UBN1_HUMAN
ID UBN1_HUMAN Reviewed; 1134 AA.
AC Q9NPG3; B7Z6D3; D3DUE8; Q13079; Q9P1P7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ubinuclein-1;
DE AltName: Full=HIRA-binding protein;
DE AltName: Full=Protein VT4;
DE AltName: Full=Ubiquitously expressed nuclear protein;
GN Name=UBN1;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), INTERACTION WITH
RP EPSTEIN-BARR VIRUS BZLF1 (MICROBIAL INFECTION) AND CEBPA, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=10725330; DOI=10.1083/jcb.148.6.1165;
RA Aho S., Buisson M., Pajunen T., Ryoo Y.W., Giot J.-F., Gruffat H.,
RA Sergeant A., Uitto J.;
RT "Ubinuclein, a novel nuclear protein interacting with cellular and viral
RT transcription factors.";
RL J. Cell Biol. 148:1165-1176(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 348-691 (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RA Tesmer V., Babin J., Rajadhyaksha A., Bina M.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A
RP COMPLEX WITH ASF1A; CABIN1; HIRA AND HISTONE H3.3.
RX PubMed=14718166; DOI=10.1016/s0092-8674(03)01064-x;
RA Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.;
RT "Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways
RT dependent or independent of DNA synthesis.";
RL Cell 116:51-61(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-175, AND
RP IDENTIFICATION BY 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 [8]
RP INTERACTION WITH TJP1; TJP2 AND TJP3, AND SUBCELLULAR LOCATION.
RX PubMed=18823282; DOI=10.1042/bc20080072;
RA Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P.,
RA Sergeant A., Manet E., Boyer V., Gruffat H.;
RT "Characterization of the ubinuclein protein as a new member of the nuclear
RT and adhesion complex components (NACos).";
RL Biol. Cell 101:319-334(2009).
RN [9]
RP FUNCTION, DNA-BINDING, INTERACTION WITH ASF1A AND HIRA, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF 138-PHE--ASP-140; PHE-160 AND ILE-162, AND TISSUE
RP SPECIFICITY.
RX PubMed=19029251; DOI=10.1128/mcb.01047-08;
RA Banumathy G., Somaiah N., Zhang R., Tang Y., Hoffmann J., Andrake M.,
RA Ceulemans H., Schultz D., Marmorstein R., Adams P.D.;
RT "Human UBN1 is an ortholog of yeast Hpc2p and has an essential role in the
RT HIRA/ASF1a chromatin-remodeling pathway in senescent cells.";
RL Mol. Cell. Biol. 29:758-770(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-660; SER-677 AND
RP SER-1025, AND 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-338 AND SER-660, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-493 AND SER-660, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Acts as a novel regulator of senescence. Involved in the
CC formation of senescence-associated heterochromatin foci (SAHF), which
CC represses expression of proliferation-promoting genes. Binds to
CC proliferation-promoting genes. May be required for replication-
CC independent chromatin assembly. {ECO:0000269|PubMed:14718166,
CC ECO:0000269|PubMed:19029251}.
CC -!- SUBUNIT: Component of a complex that includes at least ASF1A, CABIN1,
CC HIRA, histone H3.3 and UBN1. Interacts with HIRA (via WD repeat
CC domain); the interaction is direct. Interacts with ASF1A, CEBPA, TJP1,
CC TJP2 and TJP3. {ECO:0000269|PubMed:14718166,
CC ECO:0000269|PubMed:18823282, ECO:0000269|PubMed:19029251}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus BZLF1.
CC {ECO:0000269|PubMed:10725330}.
CC -!- INTERACTION:
CC Q9NPG3; P54198: HIRA; NbExp=10; IntAct=EBI-2880187, EBI-372342;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, PML body. Cell
CC junction, tight junction. Note=Localized as a nuclear speckled-like
CC pattern in proliferating primary fibroblasts. Colocalizes with HIRA,
CC PML and SP100 in PML bodies of senescent cells. Colocalizes with TJP1
CC and CLDN1. Detected along the upper granular cell layer of epidermis.
CC When overexpressed, accumulates in the nucleus in cells showing
CC defective cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NPG3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPG3-2; Sequence=VSP_036971;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Also expressed in numerous tumors and
CC cancer cell lines. {ECO:0000269|PubMed:10725330,
CC ECO:0000269|PubMed:19029251}.
CC -!- SIMILARITY: Belongs to the ubinuclein family. {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; AF108460; AAF31755.1; -; mRNA.
DR EMBL; AF108461; AAF31756.1; -; mRNA.
DR EMBL; AF108459; AAF34869.1; -; Genomic_DNA.
DR EMBL; AF108454; AAF34869.1; JOINED; Genomic_DNA.
DR EMBL; AF108455; AAF34869.1; JOINED; Genomic_DNA.
DR EMBL; AF108456; AAF34869.1; JOINED; Genomic_DNA.
DR EMBL; AF108457; AAF34869.1; JOINED; Genomic_DNA.
DR EMBL; AF108458; AAF34869.1; JOINED; Genomic_DNA.
DR EMBL; AK300131; BAH13219.1; -; mRNA.
DR EMBL; AC020663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85249.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85250.1; -; Genomic_DNA.
DR EMBL; U19346; AAA64188.1; -; mRNA.
DR CCDS; CCDS10525.1; -. [Q9NPG3-1]
DR CCDS; CCDS73822.1; -. [Q9NPG3-2]
DR PIR; G01628; G01628.
DR RefSeq; NP_001072982.1; NM_001079514.2. [Q9NPG3-1]
DR RefSeq; NP_001275585.1; NM_001288656.1. [Q9NPG3-2]
DR RefSeq; XP_016878678.1; XM_017023189.1. [Q9NPG3-2]
DR PDB; 4ZBJ; X-ray; 2.25 A; D=122-148.
DR PDBsum; 4ZBJ; -.
DR AlphaFoldDB; Q9NPG3; -.
DR SMR; Q9NPG3; -.
DR BioGRID; 118934; 67.
DR CORUM; Q9NPG3; -.
DR IntAct; Q9NPG3; 18.
DR MINT; Q9NPG3; -.
DR STRING; 9606.ENSP00000379894; -.
DR GlyGen; Q9NPG3; 16 sites, 2 O-linked glycans (16 sites).
DR iPTMnet; Q9NPG3; -.
DR PhosphoSitePlus; Q9NPG3; -.
DR BioMuta; UBN1; -.
DR DMDM; 116242836; -.
DR EPD; Q9NPG3; -.
DR jPOST; Q9NPG3; -.
DR MassIVE; Q9NPG3; -.
DR MaxQB; Q9NPG3; -.
DR PaxDb; Q9NPG3; -.
DR PeptideAtlas; Q9NPG3; -.
DR PRIDE; Q9NPG3; -.
DR ProteomicsDB; 81991; -. [Q9NPG3-1]
DR ProteomicsDB; 81992; -. [Q9NPG3-2]
DR Antibodypedia; 11234; 162 antibodies from 35 providers.
DR DNASU; 29855; -.
DR Ensembl; ENST00000262376.11; ENSP00000262376.5; ENSG00000118900.15. [Q9NPG3-1]
DR Ensembl; ENST00000396658.8; ENSP00000379894.3; ENSG00000118900.15. [Q9NPG3-1]
DR Ensembl; ENST00000590769.5; ENSP00000468740.1; ENSG00000118900.15. [Q9NPG3-2]
DR GeneID; 29855; -.
DR KEGG; hsa:29855; -.
DR MANE-Select; ENST00000262376.11; ENSP00000262376.5; NM_001079514.3; NP_001072982.1.
DR UCSC; uc002cyb.5; human. [Q9NPG3-1]
DR CTD; 29855; -.
DR DisGeNET; 29855; -.
DR GeneCards; UBN1; -.
DR HGNC; HGNC:12506; UBN1.
DR HPA; ENSG00000118900; Low tissue specificity.
DR MIM; 609771; gene.
DR neXtProt; NX_Q9NPG3; -.
DR OpenTargets; ENSG00000118900; -.
DR PharmGKB; PA37153; -.
DR VEuPathDB; HostDB:ENSG00000118900; -.
DR eggNOG; KOG4786; Eukaryota.
DR GeneTree; ENSGT00940000158857; -.
DR HOGENOM; CLU_007400_0_0_1; -.
DR InParanoid; Q9NPG3; -.
DR OMA; HQDPEPA; -.
DR OrthoDB; 469344at2759; -.
DR PhylomeDB; Q9NPG3; -.
DR TreeFam; TF326088; -.
DR PathwayCommons; Q9NPG3; -.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR SignaLink; Q9NPG3; -.
DR BioGRID-ORCS; 29855; 14 hits in 1087 CRISPR screens.
DR ChiTaRS; UBN1; human.
DR GenomeRNAi; 29855; -.
DR Pharos; Q9NPG3; Tbio.
DR PRO; PR:Q9NPG3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NPG3; protein.
DR Bgee; ENSG00000118900; Expressed in lower esophagus mucosa and 209 other tissues.
DR ExpressionAtlas; Q9NPG3; baseline and differential.
DR Genevisible; Q9NPG3; HS.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR InterPro; IPR014840; HRD.
DR InterPro; IPR026936; Ubinuclein-1.
DR InterPro; IPR026947; UBN_middle_dom.
DR PANTHER; PTHR21669:SF12; PTHR21669:SF12; 1.
DR Pfam; PF08729; HUN; 1.
DR Pfam; PF14075; UBN_AB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell junction;
KW Chromatin regulator; Coiled coil; DNA-binding; Host-virus interaction;
KW Nucleus; Phosphoprotein; Reference proteome; Tight junction.
FT CHAIN 1..1134
FT /note="Ubinuclein-1"
FT /id="PRO_0000065712"
FT REGION 1..166
FT /note="Sufficient for interaction with HIRA"
FT /evidence="ECO:0000269|PubMed:19029251"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 479..542
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1090..1119
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036971"
FT VARIANT 435
FT /note="Y -> C (in dbSNP:rs35103368)"
FT /id="VAR_051465"
FT MUTAGEN 138
FT /note="F->E: Strongly diminishes interaction with HIRA;
FT when associated with E-139 and L-140."
FT MUTAGEN 139
FT /note="I->E: Strongly diminishes interaction with HIRA;
FT when associated with E-138 and L-140."
FT MUTAGEN 140
FT /note="D->L: Strongly diminishes interaction with HIRA;
FT when associated with E-138 and L-139."
FT MUTAGEN 160
FT /note="F->E: Strongly diminishes interaction with HIRA."
FT /evidence="ECO:0000269|PubMed:19029251"
FT MUTAGEN 162
FT /note="I->E: Strongly diminishes interaction with HIRA."
FT /evidence="ECO:0000269|PubMed:19029251"
FT CONFLICT 119
FT /note="K -> N (in Ref. 2; BAH13219)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="A -> V (in Ref. 1; AAF31755/AAF31756)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="Q -> H (in Ref. 2; BAH13219)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="F -> L (in Ref. 1; AAF31755/AAF31756)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="A -> P (in Ref. 1; AAF31755/AAF31756)"
FT /evidence="ECO:0000305"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:4ZBJ"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:4ZBJ"
SQ SEQUENCE 1134 AA; 121520 MW; 8DE68C63D4E8E01B CRC64;
MSEPHRVQFT SLPGSLNPAF LKKSRKEEAG AGEQHQDCEP AAAAVRITLT LFEPDHKRCP
EFFYPELVKN IRGKVKGLQP GDKKKDLSDP FNDEEKERHK VEALARKFEE KYGGKKRRKD
RIQDLIDMGY GYDESDSFID NSEAYDELVP ASLTTKYGGF YINSGTLQFR QASESEDDFI
KEKKKKSPKK RKLKEGGEKI KKKKKDDTYD KEKKSKKSKF SKAGFTALNA SKEKKKKKYS
GALSVKEMLK KFQKEKEAQK KREEEHKPVA VPSAEAQGLR ELEGASDPLL SLFGSTSDND
LLQAATAMDS LTDLDLEHLL SESPEGSPFR DMDDGSDSLG VGLDQEFRQP SSLPEGLPAP
LEKRVKELAQ AARAAEGESR QKFFTQDING ILLDIEAQTR ELSSQVRSGV YAYLASFLPC
SKDALLKRAR KLHLYEQGGR LKEPLQKLKE AIGRAMPEQM AKYQDECQAH TQAKVAKMLE
EEKDKEQRDR ICSDEEEDEE KGGRRIMGPR KKFQWNDEIR ELLCQVVKIK LESQDLERNN
KAQAWEDCVK GFLDAEVKPL WPKGWMQART LFKESRRGHG HLTSILAKKK VMAPSKIKVK
ESSTKPDKKV SVPSGQIGGP IALPSDHQTG GLSIGASSRE LPSQASGGLA NPPPVNLEDS
LDEDLIRNPA SSVEAVSKEL AALNSRAAGN SEFTLPAPSK APAEKVGGVL CTEEKRNFAK
PSPSAPPPAS SLQSPLNFLA EQALALGQSS QEKKPESSGY KELSCQAPLN KGLPEVHQSK
AKHHSLPRTS HGPQVAVPVP GPQVKVFHAG TQQQKNFTPP SPFANKLQGP KASPTQCHRS
LLQLVKTAAK GQGFHPSAPA TSGGLSASSS SSHKTPASSS SALSHPAKPH SVSSAGSSYK
NNPFASSISK HGVSSGSSSS GGTPVQSSVS GSLVPGIQPP SVGQATSRPV PSSAGKKMPV
SQKLTLVAPP GGPNGDSSGG TQGVAKLLTS PSLKPSAVSS VTSSTSLSKG ASGTVLLAGS
SLMASPYKSS SPKLSGAMSS NSLGIITPVP IPVHVLSFSA DSSAKAGVSK DAIVTGPAPG
SFHHGLGHSL LAGLHSSPPH AAPLPHAAVP THIPQSLPGA SQLHGKGPAV PRKL
