HIR2_YEAST
ID HIR2_YEAST Reviewed; 875 AA.
AC P32480; D6W2A5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Protein HIR2;
DE AltName: Full=Histone transcription regulator 2;
GN Name=HIR2; OrderedLocusNames=YOR038C; ORFNames=OR26.31;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8417331; DOI=10.1128/mcb.13.1.28-38.1993;
RA Sherwood P.W., Tsang S.V., Osley M.A.;
RT "Characterization of HIR1 and HIR2, two genes required for regulation of
RT histone gene transcription in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:28-38(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-113.
RX PubMed=8027080; DOI=10.1016/s0021-9258(17)32434-1;
RA Reed J.C., Bidwai A.P., Glover C.V.C.;
RT "Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory
RT beta'-subunit of Saccharomyces cerevisiae casein kinase II.";
RL J. Biol. Chem. 269:18192-18200(1994).
RN [5]
RP FUNCTION, AND INTERACTION WITH HIR1.
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 [6]
RP FUNCTION.
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 [7]
RP FUNCTION.
RX PubMed=9671489; DOI=10.1128/mcb.18.8.4793;
RA Kaufman P.D., Cohen J.L., Osley M.A.;
RT "Hir proteins are required for position-dependent gene silencing in
RT Saccharomyces cerevisiae in the absence of chromatin assembly factor I.";
RL Mol. Cell. Biol. 18:4793-4806(1998).
RN [8]
RP FUNCTION, AND INTERACTION WITH SNF2; SNF5 AND SWI3.
RX PubMed=10445029; DOI=10.1016/s1097-2765(00)80189-6;
RA Dimova D., Nackerdien Z., Furgeson S., Eguchi S., Osley M.A.;
RT "A role for transcriptional repressors in targeting the yeast Swi/Snf
RT complex.";
RL Mol. Cell 4:75-83(1999).
RN [9]
RP INTERACTION WITH ASF1.
RX PubMed=11412995; DOI=10.1016/s0960-9822(01)00140-3;
RA Sharp J.A., Fouts E.T., Krawitz D.C., Kaufman P.D.;
RT "Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for
RT heterochromatic silencing.";
RL Curr. Biol. 11:463-473(2001).
RN [10]
RP FUNCTION.
RX PubMed=11937489; DOI=10.1101/gad.978902;
RA Ng H.H., Robert F., Young R.A., Struhl K.;
RT "Genome-wide location and regulated recruitment of the RSC nucleosome-
RT remodeling complex.";
RL Genes Dev. 16:806-819(2002).
RN [11]
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 [12]
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 [13]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX
RP WITH HIR1; HIR3 AND HPC2, AND INTERACTION WITH 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 [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A
RP COMPLEX WITH HIR1; HIR3 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 [15]
RP FUNCTION.
RX PubMed=16449659; DOI=10.1128/mcb.26.4.1496-1509.2006;
RA Nourani A., Robert F., Winston F.;
RT "Evidence that Spt2/Sin1, an HMG-like factor, plays roles in transcription
RT elongation, chromatin structure, and genome stability in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 26:1496-1509(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, 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 [17]
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).
CC -!- FUNCTION: Component of the HIR complex, which cooperates with ASF1 to
CC promote replication-independent chromatin assembly. The HIR complex is
CC also required for the periodic repression of three of the four histone
CC gene loci during the cell cycle as well as for autogenous regulation of
CC the HTA1-HTB1 locus by H2A and H2B. DNA-binding by the HIR complex may
CC repress transcription by inhibiting nucleosome remodeling by the
CC SWI/SNF complex. The HIR complex may also be required for
CC transcriptional silencing of centromeric, telomeric and mating-type
CC loci in the absence of CAF-1. {ECO:0000269|PubMed:10445029,
CC ECO:0000269|PubMed:11937489, ECO:0000269|PubMed:12524332,
CC ECO:0000269|PubMed:16264190, ECO:0000269|PubMed:16303565,
CC ECO:0000269|PubMed:16449659, ECO:0000269|PubMed:8417331,
CC ECO:0000269|PubMed:9001207, ECO:0000269|PubMed:9671488,
CC ECO:0000269|PubMed:9671489}.
CC -!- SUBUNIT: Component of the HIR complex, composed of HIR1, HIR2, HIR3 and
CC HPC2 (PubMed:16264190, PubMed:16303565, PubMed:9001207). This complex
CC may consist of one copy of HIR1 and HIR3 and two copies of HIR2 and
CC HPC2 (PubMed:16264190). The HIR complex interacts with ASF1
CC (PubMed:11412995, PubMed:16303565). Interacts with SNF2
CC (PubMed:10445029). Interacts with SNF5 (PubMed:10445029). Interacts
CC with SWI3 (PubMed:10445029). Interacts with RTT106 (PubMed:19683497).
CC {ECO:0000269|PubMed:10445029, ECO:0000269|PubMed:11412995,
CC ECO:0000269|PubMed:16264190, ECO:0000269|PubMed:16303565,
CC ECO:0000269|PubMed:19683497, ECO:0000269|PubMed:9001207}.
CC -!- INTERACTION:
CC P32480; P32479: HIR1; NbExp=8; IntAct=EBI-8323, EBI-8316;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8417331}. 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 WD repeat HIR1 family. {ECO:0000305}.
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DR EMBL; L03839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X87331; CAA60757.1; -; Genomic_DNA.
DR EMBL; Z74946; CAA99228.1; -; Genomic_DNA.
DR EMBL; U08849; AAA21657.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10821.1; -; Genomic_DNA.
DR PIR; S62177; S62177.
DR RefSeq; NP_014681.1; NM_001183457.1.
DR AlphaFoldDB; P32480; -.
DR SMR; P32480; -.
DR BioGRID; 34440; 451.
DR ComplexPortal; CPX-124; HIR complex.
DR DIP; DIP-2366N; -.
DR IntAct; P32480; 23.
DR MINT; P32480; -.
DR STRING; 4932.YOR038C; -.
DR iPTMnet; P32480; -.
DR MaxQB; P32480; -.
DR PaxDb; P32480; -.
DR PRIDE; P32480; -.
DR EnsemblFungi; YOR038C_mRNA; YOR038C; YOR038C.
DR GeneID; 854203; -.
DR KEGG; sce:YOR038C; -.
DR SGD; S000005564; HIR2.
DR VEuPathDB; FungiDB:YOR038C; -.
DR eggNOG; KOG0973; Eukaryota.
DR GeneTree; ENSGT00550000074919; -.
DR HOGENOM; CLU_004372_1_0_1; -.
DR InParanoid; P32480; -.
DR OMA; TICTAGD; -.
DR BioCyc; YEAST:G3O-33584-MON; -.
DR PRO; PR:P32480; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32480; protein.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
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; IDA: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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IDA:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR031120; HIR1.
DR InterPro; IPR011494; Hira.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13831; PTHR13831; 1.
DR Pfam; PF07569; Hira; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..875
FT /note="Protein HIR2"
FT /id="PRO_0000051017"
FT REPEAT 10..47
FT /note="WD 1"
FT REPEAT 118..158
FT /note="WD 2"
FT REPEAT 163..201
FT /note="WD 3"
FT REPEAT 237..277
FT /note="WD 4"
FT REPEAT 278..316
FT /note="WD 5"
FT REPEAT 320..359
FT /note="WD 6"
FT REPEAT 546..587
FT /note="WD 7"
FT REPEAT 589..626
FT /note="WD 8"
FT REGION 398..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 284..285
FT /note="KG -> NF (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 373..374
FT /note="KK -> FL (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 875 AA; 98445 MW; C77D677BF424680D CRC64;
MRLLKYPLDI HNEQVNALAA LGPYIILAGS GGHVMAWRQQ QLVDTAFDRV MIKDLKPEVS
FQVDQDTTGD IFFITGDLET LYIGSEHRLW GYSGWLCRDT NNINSVEKMN SKLLFECKSP
STITDVKYDI NLGILFVLLS NENKILLFRH KTFDKLSEIT IDKASKPITG IIDPTGQTFT
VMTSDRSILV YQINKTGTHK LINKLTQHVQ MYPLHYRISM SPQADILPVI NSVKGVPNNA
TSCTALLDRN NNYKVTKTLV TPSSNGCRVL VYSPAFYEKP NLKKGTSTRY NLIATSGSTD
GTILVWNTKR MKPLFNALQV SSTAINDMSW SQDGFTLFAI SNDATLYTFA FQEKDLGVAL
PQTEIKSLQE VNKKLPKLEE PLAEQIPKSF PENIKLEESA SAAPIPNDIG RSAVGKKPTK
KKTANNQTNG IKTIQSTSME FNTPSYTVPR DLKRKPKEAT PSNIAPGSKK QKKELQPIDF
LDTGLLLPNT SFSRIRLATP KIRSTFKYSP INNPNLILDV KNGSGNEQRP TIVKLTSKVL
DQDQVLFQDF IPKLITICTA GDTFWSFCSE DGSIYIYSDS GRKLMAPLVL GVSISFLEAC
GTYLLCLTSI GELYCWNIEQ KKLAFPTNTI YPLLNPSLRY SDDILTRAEN ITLCSITKKG
VPLVTLSNGD GYLFDKNMET WLLVSDGWWA YGSQYWDTTN TTGLSSSKAN TDSFNGSESN
INEIVSDIKN DNQSIINFLE CKTNDELNRK GRIKNLQRFA RTILMKEGFE NMEEIVTLSH
LENKILISIR LEEPEEFSKL MMVYCIRLSE LGYMDRLNDV FQWLYDDLPI SGTGSAFADK
DFKRNLLKKI LIACGDIRQV QRVTTRYAKE MNIIS
