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Database: UniProt
Entry: A0A2R9A926_PANPA
LinkDB: A0A2R9A926_PANPA
Original site: A0A2R9A926_PANPA 
ID   A0A2R9A926_PANPA        Unreviewed;       372 AA.
AC   A0A2R9A926;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Core histone macro-H2A {ECO:0000256|PIRNR:PIRNR037942};
GN   Name=MACROH2A1 {ECO:0000313|Ensembl:ENSPPAP00000012145.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000012145.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000012145.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000012145.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; AJFE02102979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02102980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02102981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003829310.1; XM_003829262.2.
DR   AlphaFoldDB; A0A2R9A926; -.
DR   SMR; A0A2R9A926; -.
DR   STRING; 9597.ENSPPAP00000012145; -.
DR   Ensembl; ENSPPAT00000034807.1; ENSPPAP00000012145.1; ENSPPAG00000029258.1.
DR   GeneTree; ENSGT00940000159541; -.
DR   OrthoDB; 235643at2759; -.
DR   Proteomes; UP000240080; Chromosome 5.
DR   Bgee; ENSPPAG00000029258; Expressed in cerebellum and 6 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:UP000240080};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          184..370
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   REGION          128..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..160
FT                   /note="Basic 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   372 AA;  39617 MW;  37DED989EF7E69DC CRC64;
     MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI
     LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS
     KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK KQGEVSKAAS ADSTTEGTPA
     DGFTVLSTKS LFLGQKLNLI HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE
     FVEAVLELRK KNGPLEVAGA AVSAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL
     ADDKKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY FVLFDSESIG
     IYVQEMAKLD AN
//
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