H2AZ_ONCMY
ID H2AZ_ONCMY Reviewed; 128 AA.
AC P22647;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Histone H2A.Z;
DE Short=H2A/z;
GN Name=h2az1;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Govoroun M., Guiguen Y., Le Gac F.;
RT "Construction and primary characterization of normalized cDNA libraries in
RT rainbow trout, Oncorhynchus mykiss.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-33, AND UBIQUITINATION.
RX PubMed=2822092; DOI=10.1021/bi00388a034;
RA Nickel B.E., Roth S.Y., Cook R.G., Allis C.D., Davie J.R.;
RT "Changes in the histone H2A variant H2A.Z and polyubiquitinated histone
RT species in developing trout testis.";
RL Biochemistry 26:4417-4421(1987).
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 (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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.
CC Acetylation disappears at mitosis (By similarity).
CC {ECO:0000250|UniProtKB:P0C0S6}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; BX080631; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A27074; A27074.
DR AlphaFoldDB; P22647; -.
DR SMR; P22647; -.
DR iPTMnet; P22647; -.
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 1: Evidence at protein level;
KW Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleosome core; Nucleus; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2822092"
FT CHAIN 2..128
FT /note="Histone H2A.Z"
FT /id="PRO_0000055304"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..100
FT /note="M6 cassette"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 8
FT /note="N6-acetyllysine"
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-lactoyllysine"
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:0000305|PubMed:2822092"
FT CONFLICT 13
FT /note="A -> T (in Ref. 1; BX080631)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="V -> I (in Ref. 1; BX080631)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="G -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 13553 MW; E024E53818230371 CRC64;
MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKGQQKTV
