H2AW_MOUSE
ID H2AW_MOUSE Reviewed; 372 AA.
AC Q8CCK0; A0JP36; Q3TNT4; Q925I6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Core histone macro-H2A.2;
DE Short=Histone macroH2A2;
DE Short=mH2A2;
GN Name=Macroh2a2 {ECO:0000312|MGI:MGI:3037658};
GN Synonyms=H2afy2 {ECO:0000312|MGI:MGI:3037658}, H2afy3;
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=11331621; DOI=10.1093/hmg/10.10.1101;
RA Chadwick B.P., Willard H.F.;
RT "Histone H2A variants and the inactive X chromosome: identification of a
RT second macroH2A variant.";
RL Hum. Mol. Genet. 10:1101-1113(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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 [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11262398; DOI=10.1074/jbc.m010919200;
RA Costanzi C., Pehrson J.R.;
RT "MACROH2A2, a new member of the MACROH2A core histone family.";
RL J. Biol. Chem. 276:21776-21784(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes where it represses transcription. Nucleosomes
CC wrap and compact DNA into chromatin, limiting DNA accessibility to the
CC cellular machineries which require DNA as a template. Histones thereby
CC play a central role in transcription regulation, DNA repair, DNA
CC replication and chromosomal stability. DNA accessibility is regulated
CC via a complex set of post-translational modifications of histones, also
CC called histone code, and nucleosome remodeling. May be involved in
CC stable X chromosome inactivation.
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.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11262398}. Chromosome
CC {ECO:0000269|PubMed:11262398}. Note=Enriched in inactive X chromosome
CC chromatin and in senescence-associated heterochromatin.
CC -!- TISSUE SPECIFICITY: Present in liver, kidney and adrenal gland (at
CC protein level). In the liver, present in cells of the bile ducts and
CC parenchymal cells, but not in hepatocytes. In the kidney, present in
CC proximal and distal convoluted tubules and in glomeruli. Present at
CC highest levels in the parietal layer of Bowman capsule. In the adrenal
CC gland, present in the outer cells of the capsule.
CC {ECO:0000269|PubMed:11262398}.
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DR EMBL; AF336305; AAK52472.1; -; mRNA.
DR EMBL; AK032636; BAC27963.1; -; mRNA.
DR EMBL; AK165020; BAE38003.1; -; mRNA.
DR EMBL; BC045140; AAH45140.1; -; mRNA.
DR EMBL; BC046794; AAH46794.1; -; mRNA.
DR EMBL; BC107279; AAI07280.1; -; mRNA.
DR EMBL; BC107280; AAI07281.1; -; mRNA.
DR EMBL; BC127144; AAI27145.1; -; mRNA.
DR CCDS; CCDS23885.1; -.
DR RefSeq; NP_996883.1; NM_207000.2.
DR AlphaFoldDB; Q8CCK0; -.
DR SMR; Q8CCK0; -.
DR BioGRID; 240403; 2.
DR IntAct; Q8CCK0; 4.
DR MINT; Q8CCK0; -.
DR STRING; 10090.ENSMUSP00000020283; -.
DR iPTMnet; Q8CCK0; -.
DR PhosphoSitePlus; Q8CCK0; -.
DR CPTAC; non-CPTAC-3795; -.
DR MaxQB; Q8CCK0; -.
DR PaxDb; Q8CCK0; -.
DR PeptideAtlas; Q8CCK0; -.
DR PRIDE; Q8CCK0; -.
DR ProteomicsDB; 270914; -.
DR Antibodypedia; 28963; 356 antibodies from 24 providers.
DR DNASU; 404634; -.
DR Ensembl; ENSMUST00000020283; ENSMUSP00000020283; ENSMUSG00000020086.
DR GeneID; 404634; -.
DR KEGG; mmu:404634; -.
DR UCSC; uc007fgm.1; mouse.
DR CTD; 55506; -.
DR MGI; MGI:3037658; Macroh2a2.
DR VEuPathDB; HostDB:ENSMUSG00000020086; -.
DR eggNOG; KOG1756; Eukaryota.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000158120; -.
DR HOGENOM; CLU_062828_0_0_1; -.
DR InParanoid; Q8CCK0; -.
DR OMA; FPKQMAA; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; Q8CCK0; -.
DR TreeFam; TF332276; -.
DR BioGRID-ORCS; 404634; 2 hits in 72 CRISPR screens.
DR ChiTaRS; H2afy2; mouse.
DR PRO; PR:Q8CCK0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8CCK0; protein.
DR Bgee; ENSMUSG00000020086; Expressed in undifferentiated genital tubercle and 220 other tissues.
DR Genevisible; Q8CCK0; MM.
DR GO; GO:0001740; C:Barr body; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0007549; P:dosage compensation; ISO:MGI.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; ISO:MGI.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:1901837; P:negative regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:MGI.
DR CDD; cd00074; H2A; 1.
DR CDD; cd02904; Macro_H2A-like; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR021171; Core_histone_macro-H2A.
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; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR035796; Macro_H2A.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR Pfam; PF01661; Macro; 1.
DR PIRSF; PIRSF037942; Core_histone_macro-H2A; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00506; A1pp; 1.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; DNA-binding; Isopeptide bond;
KW Nucleosome core; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..372
FT /note="Core histone macro-H2A.2"
FT /id="PRO_0000227906"
FT DOMAIN 2..117
FT /note="Histone H2A"
FT DOMAIN 184..370
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 114..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 9
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P0M6"
FT CONFLICT 90
FT /note="E -> D (in Ref. 2; BAC27963)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="K -> E (in Ref. 2; BAE38003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40092 MW; 471E3CDCE28F4A1D CRC64;
MSGRSGKKKM SKLSRSARAG VIFPVGRLMR YLKKGTFKYR ISVGAPVYMA AVIEYLAAEI
LELAGNAARD NKKARIAPRH ILLAVANDEE LNQLLKGVTI ASGGVLPRIH PELLAKKRGT
KGKSETILSP PPEKRGRKAA SGKKGGKKSK ATKPRTSKKS KAKDSDKEGT SNSTSEDGPG
DGFTILSSKS LVLGQKLSLT QSDISHIGSM RVEGIVHPTT AEIDLKEEIG KALEKAGGKE
FLETVKELRK SQGPLEVAEA AVSQSSGLAA KFVIHCHIPQ WGSDKCEEQL EETIKNCLSA
AEDKKLKSVA FPPFPSGRNC FPKQTAAQVT LKAISAHFDD SSSSSLKNVY FLLFDSESIG
IYVQEMAKLD TK
