H2AJ_MACFA
ID H2AJ_MACFA Reviewed; 129 AA.
AC Q4R3X5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Histone H2A.J;
DE Short=H2a/j;
GN Name=H2AJ {ECO:0000250|UniProtKB:Q9BTM1}; ORFNames=QtsA-13532;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AB179140; BAE02191.1; -; mRNA.
DR AlphaFoldDB; Q4R3X5; -.
DR SMR; Q4R3X5; -.
DR STRING; 9541.XP_005542099.1; -.
DR Ensembl; ENSMFAT00000100811; ENSMFAP00000047518; ENSMFAG00000060261.
DR VEuPathDB; HostDB:ENSMFAG00000016754; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000153118; -.
DR OMA; RTEGKHE; -.
DR Proteomes; UP000233100; Chromosome 11.
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; IEA:UniProtKB-KW.
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_0000344248"
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; 13989 MW; E350497D0B456D45 CRC64;
MSGRGKQGGK VRAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
TESQKAKSK