ID H2A1_SCHPO Reviewed; 132 AA.
AC P04909;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 174.
DE RecName: Full=Histone H2A-alpha;
DE AltName: Full=H2A.1;
GN Name=hta1; ORFNames=SPCC622.08c;
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 FUNCTION, MUTAGENESIS OF SER-129, AND PHOSPHORYLATION AT SER-129.
RX PubMed=15226425; DOI=10.1128/mcb.24.14.6215-6230.2004;
RA Nakamura T.M., Du L.-L., Redon C., Russell P.;
RT "Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks,
RT maintains checkpoint arrest, and influences DNA repair in fission yeast.";
RL Mol. Cell. Biol. 24:6215-6230(2004).
RN [5]
RP METHYLATION AT GLN-106.
RX PubMed=24352239; DOI=10.1038/nature12819;
RA Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J.,
RA Nielsen M.L., Kouzarides T.;
RT "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
RT modification.";
RL Nature 505:564-568(2014).
RN [6]
RP INTERACTION WITH MDB1, PHOSPHORYLATION AT SER-129, AND MUTAGENESIS OF
RP SER-129.
RX PubMed=24806815; DOI=10.1371/journal.pone.0097028;
RA Wei Y., Wang H.T., Zhai Y., Russell P., Du L.L.;
RT "Mdb1, a fission yeast homolog of human MDC1, modulates DNA damage response
RT and mitotic spindle function.";
RL PLoS ONE 9:E97028-E97028(2014).
CC -!- FUNCTION: Core component of nucleosome which plays a central role in
CC DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA
CC into chromatin, limiting DNA accessibility to the cellular machineries
CC which require DNA as a template. Histones thereby play a central role
CC in transcription regulation, DNA repair, DNA replication and
CC chromosomal stability. DNA accessibility is regulated via a complex set
CC of post-translational modifications of histones, also called histone
CC code, and nucleosome remodeling. {ECO:0000269|PubMed:15226425}.
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 DNA
CC (By similarity). Interacts with mdb1 (via BRCT domain) in vitro; this
CC interaction requires phosphorylation of this protein at the S/T-Q motif
CC (PubMed:24806815). {ECO:0000250|UniProtKB:P68431,
CC ECO:0000269|PubMed:24806815}.
CC -!- INTERACTION:
CC P04909; Q10337: brc1; NbExp=4; IntAct=EBI-7764873, EBI-7764855;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC from the PI3/PI4-kinase family.
CC -!- PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA
CC double-strand breaks (DSBs) generated by exogenous genotoxic agents and
CC by stalled replication forks. Phosphorylation is dependent on the DNA
CC damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side
CC of a detected DSB site and may mark the surrounding chromatin for
CC recruitment of proteins required for DNA damage signaling and repair.
CC Gamma-H2A is required for recruiting crb2, a modulator of DNA damage
CC checkpoint signaling, to DSB sites. Gamma-H2A is removed from the DNA
CC prior to the strand invasion-primer extension step of the repair
CC process and subsequently dephosphorylated. Dephosphorylation is
CC necessary for efficient recovery from the DNA damage checkpoint.
CC {ECO:0000269|PubMed:15226425}.
CC -!- PTM: Acetylated by esa1 to form H2AK4ac and H2AK7ac. {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast to vertebrates and insects, its C-terminus
CC is not monoubiquitinated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histone H2A 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: H2AK4ac =
CC acetylated Lys-5; H2AK7ac = acetylated Lys-9; H2AS128ph =
CC phosphorylated Ser-129. {ECO:0000305}.
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DR EMBL; M11494; AAA35311.1; -; Genomic_DNA.
DR EMBL; X05220; CAA28848.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21864.1; -; Genomic_DNA.
DR PIR; B27399; HSZPA2.
DR RefSeq; NP_588180.1; NM_001023170.2.
DR AlphaFoldDB; P04909; -.
DR SMR; P04909; -.
DR BioGRID; 276062; 72.
DR IntAct; P04909; 1.
DR MINT; P04909; -.
DR STRING; 284812.P04909; -.
DR iPTMnet; P04909; -.
DR MaxQB; P04909; -.
DR PaxDb; 4896-SPCC622-08c-1; -.
DR EnsemblFungi; SPCC622.08c.1; SPCC622.08c.1:pep; SPCC622.08c.
DR GeneID; 2539499; -.
DR KEGG; spo:SPCC622.08c; -.
DR PomBase; SPCC622.08c; hta1.
DR VEuPathDB; FungiDB:SPCC622.08c; -.
DR eggNOG; KOG1756; Eukaryota.
DR HOGENOM; CLU_062828_3_0_1; -.
DR InParanoid; P04909; -.
DR OMA; RRNICHA; -.
DR PhylomeDB; P04909; -.
DR Reactome; R-SPO-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-SPO-3214858; RMTs methylate histone arginines.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR PRO; PR:P04909; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0000786; C:nucleosome; ISM:PomBase.
DR GO; GO:0005634; C:nucleus; IC:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase.
DR GO; GO:0140463; F:chromatin-protein adaptor activity; IMP:PomBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; NAS:PomBase.
DR GO; GO:0006302; P:double-strand break repair; EXP:PomBase.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:PomBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:PomBase.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IDA:PomBase.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR032458; Histone_H2A_CS.
DR PANTHER; PTHR23430; HISTONE H2A; 1.
DR PANTHER; PTHR23430:SF50; HISTONE H2A; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..132
FT /note="Histone H2A-alpha"
FT /id="PRO_0000055324"
FT MOTIF 129..130
FT /note="[ST]-Q motif"
FT SITE 120
FT /note="Not ubiquitinated"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 106
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:24352239"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15226425,
FT ECO:0000269|PubMed:24806815"
FT MUTAGEN 129
FT /note="S->A: Causes hypersensitivity to DNA-damage-inducing
FT agents and impairs recruitment of crb2 to DSB sites. Loss
FT of interaction with mdb1."
FT /evidence="ECO:0000269|PubMed:15226425,
FT ECO:0000269|PubMed:24806815"
FT CONFLICT 124
FT /note="R -> G (in Ref. 1; AAA35311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 132 AA; 13878 MW; D1F5C136916AC273 CRC64;
MSGGKSGGKA AVAKSAQSRS AKAGLAFPVG RVHRLLRKGN YAQRVGAGAP VYLAAVLEYL
AAEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKLLG HVTIAQGGVV PNINAHLLPK
TSGRTGKPSQ EL
//
