BAHD1_HUMAN
ID BAHD1_HUMAN Reviewed; 780 AA.
AC Q8TBE0; Q8NDF7; Q9Y2F4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Bromo adjacent homology domain-containing 1 protein;
DE Short=BAH domain-containing protein 1;
GN Name=BAHD1; Synonyms=KIAA0945;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LYS-298.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-182
RP AND LYS-298.
RC TISSUE=Pancreas;
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 [LARGE SCALE MRNA] OF 260-780 (ISOFORM 3), AND VARIANT
RP LYS-298.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN BAH, AND INTERACTION WITH CBX5;
RP HDAC5; MBD1 AND SP1.
RX PubMed=19666599; DOI=10.1073/pnas.0901259106;
RA Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M.,
RA Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J.,
RA Cossart P.;
RT "Human BAHD1 promotes heterochromatic gene silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-121 AND SER-184, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-184, AND
RP IDENTIFICATION BY 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 [9]
RP FUNCTION IN LISTERIA INFECTION, INTERACTION WITH LNTA, AND IDENTIFICATION
RP IN A COMPLEX WITH CBX3; HDAC1; HDAC2 AND TRIM28.
RX PubMed=21252314; DOI=10.1126/science.1200120;
RA Lebreton A., Lakisic G., Job V., Fritsch L., Tham T.N., Camejo A.,
RA Mattei P.J., Regnault B., Nahori M.A., Cabanes D., Gautreau A.,
RA Ait-Si-Ali S., Dessen A., Cossart P., Bierne H.;
RT "A bacterial protein targets the BAHD1 chromatin complex to stimulate type
RT III interferon response.";
RL Science 331:1319-1321(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-121; SER-184; SER-206
RP AND THR-588, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Heterochromatin protein that acts as a transcription
CC repressor and has the ability to promote the formation of large
CC heterochromatic domains. May act by recruiting heterochromatin proteins
CC such as CBX5 (HP1 alpha), HDAC5 and MBD1. Represses IGF2 expression by
CC binding to its CpG-rich P3 promoter and recruiting heterochromatin
CC proteins. At specific stages of Listeria infection, in complex with
CC TRIM28, corepresses interferon-stimulated genes, including IFNL1, IFNL2
CC and IFNL3. {ECO:0000269|PubMed:19666599, ECO:0000269|PubMed:21252314}.
CC -!- SUBUNIT: Interacts with CBX5 (HP1 alpha), HDAC5, MBD1 and SP1. Forms a
CC transcription silencing complex with at least CBX3 (HP1 gamma), HDAC1,
CC HDAC2 and TRIM28. Interacts with L.monocytogenes LntA; this
CC interaction, occurring at a late Listeria infection stage, relieves
CC transcription repression, mostly that of interferon-stimulated genes.
CC {ECO:0000269|PubMed:19666599, ECO:0000269|PubMed:21252314}.
CC -!- INTERACTION:
CC Q8TBE0; Q03989: ARID5A; NbExp=3; IntAct=EBI-742750, EBI-948603;
CC Q8TBE0; Q86V38: ATN1; NbExp=3; IntAct=EBI-742750, EBI-11954292;
CC Q8TBE0; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-742750, EBI-1642333;
CC Q8TBE0; P46379-2: BAG6; NbExp=3; IntAct=EBI-742750, EBI-10988864;
CC Q8TBE0; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-742750, EBI-739580;
CC Q8TBE0; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-742750, EBI-3866279;
CC Q8TBE0; P83916: CBX1; NbExp=3; IntAct=EBI-742750, EBI-78129;
CC Q8TBE0; P45973: CBX5; NbExp=3; IntAct=EBI-742750, EBI-78219;
CC Q8TBE0; P28329-3: CHAT; NbExp=3; IntAct=EBI-742750, EBI-25837549;
CC Q8TBE0; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-742750, EBI-21553822;
CC Q8TBE0; P02489: CRYAA; NbExp=3; IntAct=EBI-742750, EBI-6875961;
CC Q8TBE0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-742750, EBI-3867333;
CC Q8TBE0; Q01658: DR1; NbExp=3; IntAct=EBI-742750, EBI-750300;
CC Q8TBE0; Q92997: DVL3; NbExp=4; IntAct=EBI-742750, EBI-739789;
CC Q8TBE0; P41091: EIF2S3; NbExp=3; IntAct=EBI-742750, EBI-1054228;
CC Q8TBE0; O75460-2: ERN1; NbExp=3; IntAct=EBI-742750, EBI-25852368;
CC Q8TBE0; P22607: FGFR3; NbExp=3; IntAct=EBI-742750, EBI-348399;
CC Q8TBE0; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-742750, EBI-10226858;
CC Q8TBE0; P14136: GFAP; NbExp=3; IntAct=EBI-742750, EBI-744302;
CC Q8TBE0; O14908-2: GIPC1; NbExp=3; IntAct=EBI-742750, EBI-25913156;
CC Q8TBE0; Q08379: GOLGA2; NbExp=3; IntAct=EBI-742750, EBI-618309;
CC Q8TBE0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-742750, EBI-5916454;
CC Q8TBE0; P06396: GSN; NbExp=3; IntAct=EBI-742750, EBI-351506;
CC Q8TBE0; Q00403: GTF2B; NbExp=3; IntAct=EBI-742750, EBI-389564;
CC Q8TBE0; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-742750, EBI-1054873;
CC Q8TBE0; P49639: HOXA1; NbExp=3; IntAct=EBI-742750, EBI-740785;
CC Q8TBE0; P54652: HSPA2; NbExp=3; IntAct=EBI-742750, EBI-356991;
CC Q8TBE0; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-742750, EBI-742808;
CC Q8TBE0; O75525: KHDRBS3; NbExp=4; IntAct=EBI-742750, EBI-722504;
CC Q8TBE0; O14901: KLF11; NbExp=3; IntAct=EBI-742750, EBI-948266;
CC Q8TBE0; Q92876: KLK6; NbExp=3; IntAct=EBI-742750, EBI-2432309;
CC Q8TBE0; O00505: KPNA3; NbExp=3; IntAct=EBI-742750, EBI-358297;
CC Q8TBE0; Q6A162: KRT40; NbExp=3; IntAct=EBI-742750, EBI-10171697;
CC Q8TBE0; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-742750, EBI-10172290;
CC Q8TBE0; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-742750, EBI-10171774;
CC Q8TBE0; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-742750, EBI-12811111;
CC Q8TBE0; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-742750, EBI-10241353;
CC Q8TBE0; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-742750, EBI-14065470;
CC Q8TBE0; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-742750, EBI-12111050;
CC Q8TBE0; Q14847-2: LASP1; NbExp=3; IntAct=EBI-742750, EBI-9088686;
CC Q8TBE0; P02545: LMNA; NbExp=3; IntAct=EBI-742750, EBI-351935;
CC Q8TBE0; Q9BRK4: LZTS2; NbExp=7; IntAct=EBI-742750, EBI-741037;
CC Q8TBE0; Q8TC57: M1AP; NbExp=3; IntAct=EBI-742750, EBI-748182;
CC Q8TBE0; Q99750: MDFI; NbExp=7; IntAct=EBI-742750, EBI-724076;
CC Q8TBE0; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-742750, EBI-10172526;
CC Q8TBE0; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-742750, EBI-2811583;
CC Q8TBE0; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-742750, EBI-79165;
CC Q8TBE0; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-742750, EBI-3957793;
CC Q8TBE0; P98175: RBM10; NbExp=3; IntAct=EBI-742750, EBI-721525;
CC Q8TBE0; P50454: SERPINH1; NbExp=3; IntAct=EBI-742750, EBI-350723;
CC Q8TBE0; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-742750, EBI-5235340;
CC Q8TBE0; Q13148: TARDBP; NbExp=6; IntAct=EBI-742750, EBI-372899;
CC Q8TBE0; P37173: TGFBR2; NbExp=3; IntAct=EBI-742750, EBI-296151;
CC Q8TBE0; Q08117: TLE5; NbExp=3; IntAct=EBI-742750, EBI-717810;
CC Q8TBE0; Q08117-2: TLE5; NbExp=3; IntAct=EBI-742750, EBI-11741437;
CC Q8TBE0; Q63HR2: TNS2; NbExp=3; IntAct=EBI-742750, EBI-949753;
CC Q8TBE0; Q12933: TRAF2; NbExp=4; IntAct=EBI-742750, EBI-355744;
CC Q8TBE0; Q9BUZ4: TRAF4; NbExp=6; IntAct=EBI-742750, EBI-3650647;
CC Q8TBE0; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-742750, EBI-741480;
CC Q8TBE0; Q9NSD4: ZNF275; NbExp=3; IntAct=EBI-742750, EBI-17263125;
CC Q8TBE0; Q96PQ6: ZNF317; NbExp=3; IntAct=EBI-742750, EBI-1210473;
CC Q8TBE0; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-742750, EBI-347633;
CC Q8TBE0; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-742750, EBI-11035148;
CC Q8TBE0; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-742750, EBI-11962574;
CC Q8TBE0; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-742750, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19666599}. Chromosome
CC {ECO:0000269|PubMed:19666599}. Note=Localizes to heterochromatin and
CC inactive X chromosome. Colocalizes with histone H3 trimethylated at
CC 'Lys-27' (H3K27me3).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TBE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TBE0-2; Sequence=VSP_025623;
CC Name=3;
CC IsoId=Q8TBE0-3; Sequence=VSP_025624;
CC -!- DOMAIN: The BAH domain is required for localization at H3K27me3.
CC {ECO:0000269|PubMed:19666599}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76789.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB023162; BAA76789.2; ALT_INIT; mRNA.
DR EMBL; BC022782; AAH22782.1; -; mRNA.
DR EMBL; AC013356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL833923; CAD38779.1; -; mRNA.
DR CCDS; CCDS10058.1; -. [Q8TBE0-1]
DR CCDS; CCDS73705.1; -. [Q8TBE0-2]
DR RefSeq; NP_001288061.1; NM_001301132.1. [Q8TBE0-2]
DR RefSeq; NP_055767.3; NM_014952.4. [Q8TBE0-1]
DR RefSeq; XP_011519671.1; XM_011521369.2. [Q8TBE0-1]
DR AlphaFoldDB; Q8TBE0; -.
DR BioGRID; 116558; 61.
DR IntAct; Q8TBE0; 74.
DR MINT; Q8TBE0; -.
DR STRING; 9606.ENSP00000396976; -.
DR iPTMnet; Q8TBE0; -.
DR PhosphoSitePlus; Q8TBE0; -.
DR BioMuta; BAHD1; -.
DR DMDM; 152040006; -.
DR EPD; Q8TBE0; -.
DR jPOST; Q8TBE0; -.
DR MassIVE; Q8TBE0; -.
DR MaxQB; Q8TBE0; -.
DR PaxDb; Q8TBE0; -.
DR PeptideAtlas; Q8TBE0; -.
DR PRIDE; Q8TBE0; -.
DR ProteomicsDB; 73996; -. [Q8TBE0-1]
DR ProteomicsDB; 73997; -. [Q8TBE0-2]
DR ProteomicsDB; 73998; -. [Q8TBE0-3]
DR TopDownProteomics; Q8TBE0-3; -. [Q8TBE0-3]
DR Antibodypedia; 23102; 73 antibodies from 18 providers.
DR DNASU; 22893; -.
DR Ensembl; ENST00000416165.6; ENSP00000396976.1; ENSG00000140320.12. [Q8TBE0-1]
DR Ensembl; ENST00000560846.1; ENSP00000454101.1; ENSG00000140320.12. [Q8TBE0-3]
DR Ensembl; ENST00000561234.5; ENSP00000454150.1; ENSG00000140320.12. [Q8TBE0-2]
DR GeneID; 22893; -.
DR KEGG; hsa:22893; -.
DR MANE-Select; ENST00000416165.6; ENSP00000396976.1; NM_014952.5; NP_055767.3.
DR UCSC; uc001zlt.3; human. [Q8TBE0-1]
DR CTD; 22893; -.
DR DisGeNET; 22893; -.
DR GeneCards; BAHD1; -.
DR HGNC; HGNC:29153; BAHD1.
DR HPA; ENSG00000140320; Low tissue specificity.
DR MIM; 613880; gene.
DR neXtProt; NX_Q8TBE0; -.
DR OpenTargets; ENSG00000140320; -.
DR PharmGKB; PA128394592; -.
DR VEuPathDB; HostDB:ENSG00000140320; -.
DR eggNOG; KOG1886; Eukaryota.
DR GeneTree; ENSGT00390000003967; -.
DR HOGENOM; CLU_019093_0_0_1; -.
DR InParanoid; Q8TBE0; -.
DR OMA; PRPKWAK; -.
DR OrthoDB; 11077at2759; -.
DR PhylomeDB; Q8TBE0; -.
DR TreeFam; TF350135; -.
DR PathwayCommons; Q8TBE0; -.
DR SignaLink; Q8TBE0; -.
DR BioGRID-ORCS; 22893; 18 hits in 1076 CRISPR screens.
DR ChiTaRS; BAHD1; human.
DR GenomeRNAi; 22893; -.
DR Pharos; Q8TBE0; Tbio.
DR PRO; PR:Q8TBE0; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8TBE0; protein.
DR Bgee; ENSG00000140320; Expressed in olfactory bulb and 192 other tissues.
DR ExpressionAtlas; Q8TBE0; baseline and differential.
DR Genevisible; Q8TBE0; HS.
DR GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR Gene3D; 2.30.30.490; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR Pfam; PF01426; BAH; 1.
DR SMART; SM00439; BAH; 1.
DR PROSITE; PS51038; BAH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Chromosome; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..780
FT /note="Bromo adjacent homology domain-containing 1 protein"
FT /id="PRO_0000287918"
FT DOMAIN 624..779
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..589
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 478
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_025623"
FT VAR_SEQ 685..687
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025624"
FT VARIANT 26
FT /note="E -> G (in dbSNP:rs3743143)"
FT /id="VAR_032359"
FT VARIANT 182
FT /note="D -> H (in dbSNP:rs17856679)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032360"
FT VARIANT 298
FT /note="Q -> K (in dbSNP:rs3803357)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_032361"
SQ SEQUENCE 780 AA; 84652 MW; DDCAA05DFAA6D982 CRC64;
MTHTRRKSLP MLSSGLTGRR EPLQMEDSNM EQGVEGVEPG MPESPGHLTG RRKNYPLRKR
PLVPEKPKAC KVLLTRLENV AGPRSADEAD ELPPDLPKPP SPAPSSEDPG LAQPRKRRLA
SLNAEALNNL LLEREDTSSL AGTRRSRAGD PHRSRDRDRA TGGWSSSKKR PRLGDLGGGS
RDLSPEPAPD EGPRRDGDPA PKRLASLNAA AFLKLSQERE LPLRLPRAHA EVDGRSTEPP
APKAPRPKWP KVNGKNYPKA WQGASSGEAA GPPGWQGCPD EPWPSATPCG PSVQPSHQPL
SKALESPLGL RPHLPLLMGG QAALKPEPGR PGEESPAPKQ ELHQPSFPTP QLSPLPMPGN
PADYNGLCVG PELTALGSFY LYCGQEGLQC GGYSPCPMLP EGKLSPVAAP HEEGLLLAPS
SVPSGTPFQH PPWGSSRYCS SEDTGVNGYS ICGVLPLSVT HAGTTCGGCP YKMPFAAEGC
RSLGQLEFPL PEAGHPASPA HPLLGCPVPS VPPAAEPVPH LQTPTSEPQT VARACPQSAK
PPSGSKSGLR TGSSCRHTAR SKAARRPSHP KQPRVQRPRP RRRRRRRTNG WVPVGAACEK
AVYVLDEPEP AIRKSYQAVE RHGETIRVRD TVLLKSGPRK TSTPYVAKIS ALWENPESGE
LMMSLLWYYR PEHLQGGRSP SMHEPLQNEV FASRHQDQNS VACIEEKCYV LTFAEYCRFC
AMAKRRGEGL PSRKTALVPP SADYSTPPHR TVPEDTDPEL VFLCRHVYDF RHGRILKNPQ
