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P56704

- WNT3A_HUMAN

UniProt

P56704 - WNT3A_HUMAN

Protein

Protein Wnt-3a

Gene

WNT3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (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. 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

    1. frizzled binding Source: RefGenome
    2. protein binding Source: UniProtKB
    3. receptor agonist activity Source: BHF-UCL
    4. transcription coactivator activity Source: BHF-UCL

    GO - Biological processi

    1. axis elongation involved in somitogenesis Source: Ensembl
    2. axon guidance Source: Ensembl
    3. canonical Wnt signaling pathway Source: BHF-UCL
    4. canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment Source: BHF-UCL
    5. cell proliferation in forebrain Source: BHF-UCL
    6. cellular protein localization Source: Ensembl
    7. cellular response to retinoic acid Source: UniProtKB
    8. COP9 signalosome assembly Source: BHF-UCL
    9. dorsal/ventral neural tube patterning Source: Ensembl
    10. extracellular matrix organization Source: Ensembl
    11. heart looping Source: Ensembl
    12. hemopoiesis Source: Ensembl
    13. hippocampus development Source: Ensembl
    14. inner ear morphogenesis Source: Ensembl
    15. in utero embryonic development Source: Ensembl
    16. mammary gland development Source: Ensembl
    17. negative regulation of axon extension involved in axon guidance Source: Ensembl
    18. negative regulation of fat cell differentiation Source: Ensembl
    19. negative regulation of heart induction by canonical Wnt signaling pathway Source: BHF-UCL
    20. negative regulation of neurogenesis Source: BHF-UCL
    21. negative regulation of neuron projection development Source: UniProtKB
    22. neuron differentiation Source: UniProtKB
    23. osteoblast differentiation Source: Ensembl
    24. palate development Source: BHF-UCL
    25. paraxial mesodermal cell fate commitment Source: Ensembl
    26. platelet aggregation Source: Ensembl
    27. positive regulation of B cell proliferation Source: Ensembl
    28. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
    29. positive regulation of canonical Wnt signaling pathway involved in controlling type B pancreatic cell proliferation Source: Ensembl
    30. positive regulation of cardiac muscle cell differentiation Source: BHF-UCL
    31. positive regulation of catenin import into nucleus Source: BHF-UCL
    32. positive regulation of cell-cell adhesion mediated by cadherin Source: Ensembl
    33. positive regulation of cell proliferation Source: BHF-UCL
    34. positive regulation of collateral sprouting in absence of injury Source: Ensembl
    35. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    36. positive regulation of dermatome development Source: BHF-UCL
    37. positive regulation of mesodermal cell fate specification Source: BHF-UCL
    38. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    39. positive regulation of protein binding Source: BHF-UCL
    40. positive regulation of protein phosphorylation Source: BHF-UCL
    41. positive regulation of protein tyrosine kinase activity Source: Ensembl
    42. positive regulation of receptor internalization Source: BHF-UCL
    43. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    44. positive regulation of transcription, DNA-templated Source: BHF-UCL
    45. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    46. post-anal tail morphogenesis Source: Ensembl
    47. regulation of microtubule cytoskeleton organization Source: Ensembl
    48. skeletal muscle cell differentiation Source: Ensembl
    49. spinal cord association neuron differentiation Source: Ensembl
    50. Wnt signaling pathway involved in forebrain neuroblast division Source: Ensembl

    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_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200643. negative regulation of TCF-dependent signaling by WNT ligand antagonists.
    REACT_200716. regulation of FZD by ubiquitination.
    REACT_200777. 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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:15983. WNT3A.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular region Source: Reactome
    4. extracellular space Source: BHF-UCL
    5. Golgi lumen Source: Reactome
    6. plasma membrane Source: Reactome
    7. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    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 palmitoylation. 3 Publications
    Mutagenesisi209 – 2091S → T: No effect on palmitoylation 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.

    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 ↔ 88By similarity
    Glycosylationi87 – 871N-linked (GlcNAc...)1 Publication
    Disulfide bondi128 ↔ 136By similarity
    Disulfide bondi138 ↔ 155By similarity
    Disulfide bondi203 ↔ 217By similarity
    Disulfide bondi205 ↔ 212By similarity
    Lipidationi209 – 2091O-palmitoyl serine; by PORCN3 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

    Palmitoylation at Ser-209 by PORCN is required for efficient binding to frizzled receptors. Palmitoylation is required for proper trafficking to cell surface, vacuolar acidification is critical to release palmitoylated WNT3A from WLS in secretory vesicles. A palmitoylation site was proposed at Cys-77, but it was later shown that this cysteine is engaged in a disulfide bond.3 Publications
    Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT3A.
    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.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    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.
    GenevestigatoriP56704.

    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. 4 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.
    HOGENOMiHOG000039529.
    HOVERGENiHBG001595.
    InParanoidiP56704.
    KOiK00312.
    OMAiCTTVNDS.
    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. Align

    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

    MAPLGYFLLL CSLKQALGSY PIWWSLAVGP QYSSLGSQPI LCASIPGLVP    50
    KQLRFCRNYV EIMPSVAEGI KIGIQECQHQ FRGRRWNCTT VHDSLAIFGP 100
    VLDKATRESA FVHAIASAGV AFAVTRSCAE GTAAICGCSS RHQGSPGKGW 150
    KWGGCSEDIE FGGMVSREFA DARENRPDAR SAMNRHNNEA GRQAIASHMH 200
    LKCKCHGLSG SCEVKTCWWS QPDFRAIGDF LKDKYDSASE MVVEKHRESR 250
    GWVETLRPRY TYFKVPTERD LVYYEASPNF CEPNPETGSF GTRDRTCNVS 300
    SHGIDGCDLL CCGRGHNARA ERRREKCRCV FHWCCYVSCQ ECTRVYDVHT 350
    CK 352
    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:
    EMBL
    GenBank
    DDBJ
    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. [P56704-1]
    GeneIDi89780.
    KEGGihsa:89780.
    UCSCiuc001hrp.2. human.
    uc001hrq.2. human. [P56704-1]

    Polymorphism databases

    DMDMi20532424.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1564.1. [P56704-1 ]
    RefSeqi NP_149122.1. NM_033131.3. [P56704-1 ]
    UniGenei Hs.336930.

    3D structure databases

    ProteinModelPortali P56704.
    SMRi P56704. Positions 57-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124599. 4 interactions.
    DIPi DIP-58592N.
    IntActi P56704. 3 interactions.
    STRINGi 9606.ENSP00000284523.

    Chemistry

    BindingDBi P56704.
    ChEMBLi CHEMBL1255137.

    PTM databases

    PhosphoSitei P56704.

    Polymorphism databases

    DMDMi 20532424.

    Proteomic databases

    PaxDbi P56704.
    PRIDEi P56704.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284523 ; ENSP00000284523 ; ENSG00000154342 . [P56704-1 ]
    GeneIDi 89780.
    KEGGi hsa:89780.
    UCSCi uc001hrp.2. human.
    uc001hrq.2. human. [P56704-1 ]

    Organism-specific databases

    CTDi 89780.
    GeneCardsi GC01P228194.
    HGNCi HGNC:15983. WNT3A.
    HPAi HPA050514.
    MIMi 606359. gene.
    neXtProti NX_P56704.
    Orphaneti 85193. Idiopathic juvenile osteoporosis.
    PharmGKBi PA38074.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG284879.
    HOGENOMi HOG000039529.
    HOVERGENi HBG001595.
    InParanoidi P56704.
    KOi K00312.
    OMAi CTTVNDS.
    OrthoDBi EOG7C8GJ8.
    PhylomeDBi P56704.
    TreeFami TF105310.

    Enzyme and pathway databases

    Reactomei REACT_163710. WNT ligand biogenesis and trafficking.
    REACT_18372. Class B/2 (Secretin family receptors).
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200643. negative regulation of TCF-dependent signaling by WNT ligand antagonists.
    REACT_200716. regulation of FZD by ubiquitination.
    REACT_200777. TCF dependent signaling in response to WNT.
    SignaLinki P56704.

    Miscellaneous databases

    GeneWikii WNT3A.
    GenomeRNAii 89780.
    NextBioi 76263.
    PROi P56704.
    SOURCEi Search...

    Gene expression databases

    Bgeei P56704.
    CleanExi HS_WNT3A.
    Genevestigatori P56704.

    Family and domain databases

    InterProi IPR005817. Wnt.
    IPR009141. Wnt3.
    IPR018161. Wnt_CS.
    [Graphical view ]
    PANTHERi PTHR12027. PTHR12027. 1 hit.
    Pfami PF00110. wnt. 1 hit.
    [Graphical view ]
    PRINTSi PR01843. WNT3PROTEIN.
    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] (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: PALMITOYLATION AT SER-209 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, PALMITOYLATION AT SER-209, 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, PALMITOYLATION AT SER-209 BY PORCN.

    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: October 1, 2014
    This is version 130 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. 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