JADE3_HUMAN
ID JADE3_HUMAN Reviewed; 823 AA.
AC Q92613; Q6IE79;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein Jade-3;
DE AltName: Full=Jade family PHD finger protein 3;
DE AltName: Full=PHD finger protein 16;
GN Name=JADE3; Synonyms=KIAA0215, PHF16;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY ESTRADIOL.
RX PubMed=10775800; DOI=10.1016/s0960-0760(00)00025-x;
RA Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N.V., Weill B.C.,
RA Sonnenschein C.;
RT "Identification of human estrogen-inducible transcripts that potentially
RT mediate the apoptotic response in breast cancer.";
RL J. Steroid Biochem. Mol. Biol. 72:89-102(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP IDENTIFICATION.
RX PubMed=14612400; DOI=10.1128/mcb.23.23.8553-8562.2003;
RA Tzouanacou E., Tweedie S., Wilson V.;
RT "Identification of Jade1, a gene encoding a PHD zinc finger protein, in a
RT gene trap mutagenesis screen for genes involved in anteroposterior axis
RT development.";
RL Mol. Cell. Biol. 23:8553-8562(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND IDENTIFICATION IN THE HBO1 COMPLEX.
RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
RA Lane W.S., Tan S., Yang X.-J., Cote J.;
RT "ING tumor suppressor proteins are critical regulators of chromatin
RT acetylation required for genome expression and perpetuation.";
RL Mol. Cell 21:51-64(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-566, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-776 AND SER-780, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-32 AND LYS-638, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-566 AND SER-608, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Scaffold subunit of some HBO1 complexes, which have a histone
CC H4 acetyltransferase activity. {ECO:0000269|PubMed:16387653}.
CC -!- SUBUNIT: Component of the HBO1 complex composed at least of ING4 or
CC ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3.
CC {ECO:0000269|PubMed:16387653}.
CC -!- INTERACTION:
CC Q92613; P55212: CASP6; NbExp=3; IntAct=EBI-10278909, EBI-718729;
CC Q92613; Q01658: DR1; NbExp=3; IntAct=EBI-10278909, EBI-750300;
CC Q92613; P14136: GFAP; NbExp=3; IntAct=EBI-10278909, EBI-744302;
CC Q92613; Q00403: GTF2B; NbExp=3; IntAct=EBI-10278909, EBI-389564;
CC Q92613; P13473-2: LAMP2; NbExp=3; IntAct=EBI-10278909, EBI-21591415;
CC Q92613; P43364: MAGEA11; NbExp=4; IntAct=EBI-10278909, EBI-739552;
CC Q92613; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-10278909, EBI-10178634;
CC Q92613; P19404: NDUFV2; NbExp=3; IntAct=EBI-10278909, EBI-713665;
CC Q92613; Q13148: TARDBP; NbExp=6; IntAct=EBI-10278909, EBI-372899;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC placenta and uterus. {ECO:0000269|PubMed:10775800}.
CC -!- INDUCTION: By estradiol in estrogen-responsive breast cancer cells.
CC {ECO:0000269|PubMed:10775800}.
CC -!- SIMILARITY: Belongs to the JADE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13205.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF127774; AAD51905.1; -; mRNA.
DR EMBL; D86969; BAA13205.2; ALT_INIT; mRNA.
DR EMBL; Z83822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC114487; AAI14488.1; -; mRNA.
DR EMBL; BC113880; AAI13881.1; -; mRNA.
DR EMBL; BN000289; CAE30502.1; -; mRNA.
DR CCDS; CCDS14271.1; -.
DR RefSeq; NP_001070913.1; NM_001077445.2.
DR RefSeq; NP_055550.1; NM_014735.4.
DR AlphaFoldDB; Q92613; -.
DR SMR; Q92613; -.
DR BioGRID; 115113; 43.
DR ComplexPortal; CPX-720; HBO1-4.3 histone acetyltransferase complex.
DR ComplexPortal; CPX-723; HBO1-5.3 histone acetyltransferase complex.
DR CORUM; Q92613; -.
DR IntAct; Q92613; 23.
DR MINT; Q92613; -.
DR STRING; 9606.ENSP00000481850; -.
DR iPTMnet; Q92613; -.
DR PhosphoSitePlus; Q92613; -.
DR BioMuta; JADE3; -.
DR DMDM; 34098663; -.
DR EPD; Q92613; -.
DR jPOST; Q92613; -.
DR MassIVE; Q92613; -.
DR MaxQB; Q92613; -.
DR PaxDb; Q92613; -.
DR PeptideAtlas; Q92613; -.
DR PRIDE; Q92613; -.
DR ProteomicsDB; 75357; -.
DR Antibodypedia; 416; 108 antibodies from 20 providers.
DR DNASU; 9767; -.
DR Ensembl; ENST00000611250.4; ENSP00000479377.1; ENSG00000102221.14.
DR Ensembl; ENST00000614628.5; ENSP00000481850.1; ENSG00000102221.14.
DR GeneID; 9767; -.
DR KEGG; hsa:9767; -.
DR MANE-Select; ENST00000614628.5; ENSP00000481850.1; NM_014735.5; NP_055550.1.
DR UCSC; uc033ebv.1; human.
DR CTD; 9767; -.
DR DisGeNET; 9767; -.
DR GeneCards; JADE3; -.
DR HGNC; HGNC:22982; JADE3.
DR HPA; ENSG00000102221; Low tissue specificity.
DR MIM; 300618; gene.
DR neXtProt; NX_Q92613; -.
DR OpenTargets; ENSG00000102221; -.
DR PharmGKB; PA134993233; -.
DR VEuPathDB; HostDB:ENSG00000102221; -.
DR eggNOG; KOG0954; Eukaryota.
DR GeneTree; ENSGT00940000158722; -.
DR HOGENOM; CLU_016215_1_0_1; -.
DR InParanoid; Q92613; -.
DR OMA; EFHRGQP; -.
DR OrthoDB; 1235709at2759; -.
DR PhylomeDB; Q92613; -.
DR TreeFam; TF316118; -.
DR PathwayCommons; Q92613; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q92613; -.
DR BioGRID-ORCS; 9767; 16 hits in 710 CRISPR screens.
DR ChiTaRS; JADE3; human.
DR GeneWiki; PHF16; -.
DR GenomeRNAi; 9767; -.
DR Pharos; Q92613; Tbio.
DR PRO; PR:Q92613; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q92613; protein.
DR Bgee; ENSG00000102221; Expressed in corpus epididymis and 154 other tissues.
DR ExpressionAtlas; Q92613; baseline and differential.
DR Genevisible; Q92613; HS.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0016570; P:histone modification; IDA:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:ComplexPortal.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15681; PHD_JADE3; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR039550; JADE3_PHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF10513; EPL1; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..823
FT /note="Protein Jade-3"
FT /id="PRO_0000059309"
FT ZN_FING 200..250
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 252..286
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 310..366
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 601
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE82"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 638
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 735
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE82"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 823 AA; 93808 MW; 4E47E2A124D0CE38 CRC64;
MKRHRPVSSS DSSDESPSTS FTSGSMYRIK SKIPNEHKKP AEVFRKDLIS AMKLPDSHHI
NPDSYYLFAD TWKEEWEKGV QVPASPDTVP QPSLRIIAEK VKDVLFIRPR KYIHCSSPDT
TEPGYINIME LAASVCRYDL DDMDIFWLQE LNEDLAEMGC GPVDENLMEK TVEVLERHCH
ENMNHAIETE EGLGIEYDED VICDVCRSPD SEEGNDMVFC DKCNVCVHQA CYGILKVPEG
SWLCRSCVLG IYPQCVLCPK KGGALKTTKT GTKWAHVSCA LWIPEVSIAC PERMEPITKI
SHIPPSRWAL VCNLCKLKTG ACIQCSIKSC ITAFHVTCAF EHGLEMKTIL DEGDEVKFKS
YCLKHSQNRQ KLGEAEYPHH RAKEQSQAKS EKTSLRAQKL RELEEEFYSL VRVEDVAAEL
GMPTLAVDFI YNYWKLKRKS NFNKPLFPPK EDEENGLVQP KEESIHTRMR MFMHLRQDLE
RVRNLCYMIS RREKLKLSHN KIQEQIFGLQ VQLLNQEIDA GLPLTNALEN SLFYPPPRIT
LKLKMPKSTP EDHRNSSTET DQQPHSPDSS SSVHSIRNMQ VPQESLEMRT KSYPRYPLES
KNNRLLASLS HSRSEAKESS PAWRTPSSEC YHGQSLGKPL VLQAALHGQS SIGNGKSQPN
SKFAKSNGLE GSWSGNVTQK DSSSEMFCDQ EPVFSPHLVS QGSFRKSTVE HFSRSFKETT
NRWVKNTEDL QCYVKPTKNM SPKEQFWGRQ VLRRSAGRAP YQENDGYCPD LELSDSEAES
DGNKEKVRVR KDSSDRENPP HDSRRDCHGK SKTHPLSHSS MQR
