WWOX_MOUSE
ID WWOX_MOUSE Reviewed; 414 AA.
AC Q91WL8; Q8C8J6; Q920Y2; Q9D2B3; Q9D339; Q9JLF5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=WW domain-containing oxidoreductase;
DE EC=1.1.1.-;
GN Name=Wwox; Synonyms=Wox1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF 51-LYS--ARG-54, DOMAIN, AND INTERACTION WITH TP53.
RC TISSUE=Fibroblast;
RX PubMed=11058590; DOI=10.1074/jbc.m007140200;
RA Chang N.-S., Pratt N., Heath J., Schultz L., Sleve D., Carey G.B.,
RA Zevotek N.;
RT "Hyaluronidase induction of a WW domain-containing oxidoreductase that
RT enhances tumor necrosis factor cytotoxicity.";
RL J. Biol. Chem. 276:3361-3370(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Colon, Embryo, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-414.
RX PubMed=11979549; DOI=10.1002/gcc.10047;
RA Krummel K.A., Denison S.R., Calhoun E., Phillips L.A., Smith D.I.;
RT "The common fragile site FRA16D and its associated gene WWOX are highly
RT conserved in the mouse at Fra8E1.";
RL Genes Chromosomes Cancer 34:154-167(2002).
RN [5]
RP INTERACTION WITH MAPK8 AND TP53.
RX PubMed=12514174; DOI=10.1074/jbc.m208373200;
RA Chang N.-S., Doherty J., Ensign A.;
RT "JNK1 physically interacts with WW domain-containing oxidoreductase (WOX1)
RT and inhibits WOX1-mediated apoptosis.";
RL J. Biol. Chem. 278:9195-9202(2003).
RN [6]
RP INTERACTION WITH MAPT.
RX PubMed=15126504; DOI=10.1074/jbc.m401399200;
RA Sze C.-I., Su M., Pugazhenthi S., Jambal P., Hsu L.-J., Heath J.,
RA Schultz L., Chang N.-S.;
RT "Down-regulation of WW domain-containing oxidoreductase induces Tau
RT phosphorylation in vitro. A potential role in Alzheimer's disease.";
RL J. Biol. Chem. 279:30498-30506(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15026124; DOI=10.1016/j.neuroscience.2003.12.036;
RA Chen S.-T., Chuang J.-I., Wang J.P., Tsai M.S., Li H., Chang N.-S.;
RT "Expression of WW domain-containing oxidoreductase WOX1 in the developing
RT murine nervous system.";
RL Neuroscience 124:831-839(2004).
RN [9]
RP INTERACTION WITH TP53, AND DOMAIN.
RX PubMed=16219768; DOI=10.1074/jbc.m505590200;
RA Chang N.-S., Doherty J., Ensign A., Schultz L., Hsu L.-J., Hong Q.;
RT "WOX1 is essential for tumor necrosis factor-, UV light-, staurosporine-,
RT and p53-mediated cell death, and its tyrosine 33-phosphorylated form binds
RT and stabilizes serine 46-phosphorylated p53.";
RL J. Biol. Chem. 280:43100-43108(2005).
RN [10]
RP INDUCTION.
RX PubMed=15664696; DOI=10.1016/j.neuroscience.2004.07.054;
RA Chen S.-T., Chuang J.-I., Cheng C.-L., Hsu L.-J., Chang N.-S.;
RT "Light-induced retinal damage involves tyrosine 33 phosphorylation,
RT mitochondrial and nuclear translocation of WW domain-containing
RT oxidoreductase in vivo.";
RL Neuroscience 130:397-407(2005).
RN [11]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17360458; DOI=10.1073/pnas.0609783104;
RA Aqeilan R.I., Trapasso F., Hussain S., Costinean S., Marshall D.,
RA Pekarsky Y., Hagan J.P., Zanesi N., Kaou M., Stein G.S., Lian J.B.,
RA Croce C.M.;
RT "Targeted deletion of Wwox reveals a tumor suppressor function.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3949-3954(2007).
RN [12]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18487609; DOI=10.1074/jbc.m800855200;
RA Aqeilan R.I., Hassan M.Q., de Bruin A., Hagan J.P., Volinia S., Palumbo T.,
RA Hussain S., Lee S.-H., Gaur T., Stein G.S., Lian J.B., Croce C.M.;
RT "The WWOX tumor suppressor is essential for postnatal survival and normal
RT bone metabolism.";
RL J. Biol. Chem. 283:21629-21639(2008).
RN [13]
RP FUNCTION, PHOSPHORYLATION AT TYR-33, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH HYAL2.
RX PubMed=19366691; DOI=10.1074/jbc.m806688200;
RA Hsu L.-J., Schultz L., Hong Q., Van Moer K., Heath J., Li M.-Y., Lai F.-J.,
RA Lin S.-R., Lee M.-H., Lo C.-P., Lin Y.-S., Chen S.-T., Chang N.-S.;
RT "Transforming growth factor beta1 signaling via interaction with cell
RT surface Hyal-2 and recruitment of WWOX/WOX1.";
RL J. Biol. Chem. 284:16049-16059(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12 AND SER-14, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Putative oxidoreductase. Acts as a tumor suppressor and plays
CC a role in apoptosis. May function synergistically with p53/TP53 to
CC control genotoxic stress-induced cell death. Plays a role in TGFB1
CC signaling and TGFB1-mediated cell death. Inhibits Wnt signaling,
CC probably by sequestering DVL2 in the cytoplasm (By similarity). May
CC also play a role in tumor necrosis factor (TNF)-mediated cell death.
CC Required for normal bone development. {ECO:0000250,
CC ECO:0000269|PubMed:11058590, ECO:0000269|PubMed:19366691}.
CC -!- SUBUNIT: Interacts with TP53, TP73/p73 and MAPK8. Interacts with
CC MAPT/TAU. Forms a ternary complex with TP53 and MDM2 and interacts with
CC ERBB4, LITAF and WBP1. May interact with FAM189B and SCOTIN (By
CC similarity). Interacts with HYAL2 and RUNX2. Interacts with TNK2 (By
CC similarity). Interacts with TMEM207 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19366691}. Nucleus
CC {ECO:0000269|PubMed:11058590, ECO:0000269|PubMed:19366691}.
CC Mitochondrion {ECO:0000269|PubMed:11058590}. Note=Partially localizes
CC to the mitochondria (By similarity). Translocates to the nucleus in
CC response to TGFB1 (PubMed:19366691). Translocates to the nucleus upon
CC genotoxic stress or TNF stimulation (PubMed:11058590).
CC {ECO:0000250|UniProtKB:Q9NZC7, ECO:0000269|PubMed:11058590,
CC ECO:0000269|PubMed:19366691}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Wox1;
CC IsoId=Q91WL8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WL8-2; Sequence=VSP_016370, VSP_016371;
CC Name=3;
CC IsoId=Q91WL8-3; Sequence=VSP_016373, VSP_016374;
CC Name=4;
CC IsoId=Q91WL8-4; Sequence=VSP_016372, VSP_016375;
CC -!- TISSUE SPECIFICITY: Ubiquitous. In the brain, expressed in cortex,
CC striatum, hippocampus and cerebellum (at protein level). Detected in
CC embryonic skeleton, in cranofacial bones, vertebrae and limb bones.
CC Detected in chondrocytes and osteoblasts. {ECO:0000269|PubMed:15026124,
CC ECO:0000269|PubMed:17360458, ECO:0000269|PubMed:18487609}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at 8 dpc in the developing
CC heart. Higher expression in the brain is detected between 12 dpc and 16
CC dpc. High levels of expression in dorsal root ganglia and spinal nerves
CC were observed throughout all developmental stages. In later
CC developmental stages expression is more prominent in skeletal systems
CC (at protein level). {ECO:0000269|PubMed:15026124}.
CC -!- INDUCTION: By hyaluronidase. Up-regulated in outer and inner nuclear
CC layers during retinal degeneration. {ECO:0000269|PubMed:11058590,
CC ECO:0000269|PubMed:15664696}.
CC -!- DOMAIN: The WW 1 domain mediates interaction with TP73, TFAP2C, LITAF,
CC WBP1 and probably TP53. {ECO:0000269|PubMed:11058590,
CC ECO:0000269|PubMed:16219768}.
CC -!- PTM: Phosphorylated upon genotoxic stress. Phosphorylation of Tyr-33
CC regulates interaction with TP53, TP73 and MAPK8. May also regulate
CC proapoptotic activity. Phosphorylation by TNK2 is associated with
CC polyubiquitination and degradation (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated when phosphorylated by TNK2, leading to its
CC degradation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Indistinguishable from wild-type at birth, but
CC die after three weeks due to metabolic syndrome characterized by serum
CC hypoproteinemia, hypoalbuminemia, hypoglycemia, hypocalcemia,
CC hypotriglyceridemia and hypocholesterolemia, growth retardation,
CC decreased bone formation and increased bone resorption. In addition,
CC spontaneous tumor development was observed.
CC {ECO:0000269|PubMed:17360458, ECO:0000269|PubMed:18487609}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF187014; AAF31693.1; -; mRNA.
DR EMBL; AK018507; BAB31244.1; -; mRNA.
DR EMBL; AK019911; BAB31911.1; -; mRNA.
DR EMBL; AK046903; BAC32916.1; -; mRNA.
DR EMBL; AK078528; BAC37325.1; -; mRNA.
DR EMBL; BC014716; AAH14716.1; -; mRNA.
DR EMBL; AH011063; AAL03972.1; -; Genomic_DNA.
DR CCDS; CCDS22691.1; -. [Q91WL8-1]
DR RefSeq; NP_062519.2; NM_019573.3. [Q91WL8-1]
DR RefSeq; XP_006531577.1; XM_006531514.3. [Q91WL8-3]
DR RefSeq; XP_011246860.1; XM_011248558.2. [Q91WL8-4]
DR AlphaFoldDB; Q91WL8; -.
DR SMR; Q91WL8; -.
DR BioGRID; 219796; 4.
DR STRING; 10090.ENSMUSP00000004756; -.
DR iPTMnet; Q91WL8; -.
DR PhosphoSitePlus; Q91WL8; -.
DR SwissPalm; Q91WL8; -.
DR EPD; Q91WL8; -.
DR MaxQB; Q91WL8; -.
DR PaxDb; Q91WL8; -.
DR PeptideAtlas; Q91WL8; -.
DR PRIDE; Q91WL8; -.
DR ProteomicsDB; 299997; -. [Q91WL8-1]
DR ProteomicsDB; 299998; -. [Q91WL8-2]
DR ProteomicsDB; 299999; -. [Q91WL8-3]
DR ProteomicsDB; 300000; -. [Q91WL8-4]
DR Antibodypedia; 8291; 384 antibodies from 41 providers.
DR DNASU; 80707; -.
DR Ensembl; ENSMUST00000004756; ENSMUSP00000004756; ENSMUSG00000004637. [Q91WL8-1]
DR Ensembl; ENSMUST00000109107; ENSMUSP00000104735; ENSMUSG00000004637. [Q91WL8-2]
DR Ensembl; ENSMUST00000109108; ENSMUSP00000104736; ENSMUSG00000004637. [Q91WL8-4]
DR Ensembl; ENSMUST00000160862; ENSMUSP00000125626; ENSMUSG00000004637. [Q91WL8-3]
DR GeneID; 80707; -.
DR KEGG; mmu:80707; -.
DR UCSC; uc009noc.2; mouse. [Q91WL8-2]
DR UCSC; uc009nod.2; mouse. [Q91WL8-1]
DR CTD; 51741; -.
DR MGI; MGI:1931237; Wwox.
DR VEuPathDB; HostDB:ENSMUSG00000004637; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000157389; -.
DR HOGENOM; CLU_010194_44_0_1; -.
DR InParanoid; Q91WL8; -.
DR OMA; VHPGNMV; -.
DR OrthoDB; 1413827at2759; -.
DR PhylomeDB; Q91WL8; -.
DR TreeFam; TF105428; -.
DR Reactome; R-MMU-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-MMU-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR BioGRID-ORCS; 80707; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Wwox; mouse.
DR PRO; PR:Q91WL8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91WL8; protein.
DR Bgee; ENSMUSG00000004637; Expressed in humerus cartilage element and 200 other tissues.
DR Genevisible; Q91WL8; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IGI:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd09809; human_WWOX_like_SDR_c-like; 1.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR042732; WWOX_SDR_c-like.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF00397; WW; 2.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Mitochondrion; NADP; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW Tumor suppressor; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..414
FT /note="WW domain-containing oxidoreductase"
FT /id="PRO_0000054816"
FT DOMAIN 16..49
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 57..90
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..414
FT /note="Interaction with MAPT"
FT /evidence="ECO:0000269|PubMed:15126504"
FT REGION 209..273
FT /note="Mediates targeting to the mitochondria"
FT MOTIF 50..55
FT /note="Nuclear localization signal"
FT ACT_SITE 293
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 131..137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19366691"
FT MOD_RES 287
FT /note="Phosphotyrosine; by TNK2"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC7"
FT VAR_SEQ 137..158
FT /note="GFETAKSFALHGAHVILACRNL -> ALSPLLGERCIRRRQVLCSVFG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016370"
FT VAR_SEQ 159..414
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016371"
FT VAR_SEQ 353..367
FT /note="QQGAATTVYCAVAPE -> KPCMIGHTCDPNPRN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016372"
FT VAR_SEQ 353..354
FT /note="QQ -> IL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016373"
FT VAR_SEQ 355..414
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016374"
FT VAR_SEQ 368..414
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016375"
FT MUTAGEN 51..54
FT /note="KRKR->QGTG: Abolishes the TNF-induced nuclear
FT translocation."
FT /evidence="ECO:0000269|PubMed:11058590"
FT CONFLICT 135
FT /note="G -> V (in Ref. 2; BAB31244)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="V -> A (in Ref. 1; AAF31693 and 4; AAL03972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 46512 MW; 3C83AE3085B6A931 CRC64;
MAALRYAGLD DTDSEDELPP GWEERTTKDG WVYYANHTEE KTQWEHPKTG KRKRVAGDLP
YGWEQETDEN GQVFFVDHIN KRTTYLDPRL AFTVDDNPTK PTTRQRYDGS TTAMEILQGR
DFTGKVVLVT GANSGIGFET AKSFALHGAH VILACRNLSR ASEAVSRILE EWHKAKVEAM
TLDLAVLRSV QHFAEAFKAK NVSLHVLVCN AGTFALPWGL TKDGLETTFQ VNHLGHFYLV
QLLQDVLCRS SPARVIVVSS ESHRFTDIND SSGKLDLSRL SPPRSDYWAM LAYNRSKLCN
ILFSNELHRR LSPRGVTSNA VHPGNMMYSA IHRNSWVYKL LFTLARPFTK SMQQGAATTV
YCAVAPELEG LGGMYFNNCC RCLPSEEAQS EETARALWEL SERLIQDRLG SPSS
