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Protein

Protein Wnt-5b

Gene

WNT5B

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

Functioni

Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity).By similarity

GO - Molecular functioni

  1. frizzled binding Source: GO_Central
  2. receptor binding Source: UniProtKB

GO - Biological processi

  1. cell fate commitment Source: GO_Central
  2. cellular response to retinoic acid Source: UniProtKB
  3. chondrocyte differentiation Source: UniProtKB
  4. fat cell differentiation Source: UniProtKB
  5. lens fiber cell development Source: BHF-UCL
  6. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  7. neuron differentiation Source: UniProtKB
  8. positive regulation of cell migration Source: UniProtKB
  9. positive regulation of fat cell differentiation Source: Ensembl
  10. Wnt signaling pathway Source: UniProtKB
  11. wound healing Source: Ensembl
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_264199. PCP/CE pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Wnt-5b
Gene namesi
Name:WNT5B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:16265. WNT5B.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular region Source: Reactome
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. Golgi lumen Source: Reactome
  7. plasma membrane Source: Reactome
  8. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38104.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 359342Protein Wnt-5bPRO_0000041434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi83 ↔ 94By similarity
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi133 ↔ 141By similarity
Disulfide bondi143 ↔ 161By similarity
Disulfide bondi217 ↔ 231By similarity
Disulfide bondi219 ↔ 226By similarity
Lipidationi223 – 2231O-palmitoyl serine; by PORCNBy similarity
Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi304 ↔ 319By similarity
Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi334 ↔ 349By similarity
Disulfide bondi336 ↔ 346By similarity
Disulfide bondi341 ↔ 342By similarity

Post-translational modificationi

Palmitoylation at Ser-223 is required for efficient binding to frizzled receptors. Palmitoylation is necessary for proper trafficking to cell surface (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ9H1J7.
PaxDbiQ9H1J7.
PRIDEiQ9H1J7.

PTM databases

PhosphoSiteiQ9H1J7.

Expressioni

Gene expression databases

BgeeiQ9H1J7.
CleanExiHS_WNT5B.
ExpressionAtlasiQ9H1J7. baseline and differential.
GenevestigatoriQ9H1J7.

Interactioni

Subunit structurei

Interacts with PORCN.By similarity

Protein-protein interaction databases

BioGridi123348. 2 interactions.
IntActiQ9H1J7. 1 interaction.
MINTiMINT-1485183.
STRINGi9606.ENSP00000308887.

Structurei

3D structure databases

ProteinModelPortaliQ9H1J7.
SMRiQ9H1J7. Positions 73-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Wnt family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG284879.
GeneTreeiENSGT00760000118943.
HOGENOMiHOG000039529.
HOVERGENiHBG001595.
InParanoidiQ9H1J7.
KOiK00444.
OMAiLTDANSW.
PhylomeDBiQ9H1J7.
TreeFamiTF105310.

Family and domain databases

InterProiIPR005817. Wnt.
IPR026537. Wnt5b.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PTHR12027:SF87. PTHR12027:SF87. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01349. WNTPROTEIN.
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]
PROSITEiPS00246. WNT1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H1J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSLLLLFTA ALLSSWAQLL TDANSWWSLA LNPVQRPEMF IIGAQPVCSQ
60 70 80 90 100
LPGLSPGQRK LCQLYQEHMA YIGEGAKTGI KECQHQFRQR RWNCSTADNA
110 120 130 140 150
SVFGRVMQIG SRETAFTHAV SAAGVVNAIS RACREGELST CGCSRTARPK
160 170 180 190 200
DLPRDWLWGG CGDNVEYGYR FAKEFVDARE REKNFAKGSE EQGRVLMNLQ
210 220 230 240 250
NNEAGRRAVY KMADVACKCH GVSGSCSLKT CWLQLAEFRK VGDRLKEKYD
260 270 280 290 300
SAAAMRVTRK GRLELVNSRF TQPTPEDLVY VDPSPDYCLR NESTGSLGTQ
310 320 330 340 350
GRLCNKTSEG MDGCELMCCG RGYNQFKSVQ VERCHCKFHW CCFVRCKKCT

EIVDQYICK
Length:359
Mass (Da):40,323
Last modified:May 9, 2002 - v2
Checksum:i6E35EE2B0AF1FD29
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731G → R in AAG38659 (Ref. 1) Curated
Sequence conflicti88 – 881R → P in AAG38659 (Ref. 1) Curated
Sequence conflicti93 – 931N → K in AAG38659 (Ref. 1) Curated
Sequence conflicti134 – 1341R → S in AAG38659 (Ref. 1) Curated
Sequence conflicti224 – 2241G → R in AAG38659 (Ref. 1) Curated
Sequence conflicti227 – 2271S → R in AAG38659 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY009399 mRNA. Translation: AAG38659.1.
AB060966 mRNA. Translation: BAB62039.1.
AK290430 mRNA. Translation: BAF83119.1.
CH471116 Genomic DNA. Translation: EAW88925.1.
CH471116 Genomic DNA. Translation: EAW88927.1.
BC001749 mRNA. Translation: AAH01749.1.
CCDSiCCDS8510.1.
RefSeqiNP_110402.2. NM_030775.2.
NP_116031.1. NM_032642.2.
UniGeneiHs.306051.

Genome annotation databases

EnsembliENST00000310594; ENSP00000308887; ENSG00000111186.
ENST00000397196; ENSP00000380379; ENSG00000111186.
ENST00000537031; ENSP00000439312; ENSG00000111186.
GeneIDi81029.
KEGGihsa:81029.
UCSCiuc001qjj.3. human.

Polymorphism databases

DMDMi20532427.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY009399 mRNA. Translation: AAG38659.1.
AB060966 mRNA. Translation: BAB62039.1.
AK290430 mRNA. Translation: BAF83119.1.
CH471116 Genomic DNA. Translation: EAW88925.1.
CH471116 Genomic DNA. Translation: EAW88927.1.
BC001749 mRNA. Translation: AAH01749.1.
CCDSiCCDS8510.1.
RefSeqiNP_110402.2. NM_030775.2.
NP_116031.1. NM_032642.2.
UniGeneiHs.306051.

3D structure databases

ProteinModelPortaliQ9H1J7.
SMRiQ9H1J7. Positions 73-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123348. 2 interactions.
IntActiQ9H1J7. 1 interaction.
MINTiMINT-1485183.
STRINGi9606.ENSP00000308887.

PTM databases

PhosphoSiteiQ9H1J7.

Polymorphism databases

DMDMi20532427.

Proteomic databases

MaxQBiQ9H1J7.
PaxDbiQ9H1J7.
PRIDEiQ9H1J7.

Protocols and materials databases

DNASUi81029.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310594; ENSP00000308887; ENSG00000111186.
ENST00000397196; ENSP00000380379; ENSG00000111186.
ENST00000537031; ENSP00000439312; ENSG00000111186.
GeneIDi81029.
KEGGihsa:81029.
UCSCiuc001qjj.3. human.

Organism-specific databases

CTDi81029.
GeneCardsiGC12P001639.
HGNCiHGNC:16265. WNT5B.
MIMi606361. gene.
neXtProtiNX_Q9H1J7.
PharmGKBiPA38104.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG284879.
GeneTreeiENSGT00760000118943.
HOGENOMiHOG000039529.
HOVERGENiHBG001595.
InParanoidiQ9H1J7.
KOiK00444.
OMAiLTDANSW.
PhylomeDBiQ9H1J7.
TreeFamiTF105310.

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.
REACT_264199. PCP/CE pathway.

Miscellaneous databases

ChiTaRSiWNT5B. human.
GeneWikiiWNT5B.
GenomeRNAii81029.
NextBioi71352.
PROiQ9H1J7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H1J7.
CleanExiHS_WNT5B.
ExpressionAtlasiQ9H1J7. baseline and differential.
GenevestigatoriQ9H1J7.

Family and domain databases

InterProiIPR005817. Wnt.
IPR026537. Wnt5b.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PTHR12027:SF87. PTHR12027:SF87. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01349. 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 six novel human WNT genes."
    Testa T.T., Mossakowska D.E., Carter P.S., Hu E., Zhu Y., Kelsell D.P., Murdock P.R., Herrity N.C., Lewis C.J., Cross D.A., Culbert A.A., Reith A.D., Barnes M.R.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and characterization of human WNT5B on chromosome 12p13.3 region."
    Saitoh T., Katoh M.
    Int. J. Oncol. 19:347-351(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.

Entry informationi

Entry nameiWNT5B_HUMAN
AccessioniPrimary (citable) accession number: Q9H1J7
Secondary accession number(s): A8K315
, D3DUP9, Q96S49, Q9BV04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 19, 2001
Last sequence update: May 9, 2002
Last modified: March 31, 2015
This is version 123 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 12
    Human chromosome 12: 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.