H2AJ_HUMAN
ID H2AJ_HUMAN Reviewed; 129 AA.
AC Q9BTM1; Q9NV63;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Histone H2A.J;
DE Short=H2a/j;
GN Name=H2AJ {ECO:0000312|HGNC:HGNC:14456};
GN Synonyms=H2AFJ {ECO:0000312|HGNC:HGNC:14456};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovarian carcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BTM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTM1-2; Sequence=VSP_034750;
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: 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 -!- 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 -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; AK001765; BAA91894.1; -; mRNA.
DR EMBL; CH471094; EAW96326.1; -; Genomic_DNA.
DR EMBL; BC003602; AAH03602.1; -; mRNA.
DR CCDS; CCDS31752.1; -. [Q9BTM1-1]
DR RefSeq; NP_808760.1; NM_177925.3. [Q9BTM1-1]
DR PDB; 4EDU; X-ray; 2.58 A; T=31-46.
DR PDB; 6K60; X-ray; 3.15 A; C/G=78-86.
DR PDB; 6KVD; X-ray; 2.21 A; C/G=1-129.
DR PDBsum; 4EDU; -.
DR PDBsum; 6K60; -.
DR PDBsum; 6KVD; -.
DR AlphaFoldDB; Q9BTM1; -.
DR SMR; Q9BTM1; -.
DR BioGRID; 120884; 228.
DR IntAct; Q9BTM1; 21.
DR MINT; Q9BTM1; -.
DR STRING; 9606.ENSP00000438553; -.
DR iPTMnet; Q9BTM1; -.
DR PhosphoSitePlus; Q9BTM1; -.
DR SwissPalm; Q9BTM1; -.
DR BioMuta; H2AFJ; -.
DR DMDM; 74733131; -.
DR EPD; Q9BTM1; -.
DR jPOST; Q9BTM1; -.
DR MassIVE; Q9BTM1; -.
DR MaxQB; Q9BTM1; -.
DR PaxDb; Q9BTM1; -.
DR PeptideAtlas; Q9BTM1; -.
DR PRIDE; Q9BTM1; -.
DR ProteomicsDB; 78997; -. [Q9BTM1-1]
DR ProteomicsDB; 78998; -. [Q9BTM1-2]
DR TopDownProteomics; Q9BTM1-1; -. [Q9BTM1-1]
DR Antibodypedia; 54929; 134 antibodies from 14 providers.
DR DNASU; 55766; -.
DR Ensembl; ENST00000389078.3; ENSP00000373730.3; ENSG00000246705.5. [Q9BTM1-1]
DR Ensembl; ENST00000544848.3; ENSP00000438553.1; ENSG00000246705.5. [Q9BTM1-1]
DR GeneID; 55766; -.
DR KEGG; hsa:55766; -.
DR MANE-Select; ENST00000544848.3; ENSP00000438553.1; NM_177925.5; NP_808760.1.
DR UCSC; uc009zia.4; human. [Q9BTM1-1]
DR CTD; 55766; -.
DR DisGeNET; 55766; -.
DR GeneCards; H2AJ; -.
DR HGNC; HGNC:14456; H2AJ.
DR HPA; ENSG00000246705; Tissue enhanced (testis).
DR neXtProt; NX_Q9BTM1; -.
DR OpenTargets; ENSG00000246705; -.
DR VEuPathDB; HostDB:ENSG00000246705; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000153118; -.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; Q9BTM1; -.
DR OMA; RTEGKHE; -.
DR PhylomeDB; Q9BTM1; -.
DR TreeFam; TF300137; -.
DR PathwayCommons; Q9BTM1; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-HSA-110331; Cleavage of the damaged purine.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-171306; Packaging Of Telomere Ends.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-5334118; DNA methylation.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-912446; Meiotic recombination.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR SignaLink; Q9BTM1; -.
DR SIGNOR; Q9BTM1; -.
DR BioGRID-ORCS; 55766; 203 hits in 1069 CRISPR screens.
DR GeneWiki; H2AFJ; -.
DR GenomeRNAi; 55766; -.
DR Pharos; Q9BTM1; Tbio.
DR PRO; PR:Q9BTM1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BTM1; protein.
DR Bgee; ENSG00000246705; Expressed in left testis and 179 other tissues.
DR ExpressionAtlas; Q9BTM1; baseline and differential.
DR Genevisible; Q9BTM1; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome; DNA-binding;
KW Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; 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_0000344247"
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"
FT VAR_SEQ 119..129
FT /note="KKTESQKTKSK -> VCEHSGPSSGKIPSDRAELGAGSVCGHIFQKVE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034750"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:6KVD"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:6KVD"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6KVD"
FT HELIX 48..73
FT /evidence="ECO:0007829|PDB:6KVD"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6KVD"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:6KVD"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:6KVD"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6KVD"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6KVD"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6KVD"
SQ SEQUENCE 129 AA; 14019 MW; E35049617B456D45 CRC64;
MSGRGKQGGK VRAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
TESQKTKSK
