H2AE_PSAMI
ID H2AE_PSAMI Reviewed; 124 AA.
AC P69142; P02271;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Histone H2A, embryonic;
OS Psammechinus miliaris (Green sea urchin) (Echinus miliaris).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Parechinidae;
OC Psammechinus.
OX NCBI_TaxID=7660;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE H19).
RX PubMed=7443547; DOI=10.1093/nar/8.5.957;
RA Busslinger M., Portmann R., Irminger J.C., Birnstiel M.L.;
RT "Ubiquitous and gene-specific regulatory 5' sequences in a sea urchin
RT histone DNA clone coding for histone protein variants.";
RL Nucleic Acids Res. 8:957-977(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE H22).
RX PubMed=688387; DOI=10.1016/0092-8674(78)90249-0;
RA Schaffner W., Kunz G., Daetwyler H., Telford J., Smith H.O.,
RA Birnstiel M.L.;
RT "Genes and spacers of cloned sea urchin histone DNA analyzed by
RT sequencing.";
RL Cell 14:655-671(1978).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE H22).
RA Birnstiel M.L., Portmann R., Busslinger M., Schaffner W., Probst E.,
RA Kressmann A.;
RT "Functional organization of the histone genes in the sea urchin
RT Psammechinus: a progress report.";
RL Proc. Alfred Benzon Symp. 13:117-132(1979).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
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.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Monoubiquitination of Lys-119 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250}.
CC -!- PTM: Phosphorylation of Ser-2 directly represses transcription.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The H22 clone represent the major H2A component.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; J01182; AAB59207.1; -; Genomic_DNA.
DR EMBL; M10559; AAA30027.1; -; Genomic_DNA.
DR EMBL; X01346; CAA25633.1; -; Genomic_DNA.
DR EMBL; V01143; CAA24376.1; -; Genomic_DNA.
DR PIR; A93719; HSURH9.
DR AlphaFoldDB; P69142; -.
DR SMR; P69142; -.
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 3: Inferred from homology;
KW Acetylation; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..124
FT /note="Histone H2A, embryonic"
FT /id="PRO_0000055274"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 104
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT VARIANT 16
FT /note="T -> S (in P.miliaris clone H22)"
FT VARIANT 121
FT /note="A -> G (in P.miliaris clone H22)"
SQ SEQUENCE 124 AA; 13332 MW; 8282CADDF13005E6 CRC64;
MSGRGKSGKA RTKAKTRSSR AGLQFPVGRV HRFLRKGNYA KRVGGGAPVY MAAVLEYLTA
EILELAGNAA RDNKKSRIIP RHLQLAVRND EELNKLLGGV TIAQGGVLPN IQAVLLPKKT
AKSS