymorphism and mutation databases

BioMutaiWNT3A.
DMDMi20532424.

Proteomic databases

PaxDbiP56704.
PRIDEiP56704.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284523; ENSP00000284523; ENSG00000154342.
GeneIDi89780.
KEGGihsa:89780.
UCSCiuc001hrp.2. human.
uc001hrq.2. human. [P56704-1]

Organism-specific databases

CTDi89780.
GeneCardsiGC01P228194.
HGNCiHGNC:15983. WNT3A.
HPAiHPA050514.
MIMi606359. gene.
neXtProtiNX_P56704.
Orphaneti85193. Idiopathic juvenile osteoporosis.
PharmGKBiPA38074.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG284879.
GeneTreeiENSGT00760000118943.
HOGENOMiHOG000039529.
HOVERGENiHBG001595.
InParanoidiP56704.
KOiK00312.
OMAiFLKCKCH.
OrthoDBiEOG7C8GJ8.
PhylomeDBiP56704.
TreeFamiTF105310.

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.
REACT_18372. Class B/2 (Secretin family receptors).
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264378. RNF mutants show enhanced WNT signaling and proliferation.
REACT_264383. negative regulation of TCF-dependent signaling by WNT ligand antagonists.
REACT_264580. regulation of FZD by ubiquitination.
REACT_264596. TCF dependent signaling in response to WNT.
SignaLinkiP56704.

Miscellaneous databases

GeneWikiiWNT3A.
GenomeRNAii89780.
NextBioi76263.
PROiP56704.
SOURCEiSearch...

Gene expression databases

BgeeiP56704.
CleanExiHS_WNT3A.

Family and domain databases

InterProiIPR005817. Wnt.
IPR009141. Wnt3.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01843. WNT3PROTEIN.
PR01349. WNTPROTEIN.
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]
PROSITEiPS00246. WNT1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of WNT3a and WNT14 clustered in human chromosome 1q42 region."
    Saitoh T., Hirai M., Katoh M.
    Biochem. Biophys. Res. Commun. 284:1168-1175(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  5. "Differential expression of human Wnt genes 2, 3, 4, and 7B in human breast cell lines and normal and disease states of human breast tissue."
    Huguet E.L., McMahon J.A., McMahon A.P., Bicknell R., Harris A.L.
    Cancer Res. 54:2615-2621(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 207-330.
    Tissue: Mammary gland.
  6. "Wntless, a conserved membrane protein dedicated to the secretion of Wnt proteins from signaling cells."
    Baenziger C., Soldini D., Schuett C., Zipperlen P., Hausmann G., Basler K.
    Cell 125:509-522(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WLS.
  7. "Reconstitution of a frizzled8.Wnt3a.LRP6 signaling complex reveals multiple Wnt and Dkk1 binding sites on LRP6."
    Bourhis E., Tam C., Franke Y., Bazan J.F., Ernst J., Hwang J., Costa M., Cochran A.G., Hannoush R.N.
    J. Biol. Chem. 285:9172-9179(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRP6 IN THE WNT/FZD/LRP6 COMPLEX.
  8. Cited for: PALMITOLEYLATION BY PORCN, MUTAGENESIS OF SER-209.
  9. Cited for: INTERACTION WITH APCDD1.
  10. "Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling."
    Doubravska L., Krausova M., Gradl D., Vojtechova M., Tumova L., Lukas J., Valenta T., Pospichalova V., Fafilek B., Plachy J., Sebesta O., Korinek V.
    Cell. Signal. 23:837-848(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY CYSTEINE PALMITOYLATION, PALMITOLEYLATION, GLYCOSYLATION AT ASN-87 AND ASN-298, MUTAGENESIS OF ASN-87; SER-209 AND ASN-298.
  11. Cited for: DISULFIDE BONDS, MUTAGENESIS OF SER-209; CYS-334 AND CYS-335.
  12. "Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine."
    Gao X., Hannoush R.N.
    Nat. Chem. Biol. 10:61-68(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF PALMITOYLATION AT CYS-77, PALMITOLEYLATION BY PORCN.
  13. Cited for: PALMITOLEYLATION, DEPALMITOLEYLATION.

Entry informationi

Entry nameiWNT3A_HUMAN
AccessioniPrimary (citable) accession number: P56704
Secondary accession number(s): Q3SY79, Q3SY80, Q969P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 10, 2002
Last modified: July 22, 2015
This is version 140 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

Caution

A palmitoylation site was proposed at Cys-77, but it was later shown that this cysteine is engaged in a disulfide bond (PubMed:24292069).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.