H2B1_SCHPO
ID H2B1_SCHPO Reviewed; 126 AA.
AC P04913;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Histone H2B-alpha;
DE AltName: Full=H2B.1;
GN Name=htb1; ORFNames=SPCC622.09;
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=3018512; DOI=10.1128/mcb.5.11.3261-3269.1985;
RA Choe J., Schuster T., Grunstein M.;
RT "Organization, primary structure, and evolution of histone H2A and H2B
RT genes of the fission yeast Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 5:3261-3269(1985).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH RIK1.
RX PubMed=16024659; DOI=10.1101/gad.1328005;
RA Horn P.J., Bastie J.-N., Peterson C.L.;
RT "A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for
RT heterochromatin formation.";
RL Genes Dev. 19:1705-1714(2005).
RN [5]
RP MUTAGENESIS OF GLU-35; GLY-53; PRO-103 AND LYS-120, AND UBIQUITINATION AT
RP LYS-120.
RX PubMed=16688222; DOI=10.1038/sj.emboj.7601110;
RA Maruyama T., Nakamura T., Hayashi T., Yanagida M.;
RT "Histone H2B mutations in inner region affect ubiquitination, centromere
RT function, silencing and chromosome segregation.";
RL EMBO J. 25:2420-2431(2006).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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. Interacts with rik1. {ECO:0000269|PubMed:16024659}.
CC -!- INTERACTION:
CC P04913; Q10426: rik1; NbExp=2; IntAct=EBI-1112091, EBI-1111936;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Chromosome
CC {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Monoubiquitinated by the rhp6/ubc2-bre1 complex to form
CC H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic
CC transcriptional activation and is also prerequisite for H3K4me and
CC H3K79me formation. H2BK123ub1 also modulates the formation of double-
CC strand breaks during meiosis and is a prerequisite for DNA-damage
CC checkpoint activation (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by shk1 to form H2BS10ph during progression through
CC meiotic prophase. May be correlated with chromosome condensation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylation of N-terminal lysines and particularly formation of
CC H2BK11ac has a positive effect on transcription. {ECO:0000250}.
CC -!- PTM: Sumoylation to form H2BK6su or H2BK7su occurs preferentially near
CC the telomeres and represses gene transcription. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2B 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: H2BK6ac =
CC acetylated Lys-6; H2BK6su = sumoylated Lys-6; H2BK7ac = acetylated Lys-
CC 7; H2BK7su = sumoylated Lys-7; H2BS10ph = phosphorylated Ser-10;
CC H2BK11ac = acetylated Lys-11; H2BK123ub1 = monoubiquitinated Lys-120.
CC {ECO:0000305}.
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DR EMBL; M11494; AAA35312.1; -; Genomic_DNA.
DR EMBL; X05220; CAA28847.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21865.1; -; Genomic_DNA.
DR PIR; A27399; HSZPB2.
DR RefSeq; NP_588181.1; NM_001023171.2.
DR AlphaFoldDB; P04913; -.
DR SMR; P04913; -.
DR BioGRID; 276085; 37.
DR IntAct; P04913; 1.
DR STRING; 4896.SPCC622.09.1; -.
DR iPTMnet; P04913; -.
DR SwissPalm; P04913; -.
DR MaxQB; P04913; -.
DR PaxDb; P04913; -.
DR PRIDE; P04913; -.
DR EnsemblFungi; SPCC622.09.1; SPCC622.09.1:pep; SPCC622.09.
DR GeneID; 2539523; -.
DR KEGG; spo:SPCC622.09; -.
DR PomBase; SPCC622.09; htb1.
DR VEuPathDB; FungiDB:SPCC622.09; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; P04913; -.
DR OMA; DIFDRMA; -.
DR PhylomeDB; P04913; -.
DR Reactome; R-SPO-212300; PRC2 methylates histones and DNA.
DR Reactome; R-SPO-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-SPO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SPO-3214815; HDACs deacetylate histones.
DR Reactome; R-SPO-3214847; HATs acetylate histones.
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-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
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 PRO; PR:P04913; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000786; C:nucleosome; ISM:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; 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:0006334; P:nucleosome assembly; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; PTHR23428; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..126
FT /note="Histone H2B-alpha"
FT /id="PRO_0000071937"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 7
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16688222"
FT MUTAGEN 35
FT /note="E->K: In HTB1-442; impairs growth at 36 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:16688222"
FT MUTAGEN 53
FT /note="G->D: In HTB1-72; impairs growth at 36 degrees
FT Celsius, leads to chromosome missegregetion, chromatin
FT shrinkage, and diminished chromatin silencing."
FT /evidence="ECO:0000269|PubMed:16688222"
FT MUTAGEN 103
FT /note="P->L: In HTB1-223; impairs growth at 36 degrees
FT Celsius, leads to chromosome missegregetion, chromatin
FT shrinkage, histone H2B deubiquitination and diminished
FT chromatin silencing."
FT /evidence="ECO:0000269|PubMed:16688222"
FT MUTAGEN 120
FT /note="K->R: Impairs ubiquitination."
FT /evidence="ECO:0000269|PubMed:16688222"
FT CONFLICT 43
FT /note="K -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="R -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 126 AA; 13819 MW; 64A02B9AFE7414E3 CRC64;
MSAAEKKPAS KAPAGKAPRD TMKSADKKRG KNRKETYSSY IYKVLKQVHP DTGISNQAMR
ILNSFVNDIF ERIATEASKL AAYNKKSTIS SREIQTAVRL ILPGELAKHA VTEGTKSVTK
YSSSAQ
