H31_SCHPO
ID H31_SCHPO Reviewed; 136 AA.
AC P09988;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Histone H3.1/H3.2;
GN Name=hht1; ORFNames=SPAC1834.04;
GN and
GN Name=hht2; ORFNames=pi060, SPBC8D2.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=4092687; DOI=10.1002/j.1460-2075.1985.tb04113.x;
RA Matsumoto S., Yanagida M.;
RT "Histone gene organization of fission yeast: a common upstream sequence.";
RL EMBO J. 4:3531-3538(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT2).
RC STRAIN=972 / ATCC 24843;
RX PubMed=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT1 AND HHT2).
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP METHYLATION AT LYS-10.
RX PubMed=11283354; DOI=10.1126/science.1060118;
RA Nakayama J., Rice J.C., Strahl B.D., Allis C.D., Grewal S.I.S.;
RT "Role of histone H3 lysine 9 methylation in epigenetic control of
RT heterochromatin assembly.";
RL Science 292:110-113(2001).
RN [5]
RP METHYLATION AT LYS-37.
RX PubMed=16087749; DOI=10.1128/ec.4.8.1446-1454.2005;
RA Morris S.A., Shibata Y., Noma K., Tsukamoto Y., Warren E., Temple B.,
RA Grewal S.I.S., Strahl B.D.;
RT "Histone H3 K36 methylation is associated with transcription elongation in
RT Schizosaccharomyces pombe.";
RL Eukaryot. Cell 4:1446-1454(2005).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Phosphorylated by ark1 to form H3S10ph in a cell cycle-dependent
CC manner during mitosis and meiosis. H3S10ph is also formed by ssp2,
CC promotes subsequent H3K14ac formation by gcn5, and is required for
CC transcriptional activation through TBP recruitment to the promoters.
CC Dephosphorylation is performed by sds21.
CC -!- PTM: Mono-, di- and trimethylated by the COMPASS complex to form
CC H3K4me1/2/3. H3K4me activates gene expression by regulating
CC transcription elongation and plays a role in telomere length
CC maintenance. H3K4me enrichment correlates with transcription levels,
CC and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end
CC of genes, shifting to H3K4me2 and then H3K4me1 (By similarity).
CC Methylated by clr4 to form H3K9me1. H3K9me1 represents a specific tag
CC for epigenetic transcriptional repression by recruiting swi6/HP1 to
CC methylated histones. Targeting to histone probably involves clr3 and
CC rik1. Essential for silencing of centromeres and directional switching
CC of the mating type. Methylated by set2 to form H3K36me. H3K36me
CC represses gene expression. Methylated by dot1 to form H3K79me. H3K79me
CC is required for association of SIR proteins with telomeric regions and
CC for telomeric silencing. The COMPASS-mediated formation of H3K4me2/3
CC and the dot1-mediated formation of H3K79me require H2BK123ub1 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylation of histone H3 leads to transcriptional activation.
CC H3K14ac formation by gcn5 is promoted by H3S10ph. H3K14ac can also be
CC formed by esa1. H3K56ac formation occurs predominantly in newly
CC synthesized H3 molecules during G1, S and G2/M of the cell cycle and
CC may be involved in DNA repair (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following conventions are used: H3K4me1/2/3 =
CC mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1
CC = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac =
CC acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated
CC Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24;
CC H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28;
CC H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac =
CC acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37;
CC H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3
CC = mono-, di- and trimethylated Lys-80. {ECO:0000305}.
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DR EMBL; X05222; CAA28851.1; -; Genomic_DNA.
DR EMBL; X05223; CAA28852.1; -; Genomic_DNA.
DR EMBL; AB004538; BAA21441.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB75772.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17819.1; -; Genomic_DNA.
DR PIR; E27399; HSZP3.
DR RefSeq; NP_594683.1; NM_001020112.2.
DR RefSeq; NP_595567.1; NM_001021462.2.
DR RefSeq; NP_596467.1; NM_001022386.2.
DR PDB; 2DZE; X-ray; 1.80 A; X=123-132.
DR PDB; 3G7L; X-ray; 2.20 A; P=2-17.
DR PDBsum; 2DZE; -.
DR PDBsum; 3G7L; -.
DR AlphaFoldDB; P09988; -.
DR SMR; P09988; -.
DR BioGRID; 276354; 38.
DR BioGRID; 277734; 48.
DR BioGRID; 278928; 48.
DR IntAct; P09988; 1.
DR MINT; P09988; -.
DR STRING; 4896.SPAC1834.04.1; -.
DR iPTMnet; P09988; -.
DR MaxQB; P09988; -.
DR PaxDb; P09988; -.
DR PRIDE; P09988; -.
DR EnsemblFungi; SPAC1834.04.1; SPAC1834.04.1:pep; SPAC1834.04.
DR EnsemblFungi; SPBC1105.11c.1; SPBC1105.11c.1:pep; SPBC1105.11c.
DR EnsemblFungi; SPBC8D2.04.1; SPBC8D2.04.1:pep; SPBC8D2.04.
DR GeneID; 2539804; -.
DR GeneID; 2541220; -.
DR GeneID; 2542467; -.
DR KEGG; spo:SPAC1834.04; -.
DR KEGG; spo:SPBC1105.11c; -.
DR KEGG; spo:SPBC8D2.04; -.
DR PomBase; SPAC1834.04; hht1.
DR PomBase; SPBC8D2.04; hht2.
DR VEuPathDB; FungiDB:SPAC1834.04; -.
DR VEuPathDB; FungiDB:SPBC1105.11c; -.
DR VEuPathDB; FungiDB:SPBC8D2.04; -.
DR eggNOG; KOG1745; Eukaryota.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; P09988; -.
DR OMA; HIVMART; -.
DR PhylomeDB; P09988; -.
DR Reactome; R-SPO-212300; PRC2 methylates histones and DNA.
DR Reactome; R-SPO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SPO-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-SPO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-SPO-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR Reactome; R-SPO-983231; Factors involved in megakaryocyte development and platelet production.
DR EvolutionaryTrace; P09988; -.
DR PRO; PR:P09988; -.
DR Proteomes; UP000002485; Chromosome I.
DR Proteomes; UP000002485; Chromosome II.
DR ExpressionAtlas; P09988; differential.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0000786; C:nucleosome; ISM:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; ISM:PomBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IMP:PomBase.
DR GO; GO:0006334; P:nucleosome assembly; NAS:PomBase.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; DNA-binding; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H3.1/H3.2"
FT /id="PRO_0000221366"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11283354"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16087749"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3G7L"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2DZE"
SQ SEQUENCE 136 AA; 15357 MW; 346976EDD06C2284 CRC64;
MARTKQTARK STGGKAPRKQ LASKAARKAA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAI GALQEAVEAY LVSLFEDTNL CAIHGKRVTI
QPKDMQLARR LRGERS
