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O00744

- WN10B_HUMAN

UniProt

O00744 - WN10B_HUMAN

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Protein

Protein Wnt-10b

Gene

WNT10B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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: RefGenome
  2. receptor agonist activity Source: BHF-UCL

GO - Biological processi

  1. bone trabecula formation Source: Ensembl
  2. canonical Wnt signaling pathway Source: BHF-UCL
  3. cell cycle arrest Source: Ensembl
  4. cell fate commitment Source: RefGenome
  5. cellular response to cAMP Source: Ensembl
  6. cellular response to hydrostatic pressure Source: Ensembl
  7. cellular response to parathyroid hormone stimulus Source: Ensembl
  8. cellular response to retinoic acid Source: UniProtKB
  9. chondrocyte differentiation Source: UniProtKB
  10. fungiform papilla development Source: Ensembl
  11. G2/M transition of mitotic cell cycle Source: Ensembl
  12. hematopoietic stem cell proliferation Source: BHF-UCL
  13. lipid metabolic process Source: Ensembl
  14. myoblast differentiation involved in skeletal muscle regeneration Source: Ensembl
  15. negative regulation of epithelial cell proliferation Source: Ensembl
  16. negative regulation of fat cell differentiation Source: BHF-UCL
  17. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  18. neuron differentiation Source: UniProtKB
  19. positive regulation of anagen Source: Ensembl
  20. positive regulation of apoptotic process Source: BHF-UCL
  21. positive regulation of bone mineralization Source: Ensembl
  22. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  23. positive regulation of cell proliferation Source: Ensembl
  24. positive regulation of epithelial cell differentiation Source: Ensembl
  25. positive regulation of G2/M transition of mitotic cell cycle Source: Ensembl
  26. positive regulation of osteoblast differentiation Source: Ensembl
  27. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: Ensembl
  28. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  29. protein stabilization Source: BHF-UCL
  30. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  31. regulation of skeletal muscle tissue development Source: Ensembl
  32. sensory perception of taste Source: Ensembl
  33. skeletal muscle fiber development Source: Ensembl
  34. smoothened signaling pathway Source: Ensembl
  35. Wnt signaling pathway Source: UniProtKB
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_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiO00744.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Wnt-10b
Alternative name(s):
Protein Wnt-12
Gene namesi
Name:WNT10B
Synonyms:WNT12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:12775. WNT10B.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB
  3. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Split-hand/foot malformation 6 (SHFM6) [MIM:225300]: A limb malformation involving the central rays of the autopod and presenting with syndactyly, median clefts of the hands and feet, and aplasia and/or hypoplasia of the phalanges, metacarpals, and metatarsals. Some patients have been found to have mental retardation, ectodermal and craniofacial findings, and orofacial clefting.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti332 – 3321R → W in SHFM6. 1 Publication
VAR_062516

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi225300. phenotype.
Orphaneti2440. Split hand-split foot malformation.
PharmGKBiPA37377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 389361Protein Wnt-10bPRO_0000041463Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphothreonine1 Publication
Disulfide bondi83 ↔ 94By similarity
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi136 ↔ 144By similarity
Disulfide bondi146 ↔ 199By similarity
Disulfide bondi247 ↔ 261By similarity
Disulfide bondi249 ↔ 256By similarity
Disulfide bondi334 ↔ 349By similarity
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi364 ↔ 379By similarity
Disulfide bondi366 ↔ 376By similarity
Disulfide bondi371 ↔ 372By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO00744.
PRIDEiO00744.

PTM databases

PhosphoSiteiO00744.

Expressioni

Tissue specificityi

Detected in most adult tissues. Highest levels were found in heart and skeletal muscle. Low levels are found in brain.

Developmental stagei

Infant brain has higher levels of WNT10B than adult brain.

Gene expression databases

BgeeiO00744.
CleanExiHS_WNT10B.
ExpressionAtlasiO00744. baseline and differential.
GenevestigatoriO00744.

Organism-specific databases

HPAiHPA055048.

Interactioni

Protein-protein interaction databases

BioGridi113317. 6 interactions.
STRINGi9606.ENSP00000301061.

Structurei

3D structure databases

ProteinModelPortaliO00744.
SMRiO00744. Positions 69-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Wnt family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG240772.
GeneTreeiENSGT00690000101857.
HOGENOMiHOG000039528.
HOVERGENiHBG001595.
InParanoidiO00744.
KOiK01357.
OMAiSERCNCR.
OrthoDBiEOG7C8GJ8.
PhylomeDBiO00744.
TreeFamiTF105310.

Family and domain databases

InterProiIPR005817. Wnt.
IPR013302. Wnt10.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01893. WNT10PROTEIN.
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: O00744-1) [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
MLEEPRPRPP PSGLAGLLFL ALCSRALSNE ILGLKLPGEP PLTANTVCLT
60 70 80 90 100
LSGLSKRQLG LCLRNPDVTA SALQGLHIAV HECQHQLRDQ RWNCSALEGG
110 120 130 140 150
GRLPHHSAIL KRGFRESAFS FSMLAAGVMH AVATACSLGK LVSCGCGWKG
160 170 180 190 200
SGEQDRLRAK LLQLQALSRG KSFPHSLPSP GPGSSPSPGP QDTWEWGGCN
210 220 230 240 250
HDMDFGEKFS RDFLDSREAP RDIQARMRIH NNRVGRQVVT ENLKRKCKCH
260 270 280 290 300
GTSGSCQFKT CWRAAPEFRA VGAALRERLG RAIFIDTHNR NSGAFQPRLR
310 320 330 340 350
PRRLSGELVY FEKSPDFCER DPTMGSPGTR GRACNKTSRL LDGCGSLCCG
360 370 380
RGHNVLRQTR VERCHCRFHW CCYVLCDECK VTEWVNVCK
Length:389
Mass (Da):43,000
Last modified:May 10, 2002 - v2
Checksum:iF973F2CA0DB115EF
GO
Isoform 2 (identifier: O00744-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     172-191: SFPHSLPSPGPGSSPSPGPQ → LPGTSRHECESTTTGWGARW
     192-389: Missing.

Note: No experimental confirmation available.

Show »
Length:191
Mass (Da):20,483
Checksum:i07A9A02483680C55
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601G → D in AAB51685. (PubMed:9284937)Curated
Sequence conflicti149 – 1491K → R in CAA65769. (PubMed:9121776)Curated
Sequence conflicti295 – 2951F → S in CAA65769. (PubMed:9121776)Curated
Sequence conflicti311 – 3111F → L in CAA65769. (PubMed:9121776)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771H → Y.1 Publication
Corresponds to variant rs151284263 [ dbSNP | Ensembl ].
VAR_062512
Natural varianti256 – 2561C → Y Associated with obesity; abrogates the ability of WNT10B to activate canonical Wnt signalling and blocks adipogenesis. 1 Publication
VAR_062513
Natural varianti285 – 2851I → T.1 Publication
VAR_062514
Natural varianti301 – 3011P → S.1 Publication
Corresponds to variant rs35034312 [ dbSNP | Ensembl ].
VAR_062515
Natural varianti332 – 3321R → W in SHFM6. 1 Publication
VAR_062516

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei172 – 19120SFPHS…SPGPQ → LPGTSRHECESTTTGWGARW in isoform 2. 1 PublicationVSP_056289Add
BLAST
Alternative sequencei192 – 389198Missing in isoform 2. 1 PublicationVSP_056290Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81787 mRNA. Translation: AAB51685.1.
AB070724 mRNA. Translation: BAB72181.1.
AK312906 mRNA. Translation: BAG35752.1.
AC073610 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58028.1.
BC096353 mRNA. Translation: AAH96353.1.
BC096354 mRNA. Translation: AAH96354.1.
BC096355 mRNA. Translation: AAH96355.1.
BC096356 mRNA. Translation: AAH96356.1.
X97057 mRNA. Translation: CAA65769.1.
AF028700 Genomic DNA. Translation: AAC39549.1.
CCDSiCCDS8775.1. [O00744-1]
RefSeqiNP_003385.2. NM_003394.3. [O00744-1]
UniGeneiHs.91985.

Genome annotation databases

EnsembliENST00000301061; ENSP00000301061; ENSG00000169884. [O00744-1]
ENST00000407467; ENSP00000384691; ENSG00000169884. [O00744-2]
GeneIDi7480.
KEGGihsa:7480.
UCSCiuc001rss.3. human. [O00744-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81787 mRNA. Translation: AAB51685.1 .
AB070724 mRNA. Translation: BAB72181.1 .
AK312906 mRNA. Translation: BAG35752.1 .
AC073610 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58028.1 .
BC096353 mRNA. Translation: AAH96353.1 .
BC096354 mRNA. Translation: AAH96354.1 .
BC096355 mRNA. Translation: AAH96355.1 .
BC096356 mRNA. Translation: AAH96356.1 .
X97057 mRNA. Translation: CAA65769.1 .
AF028700 Genomic DNA. Translation: AAC39549.1 .
CCDSi CCDS8775.1. [O00744-1 ]
RefSeqi NP_003385.2. NM_003394.3. [O00744-1 ]
UniGenei Hs.91985.

3D structure databases

ProteinModelPortali O00744.
SMRi O00744. Positions 69-380.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113317. 6 interactions.
STRINGi 9606.ENSP00000301061.

PTM databases

PhosphoSitei O00744.

Proteomic databases

PaxDbi O00744.
PRIDEi O00744.

Protocols and materials databases

DNASUi 7480.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301061 ; ENSP00000301061 ; ENSG00000169884 . [O00744-1 ]
ENST00000407467 ; ENSP00000384691 ; ENSG00000169884 . [O00744-2 ]
GeneIDi 7480.
KEGGi hsa:7480.
UCSCi uc001rss.3. human. [O00744-1 ]

Organism-specific databases

CTDi 7480.
GeneCardsi GC12M049359.
HGNCi HGNC:12775. WNT10B.
HPAi HPA055048.
MIMi 225300. phenotype.
601906. gene.
neXtProti NX_O00744.
Orphaneti 2440. Split hand-split foot malformation.
PharmGKBi PA37377.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG240772.
GeneTreei ENSGT00690000101857.
HOGENOMi HOG000039528.
HOVERGENi HBG001595.
InParanoidi O00744.
KOi K01357.
OMAi SERCNCR.
OrthoDBi EOG7C8GJ8.
PhylomeDBi O00744.
TreeFami TF105310.

Enzyme and pathway databases

Reactomei REACT_163710. WNT ligand biogenesis and trafficking.
REACT_18372. Class B/2 (Secretin family receptors).
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki O00744.

Miscellaneous databases

GeneWikii WNT10B.
GenomeRNAii 7480.
NextBioi 29300.
PROi O00744.
SOURCEi Search...

Gene expression databases

Bgeei O00744.
CleanExi HS_WNT10B.
ExpressionAtlasi O00744. baseline and differential.
Genevestigatori O00744.

Family and domain databases

InterProi IPR005817. Wnt.
IPR013302. Wnt10.
IPR018161. Wnt_CS.
[Graphical view ]
PANTHERi PTHR12027. PTHR12027. 1 hit.
Pfami PF00110. wnt. 1 hit.
[Graphical view ]
PRINTSi PR01893. WNT10PROTEIN.
PR01349. WNTPROTEIN.
SMARTi SM00097. WNT1. 1 hit.
[Graphical view ]
PROSITEi PS00246. WNT1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, characterization and chromosomal localization of human WNT10B."
    Hardiman G., Kastelein R.A., Bazan J.F.
    Cytogenet. Cell Genet. 77:278-282(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Proto-oncogene WNT10B is up-regulated by tumor necrosis factor alpha in human gastric cancer cell line MKN45."
    Saitoh T., Kirikoshi H., Mine T., Katoh M.
    Int. J. Oncol. 19:1187-1192(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Subthalamic nucleus.
  4. "The finished DNA sequence of human chromosome 12."
    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.H., 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.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
  7. "A novel human Wnt gene, WNT10B, maps to 12q13 and is expressed in human breast carcinomas."
    Bui T.D., Rankin J., Smith K., Huguet E.L., Ruben S., Strachan T., Harris A.L., Lindsay S.
    Oncogene 14:1249-1253(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-347 (ISOFORM 1).
    Tissue: Fetal brain.
  8. "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 253-368.
    Tissue: Placenta.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: VARIANTS TYR-77; TYR-256; THR-285 AND SER-301, ASSOCIATION OF VARIANT TYR-256 WITH OBESITY.
  11. "Homozygous WNT10b mutation and complex inheritance in Split-Hand/Foot Malformation."
    Ugur S.A., Tolun A.
    Hum. Mol. Genet. 17:2644-2653(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SHFM6 TRP-332.

Entry informationi

Entry nameiWN10B_HUMAN
AccessioniPrimary (citable) accession number: O00744
Secondary accession number(s): B2R7A5
, O00747, Q4VAJ4, Q4VAJ5, Q8WZ97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 10, 2002
Last modified: November 26, 2014
This is version 122 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. 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