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Protein

Histone H2A type 1-F

Gene

Hist1h2af

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A type 1-F
Gene namesi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2448309 Hist1h2af

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCurated
ChainiPRO_00002275022 – 130Histone H2A type 1-FAdd BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2Phosphoserine; by RPS6KA5By similarity1
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 residuei10N6-(2-hydroxyisobutyryl)lysine1 Publication1
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)lysine1 Publication1
Modified residuei105N5-methylglutamine1 Publication1
Modified residuei119N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei119N6-crotonyllysine; alternate1 Publication1
Modified residuei120N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei120N6-crotonyllysine; 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

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. 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.1 Publication
Hydroxybutyrylation of histones is induced by starvation.1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiQ8CGP5
MaxQBiQ8CGP5
PaxDbiQ8CGP5
PeptideAtlasiQ8CGP5
PRIDEiQ8CGP5
TopDownProteomicsiQ8CGP5

PTM databases

iPTMnetiQ8CGP5
PhosphoSitePlusiQ8CGP5

Expressioni

Gene expression databases

BgeeiENSMUSG00000061991
CleanExiMM_HIST1H2AF

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-protein interaction databases

BioGridi235092, 1 interactor
STRINGi10090.ENSMUSP00000072989

Structurei

3D structure databases

ProteinModelPortaliQ8CGP5
SMRiQ8CGP5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1756 Eukaryota
COG5262 LUCA
GeneTreeiENSGT00910000143981
HOGENOMiHOG000234652
HOVERGENiHBG009342
InParanoidiQ8CGP5
KOiK11251
OMAiDSSACWS
OrthoDBiEOG091G0XGD
PhylomeDBiQ8CGP5
TreeFamiTF300137

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

Sequencei

Sequence statusi: Complete.

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

Q8CGP5-1 [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 TESHHKPKGK
Length:130
Mass (Da):14,162
Last modified:January 23, 2007 - v3
Checksum:i9CFE619E02CC89F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY158916 Genomic DNA Translation: AAO06226.1
BC125011 mRNA Translation: AAI25012.1
CCDSiCCDS26341.1
RefSeqiNP_783592.1, NM_175661.2
UniGeneiMm.377878

Genome annotation databases

EnsembliENSMUST00000073261; ENSMUSP00000072989; ENSMUSG00000061991
GeneIDi319173
KEGGimmu:319173
UCSCiuc007ptw.2 mouse

Similar proteinsi

Entry informationi

Entry nameiH2A1F_MOUSE
AccessioniPrimary (citable) accession number: Q8CGP5
Secondary accession number(s): Q08AU5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 132 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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