UniProtKB - Q8CGP1 (H2B1K_MOUSE)
Histone H2B type 1-K
H2bc12
Functioni
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
GO - Molecular functioni
- DNA binding Source: GO_Central
- protein heterodimerization activity Source: InterPro
GO - Biological processi
- nucleosome assembly Source: GO_Central
Keywordsi
Molecular function | DNA-binding |
Enzyme and pathway databases
Reactomei | R-MMU-110330, Recognition and association of DNA glycosylase with site containing an affected purine R-MMU-110331, Cleavage of the damaged purine R-MMU-212300, PRC2 methylates histones and DNA R-MMU-2299718, Condensation of Prophase Chromosomes R-MMU-2559580, Oxidative Stress Induced Senescence R-MMU-2559582, Senescence-Associated Secretory Phenotype (SASP) R-MMU-2559586, DNA Damage/Telomere Stress Induced Senescence R-MMU-3214815, HDACs deacetylate histones R-MMU-3214847, HATs acetylate histones R-MMU-427359, SIRT1 negatively regulates rRNA expression R-MMU-427413, NoRC negatively regulates rRNA expression R-MMU-5250924, B-WICH complex positively regulates rRNA expression R-MMU-5578749, Transcriptional regulation by small RNAs R-MMU-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 R-MMU-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks R-MMU-5693571, Nonhomologous End-Joining (NHEJ) R-MMU-5693607, Processing of DNA double-strand break ends R-MMU-606279, Deposition of new CENPA-containing nucleosomes at the centromere R-MMU-68616, Assembly of the ORC complex at the origin of replication R-MMU-69473, G2/M DNA damage checkpoint R-MMU-73728, RNA Polymerase I Promoter Opening R-MMU-73772, RNA Polymerase I Promoter Escape R-MMU-8866654, E3 ubiquitin ligases ubiquitinate target proteins R-MMU-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-MMU-9018519, Estrogen-dependent gene expression R-MMU-9670095, Inhibition of DNA recombination at telomere |
Names & Taxonomyi
Protein namesi | Recommended name: Histone H2B type 1-K |
Gene namesi | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:2448399, H2bc12 |
VEuPathDBi | HostDB:ENSMUSG00000062727 |
Subcellular locationi
Nucleus
Other locations
Cytosol
- cytosol Source: MGI
Nucleus
- nucleoplasm Source: MGI
- nucleus Source: MGI
Other locations
- nucleosome Source: UniProtKB-KW
Keywords - Cellular componenti
Chromosome, Nucleosome core, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000244833 | 2 – 126 | Histone H2B type 1-KAdd BLAST | 125 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylprolineBy similarity | 1 | |
Modified residuei | 6 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 6 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 6 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 6 | N6-butyryllysine; alternateBy similarity | 1 | |
Modified residuei | 6 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 6 | N6-lactoyllysine; alternate1 Publication | 1 | |
Cross-linki | 6 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 12 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 12 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 12 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 12 | N6-lactoyllysine; alternate1 Publication | 1 | |
Modified residuei | 13 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 13 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 13 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 15 | Phosphoserine; by STK4/MST12 Publications | 1 | |
Modified residuei | 16 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 16 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 16 | N6-lactoyllysine; alternate1 Publication | 1 | |
Modified residuei | 17 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 17 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 17 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 17 | N6-lactoyllysine; alternate1 Publication | 1 | |
Modified residuei | 21 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 21 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 21 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 21 | N6-butyryllysine; alternateBy similarity | 1 | |
Modified residuei | 21 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 21 | N6-lactoyllysine; alternate1 Publication | 1 | |
Cross-linki | 21 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 24 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 24 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 24 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 25 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 35 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 35 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 35 | N6-crotonyllysine; alternate1 Publication | 1 | |
Modified residuei | 35 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 35 | N6-succinyllysine; alternateBy similarity | 1 | |
Cross-linki | 35 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 37 | Phosphoserine; by AMPK1 Publication | 1 | |
Modified residuei | 44 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 44 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 44 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 47 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 47 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 47 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 58 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 58 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 80 | Dimethylated arginineBy similarity | 1 | |
Modified residuei | 86 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 86 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 86 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 86 | N6-lactoyllysine; alternate1 Publication | 1 | |
Modified residuei | 87 | Omega-N-methylarginineBy similarity | 1 | |
Modified residuei | 93 | Omega-N-methylarginineBy similarity | 1 | |
Modified residuei | 109 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 109 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 109 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 109 | N6-lactoyllysine; alternate1 Publication | 1 | |
Modified residuei | 109 | N6-methyllysine; alternateBy similarity | 1 | |
Glycosylationi | 113 | O-linked (GlcNAc) serineBy similarity | 1 | |
Modified residuei | 116 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 117 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 117 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 117 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 117 | N6-lactoyllysine; alternate1 Publication | 1 | |
Modified residuei | 117 | N6-methylated lysine; alternateBy similarity | 1 | |
Modified residuei | 117 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 121 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 121 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 121 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 121 | N6-succinyllysine; alternate1 Publication | 1 | |
Cross-linki | 121 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity |
Post-translational modificationi
Keywords - PTMi
Acetylation, Glycoprotein, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
jPOSTi | Q8CGP1 |
MaxQBi | Q8CGP1 |
PaxDbi | Q8CGP1 |
PRIDEi | Q8CGP1 |
PTM databases
GlyGeni | Q8CGP1, 1 site |
iPTMneti | Q8CGP1 |
PhosphoSitePlusi | Q8CGP1 |
SwissPalmi | Q8CGP1 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000062727, Expressed in hindbrain and 67 other tissues |
Genevisiblei | Q8CGP1, MM |
Interactioni
Subunit structurei
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
GO - Molecular functioni
- protein heterodimerization activity Source: InterPro
Protein-protein interaction databases
BioGRIDi | 235103, 2 interactors |
STRINGi | 10090.ENSMUSP00000106085 |
Miscellaneous databases
RNActi | Q8CGP1, protein |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 36 | DisorderedSequence analysisAdd BLAST | 36 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 17 – 35 | Basic residuesSequence analysisAdd BLAST | 19 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1744, Eukaryota |
GeneTreei | ENSGT01040000240467 |
HOGENOMi | CLU_075666_2_1_1 |
InParanoidi | Q8CGP1 |
OrthoDBi | 1536672at2759 |
PhylomeDBi | Q8CGP1 |
TreeFami | TF300212 |
Family and domain databases
Gene3Di | 1.10.20.10, 1 hit |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR007125, Histone_H2A/H2B/H3 IPR000558, Histone_H2B |
PANTHERi | PTHR23428, PTHR23428, 1 hit |
Pfami | View protein in Pfam PF00125, Histone, 1 hit |
PRINTSi | PR00621, HISTONEH2B |
SMARTi | View protein in SMART SM00427, H2B, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00357, HISTONE_H2B, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH
60 70 80 90 100
PDTGISSKAM GIMNSFVNDI FERIASEASR LAHYNKRSTI TSREIQTAVR
110 120
LLLPGELAKH AVSEGTKAVT KYTSAK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY158931 Genomic DNA Translation: AAO06241.1 AL590614 Genomic DNA No translation available. |
CCDSi | CCDS26305.1 |
RefSeqi | NP_783596.1, NM_175665.2 |
Genome annotation databases
Ensembli | ENSMUST00000110455; ENSMUSP00000106085; ENSMUSG00000062727 |
GeneIDi | 319184 |
KEGGi | mmu:319184 |
UCSCi | uc007psb.2, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY158931 Genomic DNA Translation: AAO06241.1 AL590614 Genomic DNA No translation available. |
CCDSi | CCDS26305.1 |
RefSeqi | NP_783596.1, NM_175665.2 |
3D structure databases
AlphaFoldDBi | Q8CGP1 |
SMRi | Q8CGP1 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 235103, 2 interactors |
STRINGi | 10090.ENSMUSP00000106085 |
PTM databases
GlyGeni | Q8CGP1, 1 site |
iPTMneti | Q8CGP1 |
PhosphoSitePlusi | Q8CGP1 |
SwissPalmi | Q8CGP1 |
Proteomic databases
jPOSTi | Q8CGP1 |
MaxQBi | Q8CGP1 |
PaxDbi | Q8CGP1 |
PRIDEi | Q8CGP1 |
Protocols and materials databases
DNASUi | 319184 |
Genome annotation databases
Ensembli | ENSMUST00000110455; ENSMUSP00000106085; ENSMUSG00000062727 |
GeneIDi | 319184 |
KEGGi | mmu:319184 |
UCSCi | uc007psb.2, mouse |
Organism-specific databases
CTDi | 85236 |
MGIi | MGI:2448399, H2bc12 |
VEuPathDBi | HostDB:ENSMUSG00000062727 |
Phylogenomic databases
eggNOGi | KOG1744, Eukaryota |
GeneTreei | ENSGT01040000240467 |
HOGENOMi | CLU_075666_2_1_1 |
InParanoidi | Q8CGP1 |
OrthoDBi | 1536672at2759 |
PhylomeDBi | Q8CGP1 |
TreeFami | TF300212 |
Enzyme and pathway databases
Reactomei | R-MMU-110330, Recognition and association of DNA glycosylase with site containing an affected purine R-MMU-110331, Cleavage of the damaged purine R-MMU-212300, PRC2 methylates histones and DNA R-MMU-2299718, Condensation of Prophase Chromosomes R-MMU-2559580, Oxidative Stress Induced Senescence R-MMU-2559582, Senescence-Associated Secretory Phenotype (SASP) R-MMU-2559586, DNA Damage/Telomere Stress Induced Senescence R-MMU-3214815, HDACs deacetylate histones R-MMU-3214847, HATs acetylate histones R-MMU-427359, SIRT1 negatively regulates rRNA expression R-MMU-427413, NoRC negatively regulates rRNA expression R-MMU-5250924, B-WICH complex positively regulates rRNA expression R-MMU-5578749, Transcriptional regulation by small RNAs R-MMU-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 R-MMU-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks R-MMU-5693571, Nonhomologous End-Joining (NHEJ) R-MMU-5693607, Processing of DNA double-strand break ends R-MMU-606279, Deposition of new CENPA-containing nucleosomes at the centromere R-MMU-68616, Assembly of the ORC complex at the origin of replication R-MMU-69473, G2/M DNA damage checkpoint R-MMU-73728, RNA Polymerase I Promoter Opening R-MMU-73772, RNA Polymerase I Promoter Escape R-MMU-8866654, E3 ubiquitin ligases ubiquitinate target proteins R-MMU-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-MMU-9018519, Estrogen-dependent gene expression R-MMU-9670095, Inhibition of DNA recombination at telomere |
Miscellaneous databases
BioGRID-ORCSi | 319184, 4 hits in 32 CRISPR screens |
PROi | PR:Q8CGP1 |
RNActi | Q8CGP1, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000062727, Expressed in hindbrain and 67 other tissues |
Genevisiblei | Q8CGP1, MM |
Family and domain databases
Gene3Di | 1.10.20.10, 1 hit |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR007125, Histone_H2A/H2B/H3 IPR000558, Histone_H2B |
PANTHERi | PTHR23428, PTHR23428, 1 hit |
Pfami | View protein in Pfam PF00125, Histone, 1 hit |
PRINTSi | PR00621, HISTONEH2B |
SMARTi | View protein in SMART SM00427, H2B, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00357, HISTONE_H2B, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | H2B1K_MOUSE | |
Accessioni | Q8CGP1Primary (citable) accession number: Q8CGP1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 11, 2006 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 146 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families