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O14904

- WNT9A_HUMAN

UniProt

O14904 - WNT9A_HUMAN

Protein

Protein Wnt-9a

Gene

WNT9A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (10 May 2002)
      Previous versions | rss
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    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: RefGenome

    GO - Biological processi

    1. canonical Wnt signaling pathway Source: Ensembl
    2. cell-cell signaling Source: UniProtKB
    3. cell fate commitment Source: RefGenome
    4. cellular response to retinoic acid Source: UniProtKB
    5. cornea development in camera-type eye Source: BHF-UCL
    6. embryonic forelimb morphogenesis Source: Ensembl
    7. embryonic skeletal joint development Source: BHF-UCL
    8. embryonic skeletal system morphogenesis Source: Ensembl
    9. iris morphogenesis Source: BHF-UCL
    10. mitotic cell cycle checkpoint Source: BHF-UCL
    11. multicellular organismal development Source: UniProtKB
    12. negative regulation of cartilage development Source: Ensembl
    13. negative regulation of cell death Source: Ensembl
    14. negative regulation of cell proliferation Source: BHF-UCL
    15. negative regulation of chondrocyte differentiation Source: BHF-UCL
    16. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    17. neuron differentiation Source: UniProtKB
    18. positive regulation of cell differentiation Source: Ensembl
    19. positive regulation of smoothened signaling pathway Source: Ensembl
    20. Wnt signaling pathway Source: RefGenome

    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_200643. negative regulation of TCF-dependent signaling by WNT ligand antagonists.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein Wnt-9a
    Alternative name(s):
    Protein Wnt-14
    Gene namesi
    Name:WNT9A
    Synonyms:WNT14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12778. WNT9A.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: RefGenome
    3. extracellular vesicular exosome Source: UniProt
    4. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37379.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 365336Protein Wnt-9aPRO_0000041455Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi93 ↔ 104By similarity
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi141 ↔ 149By similarity
    Disulfide bondi151 ↔ 168By similarity
    Disulfide bondi215 ↔ 229By similarity
    Disulfide bondi217 ↔ 224By similarity
    Lipidationi221 – 2211O-palmitoyl serine; by PORCNBy similarity
    Disulfide bondi313 ↔ 324By similarity
    Disulfide bondi339 ↔ 354By similarity
    Disulfide bondi341 ↔ 351By similarity
    Disulfide bondi346 ↔ 347By similarity

    Post-translational modificationi

    Palmitoylation at Ser-221 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

    PaxDbiO14904.
    PRIDEiO14904.

    Expressioni

    Gene expression databases

    ArrayExpressiO14904.
    BgeeiO14904.
    CleanExiHS_WNT9A.
    GenevestigatoriO14904.

    Organism-specific databases

    HPAiHPA011223.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000272164.

    Structurei

    3D structure databases

    ProteinModelPortaliO14904.
    SMRiO14904. Positions 92-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Wnt family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG291879.
    HOGENOMiHOG000039529.
    HOVERGENiHBG001595.
    InParanoidiO14904.
    KOiK01064.
    OMAiVECKQCT.
    OrthoDBiEOG7G7KP9.
    PhylomeDBiO14904.
    TreeFamiTF105310.

    Family and domain databases

    InterProiIPR005817. Wnt.
    IPR013303. Wnt9a.
    IPR018161. Wnt_CS.
    [Graphical view]
    PANTHERiPTHR12027. PTHR12027. 1 hit.
    PfamiPF00110. wnt. 1 hit.
    [Graphical view]
    PRINTSiPR01894. WNT14PROTEIN.
    PR01349. 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.

    O14904-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLDGSPLARW LAAAFGLTLL LAALRPSAAY FGLTGSEPLT ILPLTLEPEA    50
    AAQAHYKACD RLKLERKQRR MCRRDPGVAE TLVEAVSMSA LECQFQFRFE 100
    RWNCTLEGRY RASLLKRGFK ETAFLYAISS AGLTHALAKA CSAGRMERCT 150
    CDEAPDLENR EAWQWGGCGD NLKYSSKFVK EFLGRRSSKD LRARVDFHNN 200
    LVGVKVIKAG VETTCKCHGV SGSCTVRTCW RQLAPFHEVG KHLKHKYETA 250
    LKVGSTTNEA AGEAGAISPP RGRASGAGGS DPLPRTPELV HLDDSPSFCL 300
    AGRFSPGTAG RRCHREKNCE SICCGRGHNT QSRVVTRPCQ CQVRWCCYVE 350
    CRQCTQREEV YTCKG 365
    Length:365
    Mass (Da):40,320
    Last modified:May 10, 2002 - v2
    Checksum:i1E1284D744C6A9B2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti260 – 2601A → T.
    Corresponds to variant rs8192633 [ dbSNP | Ensembl ].
    VAR_052956

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB060283 mRNA. Translation: BAB61051.1.
    AL360269 Genomic DNA. Translation: CAH71122.1.
    CH471098 Genomic DNA. Translation: EAW69821.1.
    BC111960 mRNA. Translation: AAI11961.1.
    BC113431 mRNA. Translation: AAI13432.1.
    AF028702 Genomic DNA. Translation: AAC39550.1.
    CCDSiCCDS31045.1.
    RefSeqiNP_003386.1. NM_003395.2.
    UniGeneiHs.149504.

    Genome annotation databases

    EnsembliENST00000272164; ENSP00000272164; ENSG00000143816.
    GeneIDi7483.
    KEGGihsa:7483.
    UCSCiuc001hri.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB060283 mRNA. Translation: BAB61051.1 .
    AL360269 Genomic DNA. Translation: CAH71122.1 .
    CH471098 Genomic DNA. Translation: EAW69821.1 .
    BC111960 mRNA. Translation: AAI11961.1 .
    BC113431 mRNA. Translation: AAI13432.1 .
    AF028702 Genomic DNA. Translation: AAC39550.1 .
    CCDSi CCDS31045.1.
    RefSeqi NP_003386.1. NM_003395.2.
    UniGenei Hs.149504.

    3D structure databases

    ProteinModelPortali O14904.
    SMRi O14904. Positions 92-356.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000272164.

    Proteomic databases

    PaxDbi O14904.
    PRIDEi O14904.

    Protocols and materials databases

    DNASUi 7483.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272164 ; ENSP00000272164 ; ENSG00000143816 .
    GeneIDi 7483.
    KEGGi hsa:7483.
    UCSCi uc001hri.2. human.

    Organism-specific databases

    CTDi 7483.
    GeneCardsi GC01M228106.
    HGNCi HGNC:12778. WNT9A.
    HPAi HPA011223.
    MIMi 602863. gene.
    neXtProti NX_O14904.
    PharmGKBi PA37379.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291879.
    HOGENOMi HOG000039529.
    HOVERGENi HBG001595.
    InParanoidi O14904.
    KOi K01064.
    OMAi VECKQCT.
    OrthoDBi EOG7G7KP9.
    PhylomeDBi O14904.
    TreeFami TF105310.

    Enzyme and pathway databases

    Reactomei REACT_163710. WNT ligand biogenesis and trafficking.
    REACT_18372. Class B/2 (Secretin family receptors).
    REACT_200643. negative regulation of TCF-dependent signaling by WNT ligand antagonists.

    Miscellaneous databases

    ChiTaRSi WNT9A. human.
    GeneWikii WNT9A.
    GenomeRNAii 7483.
    NextBioi 29314.
    PROi O14904.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14904.
    Bgeei O14904.
    CleanExi HS_WNT9A.
    Genevestigatori O14904.

    Family and domain databases

    InterProi IPR005817. Wnt.
    IPR013303. Wnt9a.
    IPR018161. Wnt_CS.
    [Graphical view ]
    PANTHERi PTHR12027. PTHR12027. 1 hit.
    Pfami PF00110. wnt. 1 hit.
    [Graphical view ]
    PRINTSi PR01894. WNT14PROTEIN.
    PR01349. WNTPROTEIN.
    SMARTi SM00097. WNT1. 1 hit.
    [Graphical view ]
    PROSITEi PS00246. WNT1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
    2. "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].
    3. 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].
    5. "Isolation of two novel WNT genes, WNT14 and WNT15, one of which (WNT15) is closely linked to WNT3 on human chromosome 17q21."
      Bergstein I., Eisenberg L.M., Bhalerao J., Jenkins N.A., Copeland N.G., Osborne M.P., Bowcock A.M., Brown A.M.C.
      Genomics 46:450-458(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 221-343.

    Entry informationi

    Entry nameiWNT9A_HUMAN
    AccessioniPrimary (citable) accession number: O14904
    Secondary accession number(s): A6NLW2
    , Q2M2J3, Q5VWU0, Q96S50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 10, 2002
    Last modified: October 1, 2014
    This is version 124 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 1
      Human chromosome 1: 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

    External Data

    Dasty 3