H1_YEAST
ID H1_YEAST Reviewed; 258 AA.
AC P53551; D6W3P0; Q6Q5R6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Histone H1;
GN Name=HHO1; OrderedLocusNames=YPL127C; ORFNames=LPI17C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP POSSIBLE FUNCTION.
RX PubMed=8772381; DOI=10.1016/s0968-0004(96)30030-3;
RA Landsman D.;
RT "Histone H1 in Saccharomyces cerevisiae: a double mystery solved?";
RL Trends Biochem. Sci. 21:287-288(1996).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9046096;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<151::aid-yea94>3.0.co;2-5;
RA Ushinsky S.C., Bussey H., Ahmed A.A., Wang Y., Friesen J.D., Williams B.A.,
RA Storms R.K.;
RT "Histone H1 in Saccharomyces cerevisiae.";
RL Yeast 13:151-161(1997).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION BY
RP 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 [8]
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).
CC -!- FUNCTION: Could act as an H1-type linker histone. Has been shown to
CC bind DNA. {ECO:0000269|PubMed:9046096}.
CC -!- INTERACTION:
CC P53551; Q12692: HTZ1; NbExp=3; IntAct=EBI-8064, EBI-8080;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC -!- MISCELLANEOUS: Present with 6560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; U43703; AAB68231.1; -; Genomic_DNA.
DR EMBL; AY557756; AAS56082.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11306.1; -; Genomic_DNA.
DR PIR; S69056; S69056.
DR RefSeq; NP_015198.1; NM_001183941.1.
DR PDB; 1UHM; NMR; -; A=41-118.
DR PDB; 1USS; NMR; -; A=171-258.
DR PDB; 1UST; NMR; -; A=38-130.
DR PDB; 1YQA; NMR; -; A=171-258.
DR PDBsum; 1UHM; -.
DR PDBsum; 1USS; -.
DR PDBsum; 1UST; -.
DR PDBsum; 1YQA; -.
DR AlphaFoldDB; P53551; -.
DR SMR; P53551; -.
DR BioGRID; 36054; 299.
DR DIP; DIP-6587N; -.
DR IntAct; P53551; 40.
DR MINT; P53551; -.
DR STRING; 4932.YPL127C; -.
DR iPTMnet; P53551; -.
DR MaxQB; P53551; -.
DR PaxDb; P53551; -.
DR PRIDE; P53551; -.
DR EnsemblFungi; YPL127C_mRNA; YPL127C; YPL127C.
DR GeneID; 855976; -.
DR KEGG; sce:YPL127C; -.
DR SGD; S000006048; HHO1.
DR VEuPathDB; FungiDB:YPL127C; -.
DR eggNOG; KOG4012; Eukaryota.
DR HOGENOM; CLU_069424_0_0_1; -.
DR InParanoid; P53551; -.
DR OMA; YLFNSAI; -.
DR BioCyc; YEAST:G3O-34026-MON; -.
DR EvolutionaryTrace; P53551; -.
DR PRO; PR:P53551; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P53551; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
DR GO; GO:0031490; F:chromatin DNA binding; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0042301; F:phosphate ion binding; IMP:CAFA.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0097100; F:supercoiled DNA binding; IMP:CAFA.
DR GO; GO:0030261; P:chromosome condensation; IMP:SGD.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
DR CDD; cd00073; H15; 1.
DR DisProt; DP00423; -.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00538; Linker_histone; 2.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR PROSITE; PS51504; H15; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..258
FT /note="Histone H1"
FT /id="PRO_0000196001"
FT DOMAIN 43..117
FT /note="H15 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 176..251
FT /note="H15 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 8
FT /note="T -> I (in Ref. 3; AAS56082)"
FT /evidence="ECO:0000305"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:1UHM"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:1UHM"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1UHM"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1UHM"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:1UHM"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1UHM"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1UHM"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:1USS"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1YQA"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:1USS"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:1USS"
FT HELIX 220..234
FT /evidence="ECO:0007829|PDB:1USS"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1USS"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1YQA"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:1USS"
SQ SEQUENCE 258 AA; 27804 MW; B0C53AC186E49F96 CRC64;
MAPKKSTTKT TSKGKKPATS KGKEKSTSKA AIKKTTAKKE EASSKSYREL IIEGLTALKE
RKGSSRPALK KFIKENYPIV GSASNFDLYF NNAIKKGVEA GDFEQPKGPA GAVKLAKKKS
PEVKKEKEVS PKPKQAATSV SATASKAKAA STKLAPKKVV KKKSPTVTAK KASSPSSLTY
KEMILKSMPQ LNDGKGSSRI VLKKYVKDTF SSKLKTSSNF DYLFNSAIKK CVENGELVQP
KGPSGIIKLN KKKVKLST
