H2AJ_RAT
ID H2AJ_RAT Reviewed; 129 AA.
AC A9UMV8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Histone H2A.J;
DE Short=H2a/j;
GN Name=H2aj {ECO:0000312|RGD:1592176};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Monoubiquitination of Lys-120 (H2AXK119ub) gives a specific tag
CC for epigenetic transcriptional repression. Following DNA double-strand
CC breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of
CC ubiquitin moieties (By similarity). {ECO:0000250}.
CC -!- PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is
CC specifically dedicated to polymerase I. It is present at 35S ribosomal
CC DNA locus and impairs binding of the FACT complex (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis.
CC Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses
CC transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by
CC RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is
CC present in the regulatory region of many tumor suppresor genes and
CC down-regulates their transcription (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH473964; EDM01605.1; -; Genomic_DNA.
DR EMBL; BC157816; AAI57817.1; -; mRNA.
DR RefSeq; NP_001103080.1; NM_001109610.2.
DR RefSeq; XP_008761669.1; XM_008763447.2.
DR AlphaFoldDB; A9UMV8; -.
DR SMR; A9UMV8; -.
DR BioGRID; 605606; 1.
DR IntAct; A9UMV8; 1.
DR MINT; A9UMV8; -.
DR STRING; 10116.ENSRNOP00000044986; -.
DR iPTMnet; A9UMV8; -.
DR PhosphoSitePlus; A9UMV8; -.
DR jPOST; A9UMV8; -.
DR PaxDb; A9UMV8; -.
DR PeptideAtlas; A9UMV8; -.
DR PRIDE; A9UMV8; -.
DR GeneID; 690795; -.
DR KEGG; rno:690795; -.
DR UCSC; RGD:1592176; rat.
DR CTD; 55766; -.
DR RGD; 1592176; H2aj.
DR VEuPathDB; HostDB:ENSRNOG00000045819; -.
DR eggNOG; KOG1756; Eukaryota.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; A9UMV8; -.
DR OMA; PKKTEIC; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; A9UMV8; -.
DR TreeFam; TF300137; -.
DR Reactome; R-RNO-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-RNO-110331; Cleavage of the damaged purine.
DR Reactome; R-RNO-171306; Packaging Of Telomere Ends.
DR Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-RNO-212300; PRC2 methylates histones and DNA.
DR Reactome; R-RNO-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-RNO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-RNO-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-RNO-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-RNO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-RNO-5689901; Metalloprotease DUBs.
DR Reactome; R-RNO-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-RNO-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-RNO-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR Reactome; R-RNO-9670095; Inhibition of DNA recombination at telomere.
DR PRO; PR:A9UMV8; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Proteomes; UP000234681; Chromosome 4.
DR Bgee; ENSRNOG00000033045; Expressed in duodenum and 19 other tissues.
DR Genevisible; A9UMV8; RN.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR032458; Histone_H2A_CS.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..129
FT /note="Histone H2A.J"
FT /id="PRO_0000344250"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1M2"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1M2"
FT MOD_RES 10
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 105
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 121
FT /note="Phosphothreonine; by DCAF1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 129 AA; 14045 MW; E35049621B5DFCCC CRC64;
MSGRGKQGGK VRAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR VTIAQGGVLP NIQAVLLPKK
TESQKVKSK
