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- F5H034_HUMAN


F5H034 - F5H034_HUMAN

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Protein Wnt



Homo sapiens (Human)
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi


Ligand for members of the frizzled family of seven transmembrane receptors.UniRule annotation

GO - Biological processi

  1. multicellular organismal development Source: UniProtKB-KW
  2. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  3. positive regulation of fat cell differentiation Source: Ensembl
  4. Wnt signaling pathway Source: UniProtKB-KW
  5. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental proteinUniRule annotationSAAS annotation

Keywords - Biological processi

Wnt signaling pathwayUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein WntUniRule annotation
Gene namesi
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases


Subcellular locationi

Secretedextracellular spaceextracellular matrix UniRule annotation

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrixSAAS annotation, Secreted

PTM / Processingi

Keywords - PTMi

Disulfide bondSAAS annotation


Gene expression databases

ExpressionAtlasiF5H034. baseline and differential.


3D structure databases


Family & Domainsi

Sequence similaritiesi

Belongs to the Wnt family.UniRule annotation

Phylogenomic databases


Family and domain databases

InterProiIPR005817. Wnt.
IPR026537. Wnt5b.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PTHR12027:SF87. PTHR12027:SF87. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]


Sequence statusi: Fragment.

F5H034-1 [UniParc]FASTAAdd to Basket

« Hide

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60 70 80 90 100
Mass (Da):13,238
Last modified:June 28, 2011 - v1

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei118 – 1181Imported

Sequence databases

Select the link destinations:
Links Updated
AC004671 Genomic DNA. No translation available.
AC005182 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000539198; ENSP00000438414; ENSG00000111186.


Sequence databases

Select the link destinations:
Links Updated
AC004671 Genomic DNA. No translation available.
AC005182 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortali F5H034.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000539198 ; ENSP00000438414 ; ENSG00000111186 .

Organism-specific databases

HGNCi HGNC:16265. WNT5B.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00760000118943.

Miscellaneous databases

ChiTaRSi WNT5B. human.
NextBioi 35507947.

Gene expression databases

Bgeei F5H034.
ExpressionAtlasi F5H034. baseline and differential.

Family and domain databases

InterProi IPR005817. Wnt.
IPR026537. Wnt5b.
[Graphical view ]
PANTHERi PTHR12027. PTHR12027. 1 hit.
PTHR12027:SF87. PTHR12027:SF87. 1 hit.
Pfami PF00110. wnt. 1 hit.
[Graphical view ]
SMARTi SM00097. WNT1. 1 hit.
[Graphical view ]
ProtoNeti Search...


« Hide 'large scale' publications
  1. "The finished DNA sequence of human chromosome 12."
    Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A., null.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiF5H034_HUMAN
AccessioniPrimary (citable) accession number: F5H034
Entry historyi
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: January 7, 2015
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.



The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.