GenomeNet

Database: UniProt
Entry: Q5XJK2_DANRE
LinkDB: Q5XJK2_DANRE
Original site: Q5XJK2_DANRE 
ID   Q5XJK2_DANRE            Unreviewed;       128 AA.
AC   Q5XJK2; B2GP66;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Histone H2A {ECO:0000256|RuleBase:RU003767};
GN   Name=h2ax1 {ECO:0000313|Ensembl:ENSDARP00000090794,
GN   ECO:0000313|RefSeq:NP_001005967.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-041010-42};
GN   ORFNames=zgc:101846 {ECO:0000313|EMBL:AAI64227.1,
GN   ECO:0000313|RefSeq:NP_001005967.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI64227.1};
RN   [1] {ECO:0000313|EMBL:AAI64227.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Larvae {ECO:0000313|EMBL:AAH83299.1}, and PCR rescue
RC   {ECO:0000313|EMBL:AAI64227.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000090794}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000090794};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000090794, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000090794};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000313|RefSeq:NP_001005967.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27189481;
RA   Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA   Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA   Bobe J.;
RT   "Gene evolution and gene expression after whole genome duplication in fish:
RT   the PhyloFish database.";
RL   BMC Genomics 17:368-368(2016).
RN   [5] {ECO:0000313|RefSeq:NP_001005967.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28223110;
RA   Kong X., Wu X., Pei C., Zhang J., Zhao X., Li L., Nie G., Li X.;
RT   "H2A and Ca-L-hipposin gene: Characteristic analysis and expression
RT   responses to Aeromonas hydrophila infection in Carassius aurutus.";
RL   Fish Shellfish Immunol. 63:344-352(2017).
RN   [6] {ECO:0000313|RefSeq:NP_001005967.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28252024;
RA   Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA   Choudhary J.S., Emes R.D., Grant S.G.;
RT   "Evolution of complexity in the zebrafish synapse proteome.";
RL   Nat. Commun. 8:14613-14613(2017).
RN   [7] {ECO:0000313|Ensembl:ENSDARP00000149636}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000149636};
RG   Ensembl;
RL   Submitted (APR-2018) to UniProtKB.
RN   [8] {ECO:0000313|RefSeq:NP_001005967.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU003767}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU003767}.
CC   -!- SIMILARITY: Belongs to the histone H2A family.
CC       {ECO:0000256|ARBA:ARBA00010691, ECO:0000256|RuleBase:RU003767}.
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; BX120005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC083299; AAH83299.1; -; mRNA.
DR   EMBL; BC164227; AAI64227.1; -; mRNA.
DR   RefSeq; NP_001005967.1; NM_001005967.1.
DR   STRING; 7955.ENSDARP00000090794; -.
DR   PaxDb; 7955-ENSDARP00000090794; -.
DR   Ensembl; ENSDART00000100022.5; ENSDARP00000090794.3; ENSDARG00000068995.5.
DR   Ensembl; ENSDART00000192552.1; ENSDARP00000149636.1; ENSDARG00000110429.1.
DR   GeneID; 449794; -.
DR   KEGG; dre:449794; -.
DR   AGR; ZFIN:ZDB-GENE-041010-42; -.
DR   CTD; 449794; -.
DR   ZFIN; ZDB-GENE-041010-42; h2ax1.
DR   eggNOG; KOG1756; Eukaryota.
DR   HOGENOM; CLU_062828_3_3_1; -.
DR   OMA; ELAHNTC; -.
DR   OrthoDB; 235643at2759; -.
DR   TreeFam; TF300137; -.
DR   Reactome; R-DRE-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR   Reactome; R-DRE-110331; Cleavage of the damaged purine.
DR   Reactome; R-DRE-171306; Packaging Of Telomere Ends.
DR   Reactome; R-DRE-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-DRE-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-DRE-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-DRE-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-DRE-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-DRE-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; R-DRE-3214815; HDACs deacetylate histones.
DR   Reactome; R-DRE-3214847; HATs acetylate histones.
DR   Reactome; R-DRE-3214858; RMTs methylate histone arginines.
DR   Reactome; R-DRE-427359; SIRT1 negatively regulates rRNA expression.
DR   Reactome; R-DRE-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-DRE-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-DRE-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-DRE-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   Reactome; R-DRE-5689603; UCH proteinases.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   Reactome; R-DRE-5689901; Metalloprotease DUBs.
DR   Reactome; R-DRE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-DRE-5693571; Nonhomologous End-Joining (NHEJ).
DR   Reactome; R-DRE-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-DRE-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   Reactome; R-DRE-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-DRE-69473; G2/M DNA damage checkpoint.
DR   Reactome; R-DRE-73728; RNA Polymerase I Promoter Opening.
DR   Reactome; R-DRE-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-DRE-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-DRE-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-DRE-9670095; Inhibition of DNA recombination at telomere.
DR   Proteomes; UP000000437; Alternate scaffold 10.
DR   Proteomes; UP000000437; Chromosome 10.
DR   Bgee; ENSDARG00000068995; Expressed in retina and 21 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; ISS:AgBase.
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   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:AgBase.
DR   GO; GO:0051673; P:disruption of plasma membrane integrity in another organism; ISS:AgBase.
DR   GO; GO:0045087; P:innate immune response; ISS:AgBase.
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:SF72; HISTONE H2A TYPE 2-B; 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.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU003767};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003767};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW   ECO:0000256|RuleBase:RU003767};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU003767};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          8..89
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   DOMAIN          92..126
FT                   /note="Histone H2A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16211"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   128 AA;  13731 MW;  8FF52164A8052D6D CRC64;
     MSGRGKTGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT
     AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG VTIAQGGVLP NIQAVLLPKK
     TEKPAKSK
//
DBGET integrated database retrieval system