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 27-MAR-2024, entry version 176. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 53. 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; 24. 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; 9606-ENSP00000481850; -. DR PeptideAtlas; Q92613; -. DR ProteomicsDB; 75357; -. DR Pumba; Q92613; -. DR Antibodypedia; 416; 117 antibodies from 21 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 AGR; HGNC:22982; -. 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; MFCDQES; -. DR OrthoDB; 163389at2759; -. DR PhylomeDB; Q92613; -. DR TreeFam; TF316118; -. DR PathwayCommons; Q92613; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR SignaLink; Q92613; -. DR BioGRID-ORCS; 9767; 24 hits in 795 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 156 other cell types or tissues. DR ExpressionAtlas; Q92613; baseline and differential. 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:0051726; P:regulation of cell cycle; IDA:ComplexPortal. DR GO; GO:0001558; P:regulation of cell growth; ISS: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:0006355; P:regulation of DNA-templated transcription; ISS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd15706; ePHD_JADE3; 1. DR CDD; cd15681; PHD_JADE3; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR13793; PHD FINGER PROTEINS; 1. DR PANTHER; PTHR13793:SF27; PROTEIN JADE-3; 1. DR Pfam; PF10513; EPL1; 1. DR Pfam; PF13831; PHD_2; 1. DR Pfam; PF13832; zf-HC5HC2H_2; 1. DR SMART; SM00249; PHD; 2. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR PROSITE; PS51805; EPHD; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q92613; HS. 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 //