H2B1A_RAT
ID H2B1A_RAT Reviewed; 127 AA.
AC Q00729; Q64677;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Histone H2B type 1-A;
DE AltName: Full=Histone H2B, testis;
DE AltName: Full=Testis-specific histone H2B;
GN Name=H2bc1 {ECO:0000312|RGD:3855};
GN Synonyms=Hist1h2ba {ECO:0000312|RGD:3855}, Th2b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=3666307; DOI=10.1016/0012-1606(87)90455-6;
RA Kim Y.-J., Hwang I., Tres L.L., Kierszenbaum A.L., Chae C.-B.;
RT "Molecular cloning and differential expression of somatic and testis-
RT specific H2B histone genes during rat spermatogenesis.";
RL Dev. Biol. 124:23-34(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=2011515; DOI=10.1093/nar/19.1.93;
RA Huh N.E., Hwang I., Lim K., You K.H., Chae C.-B.;
RT "Presence of a bi-directional S phase-specific transcription regulatory
RT element in the promoter shared by testis-specific TH2A and TH2B histone
RT genes.";
RL Nucleic Acids Res. 19:93-98(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=2725487; DOI=10.1128/mcb.9.3.1005-1013.1989;
RA Hwang I., Chae C.-B.;
RT "S-phase-specific transcription regulatory elements are present in a
RT replication-independent testis-specific H2B histone gene.";
RL Mol. Cell. Biol. 9:1005-1013(1989).
RN [4]
RP PROTEIN SEQUENCE OF 49-74 AND 102-110, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP ACETYLATION AT LYS-7; LYS-14; LYS-17 AND LYS-22.
RX PubMed=16283522; DOI=10.1007/s11010-005-8285-1;
RA Golebiowski F., Kasprzak K.S.;
RT "Inhibition of core histones acetylation by carcinogenic nickel(II).";
RL Mol. Cell. Biochem. 279:133-139(2005).
RN [6]
RP ACETYLATION AT LYS-14; LYS-17; LYS-18 AND LYS-22, METHYLATION AT LYS-118,
RP AND PHOSPHORYLATION AT THR-117.
RX PubMed=19346237; DOI=10.1093/molehr/gap028;
RA Lu S., Xie Y.M., Li X., Luo J., Shi X.Q., Hong X., Pan Y.H., Ma X.;
RT "Mass spectrometry analysis of dynamic post-translational modifications of
RT TH2B during spermatogenesis.";
RL Mol. Hum. Reprod. 15:373-378(2009).
CC -!- FUNCTION: Variant histone specifically required to direct the
CC transformation of dissociating nucleosomes to protamine in male germ
CC cells. Entirely replaces classical histone H2B prior nucleosome to
CC protamine transition and probably acts as a nucleosome dissociating
CC factor that creates a more dynamic chromatin, facilitating the large-
CC scale exchange of histones. Core component of nucleosome. Nucleosomes
CC wrap and compact DNA into chromatin, limiting DNA accessibility to the
CC cellular machineries which require DNA as a template. Histones thereby
CC play a central role in transcription regulation, DNA repair, DNA
CC replication and chromosomal stability. DNA accessibility is regulated
CC via a complex set of post-translational modifications of histones, also
CC called histone code, and nucleosome remodeling.
CC {ECO:0000250|UniProtKB:P70696}.
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. {ECO:0000250|UniProtKB:P70696}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P70696}.
CC Chromosome {ECO:0000250|UniProtKB:P70696}.
CC -!- TISSUE SPECIFICITY: Testis. Expressed in pachytene spermatocytes during
CC meiotic prophase I in the absence of any significant DNA synthesis.
CC {ECO:0000269|PubMed:2725487}.
CC -!- PTM: Monoubiquitination at Lys-36 by the MSL1/MSL2 dimer is required
CC for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and
CC transcription activation at specific gene loci, such as HOXA9 and MEIS1
CC loci. Similarly, monoubiquitination of Lys-122 (H2BK120Ub) by the
CC RNF20/40 complex gives a specific tag for epigenetic transcriptional
CC activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79'
CC methylation. It also functions cooperatively with the FACT dimer to
CC stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a
CC regulator of mRNA splicing: deubiquitination by USP49 is required for
CC efficient cotranscriptional splicing of a large set of exons (By
CC similarity). {ECO:0000250|UniProtKB:Q96A08}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes (By similarity).
CC {ECO:0000250|UniProtKB:P70696}.
CC -!- PTM: Acetylated during spermatogenesis. Acetylated form is most
CC abundant in spermatogonia compared to spermatocytes and round
CC spermatids. {ECO:0000269|PubMed:16283522, ECO:0000269|PubMed:19346237}.
CC -!- PTM: Phosphorylated at Thr-117 in spermatogonia, spermatocytes and
CC round spermatids. {ECO:0000269|PubMed:19346237}.
CC -!- PTM: Methylated at Lys-118 in spermatogonia, spermatocytes and round
CC spermatids. {ECO:0000269|PubMed:19346237}.
CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC directly derived from endogenous or exogenous lactate, leading to
CC stimulates gene transcription. {ECO:0000250|UniProtKB:P33778}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; M18045; AAA74755.1; -; mRNA.
DR EMBL; M18046; AAA74756.1; -; mRNA.
DR EMBL; X59962; CAA42587.1; -; Genomic_DNA.
DR EMBL; M25771; AAA74754.1; -; Genomic_DNA.
DR PIR; A45945; A45945.
DR PIR; S26187; S26187.
DR RefSeq; NP_072169.1; NM_022643.1.
DR AlphaFoldDB; Q00729; -.
DR SMR; Q00729; -.
DR STRING; 10116.ENSRNOP00000022630; -.
DR iPTMnet; Q00729; -.
DR PhosphoSitePlus; Q00729; -.
DR jPOST; Q00729; -.
DR PaxDb; Q00729; -.
DR PRIDE; Q00729; -.
DR GeneID; 24829; -.
DR KEGG; rno:24829; -.
DR UCSC; RGD:3855; rat.
DR CTD; 255626; -.
DR RGD; 3855; H2bc1.
DR VEuPathDB; HostDB:ENSRNOG00000069905; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; Q00729; -.
DR OMA; ELAKHAX; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; Q00729; -.
DR TreeFam; TF300212; -.
DR PRO; PR:Q00729; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000016865; Expressed in testis and 8 other tissues.
DR Genevisible; Q00729; RN.
DR GO; GO:0044815; C:DNA packaging complex; ISO:RGD.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0001674; C:female germ cell nucleus; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; ISO:RGD.
DR GO; GO:0051276; P:chromosome organization; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0071674; P:mononuclear cell migration; ISO:RGD.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0006337; P:nucleosome disassembly; ISS:UniProtKB.
DR GO; GO:0031639; P:plasminogen activation; ISO:RGD.
DR GO; GO:0051099; P:positive regulation of binding; ISO:RGD.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
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; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23527"
FT CHAIN 2..127
FT /note="Histone H2B type 1-A"
FT /id="PRO_0000071844"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P23527"
FT MOD_RES 7
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522"
FT MOD_RES 7
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P70696"
FT MOD_RES 7
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 13
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P70696"
FT MOD_RES 13
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 14
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522,
FT ECO:0000269|PubMed:19346237"
FT MOD_RES 14
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P70696"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522,
FT ECO:0000269|PubMed:19346237"
FT MOD_RES 17
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P70696"
FT MOD_RES 17
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 18
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19346237"
FT MOD_RES 18
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P70696"
FT MOD_RES 18
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 22
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522,
FT ECO:0000269|PubMed:19346237"
FT MOD_RES 22
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P70696"
FT MOD_RES 22
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 25
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 25
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P70696"
FT MOD_RES 25
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 36
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P70696"
FT MOD_RES 36
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 45
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 48
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 59
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 81
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 87
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 87
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 87
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 88
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 94
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 110
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 110
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19346237"
FT MOD_RES 118
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 118
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000269|PubMed:19346237"
FT MOD_RES 118
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 122
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P58876"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5QNW6"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT CONFLICT 36
FT /note="K -> E (in Ref. 1; AAA74755/AAA74756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 14225 MW; 14CE190F91769548 CRC64;
MPEVSAKGTT ISKKGFKKAV TKTQKKEGRK RKRCRKESYS IYIYKVLKQV HPDTGISSKA
MSIMNSFVTD IFERIAGEAS RLAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV
TKYTSSK
