HPC2_YEAST
ID HPC2_YEAST Reviewed; 625 AA.
AC Q01448; A2TBP6; D6VQL1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Histone promoter control protein 2;
GN Name=HPC2; OrderedLocusNames=YBR215W; ORFNames=YBR1503;
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].
RX PubMed=1406694; DOI=10.1128/mcb.12.11.5249-5259.1992;
RA Xu H., Kim U.J., Schuster T., Grunstein M.;
RT "Identification of a new set of cell cycle-regulatory genes that regulate
RT S-phase transcription of histone genes in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:5249-5259(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 [MRNA] OF 1-83.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
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 [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX
RP WITH HIR1; HIR2 AND HIR3, 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 [9]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A
RP COMPLEX WITH HIR1; HIR2 AND HIR3.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49 AND SER-435, AND
RP IDENTIFICATION BY 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, 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: Component of the HIR complex, which functions as a histone
CC chaperone that cooperates with ASF1 to promote replication-independent
CC chromatin assembly. The HIR complex is also required for the periodic
CC repression of three of the four histone gene loci during cell cycle as
CC well as for autogenous regulation of the HTA1-HTB1 locus by H2A and
CC H2B. DNA-binding by the HIR complex may repress transcription by
CC inhibiting nucleosome remodeling by the SWI/SNF complex. The HIR
CC complex may also be required for transcriptional silencing of
CC centromeric, telomeric and mating-type loci in the absence of CAF-1.
CC {ECO:0000269|PubMed:12524332, ECO:0000269|PubMed:16264190,
CC ECO:0000269|PubMed:16303565}.
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 -!- INTERACTION:
CC Q01448; P32479: HIR1; NbExp=6; IntAct=EBI-8520, EBI-8316;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. 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 HIR1 and RTT106 to the
CC HTA1-HTB1 promoter. {ECO:0000269|PubMed:19683497}.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HPC2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34684.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA85179.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M94207; AAA34684.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z36084; CAA85179.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EF123149; ABM97493.1; -; mRNA.
DR EMBL; BK006936; DAA07331.1; -; Genomic_DNA.
DR PIR; A48123; A48123.
DR RefSeq; NP_009774.4; NM_001178563.3.
DR AlphaFoldDB; Q01448; -.
DR BioGRID; 32912; 320.
DR ComplexPortal; CPX-124; HIR complex.
DR DIP; DIP-4587N; -.
DR IntAct; Q01448; 10.
DR MINT; Q01448; -.
DR STRING; 4932.YBR215W; -.
DR CarbonylDB; Q01448; -.
DR iPTMnet; Q01448; -.
DR MaxQB; Q01448; -.
DR PaxDb; Q01448; -.
DR PRIDE; Q01448; -.
DR EnsemblFungi; YBR215W_mRNA; YBR215W; YBR215W.
DR GeneID; 852516; -.
DR KEGG; sce:YBR215W; -.
DR SGD; S000000419; HPC2.
DR VEuPathDB; FungiDB:YBR215W; -.
DR eggNOG; ENOG502RG9A; Eukaryota.
DR HOGENOM; CLU_023932_0_0_1; -.
DR InParanoid; Q01448; -.
DR OMA; HINDTNG; -.
DR BioCyc; YEAST:G3O-29152-MON; -.
DR Reactome; R-SCE-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR PRO; PR:Q01448; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; Q01448; 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; HDA: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:0006334; P:nucleosome assembly; IDA:ComplexPortal.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR InterPro; IPR014840; HRD.
DR Pfam; PF08729; HUN; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..625
FT /note="Histone promoter control protein 2"
FT /id="PRO_0000084039"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 625 AA; 67775 MW; 9F787D6EA37A8374 CRC64;
MDQKAIVLDN SKSGSKQTKS SGKMQTQTDT NAEVLNTDNS IKKETGSDSE DLFNKFSNKK
TNRKIPNIAE ELAKNRNYVK GASPSPIIIS GSSSTSPSGP SSSSTNPMGI PTNRFNKNTV
ELYQHSPSPV MTTNKTDTEE KRQNNRNMDN KNTPERGSSS FAAKQLKISS LLTISSNEDS
KTLHINDTNG NKNSNAASNN IPSAYAELHT EGNSIESLIK PPSSPRNKSL TPKVILPTQN
MDGTIAKDPH LGDNTPGILI AKTSSPVNLD VESTAQSLGK FNKSTNSLKA ALTKAPAEKV
SLKRSISSVT NSDSNISSSK KPTSEKAKKS SSASAILPKP TTTKTSKKAA SNSSDSTRKK
NASNKTTSAI KKESNAGSKL NTVKKENSSL SSIKATEKEK DKGGNSTEAK NSTSNVRKEP
TAKSPKRLVA APTVSPPKIL QTAETKAKEP SILIDVPLYQ ADTNDYLDEN GQVIFNLSTL
IKEKYHPKSK ELAQLKDSKR NLLMQLSDHS NGSLEKEKDE EGDVIELDDD EDMEEDEGEI
DTETNTVTTT ISPKKKSHPM KGKNLIGKYD VEDPFIDDSE LLWEEQRAAT KDGFFVYFGP
LIEKGHYASL ERANGTMKRG GVKNK
