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   24-JAN-2024, entry version 156.
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; 10090-ENSMUSP00000020283; -.
DR   PeptideAtlas; Q8CCK0; -.
DR   ProteomicsDB; 270914; -.
DR   Pumba; Q8CCK0; -.
DR   Antibodypedia; 28963; 402 antibodies from 24 providers.
DR   DNASU; 404634; -.
DR   Ensembl; ENSMUST00000020283.5; ENSMUSP00000020283.5; ENSMUSG00000020086.7.
DR   GeneID; 404634; -.
DR   KEGG; mmu:404634; -.
DR   UCSC; uc007fgm.1; mouse.
DR   AGR; MGI:3037658; -.
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; LVLGQKX; -.
DR   OrthoDB; 235643at2759; -.
DR   PhylomeDB; Q8CCK0; -.
DR   TreeFam; TF332276; -.
DR   BioGRID-ORCS; 404634; 2 hits in 78 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 223 other cell types or tissues.
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: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: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   GO; GO:0007549; P:sex-chromosome dosage compensation; ISO:MGI.
DR   CDD; cd00074; H2A; 1.
DR   CDD; cd02904; Macro_H2A-like; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 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:SF37; CORE HISTONE MACRO-H2A.2; 1.
DR   PANTHER; PTHR23430; HISTONE H2A; 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; Histone-fold; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   PROSITE; PS51154; MACRO; 1.
DR   Genevisible; Q8CCK0; MM.
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
//