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Protein

WW domain-containing oxidoreductase

Gene

Wwox

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm (By similarity). May also play a role in tumor necrosis factor (TNF)-mediated cell death. Required for normal bone development.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei260 – 2601SubstrateBy similarity
Active sitei293 – 2931Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi131 – 1377NADPBy similarity

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  • cellular response to transforming growth factor beta stimulus Source: BHF-UCL
  • extrinsic apoptotic signaling pathway Source: MGI
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  • negative regulation of Wnt signaling pathway Source: UniProtKB
  • osteoblast differentiation Source: MGI
  • positive regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • skeletal system morphogenesis Source: MGI
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis, Wnt signaling pathway

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-MMU-1251985. Nuclear signaling by ERBB4.

Names & Taxonomyi

Protein namesi
Recommended name:
WW domain-containing oxidoreductase (EC:1.1.1.-)
Gene namesi
Name:Wwox
Synonyms:Wox1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1931237. Wwox.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • Golgi apparatus Source: MGI
  • microvillus Source: Ensembl
  • mitochondrion Source: MGI
  • nucleus Source: BHF-UCL
  • plasma membrane Source: Ensembl
  • RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Indistinguishable from wild-type at birth, but die after three weeks due to metabolic syndrome characterized by serum hypoproteinemia, hypoalbuminemia, hypoglycemia, hypocalcemia, hypotriglyceridemia and hypocholesterolemia, growth retardation, decreased bone formation and increased bone resorption. In addition, spontaneous tumor development was observed.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 544KRKR → QGTG: Abolishes the TNF-induced nuclear translocation. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414WW domain-containing oxidoreductasePRO_0000054816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphothreonineCombined sources
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei33 – 331Phosphotyrosine1 Publication
Modified residuei287 – 2871Phosphotyrosine; by TNK2By similarity

Post-translational modificationi

Phosphorylated upon genotoxic stress. Phosphorylation of Tyr-33 regulates interaction with TP53, TP73 and MAPK8. May also regulate proapoptotic activity. Phosphorylation by TNK2 is associated with polyubiquitination and degradation (By similarity).By similarity
Ubiquitinated when phosphorylated by TNK2, leading to its degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ91WL8.
MaxQBiQ91WL8.
PaxDbiQ91WL8.
PRIDEiQ91WL8.

PTM databases

iPTMnetiQ91WL8.
PhosphoSiteiQ91WL8.

Expressioni

Tissue specificityi

Ubiquitous. In the brain, expressed in cortex, striatum, hippocampus and cerebellum (at protein level). Detected in embryonic skeleton, in cranofacial bones, vertebrae and limb bones. Detected in chondrocytes and osteoblasts.3 Publications

Developmental stagei

Expression starts at E8 in the developing heart. Higher expression in the brain is detected between E12 and E16. High levels of expression in dorsal root ganglia and spinal nerves were observed throughout all developmental stages. In later developmental stages expression is more prominent in skeletal systems (at protein level).1 Publication

Inductioni

By hyaluronidase. Up-regulated in outer and inner nuclear layers during retinal degeneration.2 Publications

Gene expression databases

BgeeiQ91WL8.
CleanExiMM_WWOX.
GenevisibleiQ91WL8. MM.

Interactioni

Subunit structurei

Interacts with TP53, TP73/p73 and MAPK8. Interacts with MAPT/TAU. Forms a ternary complex with TP53 and MDM2 and interacts with ERBB4, LITAF and WBP1. May interact with FAM189B and SCOTIN (By similarity). Interacts with HYAL2 and RUNX2. Interacts with TNK2 (By similarity). Interacts with TMEM207 (By similarity).By similarity

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi219796. 4 interactions.
STRINGi10090.ENSMUSP00000004756.

Structurei

3D structure databases

ProteinModelPortaliQ91WL8.
SMRiQ91WL8. Positions 18-101, 121-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 4934WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini57 – 9034WW 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 414290Interaction with MAPTAdd
BLAST
Regioni209 – 27365Mediates targeting to the mitochondriaAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi50 – 556Nuclear localization signal

Domaini

The WW 1 domain mediates interaction with TP73, TFAP2C, LITAF, WBP1 and probably TP53.2 Publications

Sequence similaritiesi

Contains 2 WW domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1208. Eukaryota.
COG1028. LUCA.
COG5021. LUCA.
GeneTreeiENSGT00760000119068.
HOGENOMiHOG000169779.
HOVERGENiHBG078800.
InParanoidiQ91WL8.
KOiK19329.
OMAiYSNIHRS.
OrthoDBiEOG73Z2TK.
PhylomeDBiQ91WL8.
TreeFamiTF105428.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF00397. WW. 2 hits.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SMARTiSM00456. WW. 2 hits.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiPS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q91WL8-1) [UniParc]FASTAAdd to basket

Also known as: Wox1

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
MAALRYAGLD DTDSEDELPP GWEERTTKDG WVYYANHTEE KTQWEHPKTG
60 70 80 90 100
KRKRVAGDLP YGWEQETDEN GQVFFVDHIN KRTTYLDPRL AFTVDDNPTK
110 120 130 140 150
PTTRQRYDGS TTAMEILQGR DFTGKVVLVT GANSGIGFET AKSFALHGAH
160 170 180 190 200
VILACRNLSR ASEAVSRILE EWHKAKVEAM TLDLAVLRSV QHFAEAFKAK
210 220 230 240 250
NVSLHVLVCN AGTFALPWGL TKDGLETTFQ VNHLGHFYLV QLLQDVLCRS
260 270 280 290 300
SPARVIVVSS ESHRFTDIND SSGKLDLSRL SPPRSDYWAM LAYNRSKLCN
310 320 330 340 350
ILFSNELHRR LSPRGVTSNA VHPGNMMYSA IHRNSWVYKL LFTLARPFTK
360 370 380 390 400
SMQQGAATTV YCAVAPELEG LGGMYFNNCC RCLPSEEAQS EETARALWEL
410
SERLIQDRLG SPSS
Length:414
Mass (Da):46,512
Last modified:December 1, 2001 - v1
Checksum:i3C83AE3085B6A931
GO
Isoform 2 (identifier: Q91WL8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     137-158: GFETAKSFALHGAHVILACRNL → ALSPLLGERCIRRRQVLCSVFG
     159-414: Missing.

Note: No experimental confirmation available.
Show »
Length:158
Mass (Da):17,970
Checksum:iE9730E89E24FBFBD
GO
Isoform 3 (identifier: Q91WL8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     353-354: QQ → IL
     355-414: Missing.

Note: No experimental confirmation available.
Show »
Length:354
Mass (Da):40,018
Checksum:i41CBA77635E5E985
GO
Isoform 4 (identifier: Q91WL8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     353-367: QQGAATTVYCAVAPE → KPCMIGHTCDPNPRN
     368-414: Missing.

Note: No experimental confirmation available.
Show »
Length:367
Mass (Da):41,457
Checksum:iFA7DA8F79742CB91
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351G → V in BAB31244 (PubMed:16141072).Curated
Sequence conflicti231 – 2311V → A in AAF31693 (PubMed:11058590).Curated
Sequence conflicti231 – 2311V → A in AAL03972 (PubMed:11979549).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei137 – 15822GFETA…ACRNL → ALSPLLGERCIRRRQVLCSV FG in isoform 2. 1 PublicationVSP_016370Add
BLAST
Alternative sequencei159 – 414256Missing in isoform 2. 1 PublicationVSP_016371Add
BLAST
Alternative sequencei353 – 36715QQGAA…AVAPE → KPCMIGHTCDPNPRN in isoform 4. 1 PublicationVSP_016372Add
BLAST
Alternative sequencei353 – 3542QQ → IL in isoform 3. 1 PublicationVSP_016373
Alternative sequencei355 – 41460Missing in isoform 3. 1 PublicationVSP_016374Add
BLAST
Alternative sequencei368 – 41447Missing in isoform 4. 1 PublicationVSP_016375Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF187014 mRNA. Translation: AAF31693.1.
AK018507 mRNA. Translation: BAB31244.1.
AK019911 mRNA. Translation: BAB31911.1.
AK046903 mRNA. Translation: BAC32916.1.
AK078528 mRNA. Translation: BAC37325.1.
BC014716 mRNA. Translation: AAH14716.1.
AH011063 Genomic DNA. Translation: AAL03972.1.
CCDSiCCDS22691.1. [Q91WL8-1]
RefSeqiNP_062519.2. NM_019573.3. [Q91WL8-1]
XP_006531577.1. XM_006531514.2. [Q91WL8-3]
XP_011246860.1. XM_011248558.1. [Q91WL8-4]
UniGeneiMm.440420.

Genome annotation databases

EnsembliENSMUST00000004756; ENSMUSP00000004756; ENSMUSG00000004637. [Q91WL8-1]
ENSMUST00000109107; ENSMUSP00000104735; ENSMUSG00000004637. [Q91WL8-2]
ENSMUST00000109108; ENSMUSP00000104736; ENSMUSG00000004637. [Q91WL8-4]
ENSMUST00000160862; ENSMUSP00000125626; ENSMUSG00000004637. [Q91WL8-3]
GeneIDi80707.
KEGGimmu:80707.
UCSCiuc009noc.2. mouse. [Q91WL8-2]
uc009nod.2. mouse. [Q91WL8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF187014 mRNA. Translation: AAF31693.1.
AK018507 mRNA. Translation: BAB31244.1.
AK019911 mRNA. Translation: BAB31911.1.
AK046903 mRNA. Translation: BAC32916.1.
AK078528 mRNA. Translation: BAC37325.1.
BC014716 mRNA. Translation: AAH14716.1.
AH011063 Genomic DNA. Translation: AAL03972.1.
CCDSiCCDS22691.1. [Q91WL8-1]
RefSeqiNP_062519.2. NM_019573.3. [Q91WL8-1]
XP_006531577.1. XM_006531514.2. [Q91WL8-3]
XP_011246860.1. XM_011248558.1. [Q91WL8-4]
UniGeneiMm.440420.

3D structure databases

ProteinModelPortaliQ91WL8.
SMRiQ91WL8. Positions 18-101, 121-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219796. 4 interactions.
STRINGi10090.ENSMUSP00000004756.

PTM databases

iPTMnetiQ91WL8.
PhosphoSiteiQ91WL8.

Proteomic databases

EPDiQ91WL8.
MaxQBiQ91WL8.
PaxDbiQ91WL8.
PRIDEiQ91WL8.

Protocols and materials databases

DNASUi80707.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004756; ENSMUSP00000004756; ENSMUSG00000004637. [Q91WL8-1]
ENSMUST00000109107; ENSMUSP00000104735; ENSMUSG00000004637. [Q91WL8-2]
ENSMUST00000109108; ENSMUSP00000104736; ENSMUSG00000004637. [Q91WL8-4]
ENSMUST00000160862; ENSMUSP00000125626; ENSMUSG00000004637. [Q91WL8-3]
GeneIDi80707.
KEGGimmu:80707.
UCSCiuc009noc.2. mouse. [Q91WL8-2]
uc009nod.2. mouse. [Q91WL8-1]

Organism-specific databases

CTDi51741.
MGIiMGI:1931237. Wwox.

Phylogenomic databases

eggNOGiKOG1208. Eukaryota.
COG1028. LUCA.
COG5021. LUCA.
GeneTreeiENSGT00760000119068.
HOGENOMiHOG000169779.
HOVERGENiHBG078800.
InParanoidiQ91WL8.
KOiK19329.
OMAiYSNIHRS.
OrthoDBiEOG73Z2TK.
PhylomeDBiQ91WL8.
TreeFamiTF105428.

Enzyme and pathway databases

ReactomeiR-MMU-1251985. Nuclear signaling by ERBB4.

Miscellaneous databases

ChiTaRSiWwox. mouse.
NextBioi350059.
PROiQ91WL8.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WL8.
CleanExiMM_WWOX.
GenevisibleiQ91WL8. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF00397. WW. 2 hits.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SMARTiSM00456. WW. 2 hits.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiPS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Hyaluronidase induction of a WW domain-containing oxidoreductase that enhances tumor necrosis factor cytotoxicity."
    Chang N.-S., Pratt N., Heath J., Schultz L., Sleve D., Carey G.B., Zevotek N.
    J. Biol. Chem. 276:3361-3370(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 51-LYS--ARG-54, DOMAIN, INTERACTION WITH TP53.
    Tissue: Fibroblast.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Colon, Embryo and Pituitary.
  3. "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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Kidney.
  4. "The common fragile site FRA16D and its associated gene WWOX are highly conserved in the mouse at Fra8E1."
    Krummel K.A., Denison S.R., Calhoun E., Phillips L.A., Smith D.I.
    Genes Chromosomes Cancer 34:154-167(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-414.
  5. "JNK1 physically interacts with WW domain-containing oxidoreductase (WOX1) and inhibits WOX1-mediated apoptosis."
    Chang N.-S., Doherty J., Ensign A.
    J. Biol. Chem. 278:9195-9202(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK8 AND TP53.
  6. "Down-regulation of WW domain-containing oxidoreductase induces Tau phosphorylation in vitro. A potential role in Alzheimer's disease."
    Sze C.-I., Su M., Pugazhenthi S., Jambal P., Hsu L.-J., Heath J., Schultz L., Chang N.-S.
    J. Biol. Chem. 279:30498-30506(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPT.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  8. "Expression of WW domain-containing oxidoreductase WOX1 in the developing murine nervous system."
    Chen S.-T., Chuang J.-I., Wang J.P., Tsai M.S., Li H., Chang N.-S.
    Neuroscience 124:831-839(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  9. "WOX1 is essential for tumor necrosis factor-, UV light-, staurosporine-, and p53-mediated cell death, and its tyrosine 33-phosphorylated form binds and stabilizes serine 46-phosphorylated p53."
    Chang N.-S., Doherty J., Ensign A., Schultz L., Hsu L.-J., Hong Q.
    J. Biol. Chem. 280:43100-43108(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53, DOMAIN.
  10. "Light-induced retinal damage involves tyrosine 33 phosphorylation, mitochondrial and nuclear translocation of WW domain-containing oxidoreductase in vivo."
    Chen S.-T., Chuang J.-I., Cheng C.-L., Hsu L.-J., Chang N.-S.
    Neuroscience 130:397-407(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  12. "The WWOX tumor suppressor is essential for postnatal survival and normal bone metabolism."
    Aqeilan R.I., Hassan M.Q., de Bruin A., Hagan J.P., Volinia S., Palumbo T., Hussain S., Lee S.-H., Gaur T., Stein G.S., Lian J.B., Croce C.M.
    J. Biol. Chem. 283:21629-21639(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  13. "Transforming growth factor beta1 signaling via interaction with cell surface Hyal-2 and recruitment of WWOX/WOX1."
    Hsu L.-J., Schultz L., Hong Q., Van Moer K., Heath J., Li M.-Y., Lai F.-J., Lin S.-R., Lee M.-H., Lo C.-P., Lin Y.-S., Chen S.-T., Chang N.-S.
    J. Biol. Chem. 284:16049-16059(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT TYR-33, SUBCELLULAR LOCATION, INTERACTION WITH HYAL2.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12 AND SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiWWOX_MOUSE
AccessioniPrimary (citable) accession number: Q91WL8
Secondary accession number(s): Q8C8J6
, Q920Y2, Q9D2B3, Q9D339, Q9JLF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: December 1, 2001
Last modified: April 13, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.