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H2B1_RAT
ID   H2B1_RAT                Reviewed;         125 AA.
AC   Q00715;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Histone H2B type 1;
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 [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [3]
RP   PROTEIN SEQUENCE OF 36-44; 48-73 AND 100-108, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
RN   [4]
RP   ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
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).
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   -!- FUNCTION: Has broad antibacterial activity. May contribute to the
CC       formation of the functional antimicrobial barrier of the colonic
CC       epithelium, and to the bactericidal activity of amniotic fluid (By
CC       similarity). {ECO:0000250}.
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. Chromosome.
CC   -!- PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is
CC       required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me)
CC       methylation and transcription activation at specific gene loci, such as
CC       HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-120
CC       (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic
CC       transcriptional activation and is also prerequisite for histone H3
CC       'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with
CC       the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub
CC       also acts as a regulator of mRNA splicing: deubiquitination by USP49 is
CC       required for efficient cotranscriptional splicing of a large set of
CC       exons (By similarity). {ECO:0000250|UniProtKB:P33778}.
CC   -!- PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis;
CC       which facilitates apoptotic chromatin condensation. Also phosphorylated
CC       on Ser-15 in response to DNA double strand breaks (DSBs), and in
CC       correlation with somatic hypermutation and immunoglobulin class-switch
CC       recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response
CC       to stress promotes transcription (By similarity).
CC       {ECO:0000250|UniProtKB:P33778, ECO:0000250|UniProtKB:Q64475}.
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:P33778}.
CC   -!- PTM: GlcNAcylation at Ser-112 promotes monoubiquitination of Lys-120.
CC       It fluctuates in response to extracellular glucose, and associates with
CC       transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.
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; X59961; CAA42585.1; -; Genomic_DNA.
DR   PIR; B45945; B45945.
DR   PIR; S26185; S26185.
DR   RefSeq; NP_072173.1; NM_022647.1.
DR   AlphaFoldDB; Q00715; -.
DR   SMR; Q00715; -.
DR   BioGRID; 249180; 5.
DR   IntAct; Q00715; 3.
DR   MINT; Q00715; -.
DR   STRING; 10116.ENSRNOP00000028779; -.
DR   CarbonylDB; Q00715; -.
DR   GlyGen; Q00715; 1 site.
DR   iPTMnet; Q00715; -.
DR   PhosphoSitePlus; Q00715; -.
DR   jPOST; Q00715; -.
DR   PaxDb; Q00715; -.
DR   PRIDE; Q00715; -.
DR   GeneID; 64647; -.
DR   KEGG; rno:64647; -.
DR   UCSC; RGD:621439; rat.
DR   CTD; 64647; -.
DR   eggNOG; KOG1744; Eukaryota.
DR   OrthoDB; 1536672at2759; -.
DR   PhylomeDB; Q00715; -.
DR   PRO; PR:Q00715; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; Antibiotic; Antimicrobial; Chromosome;
KW   Direct protein sequencing; DNA-binding; Glycoprotein; Hydroxylation;
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..125
FT                   /note="Histone H2B type 1"
FT                   /id="PRO_0000071841"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..36
FT                   /note="Basic and acidic 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         6
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         6
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64475"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16283522"
FT   MOD_RES         6
FT                   /note="N6-butyryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         6
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         6
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         12
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64475"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   MOD_RES         12
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         12
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         13
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         13
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16283522"
FT   MOD_RES         13
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         15
FT                   /note="Phosphoserine; by STK4/MST1"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16283522"
FT   MOD_RES         16
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         16
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         17
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         17
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         17
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         21
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         21
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64475"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16283522"
FT   MOD_RES         21
FT                   /note="N6-butyryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         21
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         21
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         24
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         24
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         24
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         25
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         35
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         35
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64475"
FT   MOD_RES         35
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         35
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         35
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         37
FT                   /note="Phosphoserine; by AMPK"
FT                   /evidence="ECO:0000250|UniProtKB:Q64475"
FT   MOD_RES         44
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         44
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         44
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         47
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         47
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         47
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   MOD_RES         58
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   MOD_RES         58
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         79
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         85
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         85
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         85
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         85
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         86
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         92
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         108
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         108
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         108
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         108
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   MOD_RES         115
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00729"
FT   MOD_RES         116
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         116
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64475"
FT   MOD_RES         116
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         116
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         116
FT                   /note="N6-methylated lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00729"
FT   MOD_RES         116
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         120
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         120
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         120
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         120
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   CARBOHYD        112
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   CROSSLNK        6
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P58876"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5QNW6"
FT   CROSSLNK        35
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   CROSSLNK        120
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62808"
SQ   SEQUENCE   125 AA;  13990 MW;  43BF1F86A6DA221A CRC64;
     MPEPAKSRPA PKKGSKKAVT KAQKKDGKER KRSRKESYSV YVYKVLKQVH PDTGISSKAM
     GIMNSFVNDI FERIAGERRL AHYNKRSTIT SREIQTAVRL LLPGELAKHA VSEGTKAVTK
     YTSSK
 
 
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