HIRA_HUMAN
ID HIRA_HUMAN Reviewed; 1017 AA.
AC P54198; Q05BU9; Q8IXN2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Protein HIRA;
DE AltName: Full=TUP1-like enhancer of split protein 1;
GN Name=HIRA; Synonyms=DGCR1, HIR, TUPLE1;
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] (ISOFORM LONG).
RC TISSUE=Brain;
RX PubMed=7633437; DOI=10.1093/hmg/4.5.791;
RA Lamour V., Lecluse Y., Desmaze C., Spector M., Bodescot M., Aurias A.,
RA Osley M.A., Lipinski M.;
RT "A human homolog of the S. cerevisiae HIR1 and HIR2 transcriptional
RT repressors cloned from the DiGeorge syndrome critical region.";
RL Hum. Mol. Genet. 4:791-799(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG).
RX PubMed=8681138; DOI=10.1101/gr.6.1.43;
RA Lorain S., Demczuk S., Lamour V., Toth S., Aurias A., Roe B.A.,
RA Lipinski M.;
RT "Structural organization of the WD repeat protein-encoding gene HIRA in the
RT DiGeorge syndrome critical region of human chromosome 22.";
RL Genome Res. 6:43-50(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Eye, and Lymph;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 45-1017 (ISOFORM SHORT).
RC TISSUE=Fetal brain;
RX PubMed=8111380; DOI=10.1093/hmg/2.12.2099;
RA Halford S., Wadey R., Roberts C., Daw S.C.M., Whiting J.A., O'Donnell H.,
RA Dunham I., Bentley D., Lindsay E., Baldini A., Francis F., Lehrach H.,
RA Williamson R., Wilson D.I., Goodship J., Cross I., Burn J., Scambler P.J.;
RT "Isolation of a putative transcriptional regulator from the region of 22q11
RT deleted in DiGeorge syndrome, Shprintzen syndrome and familial congenital
RT heart disease.";
RL Hum. Mol. Genet. 2:2099-2107(1993).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=9063745; DOI=10.1093/hmg/6.2.247;
RA Wilming L.G., Snoeren C.A.S., van Rijswijk A., Grosveld F., Meijers C.;
RT "The murine homologue of HIRA, a DiGeorge syndrome candidate gene, is
RT expressed in embryonic structures affected in human CATCH22 patients.";
RL Hum. Mol. Genet. 6:247-258(1997).
RN [7]
RP INTERACTION WITH HIRIP3; HISTONE H2B; HISTONE H4 AND NFU1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9710638; DOI=10.1128/mcb.18.9.5546;
RA Lorain S., Quivy J.-P., Monier-Gavelle F., Scamps C., Lecluse Y.,
RA Almouzni G., Lipinski M.;
RT "Core histones and HIRIP3, a novel histone-binding protein, directly
RT interact with WD repeat protein HIRA.";
RL Mol. Cell. Biol. 18:5546-5556(1998).
RN [8]
RP INTERACTION WITH CCNA1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-555
RP AND SER-687, AND MUTAGENESIS OF THR-555 AND 628-LYS--LEU-631.
RX PubMed=11238922; DOI=10.1128/mcb.21.5.1854-1865.2001;
RA Hall C., Nelson D.M., Ye X., Baker K., DeCaprio J.A., Seeholzer S.,
RA Lipinski M., Adams P.D.;
RT "HIRA, the human homologue of yeast Hir1p and Hir2p, is a novel cyclin-cdk2
RT substrate whose expression blocks S-phase progression.";
RL Mol. Cell. Biol. 21:1854-1865(2001).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12370293; DOI=10.1128/mcb.22.21.7459-7472.2002;
RA Nelson D.M., Ye X., Hall C., Santos H., Ma T., Kao G.D., Yen T.J.,
RA Harper J.W., Adams P.D.;
RT "Coupling of DNA synthesis and histone synthesis in S phase independent of
RT cyclin/cdk2 activity.";
RL Mol. Cell. Biol. 22:7459-7472(2002).
RN [10]
RP INTERACTION WITH ASF1A.
RX PubMed=14680630; DOI=10.1016/j.cub.2003.11.027;
RA Daganzo S.M., Erzberger J.P., Lam W.M., Skordalakes E., Zhang R.,
RA Franco A.A., Brill S.J., Adams P.D., Berger J.M., Kaufman P.D.;
RT "Structure and function of the conserved core of histone deposition protein
RT Asf1.";
RL Curr. Biol. 13:2148-2158(2003).
RN [11]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A
RP COMPLEX WITH ASF1A; CABIN1; HISTONE H3.3 AND UBN1.
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 [12]
RP FUNCTION, INTERACTION WITH ASF1A, AND SUBCELLULAR LOCATION.
RX PubMed=15621527; DOI=10.1016/j.devcel.2004.10.019;
RA Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W., Daganzo S.M.,
RA Erzberger J.P., Serebriiskii I.G., Canutescu A.A., Dunbrack R.L.,
RA Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D.;
RT "Formation of MacroH2A-containing senescence-associated heterochromatin
RT foci and senescence driven by ASF1a and HIRA.";
RL Dev. Cell 8:19-30(2005).
RN [13]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584 AND THR-586, 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 [15]
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 [16]
RP INTERACTION WITH UBN1.
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549; SER-557; THR-576 AND
RP THR-586, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-586 AND SER-661, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610; SER-611; SER-612;
RP SER-614 AND SER-661, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-549; SER-584;
RP THR-586; SER-612; SER-661 AND SER-675, AND IDENTIFICATION BY MASS
RP 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).
RN [21]
RP INTERACTION WITH H3.Y.
RX PubMed=28334823; DOI=10.1093/nar/gkx131;
RA Zink L.M., Delbarre E., Eberl H.C., Keilhauer E.C., Boenisch C.,
RA Puenzeler S., Bartkuhn M., Collas P., Mann M., Hake S.B.;
RT "H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals
RT unexpected insights into human DAXX-H3.3-H4 binding and deposition
RT requirements.";
RL Nucleic Acids Res. 45:5691-5706(2017).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 425-472 IN COMPLEX WITH ASF1A, AND
RP MUTAGENESIS OF 449-GLN--ARG-458; 459-ARG--GLN-468; ARG-459; ARG-460;
RP ILE-461; LEU-464 AND ILE-466.
RX PubMed=16980972; DOI=10.1038/nsmb1147;
RA Tang Y., Poustovoitov M.V., Zhao K., Garfinkel M., Canutescu A.,
RA Dunbrack R., Adams P.D., Marmorstein R.;
RT "Structure of a human ASF1a-HIRA complex and insights into specificity of
RT histone chaperone complex assembly.";
RL Nat. Struct. Mol. Biol. 13:921-929(2006).
CC -!- FUNCTION: Cooperates with ASF1A to promote replication-independent
CC chromatin assembly. Required for the periodic repression of histone
CC gene transcription during the cell cycle. Required for the formation of
CC senescence-associated heterochromatin foci (SAHF) and efficient
CC senescence-associated cell cycle exit. {ECO:0000269|PubMed:12370293,
CC ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15621527}.
CC -!- SUBUNIT: Interacts with histone H3-3B, PAX3 and PAX7 (By similarity).
CC Interacts with histone H3.Y (PubMed:28334823). Interacts with CCNA1,
CC HIRIP3, NFU1/HIRIP5 and histone H2B. Part of a complex which includes
CC ASF1A, CABIN1, histone H3.3, histone H4 and UBN1 (PubMed:11238922,
CC PubMed:14680630, PubMed:14718166, PubMed:15621527, PubMed:16980972,
CC PubMed:19029251, PubMed:9710638). {ECO:0000250|UniProtKB:Q61666,
CC ECO:0000269|PubMed:11238922, ECO:0000269|PubMed:14680630,
CC ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15621527,
CC ECO:0000269|PubMed:16980972, ECO:0000269|PubMed:19029251,
CC ECO:0000269|PubMed:28334823, ECO:0000269|PubMed:9710638}.
CC -!- INTERACTION:
CC P54198; Q9Y294: ASF1A; NbExp=14; IntAct=EBI-372342, EBI-749553;
CC P54198; Q9NVP2: ASF1B; NbExp=4; IntAct=EBI-372342, EBI-1055650;
CC P54198; Q9NPG3: UBN1; NbExp=10; IntAct=EBI-372342, EBI-2880187;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Primarily,
CC though not exclusively, localized to the nucleus. Localizes to PML
CC bodies immediately prior to onset of senescence.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P54198-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P54198-2; Sequence=VSP_006772;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in kidney, pancreas and
CC skeletal muscle and at lower levels in brain, heart, liver, lung, and
CC placenta. {ECO:0000269|PubMed:9063745}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC -!- PTM: Phosphorylated by CDK2/CCNA1 and CDK2/CCNE1 on Thr-555 in vitro.
CC Also phosphorylated on Thr-555 and Ser-687 in vivo.
CC {ECO:0000269|PubMed:11238922}.
CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA54721.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA57436.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X81844; CAA57436.1; ALT_INIT; mRNA.
DR EMBL; X77633; CAA54721.1; ALT_INIT; mRNA.
DR EMBL; X89887; CAA61979.1; -; mRNA.
DR EMBL; X91501; CAA62800.1; -; Genomic_DNA.
DR EMBL; CR456503; CAG30389.1; -; mRNA.
DR EMBL; BC032721; AAH32721.1; -; mRNA.
DR EMBL; BC039835; AAH39835.1; -; mRNA.
DR EMBL; X75296; CAA53044.1; ALT_INIT; mRNA.
DR CCDS; CCDS13759.1; -. [P54198-1]
DR PIR; I37465; I37465.
DR PIR; S45344; S45344.
DR RefSeq; NP_003316.3; NM_003325.3. [P54198-1]
DR PDB; 2I32; X-ray; 2.70 A; E/F=425-472.
DR PDB; 5YJE; X-ray; 2.45 A; A/B/C=644-1017.
DR PDBsum; 2I32; -.
DR PDBsum; 5YJE; -.
DR AlphaFoldDB; P54198; -.
DR SMR; P54198; -.
DR BioGRID; 113141; 137.
DR CORUM; P54198; -.
DR DIP; DIP-29240N; -.
DR ELM; P54198; -.
DR IntAct; P54198; 40.
DR MINT; P54198; -.
DR STRING; 9606.ENSP00000263208; -.
DR GlyGen; P54198; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P54198; -.
DR PhosphoSitePlus; P54198; -.
DR BioMuta; HIRA; -.
DR DMDM; 88984228; -.
DR EPD; P54198; -.
DR jPOST; P54198; -.
DR MassIVE; P54198; -.
DR MaxQB; P54198; -.
DR PaxDb; P54198; -.
DR PeptideAtlas; P54198; -.
DR PRIDE; P54198; -.
DR ProteomicsDB; 56652; -. [P54198-1]
DR ProteomicsDB; 56653; -. [P54198-2]
DR Antibodypedia; 34961; 278 antibodies from 30 providers.
DR DNASU; 7290; -.
DR Ensembl; ENST00000263208.5; ENSP00000263208.5; ENSG00000100084.14. [P54198-1]
DR Ensembl; ENST00000340170.8; ENSP00000345350.4; ENSG00000100084.14. [P54198-2]
DR GeneID; 7290; -.
DR KEGG; hsa:7290; -.
DR MANE-Select; ENST00000263208.5; ENSP00000263208.5; NM_003325.4; NP_003316.3.
DR UCSC; uc002zpf.2; human. [P54198-1]
DR CTD; 7290; -.
DR DisGeNET; 7290; -.
DR GeneCards; HIRA; -.
DR HGNC; HGNC:4916; HIRA.
DR HPA; ENSG00000100084; Tissue enhanced (thyroid).
DR MalaCards; HIRA; -.
DR MIM; 600237; gene.
DR neXtProt; NX_P54198; -.
DR OpenTargets; ENSG00000100084; -.
DR Orphanet; 567; 22q11.2 deletion syndrome.
DR PharmGKB; PA29293; -.
DR VEuPathDB; HostDB:ENSG00000100084; -.
DR eggNOG; KOG0973; Eukaryota.
DR GeneTree; ENSGT00550000074919; -.
DR HOGENOM; CLU_004372_0_0_1; -.
DR InParanoid; P54198; -.
DR OMA; RGSWDGD; -.
DR OrthoDB; 685536at2759; -.
DR PhylomeDB; P54198; -.
DR TreeFam; TF323161; -.
DR PathwayCommons; P54198; -.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR SignaLink; P54198; -.
DR SIGNOR; P54198; -.
DR BioGRID-ORCS; 7290; 468 hits in 1092 CRISPR screens.
DR ChiTaRS; HIRA; human.
DR EvolutionaryTrace; P54198; -.
DR GeneWiki; HIRA; -.
DR GenomeRNAi; 7290; -.
DR Pharos; P54198; Tbio.
DR PRO; PR:P54198; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P54198; protein.
DR Bgee; ENSG00000100084; Expressed in left lobe of thyroid gland and 166 other tissues.
DR ExpressionAtlas; P54198; baseline and differential.
DR Genevisible; P54198; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000417; C:HIR complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:ARUK-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IEA:Ensembl.
DR GO; GO:0042692; P:muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 2.
DR IDEAL; IID00154; -.
DR InterPro; IPR031120; HIR1.
DR InterPro; IPR011494; Hira.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13831; PTHR13831; 1.
DR Pfam; PF07569; Hira; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT CHAIN 1..1017
FT /note="Protein HIRA"
FT /id="PRO_0000051019"
FT REPEAT 11..53
FT /note="WD 1"
FT REPEAT 68..107
FT /note="WD 2"
FT REPEAT 129..168
FT /note="WD 3"
FT REPEAT 172..211
FT /note="WD 4"
FT REPEAT 220..263
FT /note="WD 5"
FT REPEAT 266..322
FT /note="WD 6"
FT REPEAT 326..367
FT /note="WD 7"
FT REGION 421..729
FT /note="Interaction with CCNA1"
FT /evidence="ECO:0000269|PubMed:11238922"
FT REGION 421..479
FT /note="Interaction with ASF1A"
FT REGION 439..475
FT /note="Required for repression of histone gene
FT transcription"
FT REGION 494..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..826
FT /note="Interaction with histone H2B"
FT REGION 594..739
FT /note="Interaction with PAX3"
FT /evidence="ECO:0000250"
FT REGION 604..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..1017
FT /note="Interaction with histone H4"
FT REGION 740..828
FT /note="Interaction with PAX3"
FT /evidence="ECO:0000250"
FT COMPBIAS 494..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 555
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000269|PubMed:11238922"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 576
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 586
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11238922"
FT VAR_SEQ 593..799
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8111380"
FT /id="VSP_006772"
FT MUTAGEN 449..458
FT /note="Missing: Impairs binding to ASF1A."
FT /evidence="ECO:0000269|PubMed:16980972"
FT MUTAGEN 458..460
FT /note="RRR->AKK: Abrogates binding to ASF1A."
FT MUTAGEN 458..460
FT /note="RRR->KKK: Impairs binding to ASF1A."
FT MUTAGEN 458..459
FT /note="RR->AK: Impairs binding to ASF1A."
FT MUTAGEN 458
FT /note="R->A: Impairs binding to ASF1A."
FT MUTAGEN 458
FT /note="R->K: Impairs binding to ASF1A; when associated with
FT K-460."
FT MUTAGEN 459..468
FT /note="Missing: Abrogates binding to ASF1A."
FT /evidence="ECO:0000269|PubMed:16980972"
FT MUTAGEN 459
FT /note="R->A: Abrogates binding to ASF1A."
FT /evidence="ECO:0000269|PubMed:16980972"
FT MUTAGEN 460
FT /note="R->A: Abrogates binding to ASF1A."
FT /evidence="ECO:0000269|PubMed:16980972"
FT MUTAGEN 460
FT /note="R->K: Impairs binding to ASF1A; when associated with
FT K-458."
FT /evidence="ECO:0000269|PubMed:16980972"
FT MUTAGEN 461
FT /note="I->D: Abrogates binding to ASF1A."
FT /evidence="ECO:0000269|PubMed:16980972"
FT MUTAGEN 464
FT /note="L->D: Impairs binding to ASF1A."
FT /evidence="ECO:0000269|PubMed:16980972"
FT MUTAGEN 466
FT /note="I->D: Impairs binding to ASF1A."
FT /evidence="ECO:0000269|PubMed:16980972"
FT MUTAGEN 555
FT /note="T->A: Impairs phosphorylation by CDK2."
FT /evidence="ECO:0000269|PubMed:11238922"
FT MUTAGEN 628..631
FT /note="KRKL->AAAA: Impairs binding to CCNA1 and
FT phosphorylation by CDK2."
FT /evidence="ECO:0000269|PubMed:11238922"
FT CONFLICT 9
FT /note="V -> G (in Ref. 1; CAA54721)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="I -> N (in Ref. 1; CAA54721/CAA57436 and 2;
FT CAA61979)"
FT /evidence="ECO:0000305"
FT CONFLICT 990
FT /note="L -> M (in Ref. 5; CAA53044)"
FT /evidence="ECO:0000305"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:2I32"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:2I32"
FT STRAND 690..695
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 702..713
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 716..725
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 728..736
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 738..743
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 745..752
FT /evidence="ECO:0007829|PDB:5YJE"
FT TURN 753..755
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 756..761
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 766..772
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 777..783
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 786..791
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 794..800
FT /evidence="ECO:0007829|PDB:5YJE"
FT TURN 801..804
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 805..813
FT /evidence="ECO:0007829|PDB:5YJE"
FT HELIX 814..817
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 824..829
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 835..839
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 842..848
FT /evidence="ECO:0007829|PDB:5YJE"
FT TURN 849..852
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 853..859
FT /evidence="ECO:0007829|PDB:5YJE"
FT HELIX 860..862
FT /evidence="ECO:0007829|PDB:5YJE"
FT TURN 865..867
FT /evidence="ECO:0007829|PDB:5YJE"
FT HELIX 885..890
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 904..906
FT /evidence="ECO:0007829|PDB:5YJE"
FT HELIX 908..928
FT /evidence="ECO:0007829|PDB:5YJE"
FT HELIX 932..949
FT /evidence="ECO:0007829|PDB:5YJE"
FT HELIX 952..963
FT /evidence="ECO:0007829|PDB:5YJE"
FT STRAND 976..978
FT /evidence="ECO:0007829|PDB:5YJE"
FT HELIX 983..995
FT /evidence="ECO:0007829|PDB:5YJE"
FT HELIX 998..1000
FT /evidence="ECO:0007829|PDB:5YJE"
FT HELIX 1001..1015
FT /evidence="ECO:0007829|PDB:5YJE"
SQ SEQUENCE 1017 AA; 111835 MW; 475784B2FF9D16D6 CRC64;
MKLLKPTWVN HNGKPIFSVD IHPDGTKFAT GGQGQDSGKV VIWNMSPVLQ EDDEKDENIP
KMLCQMDNHL ACVNCVRWSN SGMYLASGGD DKLIMVWKRA TYIGPSTVFG SSGKLANVEQ
WRCVSILRNH SGDVMDVAWS PHDAWLASCS VDNTVVIWNA VKFPEILATL RGHSGLVKGL
TWDPVGKYIA SQADDRSLKV WRTLDWQLET SITKPFDECG GTTHVLRLSW SPDGHYLVSA
HAMNNSGPTA QIIEREGWKT NMDFVGHRKA VTVVKFNPKI FKKKQKNGSS AKPSCPYCCC
AVGSKDRSLS VWLTCLKRPL VVIHELFDKS IMDISWTLNG LGILVCSMDG SVAFLDFSQD
ELGDPLSEEE KSRIHQSTYG KSLAIMTEAQ LSTAVIENPE MLKYQRRQQQ QQLDQKSAAT
REMGSATSVA GVVNGESLED IRKNLLKKQV ETRTADGRRR ITPLCIAQLD TGDFSTAFFN
SIPLSGSLAG TMLSSHSSPQ LLPLDSSTPN SFGASKPCTE PVVAASARPA GDSVNKDSMN
ATSTPAALSP SVLTTPSKIE PMKAFDSRFT ERSKATPGAP ALTSMTPTAV ERLKEQNLVK
ELRPRDLLES SSDSDEKVPL AKASSLSKRK LELEVETVEK KKKGRPRKDS RLMPVSLSVQ
SPAALTAEKE AMCLSAPALA LKLPIPSPQR AFTLQVSSDP SMYIEVENEV TVVGGVKLSR
LKCNREGKEW ETVLTSRILT AAGSCDVVCV ACEKRMLSVF STCGRRLLSP ILLPSPISTL
HCTGSYVMAL TAAATLSVWD VHRQVVVVKE ESLHSILAGS DMTVSQILLT QHGIPVMNLS
DGKAYCFNPS LSTWNLVSDK QDSLAQCADF RSSLPSQDAM LCSGPLAIIQ GRTSNSGRQA
ARLFSVPHVV QQETTLAYLE NQVAAALTLQ SSHEYRHWLL VYARYLVNEG FEYRLREICK
DLLGPVHYST GSQWESTVVG LRKRELLKEL LPVIGQNLRF QRLFTECQEQ LDILRDK
