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H2A5_WHEAT
ID   H2A5_WHEAT              Reviewed;         145 AA.
AC   Q43213;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Protein H2A.5;
DE   AltName: Full=wcH2A-2;
GN   Name=H2A-2;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=7893754; DOI=10.1016/0167-4781(95)00017-b;
RA   Huh G.H., Matsuura Y., Meshi T., Iwabuchi M.;
RT   "Differential expression of the two types of histone H2A genes in wheat.";
RL   Biochim. Biophys. Acta 1261:155-160(1995).
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 {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Abundant in meristematic tissues.
CC       {ECO:0000269|PubMed:7893754}.
CC   -!- DEVELOPMENTAL STAGE: Induced during germination.
CC       {ECO:0000269|PubMed:7893754}.
CC   -!- DOMAIN: Contains one SPKK motif which may interact with the minor
CC       groove of A/T-rich DNA sites. Phosphorylation of this motif may
CC       regulate DNA binding. This motif is reiterated in both termini of
CC       histone H1 and in the N-terminus of sea urchin histones H2B, but its
CC       presence in the C-terminus seems to be unique to plant H2A.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; D38087; BAA07276.1; -; mRNA.
DR   PIR; S53518; S53518.
DR   AlphaFoldDB; Q43213; -.
DR   SMR; Q43213; -.
DR   EnsemblPlants; TraesCAD_scaffold_044661_01G000200.1; TraesCAD_scaffold_044661_01G000200.1; TraesCAD_scaffold_044661_01G000200.
DR   EnsemblPlants; TraesCLE_scaffold_047276_01G000200.1; TraesCLE_scaffold_047276_01G000200.1; TraesCLE_scaffold_047276_01G000200.
DR   EnsemblPlants; TraesCS6D02G062800.1; TraesCS6D02G062800.1; TraesCS6D02G062800.
DR   EnsemblPlants; TraesPAR_scaffold_047534_01G000200.1; TraesPAR_scaffold_047534_01G000200.1; TraesPAR_scaffold_047534_01G000200.
DR   EnsemblPlants; TraesROB_scaffold_043725_01G000200.1; TraesROB_scaffold_043725_01G000200.1; TraesROB_scaffold_043725_01G000200.
DR   EnsemblPlants; TraesWEE_scaffold_043343_01G000200.1; TraesWEE_scaffold_043343_01G000200.1; TraesWEE_scaffold_043343_01G000200.
DR   Gramene; TraesCAD_scaffold_044661_01G000200.1; TraesCAD_scaffold_044661_01G000200.1; TraesCAD_scaffold_044661_01G000200.
DR   Gramene; TraesCLE_scaffold_047276_01G000200.1; TraesCLE_scaffold_047276_01G000200.1; TraesCLE_scaffold_047276_01G000200.
DR   Gramene; TraesCS6D02G062800.1; TraesCS6D02G062800.1; TraesCS6D02G062800.
DR   Gramene; TraesPAR_scaffold_047534_01G000200.1; TraesPAR_scaffold_047534_01G000200.1; TraesPAR_scaffold_047534_01G000200.
DR   Gramene; TraesROB_scaffold_043725_01G000200.1; TraesROB_scaffold_043725_01G000200.1; TraesROB_scaffold_043725_01G000200.
DR   Gramene; TraesWEE_scaffold_043343_01G000200.1; TraesWEE_scaffold_043343_01G000200.1; TraesWEE_scaffold_043343_01G000200.
DR   OMA; YLKIGRY; -.
DR   Proteomes; UP000019116; Unplaced.
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; IBA:GO_Central.
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   Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..145
FT                   /note="Protein H2A.5"
FT                   /id="PRO_0000244648"
FT   REGION          118..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           135..138
FT                   /note="SPKK motif"
FT   COMPBIAS        120..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   145 AA;  15388 MW;  CD5DA020355237A3 CRC64;
     MAGRKGGDRK KAVTRSVKAG LQFPVGRIGR YLKKGRYAQR VGSGAPVYLA AVLEYLAAEV
     LELAGNAAKD NKKTRIIPRH LLLAVRNDQE LGRLLAGVTI AHGGVIPNIN SVLLPKKSPA
     AAEKEAKSQK AAAKSPKKKT AATKE
 
 
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