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UniProtKB - C0HKE4 (H2A1E_MOUSE)

Entry version 19 (13 Nov 2019)
Sequence version 1 (10 May 2017)
Previous versions | rss
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Protein

Histone H2A type 1-E

Gene

H2ac8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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.

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...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-171306 Packaging Of Telomere Ends
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
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-3214858 RMTs methylate histone arginines
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-5689603 UCH proteinases
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689901 Metalloprotease DUBs
R-MMU-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-MMU-73728 RNA Polymerase I Promoter Opening
R-MMU-73772 RNA Polymerase I Promoter Escape
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-9018519 Estrogen-dependent gene expression

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone H2A type 1-ECurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:H2ac8Imported
Synonyms:Hist1h2aeImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:2448290 H2ac8

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004397182 – 130Histone H2A type 1-EAdd BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine1 Publication1
Modified residuei2Phosphoserine; by RPS6KA51 Publication1
Modified residuei4Citrulline; alternateBy similarity1
Modified residuei4Symmetric dimethylarginine; by PRMT5; alternate1 Publication1
Modified residuei6N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei6N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei6N6-acetyllysine; alternate1 Publication1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-succinyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei37N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei37N6-crotonyllysine; alternate1 Publication1
Modified residuei75N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei76N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei96N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei96N6-glutaryllysine; alternateBy similarity1
Modified residuei96N6-succinyllysine; alternateBy similarity1
Modified residuei105N5-methylglutamine1 Publication1
Modified residuei119N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei119N6-crotonyllysine; alternate1 Publication1
Modified residuei119N6-glutaryllysine; alternateBy similarity1
Modified residuei120N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei120N6-crotonyllysine; alternateBy similarity1
Modified residuei120N6-glutaryllysine; alternateBy similarity1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
Modified residuei121Phosphothreonine; by DCAF1By similarity1
Modified residuei126N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei126N6-crotonyllysine; alternateBy similarity1
Modified residuei126N6-glutaryllysine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 similarity1 Publication
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.1 Publication
Hydroxybutyrylation of histones is induced by starvation.1 Publication

Keywords - PTMi

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

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		C0HKE4

PRoteomics IDEntifications database

More...PRIDEi		C0HKE4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		C0HKE4

<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

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		C0HKE4 baseline and differential

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

Complete GO annotation on QuickGO ...

<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

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		C0HKE4

Database of comparative protein structure models

More...ModBasei		Search...

<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

Belongs to the histone H2A family.Curated

Phylogenomic databases

KEGG Orthology (KO)

More...KOi		K11251

Identification of Orthologs from Complete Genome Data

More...OMAi		RSHKPET

Database of Orthologous Groups

More...OrthoDBi		1504122at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd00074 H2A, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00620 HISTONEH2A

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00414 H2A, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47113 SSF47113, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00046 HISTONE_H2A, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

C0HKE4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV 
        60         70         80         90        100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR 
       110        120        130
VTIAQGGVLP NIQAVLLPKK TESHHKAKGK
Length:130
Mass (Da):14,135
Last modified:May 10, 2017 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9CFE6184B2CC89F5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AY158917 Genomic DNA Translation: AAO06227.1
AK028026 mRNA Translation: BAC25706.1
AL592149 Genomic DNA Translation: CAI24893.1
BC058544 mRNA Translation: AAH58544.1
BC076498 mRNA Translation: AAH76498.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS26348.1

NCBI Reference Sequences

More...RefSeqi		NP_001171015.1, NM_001177544.2
NP_783591.2, NM_175660.3
NP_835489.1, NM_178182.2
NP_835491.1, NM_178184.2
NP_835492.1, NM_178185.2
NP_835493.1, NM_178186.3
NP_835494.1, NM_178187.4
NP_835495.1, NM_178188.4
NP_835496.1, NM_178189.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000070124; ENSMUSP00000088285; ENSMUSG00000071516
ENSMUST00000078369; ENSMUSP00000077477; ENSMUSG00000061615
ENSMUST00000081342; ENSMUSP00000080088; ENSMUSG00000094777
ENSMUST00000090776; ENSMUSP00000088281; ENSMUSG00000071478
ENSMUST00000091741; ENSMUSP00000089335; ENSMUSG00000069301
ENSMUST00000091745; ENSMUSP00000089339; ENSMUSG00000094248
ENSMUST00000091751; ENSMUSP00000089345; ENSMUSG00000069309
ENSMUST00000102969; ENSMUSP00000100034; ENSMUSG00000069272
ENSMUST00000171127; ENSMUSP00000127684; ENSMUSG00000069270

Database of genes from NCBI RefSeq genomes

More...GeneIDi		319164
319165
319166
319167
319170
319171
319172
319191
665433

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:319164
mmu:319165
mmu:319166
mmu:319167
mmu:319170
mmu:319171
mmu:319172
mmu:319191
mmu:665433

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY158917 Genomic DNA Translation: AAO06227.1
AK028026 mRNA Translation: BAC25706.1
AL592149 Genomic DNA Translation: CAI24893.1
BC058544 mRNA Translation: AAH58544.1
BC076498 mRNA Translation: AAH76498.1
CCDSiCCDS26348.1
RefSeqiNP_001171015.1, NM_001177544.2
NP_783591.2, NM_175660.3
NP_835489.1, NM_178182.2
NP_835491.1, NM_178184.2
NP_835492.1, NM_178185.2
NP_835493.1, NM_178186.3
NP_835494.1, NM_178187.4
NP_835495.1, NM_178188.4
NP_835496.1, NM_178189.5

3D structure databases

SMRiC0HKE4
ModBaseiSearch...

PTM databases

iPTMnetiC0HKE4

Proteomic databases

jPOSTiC0HKE4
PRIDEiC0HKE4

Genome annotation databases

EnsembliENSMUST00000070124; ENSMUSP00000088285; ENSMUSG00000071516
ENSMUST00000078369; ENSMUSP00000077477; ENSMUSG00000061615
ENSMUST00000081342; ENSMUSP00000080088; ENSMUSG00000094777
ENSMUST00000090776; ENSMUSP00000088281; ENSMUSG00000071478
ENSMUST00000091741; ENSMUSP00000089335; ENSMUSG00000069301
ENSMUST00000091745; ENSMUSP00000089339; ENSMUSG00000094248
ENSMUST00000091751; ENSMUSP00000089345; ENSMUSG00000069309
ENSMUST00000102969; ENSMUSP00000100034; ENSMUSG00000069272
ENSMUST00000171127; ENSMUSP00000127684; ENSMUSG00000069270
GeneIDi319164
319165
319166
319167
319170
319171
319172
319191
665433
KEGGimmu:319164
mmu:319165
mmu:319166
mmu:319167
mmu:319170
mmu:319171
mmu:319172
mmu:319191
mmu:665433

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3012
3013
319170
319171
665433
8329
8334
8335
8969
MGIiMGI:2448290 H2ac8

Phylogenomic databases

KOiK11251
OMAiRSHKPET
OrthoDBi1504122at2759

Enzyme and pathway databases

ReactomeiR-MMU-110330 Recognition and association of DNA glycosylase with site containing an affected purine
R-MMU-110331 Cleavage of the damaged purine
R-MMU-171306 Packaging Of Telomere Ends
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
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-3214858 RMTs methylate histone arginines
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-5689603 UCH proteinases
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689901 Metalloprotease DUBs
R-MMU-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-MMU-73728 RNA Polymerase I Promoter Opening
R-MMU-73772 RNA Polymerase I Promoter Escape
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-9018519 Estrogen-dependent gene expression

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Hist1h2ae mouse

Protein Ontology

More...PROi		PR:C0HKE4

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

ExpressionAtlasiC0HKE4 baseline and differential

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiH2A1E_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: C0HKE4
Secondary accession number(s): P10812
, P22752, Q149U0, Q5SZZ2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
Last sequence update: May 10, 2017
Last modified: November 13, 2019
This is version 19 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

Complete proteome, Reference proteome

Documents

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