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H2AZ_PONAB
ID   H2AZ_PONAB              Reviewed;         128 AA.
AC   Q5RC42;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Histone H2A.Z;
DE            Short=H2A/z;
GN   Name=H2AZ1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC       subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin,
CC       limiting DNA accessibility to the cellular machineries which require
CC       DNA as a template. Histones thereby play a central role in
CC       transcription regulation, DNA repair, DNA replication and chromosomal
CC       stability. DNA accessibility is regulated via a complex set of post-
CC       translational modifications of histones, also called histone code, and
CC       nucleosome remodeling. May be involved in the formation of constitutive
CC       heterochromatin. May be required for chromosome segregation during cell
CC       division (By similarity). {ECO:0000250|UniProtKB:P0C0S5,
CC       ECO:0000250|UniProtKB:P0C0S6}.
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. H2A or its variant H2AZ1 forms a heterodimer with H2B. H2AZ1
CC       interacts with INCENP. Interacts (via M6 cassette) with ANP32E; leading
CC       to removal of H2A.Z/H2AZ1 from the nucleosome. Interacts with VPS72
CC       (via N-terminal domain). Interacts with PWWP2A. Interacts with FH (when
CC       phosphorylated by PRKDC). {ECO:0000250|UniProtKB:P0C0S5,
CC       ECO:0000250|UniProtKB:P0C0S6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic
CC       transcriptional repression. {ECO:0000250|UniProtKB:P0C0S5}.
CC   -!- PTM: Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is
CC       recruited by the XPC complex in absence of DNA damage (By similarity).
CC       Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation
CC       disappears at mitosis (By similarity). Acetylation by the NuA4 histone
CC       acetyltransferase complex is required for hematopoietic stem cell
CC       maintenance (By similarity). {ECO:0000250|UniProtKB:P0C0S5,
CC       ECO:0000250|UniProtKB:P0C0S6}.
CC   -!- PTM: Not phosphorylated. {ECO:0000250|UniProtKB:P0C0S4}.
CC   -!- PTM: Monomethylated on Lys-5 and Lys-8 by SETD6. SETD6 predominantly
CC       methylates Lys-8, lys-5 being a possible secondary site.
CC       {ECO:0000250|UniProtKB:P0C0S5}.
CC   -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC       directly derived from endogenous or exogenous lactate, leading to
CC       stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; CR858439; CAH90668.1; -; mRNA.
DR   RefSeq; NP_001127318.1; NM_001133846.2.
DR   AlphaFoldDB; Q5RC42; -.
DR   SMR; Q5RC42; -.
DR   STRING; 9601.ENSPPYP00000016702; -.
DR   Ensembl; ENSPPYT00000017381; ENSPPYP00000016702; ENSPPYG00000014957.
DR   GeneID; 100174379; -.
DR   KEGG; pon:100174379; -.
DR   CTD; 3015; -.
DR   eggNOG; KOG1757; Eukaryota.
DR   GeneTree; ENSGT00900000140979; -.
DR   HOGENOM; CLU_062828_2_2_1; -.
DR   InParanoid; Q5RC42; -.
DR   OMA; WHCQAGG; -.
DR   OrthoDB; 1504122at2759; -.
DR   TreeFam; TF354232; -.
DR   Proteomes; UP000001595; Chromosome 4.
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; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   CDD; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; -; 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; PTHR23430; 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; SSF47113; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW   Nucleosome core; Nucleus; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   CHAIN           2..128
FT                   /note="Histone H2A.Z"
FT                   /id="PRO_0000055299"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..17
FT                   /note="Required for interaction with INCENP"
FT                   /evidence="ECO:0000250"
FT   REGION          89..100
FT                   /note="M6 cassette"
FT                   /evidence="ECO:0000250"
FT   REGION          93..103
FT                   /note="Required for interaction with INCENP"
FT                   /evidence="ECO:0000250"
FT   REGION          120..128
FT                   /note="Required for interaction with PWWP2A"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         5
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         8
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         12
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         14
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         116
FT                   /note="N6-lactoyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   CROSSLNK        122
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
SQ   SEQUENCE   128 AA;  13553 MW;  E024E53818230371 CRC64;
     MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE
     YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
     KKGQQKTV
 
 
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