YAP1_DROME
ID YAP1_DROME Reviewed; 395 AA.
AC Q45VV3; A2RVH0; A2RVH4; Q0E8X1; Q7KVG6; Q95TU5; Q9W1B6;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transcriptional coactivator yorkie {ECO:0000305};
DE AltName: Full=Protein yorkie {ECO:0000303|PubMed:16096061};
DE AltName: Full=Transcriptional coactivator YAP1 homolog {ECO:0000305};
GN Name=yki; ORFNames=CG4005;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), FUNCTION, INTERACTION WITH WTS, AND
RP PHOSPHORYLATION.
RX PubMed=16096061; DOI=10.1016/j.cell.2005.06.007;
RA Huang J., Wu S., Barrera J., Matthews K., Pan D.;
RT "The Hippo signaling pathway coordinately regulates cell proliferation and
RT apoptosis by inactivating Yorkie, the Drosophila Homolog of YAP.";
RL Cell 122:421-434(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND F).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SD.
RX PubMed=18313299; DOI=10.1016/j.cub.2008.02.034;
RA Goulev Y., Fauny J.D., Gonzalez-Marti B., Flagiello D., Silber J.,
RA Zider A.;
RT "SCALLOPED interacts with YORKIE, the nuclear effector of the hippo tumor-
RT suppressor pathway in Drosophila.";
RL Curr. Biol. 18:435-441(2008).
RN [7]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-145, INTERACTION WITH 14-3-3
RP EPSILON AND 14-3-3 ZETA, AND MUTAGENESIS OF SER-145.
RX PubMed=18256197; DOI=10.1242/dev.015255;
RA Oh H., Irvine K.D.;
RT "In vivo regulation of Yorkie phosphorylation and localization.";
RL Development 135:1081-1088(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-88; SER-100; SER-145;
RP SER-149; SER-227; TYR-228 AND SER-232, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-88;
RP SER-145 AND SER-227.
RX PubMed=19900439; DOI=10.1016/j.ydbio.2009.10.046;
RA Ren F., Zhang L., Jiang J.;
RT "Hippo signaling regulates Yorkie nuclear localization and activity through
RT 14-3-3 dependent and independent mechanisms.";
RL Dev. Biol. 337:303-312(2010).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22615583; DOI=10.1371/journal.pgen.1002725;
RA Schoenherr J.A., Drennan J.M., Martinez J.S., Chikka M.R., Hall M.C.,
RA Chang H.C., Clemens J.C.;
RT "Drosophila activated Cdc42 kinase has an anti-apoptotic function.";
RL PLoS Genet. 8:E1002725-E1002725(2012).
RN [11]
RP FUNCTION, AND INTERACTION WITH ACK AND EX.
RX PubMed=27462444; DOI=10.1038/celldisc.2015.47;
RA Hu L., Xu J., Yin M.X., Zhang L., Lu Y., Wu W., Xue Z., Ho M.S., Gao G.,
RA Zhao Y., Zhang L.;
RT "Ack promotes tissue growth via phosphorylation and suppression of the
RT Hippo pathway component Expanded.";
RL Cell Discov. 2:15047-15047(2016).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=26954546; DOI=10.1016/j.devcel.2016.02.004;
RA Chung H.L., Augustine G.J., Choi K.W.;
RT "Drosophila Schip1 links Expanded and Tao-1 to regulate hippo signaling.";
RL Dev. Cell 36:511-524(2016).
RN [13]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-146, UBIQUITINATION, AND
RP MUTAGENESIS OF SER-146.
RX PubMed=31857346; DOI=10.1101/gad.333146.119;
RA Cho Y.S., Li S., Wang X., Zhu J., Zhuo S., Han Y., Yue T., Yang Y.,
RA Jiang J.;
RT "CDK7 regulates organ size and tumor growth by safeguarding the Hippo
RT pathway effector Yki/Yap/Taz in the nucleus.";
RL Genes Dev. 34:53-71(2020).
CC -!- FUNCTION: Transcriptional coactivator which is the critical downstream
CC regulatory target in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway that
CC plays a pivotal role in organ size control and tumor suppression by
CC restricting proliferation and promoting apoptosis (PubMed:16096061,
CC PubMed:18313299, PubMed:22615583, PubMed:27462444). The core of this
CC pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex
CC with its regulatory protein Salvador (Sav), phosphorylates and
CC activates Warts (Wts) in complex with its regulatory protein Mats,
CC which in turn phosphorylates and inactivates the Yorkie (Yki)
CC oncoprotein (PubMed:16096061, PubMed:19900439). The Hippo/SWH signaling
CC pathway inhibits the activity of the transcriptional complex formed by
CC Scalloped (sd) and Yki and the target genes of this pathway include
CC cyclin-E (cycE), diap1 and bantam (PubMed:16096061, PubMed:18313299).
CC Regulates the expression of G1/S-specific CycE and diap1, thereby
CC promoting cell proliferation and inhibiting apoptosis
CC (PubMed:18313299). Required for transcriptional activity of sd in wing
CC imaginal disks (PubMed:18313299). Induces expression of expression of
CC vestigial (vg) in wing and haltere disks and the expression of
CC transcription factor E2f (E2f) (PubMed:18313299).
CC {ECO:0000269|PubMed:16096061, ECO:0000269|PubMed:18313299,
CC ECO:0000269|PubMed:19900439, ECO:0000269|PubMed:22615583,
CC ECO:0000269|PubMed:27462444}.
CC -!- SUBUNIT: Interacts (via WW domains) with wts (PubMed:16096061).
CC Interacts (via N-terminus) with sd (via C-terminus) and this
CC interaction enhances the transcriptional activity of sd
CC (PubMed:18313299). The phosphorylated form interacts with 14-3-3epsilon
CC and 14-3-3zeta (PubMed:18256197). Interacts with Ack and ex
CC (PubMed:27462444). {ECO:0000269|PubMed:16096061,
CC ECO:0000269|PubMed:18256197, ECO:0000269|PubMed:18313299,
CC ECO:0000269|PubMed:27462444}.
CC -!- INTERACTION:
CC Q45VV3; P42003: Mad; NbExp=2; IntAct=EBI-141254, EBI-162238;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18256197,
CC ECO:0000269|PubMed:18313299, ECO:0000269|PubMed:19900439,
CC ECO:0000269|PubMed:22615583, ECO:0000269|PubMed:26954546}. Nucleus
CC {ECO:0000269|PubMed:18256197, ECO:0000269|PubMed:18313299,
CC ECO:0000269|PubMed:19900439, ECO:0000269|PubMed:31857346}.
CC Note=Predominantly cytoplasmic (PubMed:18313299, PubMed:18256197,
CC PubMed:19900439). sd promotes its nuclear localization
CC (PubMed:18313299). 14-3-3epsilon, 14-3-3zeta and wts inhibit its
CC nuclear localization (PubMed:18256197, PubMed:19900439).
CC {ECO:0000269|PubMed:18256197, ECO:0000269|PubMed:18313299,
CC ECO:0000269|PubMed:19900439}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=F;
CC IsoId=Q45VV3-1; Sequence=Displayed;
CC Name=D;
CC IsoId=Q45VV3-2; Sequence=VSP_038903;
CC -!- PTM: Its activity is regulated by multiple phosphorylation events
CC (PubMed:16096061, PubMed:18256197, PubMed:19900439, PubMed:31857346).
CC Phosphorylation at Ser-88, Ser-145 and Ser-227 negatively regulate its
CC activity and restrict its nuclear localization (PubMed:19900439). Wts-
CC mediated phosphorylation at Ser-145 promotes interaction with 14-3-
CC 3epsilon and 14-3-3zeta (PubMed:18256197). Phosphorylation at Ser-88
CC and Ser-227 regulate nuclear localization and activity independent of
CC 14-3-3 association (PubMed:19900439). Phosphorylation at Ser-146 by
CC Cdk7 promotes its stability by preventing ubiquitination by the
CC DCX(DCAF12) complex (PubMed:31857346). {ECO:0000269|PubMed:16096061,
CC ECO:0000269|PubMed:18256197, ECO:0000269|PubMed:19900439,
CC ECO:0000269|PubMed:31857346}.
CC -!- PTM: Ubiquitinated by the DCX(DCAF12) complex, leading to its
CC degradation (PubMed:31857346). Phosphorylation at Ser-146 by Cdk7
CC prevents ubiquitination by the DCX(DCAF12) complex (PubMed:31857346).
CC {ECO:0000269|PubMed:31857346}.
CC -!- MISCELLANEOUS: Named for its loss-of-function phenotype after a very
CC small breed of dog, the Yorkshire Terrier.
CC {ECO:0000305|PubMed:16096061}.
CC -!- SIMILARITY: Belongs to the YAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13735.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAZ42161.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABM92835.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABM92835.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ABM92839.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABM92839.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ099897; AAZ42161.1; ALT_INIT; mRNA.
DR EMBL; AE013599; ABI31113.2; -; Genomic_DNA.
DR EMBL; AE013599; AAF47156.4; -; Genomic_DNA.
DR EMBL; AY058506; AAL13735.1; ALT_INIT; mRNA.
DR EMBL; BT029961; ABM92835.1; ALT_SEQ; mRNA.
DR EMBL; BT029965; ABM92839.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001036568.2; NM_001043103.2. [Q45VV3-1]
DR RefSeq; NP_611879.4; NM_138035.3. [Q45VV3-2]
DR RefSeq; NP_726414.3; NM_166657.5. [Q45VV3-1]
DR AlphaFoldDB; Q45VV3; -.
DR SMR; Q45VV3; -.
DR BioGRID; 63430; 131.
DR IntAct; Q45VV3; 7.
DR STRING; 7227.FBpp0288697; -.
DR iPTMnet; Q45VV3; -.
DR PaxDb; Q45VV3; -.
DR DNASU; 37851; -.
DR EnsemblMetazoa; FBtr0290256; FBpp0288695; FBgn0034970. [Q45VV3-2]
DR EnsemblMetazoa; FBtr0290258; FBpp0288697; FBgn0034970. [Q45VV3-1]
DR EnsemblMetazoa; FBtr0309372; FBpp0301274; FBgn0034970. [Q45VV3-1]
DR GeneID; 37851; -.
DR KEGG; dme:Dmel_CG4005; -.
DR UCSC; CG4005-RD; d. melanogaster.
DR CTD; 37851; -.
DR FlyBase; FBgn0034970; yki.
DR VEuPathDB; VectorBase:FBgn0034970; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00510000046760; -.
DR HOGENOM; CLU_757093_0_0_1; -.
DR InParanoid; Q45VV3; -.
DR OMA; WNDPRMQ; -.
DR PhylomeDB; Q45VV3; -.
DR Reactome; R-DME-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-DME-2028269; Signaling by Hippo.
DR Reactome; R-DME-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-DME-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-DME-390098; Phosphorylation-dependent inhibition of YKI.
DR Reactome; R-DME-390193; Transcriptional activation by YKI.
DR Reactome; R-DME-451806; Phosphorylation-independent inhibition of YKI.
DR Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-DME-8951671; RUNX3 regulates YAP1-mediated transcription.
DR SignaLink; Q45VV3; -.
DR BioGRID-ORCS; 37851; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37851; -.
DR PRO; PR:Q45VV3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034970; Expressed in adult Malpighian tubule (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q45VV3; baseline and differential.
DR Genevisible; Q45VV3; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0097575; C:lateral cell cortex; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:FlyBase.
DR GO; GO:0071889; F:14-3-3 protein binding; IPI:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
DR GO; GO:0045176; P:apical protein localization; IGI:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
DR GO; GO:0001708; P:cell fate specification; IMP:FlyBase.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; IMP:FlyBase.
DR GO; GO:0035329; P:hippo signaling; IDA:FlyBase.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:FlyBase.
DR GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:FlyBase.
DR GO; GO:1905437; P:positive regulation of histone H3-K4 trimethylation; IMP:FlyBase.
DR GO; GO:0045572; P:positive regulation of imaginal disc growth; IDA:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045463; P:R8 cell development; IMP:FlyBase.
DR GO; GO:0090210; P:regulation of establishment of blood-brain barrier; IMP:FlyBase.
DR GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IMP:FlyBase.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IMP:FlyBase.
DR GO; GO:0072089; P:stem cell proliferation; IDA:FlyBase.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..395
FT /note="Transcriptional coactivator yorkie"
FT /id="PRO_0000393269"
FT DOMAIN 241..274
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 310..343
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 73..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18256197,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 146
FT /note="Phosphoserine; by CDK7"
FT /evidence="ECO:0000269|PubMed:31857346"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 292..344
FT /note="DVLQTTKQTTTSTIANNLGPLPDGWEQAVTESGDLYFINHIDRTTSWNDPRM
FT Q -> E (in isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_038903"
FT MUTAGEN 88
FT /note="S->A: Increased activity and nuclear localization
FT and decreased sensitivity to Hpo/Wts-mediated inhibition;
FT when associated with A-227."
FT /evidence="ECO:0000269|PubMed:19900439"
FT MUTAGEN 145
FT /note="S->A: Increased activity and nuclear localization,
FT decreased sensitivity to Hpo/Wts-mediated inhibition, loss
FT of interaction with 14-3-3epsilon and 14-3-3zeta."
FT /evidence="ECO:0000269|PubMed:18256197,
FT ECO:0000269|PubMed:19900439"
FT MUTAGEN 146
FT /note="S->A: Abolished phosphorylation by Cdk7, leading to
FT increased ubiquitination by the DCX(DCAF12) complex."
FT /evidence="ECO:0000269|PubMed:31857346"
FT MUTAGEN 146
FT /note="S->D: Phosphomimetic mutant; decreased
FT ubiquitination by the DCX(DCAF12) complex."
FT /evidence="ECO:0000269|PubMed:31857346"
FT MUTAGEN 227
FT /note="S->A: Increased activity and nuclear localization
FT and decreased sensitivity to Hpo/Wts-mediated inhibition;
FT when associated with A-88."
FT /evidence="ECO:0000269|PubMed:19900439"
SQ SEQUENCE 395 AA; 43594 MW; 0F04A0C73D52C507 CRC64;
MLTTMSASSN TNSLIEKEID DEDMLSPIKS NNLVVRVNQD TDDNLQALFD SVLNPGDAKR
PLQLPLRMRK LPNSFFTPPA PSHSRANSAD STYDAGSQSS INIGNKASIV QQPDGQSPIA
AIPQLQIQPS PQHSRLAIHH SRARSSPASL QQNYNVRARS DAAAANNPNA NPSSQQQPAG
PTFPENSAQE FPSGAPASSA IDLDAMNTCM SQDIPMSMQT VHKKQRSYDV ISPIQLNRQL
GALPPGWEQA KTNDGQIYYL NHTTKSTQWE DPRIQYRQQQ QILMAERIKQ NDVLQTTKQT
TTSTIANNLG PLPDGWEQAV TESGDLYFIN HIDRTTSWND PRMQSGLSVL DCPDNLVSSL
QIEDNLCSNL FNDAQAIVNP PSSHKPDDLE WYKIN
