Hist2h2ab

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
Inferred from biological aspect of ancestorⁱ
- 21873635
protein heterodimerization activity Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

chromatin organization
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding

Molecular function

DNA-binding

Enzyme and pathway databases

Reactomeⁱ	R-MMU-3214815 HDACs deacetylate histones R-MMU-3214847 HATs acetylate 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

Reactomeⁱ

R-MMU-3214815 HDACs deacetylate histones
R-MMU-3214847 HATs acetylate 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-B Alternative name(s): H2a-613A
Gene namesⁱ	Name:Hist2h2ab
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 3

Organism-specific databases

MGIⁱ	MGI:2448314 Hist2h2ab

Keywords - Cellular componentⁱ

Chromosome, Nucleosome core, Nucleus

PTM / 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	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-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	120	N6-(beta-hydroxybutyryl)lysine; alternate1 Publication	1
Modified residueⁱ	120	N6-crotonyllysine; 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, TRIM27 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

Keywords - PTMⁱ

Acetylation, Citrullination, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q64522
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q64522
PaxDbⁱ	Q64522
PeptideAtlas More...PeptideAtlasⁱ	Q64522
PRIDEⁱ	Q64522
TopDownProteomicsⁱ	Q64522

PTM databases

iPTMnetⁱ	Q64522
PhosphoSitePlusⁱ	Q64522
SwissPalmⁱ	Q64522

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000063689 Expressed in 25 organ(s), highest expression level in bone marrow
CleanExⁱ	MM_HIST2H2AB

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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	548803, 3 interactors
IntActⁱ	Q64522, 1 interactor
STRINGⁱ	10090.ENSMUSP00000072858

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q64522
SMRⁱ	Q64522
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1756 Eukaryota COG5262 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00910000143981
HOGENOMⁱ	HOG000234652
HOVERGENⁱ	HBG009342
InParanoidⁱ	Q64522
KEGG Orthology (KO) More...KOⁱ	K11251
OMAⁱ	HAYLYSA
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0XGD
PhylomeDBⁱ	Q64522
TreeFamⁱ	TF300137

Family and domain databases

Conserved Domains Database More...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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

Q64522-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:130

Mass (Da):14,013

Last modified:January 23, 2007 - v3

Checksum:ⁱECE2F541F53F5FD7

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U62673 Genomic DNA Translation: AAB04767.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS38553.1
NCBI Reference Sequences More...RefSeqⁱ	NP_835585.3, NM_178213.4

Genome annotation databases

Ensemblⁱ	ENSMUST00000073115; ENSMUSP00000072858; ENSMUSG00000063689
GeneIDⁱ	621893
KEGGⁱ	mmu:621893
UCSC genome browser More...UCSCⁱ	uc008qmh.2 mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q64522	Histone H2A		NEOLE		144	UniRef100_Q64522
Histone H2A		MYOBR		130
Histone H2A		LEPWE		130
Histone H2A		DIPOR		130

Protein	Similar proteins		Species	Score	Length	Source
Q64522	Histone H2A		NEOLE		144	UniRef90_Q64522
Histone H2A		MYOBR		130
Histone H2A		LEPWE		130
Histone H2A		DIPOR		130
Histone H2A		PELSI		158
+1

Protein	Similar proteins		Species	Score	Length	Source
Q64522	Histone H2A type 1-C	)	HUMAN		130	UniRef50_Q93077
Histone H2A type 1-C		RAT		130
Histone H2A.Z		SCHPO		139
Histone H2A		MAGO7		136
Histone H2A		MAGOY		136
+1234

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

ProteinModelPortalⁱ	Q64522
SMRⁱ	Q64522
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	548803, 3 interactors
IntActⁱ	Q64522, 1 interactor
STRINGⁱ	10090.ENSMUSP00000072858

PTM databases

iPTMnetⁱ	Q64522
PhosphoSitePlusⁱ	Q64522
SwissPalmⁱ	Q64522

Proteomic databases

EPDⁱ	Q64522
MaxQBⁱ	Q64522
PaxDbⁱ	Q64522
PeptideAtlasⁱ	Q64522
PRIDEⁱ	Q64522
TopDownProteomicsⁱ	Q64522

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000073115; ENSMUSP00000072858; ENSMUSG00000063689
GeneIDⁱ	621893
KEGGⁱ	mmu:621893
UCSCⁱ	uc008qmh.2 mouse

Organism-specific databases

CTDⁱ	317772
MGIⁱ	MGI:2448314 Hist2h2ab

Phylogenomic databases

eggNOGⁱ	KOG1756 Eukaryota COG5262 LUCA
GeneTreeⁱ	ENSGT00910000143981
HOGENOMⁱ	HOG000234652
HOVERGENⁱ	HBG009342
InParanoidⁱ	Q64522
KOⁱ	K11251
OMAⁱ	HAYLYSA
OrthoDBⁱ	EOG091G0XGD
PhylomeDBⁱ	Q64522
TreeFamⁱ	TF300137

Enzyme and pathway databases

Reactomeⁱ	R-MMU-3214815 HDACs deacetylate histones R-MMU-3214847 HATs acetylate 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

Reactomeⁱ

R-MMU-3214815 HDACs deacetylate histones
R-MMU-3214847 HATs acetylate 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

Protein Ontology More...PROⁱ	PR:Q64522
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000063689 Expressed in 25 organ(s), highest expression level in bone marrow
CleanExⁱ	MM_HIST2H2AB

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...

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:	November 7, 2018
	This is version 149 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

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

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Supporting data

UniProtKB - Q64522 (H2A2B_MOUSE)

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Histone H2A type 2-B

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ