UniProtKB - Q64522 (H2A2B_MOUSE)
Protein
Histone H2A type 2-B
Gene
H2ac21
Organism
Mus musculus (Mouse)
Status
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
- chromatin organization Source: GO_Central
- chromatin silencing Source: GO_Central
Keywordsi
Molecular function | DNA-binding |
Enzyme and pathway databases
Reactomei | R-MMU-3214815, HDACs deacetylate histones R-MMU-3214858, RMTs methylate histone arginines R-MMU-5689603, UCH proteinases R-MMU-5689880, Ub-specific processing proteases R-MMU-5689901, Metalloprotease DUBs |
Names & Taxonomyi
Protein namesi | Recommended name: Histone H2A type 2-BAlternative name(s): H2A-clustered histone 21Imported H2a-613A |
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:2448314, H2ac21 |
Subcellular locationi
Nucleus
Other locations
Nucleus
- nuclear chromatin Source: GO_Central
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_0000227506 | 2 – 130 | Histone H2A type 2-BAdd BLAST | 129 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineBy similarity | 1 | |
Modified residuei | 2 | Phosphoserine; by RPS6KA5By similarity | 1 | |
Modified residuei | 4 | Citrulline; alternateBy similarity | 1 | |
Modified residuei | 4 | Symmetric dimethylarginine; by PRMT5; alternate1 Publication | 1 | |
Modified residuei | 6 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 6 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 10 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 10 | N6-succinyllysine; alternateBy similarity | 1 | |
Cross-linki | 14 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 16 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 37 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 37 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 37 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 75 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 76 | N6-(2-hydroxyisobutyryl)lysine1 Publication | 1 | |
Modified residuei | 96 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 96 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 96 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 105 | N5-methylglutamine1 Publication | 1 | |
Modified residuei | 119 | N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 119 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 119 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 120 | N6-(beta-hydroxybutyryl)lysine; alternate1 Publication | 1 | |
Modified residuei | 120 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 120 | N6-glutaryllysine; alternateBy similarity | 1 | |
Cross-linki | 120 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications | ||
Modified residuei | 121 | Phosphothreonine; by DCAF1By similarity | 1 |
Post-translational modificationi
Deiminated on Arg-4 in granulocytes upon calcium entry.By similarity
Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.By similarity3 Publications
Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription.By similarity
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.1 Publication
Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex.1 Publication
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.By similarity
Hydroxybutyrylation of histones is induced by starvation.1 Publication
Keywords - PTMi
Acetylation, Citrullination, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | Q64522 |
jPOSTi | Q64522 |
MaxQBi | Q64522 |
PaxDbi | Q64522 |
PeptideAtlasi | Q64522 |
PRIDEi | Q64522 |
TopDownProteomicsi | Q64522 |
PTM databases
iPTMneti | Q64522 |
PhosphoSitePlusi | Q64522 |
SwissPalmi | Q64522 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000063689, Expressed in undifferentiated genital tubercle and 54 other tissues |
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 | 548803, 6 interactors |
IntActi | Q64522, 2 interactors |
STRINGi | 10090.ENSMUSP00000072858 |
Miscellaneous databases
RNActi | Q64522, protein |
Family & Domainsi
Sequence similaritiesi
Belongs to the histone H2A family.Curated
Phylogenomic databases
eggNOGi | KOG1756, Eukaryota |
GeneTreei | ENSGT00940000153118 |
HOGENOMi | CLU_062828_3_1_1 |
InParanoidi | Q64522 |
OMAi | CLCGFLR |
OrthoDBi | 1504122at2759 |
PhylomeDBi | Q64522 |
TreeFami | TF300137 |
Family and domain databases
CDDi | cd00074, H2A, 1 hit |
Gene3Di | 1.10.20.10, 1 hit |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR002119, Histone_H2A IPR007125, Histone_H2A/H2B/H3 IPR032454, Histone_H2A_C IPR032458, Histone_H2A_CS |
Pfami | View protein in Pfam PF00125, Histone, 1 hit PF16211, Histone_H2A_C, 1 hit |
PRINTSi | PR00620, HISTONEH2A |
SMARTi | View protein in SMART SM00414, H2A, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00046, HISTONE_H2A, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q64522-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV
60 70 80 90 100
YMAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG
110 120 130
VTIAQGGVLP NIQAVLLPKK TESHKPGKNK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U62673 Genomic DNA Translation: AAB04767.1 |
CCDSi | CCDS38553.1 |
RefSeqi | NP_835585.3, NM_178213.4 |
Genome annotation databases
Ensembli | ENSMUST00000073115; ENSMUSP00000072858; ENSMUSG00000063689 |
GeneIDi | 621893 |
KEGGi | mmu:621893 |
UCSCi | uc008qmh.2, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U62673 Genomic DNA Translation: AAB04767.1 |
CCDSi | CCDS38553.1 |
RefSeqi | NP_835585.3, NM_178213.4 |
3D structure databases
SMRi | Q64522 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 548803, 6 interactors |
IntActi | Q64522, 2 interactors |
STRINGi | 10090.ENSMUSP00000072858 |
PTM databases
iPTMneti | Q64522 |
PhosphoSitePlusi | Q64522 |
SwissPalmi | Q64522 |
Proteomic databases
EPDi | Q64522 |
jPOSTi | Q64522 |
MaxQBi | Q64522 |
PaxDbi | Q64522 |
PeptideAtlasi | Q64522 |
PRIDEi | Q64522 |
TopDownProteomicsi | Q64522 |
Protocols and materials databases
Antibodypediai | 68019, 52 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000073115; ENSMUSP00000072858; ENSMUSG00000063689 |
GeneIDi | 621893 |
KEGGi | mmu:621893 |
UCSCi | uc008qmh.2, mouse |
Organism-specific databases
CTDi | 317772 |
MGIi | MGI:2448314, H2ac21 |
Phylogenomic databases
eggNOGi | KOG1756, Eukaryota |
GeneTreei | ENSGT00940000153118 |
HOGENOMi | CLU_062828_3_1_1 |
InParanoidi | Q64522 |
OMAi | CLCGFLR |
OrthoDBi | 1504122at2759 |
PhylomeDBi | Q64522 |
TreeFami | TF300137 |
Enzyme and pathway databases
Reactomei | R-MMU-3214815, HDACs deacetylate histones R-MMU-3214858, RMTs methylate histone arginines R-MMU-5689603, UCH proteinases R-MMU-5689880, Ub-specific processing proteases R-MMU-5689901, Metalloprotease DUBs |
Miscellaneous databases
BioGRID-ORCSi | 621893, 3 hits in 17 CRISPR screens |
PROi | PR:Q64522 |
RNActi | Q64522, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000063689, Expressed in undifferentiated genital tubercle and 54 other tissues |
Family and domain databases
CDDi | cd00074, H2A, 1 hit |
Gene3Di | 1.10.20.10, 1 hit |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR002119, Histone_H2A IPR007125, Histone_H2A/H2B/H3 IPR032454, Histone_H2A_C IPR032458, Histone_H2A_CS |
Pfami | View protein in Pfam PF00125, Histone, 1 hit PF16211, Histone_H2A_C, 1 hit |
PRINTSi | PR00620, HISTONEH2A |
SMARTi | View protein in SMART SM00414, H2A, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00046, HISTONE_H2A, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | H2A2B_MOUSE | |
Accessioni | Q64522Primary (citable) accession number: Q64522 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 7, 2006 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 163 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