ID   H2AJ_MOUSE              Reviewed;         129 AA.
AC   Q8R1M2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Histone H2A.J;
DE            Short=H2a/j;
GN   Name=H2aj {ECO:0000312|MGI:MGI:3606192};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
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).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-10, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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; AK053755; BAC35508.1; -; mRNA.
DR   EMBL; BC024397; AAH24397.1; -; mRNA.
DR   EMBL; BC099606; AAH99606.1; -; mRNA.
DR   CCDS; CCDS20654.1; -.
DR   RefSeq; NP_808356.1; NM_177688.4.
DR   AlphaFoldDB; Q8R1M2; -.
DR   SMR; Q8R1M2; -.
DR   BioGRID; 231262; 2.
DR   IntAct; Q8R1M2; 2.
DR   STRING; 10090.ENSMUSP00000074142; -.
DR   GlyGen; Q8R1M2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8R1M2; -.
DR   PhosphoSitePlus; Q8R1M2; -.
DR   SwissPalm; Q8R1M2; -.
DR   jPOST; Q8R1M2; -.
DR   MaxQB; Q8R1M2; -.
DR   PaxDb; 10090-ENSMUSP00000074142; -.
DR   PeptideAtlas; Q8R1M2; -.
DR   TopDownProteomics; Q8R1M2; -.
DR   Antibodypedia; 54929; 153 antibodies from 14 providers.
DR   DNASU; 232440; -.
DR   Ensembl; ENSMUST00000074556.7; ENSMUSP00000074142.5; ENSMUSG00000060032.7.
DR   GeneID; 232440; -.
DR   KEGG; mmu:232440; -.
DR   UCSC; uc009eme.1; mouse.
DR   AGR; MGI:3606192; -.
DR   CTD; 55766; -.
DR   MGI; MGI:3606192; H2aj.
DR   VEuPathDB; HostDB:ENSMUSG00000060032; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   GeneTree; ENSGT00940000153118; -.
DR   HOGENOM; CLU_062828_3_1_1; -.
DR   InParanoid; Q8R1M2; -.
DR   OMA; HINWSIN; -.
DR   OrthoDB; 235643at2759; -.
DR   PhylomeDB; Q8R1M2; -.
DR   TreeFam; TF300137; -.
DR   Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   BioGRID-ORCS; 232440; 6 hits in 80 CRISPR screens.
DR   ChiTaRS; H2afj; mouse.
DR   PRO; PR:Q8R1M2; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q8R1M2; Protein.
DR   Bgee; ENSMUSG00000060032; Expressed in paneth cell and 244 other cell types or tissues.
DR   ExpressionAtlas; Q8R1M2; baseline and differential.
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; Histone, subunit A; 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; HISTONE H2A; 1.
DR   PANTHER; PTHR23430:SF28; HISTONE H2A TYPE 1-C; 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; Histone-fold; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
DR   Genevisible; Q8R1M2; MM.
PE   1: Evidence at protein 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_0000344249"
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:0007744|PubMed:23806337"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
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
//