ID   HIR3_YEAST              Reviewed;        1648 AA.
AC   P47171; D6VWV9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Histone transcription regulator 3;
GN   Name=HIR3; Synonyms=HPC1; OrderedLocusNames=YJR140C; ORFNames=J2161;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=9001207; DOI=10.1128/mcb.17.2.545;
RA   Spector M.S., Raff A., DeSilva H., Lee K., Osley M.A.;
RT   "Hir1p and Hir2p function as transcriptional corepressors to regulate
RT   histone gene transcription in the Saccharomyces cerevisiae cell cycle.";
RL   Mol. Cell. Biol. 17:545-552(1997).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9671488; DOI=10.1128/mcb.18.8.4783;
RA   Qian Z., Huang H., Hong J.Y., Burck C.L., Johnston S.D., Berman J.,
RA   Carol A., Liebman S.W.;
RT   "Yeast Ty1 retrotransposition is stimulated by a synergistic interaction
RT   between mutations in chromatin assembly factor I and histone regulatory
RT   proteins.";
RL   Mol. Cell. Biol. 18:4783-4792(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=12524332; DOI=10.1093/genetics/162.4.1557;
RA   Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y.,
RA   Rhoades A.R., Kaufman P.D., Stillman D.J.;
RT   "Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause
RT   dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin
RT   structure.";
RL   Genetics 162:1557-1571(2002).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION IN A COMPLEX WITH HIR1; HIR2 AND HPC2, AND INTERACTION WITH
RP   ASF1.
RX   PubMed=16303565; DOI=10.1016/j.cub.2005.10.053;
RA   Green E.M., Antczak A.J., Bailey A.O., Franco A.A., Wu K.J.,
RA   Yates J.R. III, Kaufman P.D.;
RT   "Replication-independent histone deposition by the HIR complex and Asf1.";
RL   Curr. Biol. 15:2044-2049(2005).
RN   [8]
RP   IDENTIFICATION IN A COMPLEX WITH HIR1; HIR2 AND HPC2.
RX   PubMed=16264190; DOI=10.1101/gad.1341105;
RA   Prochasson P., Florens L., Swanson S.K., Washburn M.P., Workman J.L.;
RT   "The HIR corepressor complex binds to nucleosomes generating a distinct
RT   protein/DNA complex resistant to remodeling by SWI/SNF.";
RL   Genes Dev. 19:2534-2539(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   INTERACTION WITH RTT106, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023;
RA   Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K.,
RA   Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J.,
RA   Andrews B.J.;
RT   "Two-color cell array screen reveals interdependent roles for histone
RT   chaperones and a chromatin boundary regulator in histone gene repression.";
RL   Mol. Cell 35:340-351(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: HIR1, HIR2 and HIR3 are repressors of histone gene
CC       transcription. They are required for the periodic repression of three
CC       of the four histone gene loci during cell cycle as well as for
CC       autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. Also has a
CC       role in nucleosome assembly. {ECO:0000269|PubMed:12524332,
CC       ECO:0000269|PubMed:9001207}.
CC   -!- SUBUNIT: Component of the HIR complex, composed of HIR1, HIR2, HIR3 and
CC       HPC2 (PubMed:16264190, PubMed:16303565). This complex may consist of
CC       one copy of HIR1 and HIR3 and two copies of HIR2 and HPC2
CC       (PubMed:16264190). The HIR complex interacts with ASF1
CC       (PubMed:16303565). Interacts with RTT106 (PubMed:19683497).
CC       {ECO:0000269|PubMed:16264190, ECO:0000269|PubMed:16303565,
CC       ECO:0000269|PubMed:19683497}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9671488}. Chromosome
CC       {ECO:0000269|PubMed:19683497}. Note=Localizes to the promoter region of
CC       histones HTA1-HTB1. {ECO:0000269|PubMed:19683497}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes localization of RTT106 to the HTA1-HTB1
CC       promoter. {ECO:0000269|PubMed:19683497}.
CC   -!- MISCELLANEOUS: Present with 922 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HIR3 family. {ECO:0000305}.
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DR   EMBL; Z49640; CAA89672.1; -; Genomic_DNA.
DR   EMBL; Z49641; CAA89674.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08925.1; -; Genomic_DNA.
DR   PIR; S57163; S57163.
DR   RefSeq; NP_012674.1; NM_001181798.1.
DR   AlphaFoldDB; P47171; -.
DR   BioGRID; 33896; 363.
DR   ComplexPortal; CPX-124; HIR complex.
DR   DIP; DIP-2631N; -.
DR   IntAct; P47171; 9.
DR   MINT; P47171; -.
DR   STRING; 4932.YJR140C; -.
DR   iPTMnet; P47171; -.
DR   MaxQB; P47171; -.
DR   PaxDb; P47171; -.
DR   PRIDE; P47171; -.
DR   EnsemblFungi; YJR140C_mRNA; YJR140C; YJR140C.
DR   GeneID; 853605; -.
DR   KEGG; sce:YJR140C; -.
DR   SGD; S000003901; HIR3.
DR   VEuPathDB; FungiDB:YJR140C; -.
DR   eggNOG; ENOG502QQX4; Eukaryota.
DR   HOGENOM; CLU_001316_0_0_1; -.
DR   InParanoid; P47171; -.
DR   OMA; WETWYRL; -.
DR   BioCyc; YEAST:G3O-31755-MON; -.
DR   Reactome; R-SCE-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR   PRO; PR:P47171; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47171; protein.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000417; C:HIR complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003714; F:transcription corepressor activity; IMP:SGD.
DR   GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:SGD.
DR   GO; GO:1905268; P:negative regulation of chromatin organization; IDA:ComplexPortal.
DR   GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0006334; P:nucleosome assembly; IDA:ComplexPortal.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IMP:SGD.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR   InterPro; IPR033053; Hir3/CABIN1.
DR   PANTHER; PTHR15502; PTHR15502; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..1648
FT                   /note="Histone transcription regulator 3"
FT                   /id="PRO_0000203124"
FT   REGION          301..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1597..1630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1597..1623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         302
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   1648 AA;  191680 MW;  B1F31815797852D4 CRC64;
     MSMFNALNSN IEGEQYEAEE HSRELQIEQS FNILQDALID LKNKDFEKSD SKFQELFQID
     VVKPDRWGMY RNSSPTLDNL RYLCYRNRGM YYHLYLENNY ERLNSQELVN CILKAVENLV
     ESIQHSDADF AVTDLLARIF KSFNSVKLER LISEYEFTKQ ENLSLLLGRH RKFLLNDLTL
     MMNNYVELTN KLLVPNLSDN TIFERYHLEK YKDIKPEPLA FGPILSRISE MKKQDEEIMK
     KLDVFNVTLN EESWDEVAKA LKNLLPSVKT SSLIGRNMDP YNEIEEPIEA VKFELSEAIN
     NTPSLDRESE RQEEEQDNES VRADDKSGNL APSDIQTNEE ARPNKRTDEH IDSTKPLQRS
     SKRFKEREQE NSKELVMDVH KRFFGEFNTL LSYIHILPFC DFDTFASKFI IGSSDKQPEK
     FIPYTDLYEC LKSWSSRYTD IFNQNDYLSS GSNENEELFQ LNALLKSNAF DDKESFPRYL
     NDLDSDHIRS FISEVNAGNL HFHQVRLKLL FKLLGTYDEG NGRRLIIDYL WESQLLKIVL
     WFVFGIESNI FALINKNKRQ CKYLALSIYE LLVNHLGNIV EEITNKRIQG HKSADLKSQR
     NKVEKRIRSW HTLLEQIADE KDKELYVHFQ WTHYCFLQYT CDIVDSRLSE TLTSLENTIK
     DSDSSLDIAY PNYRHIPALN LNTVQSQKRK IRIIQNITVE DISEDTNSDT HSENHLETLE
     KVLLHILHPS TNHSNIDEEM VSFIFNSPFL LKIRLWGVLF SSYVKKSSIQ DVQRIYFHVL
     DFMKGALTSP VYKESNPHGR HQMLLTVLTA IGYLSSQLTA ILNSNRWESS DFVLEDYMFE
     KLLQTFFFFY TVLFYESSAV NDVSNKSFFK RASKSSGKMK DIMIDLATLI LYYYDLQAKL
     RTPAEQGIET TELIWSLHTL FGHFHFCDAS NGKFLDLAEK LLCQFINNDS FLQLKQILWC
     RYHYAIASDN FSPDLHDTKA VEMEKIHSLP LGTYLIKLQY QNKNPYLSSS KTTLKQIMDN
     IIEKIGDPST LDNHIISRNS FLLNEYLSRP ITADLLKHTF SGATSLYLTS PNDELQQGMT
     AGLFYVSSLQ SLGLYKMRKK SMQARPSELD SIIRMLKNDI IYNTNRFESW ILLGKCYSYI
     VEDDLIWTSD KITVPEKKDV IALTQRKAIL CYLMAISIYY SKLDRTIDDK KIILEALDDL
     GSMLISGYYN PMNKLCFSWK SSAENTMRLS ETGEVVMEKT KKITTISDFN IEQSIFLCFN
     RACSLSGDIK SQDDVFVLNW SSFYNLAKFF FKTDGGNNCK LVAKYITQGC QIAYESSPAK
     DPIIEPHYLL VNACYKWVKR GVIGVNEALT LLSKDNQFFQ EQEEFWVNDE GLAWDYQEKF
     FFDKIIRLLR HLLSVDKKKW QHRPRYRIAR ILFDDLGDVN GALEEMDSLI SAKSINKNLV
     NIWKPDFERP GKHFIYTYQY LVLYLDLLFA IKDFNTTGLV IKKLRRFGSG TVNVNELLER
     AINVYTQSAK IKLQLQDKSY VEQILPTLNY QEFLKISEQL NQVFDQGKYP EEISSGLKLA
     FQLKKGHSGI AFDSVCLGIY FEYLYFPLAR QDQSLTDVND ENNPALPSSG SVTSKSTPDP
     TSKPSAIKKR VTKKEVFDRV RLLVDKIT