ID A0A2K5MP24_CERAT Unreviewed; 371 AA.
AC A0A2K5MP24;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Core histone macro-H2A {ECO:0000256|PIRNR:PIRNR037942};
GN Name=MACROH2A1 {ECO:0000313|Ensembl:ENSCATP00000026951.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000026951.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000026951.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes. {ECO:0000256|PIRNR:PIRNR037942}.
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. {ECO:0000256|PIRNR:PIRNR037942}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037942}.
CC Chromosome {ECO:0000256|PIRNR:PIRNR037942}.
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DR RefSeq; XP_011945704.1; XM_012090314.1.
DR AlphaFoldDB; A0A2K5MP24; -.
DR SMR; A0A2K5MP24; -.
DR STRING; 9531.ENSCATP00000026951; -.
DR Ensembl; ENSCATT00000051193.1; ENSCATP00000026951.1; ENSCATG00000036866.1.
DR GeneID; 105599793; -.
DR GeneTree; ENSGT00940000159541; -.
DR OrthoDB; 235643at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000036866; Expressed in lung and 12 other cell types or tissues.
DR GO; GO:0001740; C:Barr body; IEA:Ensembl.
DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0090734; C:site of DNA damage; IEA:Ensembl.
DR GO; GO:0160002; F:ADP-D-ribose modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IEA:Ensembl.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:Ensembl.
DR GO; GO:0000182; F:rDNA binding; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; IEA:Ensembl.
DR GO; GO:1902750; P:negative regulation of cell cycle G2/M phase transition; IEA:Ensembl.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IEA:Ensembl.
DR GO; GO:1904815; P:negative regulation of protein localization to chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1901837; P:negative regulation of transcription of nucleolar large rRNA by RNA polymerase I; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IEA:UniProtKB-UniRule.
DR GO; GO:1903226; P:positive regulation of endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; IEA:Ensembl.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR GO; GO:1902688; P:regulation of NAD metabolic process; IEA:Ensembl.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IEA:Ensembl.
DR GO; GO:1902882; P:regulation of response to oxidative stress; IEA:Ensembl.
DR GO; GO:0007549; P:sex-chromosome dosage compensation; IEA:Ensembl.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:Ensembl.
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:SF20; CORE HISTONE MACRO-H2A.1; 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.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR037942}; Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037942};
KW Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW ECO:0000256|PIRNR:PIRNR037942}; Nucleus {ECO:0000256|PIRNR:PIRNR037942};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 183..369
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 128..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037942-1"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR037942-1"
SQ SEQUENCE 371 AA; 39489 MW; 54320BFD118454D1 CRC64;
MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS
KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK QGEVSKAASA DSTTEGTPAD
GFTVLSTKSL FLGQKLNLIH SEISNLAGFE VEAIINPTNA DIDLKDDLGN TLEKKGGKEF
VEAVLELRKK NGPLEVAGAA VSAGHGLPAK FVIHCNSPVW GADKCEELLE KTVKNCLALA
DDKKLKSIAF PSIGSGRNGF PKQTAAQLIL KAISSYFVST MSSSIKTVYF VLFDSESIGI
YVQEMAKLDA N
//
