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H2B1_CAEEL
ID   H2B1_CAEEL              Reviewed;         122 AA.
AC   P04255; O02656;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Histone H2B 1;
GN   Name=his-11; ORFNames=ZK131.5;
GN   and
GN   Name=his-15; ORFNames=ZK131.9;
GN   and
GN   Name=his-29; ORFNames=F35H10.11;
GN   and
GN   Name=his-34; ORFNames=F17E9.9;
GN   and
GN   Name=his-44; ORFNames=F08G2.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2544730; DOI=10.1016/0022-2836(89)90566-4;
RA   Roberts S.B., Emmons S.W., Childs G.;
RT   "Nucleotide sequences of Caenorhabditis elegans core histone genes. Genes
RT   for different histone classes share common flanking sequence elements.";
RL   J. Mol. Biol. 206:567-577(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-122.
RX   PubMed=3753445; DOI=10.1042/bj2350769;
RA   Vanfleteren J.R., van Bun S.M., Delcambe L.L., van Beeumen J.J.;
RT   "Multiple forms of histone H2B from the nematode Caenorhabditis elegans.";
RL   Biochem. J. 235:769-773(1986).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2583267; DOI=10.1016/0014-5793(89)81541-8;
RA   Vanfleteren J.R., van Bun S.M., van Beeumen J.J.;
RT   "The histones of Caenorhabditis elegans: no evidence of stage-specific
RT   isoforms. An overview.";
RL   FEBS Lett. 257:233-237(1989).
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-117 gives a specific tag for epigenetic
CC       transcriptional activation and is also prerequisite for histone H3
CC       'Lys-4' and 'Lys-79' methylation. {ECO:0000250}.
CC   -!- PTM: GlcNAcylation at Ser-109 promotes monoubiquitination of Lys-117.
CC       It fluctuates in response to extracellular glucose, and associates with
CC       transcribed genes (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   EMBL; X15633; CAA33642.1; -; Genomic_DNA.
DR   EMBL; FO081169; CCD69642.1; -; Genomic_DNA.
DR   EMBL; Z81495; CAB04061.1; -; Genomic_DNA.
DR   EMBL; Z83245; CAB05830.1; -; Genomic_DNA.
DR   EMBL; Z83245; CAB05832.1; -; Genomic_DNA.
DR   EMBL; FO081018; CCD68530.1; -; Genomic_DNA.
DR   PIR; D88357; D88357.
DR   PIR; D88753; D88753.
DR   RefSeq; NP_496888.1; NM_064487.1.
DR   RefSeq; NP_496892.1; NM_064491.6.
DR   RefSeq; NP_496897.1; NM_064496.1.
DR   RefSeq; NP_501403.1; NM_069002.1.
DR   RefSeq; NP_501409.1; NM_069008.1.
DR   PDB; 6K00; X-ray; 2.20 A; D=30-122.
DR   PDB; 6K03; X-ray; 2.86 A; D=30-122.
DR   PDB; 6K09; X-ray; 2.25 A; D=30-122.
DR   PDBsum; 6K00; -.
DR   PDBsum; 6K03; -.
DR   PDBsum; 6K09; -.
DR   AlphaFoldDB; P04255; -.
DR   SMR; P04255; -.
DR   BioGRID; 40312; 1.
DR   BioGRID; 40315; 2.
DR   BioGRID; 40319; 1.
DR   BioGRID; 50107; 1.
DR   BioGRID; 56179; 1.
DR   STRING; 6239.F08G2.1; -.
DR   EPD; P04255; -.
DR   PaxDb; P04255; -.
DR   PeptideAtlas; P04255; -.
DR   PRIDE; P04255; -.
DR   EnsemblMetazoa; F08G2.1.1; F08G2.1.1; WBGene00001918.
DR   EnsemblMetazoa; F17E9.9.1; F17E9.9.1; WBGene00001908.
DR   EnsemblMetazoa; F35H10.11.1; F35H10.11.1; WBGene00001903.
DR   EnsemblMetazoa; ZK131.5.1; ZK131.5.1; WBGene00001885.
DR   EnsemblMetazoa; ZK131.9.1; ZK131.9.1; WBGene00001889.
DR   GeneID; 175026; -.
DR   GeneID; 175029; -.
DR   GeneID; 175033; -.
DR   GeneID; 185332; -.
DR   GeneID; 191679; -.
DR   KEGG; cel:CELE_F08G2.1; -.
DR   KEGG; cel:CELE_F17E9.9; -.
DR   KEGG; cel:CELE_F35H10.11; -.
DR   KEGG; cel:CELE_ZK131.5; -.
DR   KEGG; cel:CELE_ZK131.9; -.
DR   UCSC; ZK131.9; c. elegans.
DR   CTD; 175026; -.
DR   CTD; 175029; -.
DR   CTD; 175033; -.
DR   CTD; 185332; -.
DR   CTD; 191679; -.
DR   WormBase; F08G2.1; CE07075; WBGene00001918; his-44.
DR   WormBase; F17E9.9; CE07075; WBGene00001908; his-34.
DR   WormBase; F35H10.11; CE07075; WBGene00001903; his-29.
DR   WormBase; ZK131.5; CE07075; WBGene00001885; his-11.
DR   WormBase; ZK131.9; CE07075; WBGene00001889; his-15.
DR   eggNOG; KOG1744; Eukaryota.
DR   GeneTree; ENSGT01050000244943; -.
DR   HOGENOM; CLU_075666_2_1_1; -.
DR   InParanoid; P04255; -.
DR   OrthoDB; 1536672at2759; -.
DR   PhylomeDB; P04255; -.
DR   Reactome; R-CEL-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-CEL-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-CEL-3214815; HDACs deacetylate histones.
DR   Reactome; R-CEL-3214847; HATs acetylate histones.
DR   Reactome; R-CEL-427359; SIRT1 negatively regulates rRNA expression.
DR   Reactome; R-CEL-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-CEL-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-CEL-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR   Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-CEL-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-CEL-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR   PRO; PR:P04255; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00001885; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0000785; C:chromatin; IDA:WormBase.
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:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000558; Histone_H2B.
DR   PANTHER; PTHR23428; PTHR23428; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00621; HISTONEH2B.
DR   SMART; SM00427; H2B; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00357; HISTONE_H2B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromosome; Direct protein sequencing; DNA-binding;
KW   Glycoprotein; Isopeptide bond; Nucleosome core; Nucleus;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3753445"
FT   CHAIN           2..122
FT                   /note="Histone H2B 1"
FT                   /id="PRO_0000071867"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        109
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        117
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        27..28
FT                   /note="RH -> KK (in Ref. 3; AA sequence and 4; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           35..45
FT                   /evidence="ECO:0007829|PDB:6K00"
FT   HELIX           53..78
FT                   /evidence="ECO:0007829|PDB:6K00"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:6K00"
FT   HELIX           88..98
FT                   /evidence="ECO:0007829|PDB:6K00"
FT   HELIX           101..119
FT                   /evidence="ECO:0007829|PDB:6K00"
SQ   SEQUENCE   122 AA;  13501 MW;  C7D161DDEB329401 CRC64;
     MPPKPSAKGA KKAAKTVTKP KDGKKRRHAR KESYSVYIYR VLKQVHPDTG VSSKAMSIMN
     SFVNDVFERI AAEASRLAHY NKRSTISSRE IQTAVRLILP GELAKHAVSE GTKAVTKYTS
     SK
 
 
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