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H32_CHLRE
ID   H32_CHLRE               Reviewed;         135 AA.
AC   Q6LCW8;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Histone H3 type 2;
GN   Name=ch3-II;
GN   and
GN   Name=ch3-III;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8590479; DOI=10.1007/bf00326431;
RA   Fabry S., Mueller K., Lindauer A., Park P.B., Cornelius T., Schmitt R.;
RT   "The organization structure and regulatory elements of Chlamydomonas
RT   histone genes reveal features linking plant and animal genes.";
RL   Curr. Genet. 28:333-345(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16, AND METHYLATION AT LYS-5.
RX   PubMed=16100335; DOI=10.1105/tpc.105.034165;
RA   van Dijk K., Marley K.E., Jeong B.-R., Xu J., Hesson J., Cerny R.L.,
RA   Waterborg J.H., Cerutti H.;
RT   "Monomethyl histone H3 lysine 4 as an epigenetic mark for silenced
RT   euchromatin in Chlamydomonas.";
RL   Plant Cell 17:2439-2453(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-49, ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND
RP   LYS-28, METHYLATION AT LYS-5; LYS-10; LYS-28; LYS-36 AND LYS-37, AND LACK
RP   OF PHOSPHORYLATION.
RX   PubMed=7480339; DOI=10.1104/pp.109.2.393;
RA   Waterborg J.H., Robertson A.J., Tatar D.L., Borza C.M., Davie J.R.;
RT   "Histones of Chlamydomonas reinhardtii. Synthesis, acetylation, and
RT   methylation.";
RL   Plant Physiol. 109:393-407(1995).
RN   [4]
RP   ACETYLATION.
RX   PubMed=9765294; DOI=10.1074/jbc.273.42.27602;
RA   Waterborg J.H.;
RT   "Dynamics of histone acetylation in Chlamydomonas reinhardtii.";
RL   J. Biol. Chem. 273:27602-27609(1998).
RN   [5]
RP   METHYLATION AT LYS-10.
RX   PubMed=17251191; DOI=10.1093/nar/gkl1149;
RA   Casas-Mollano J.A., van Dijk K., Eisenhart J., Cerutti H.;
RT   "SET3p monomethylates histone H3 on lysine 9 and is required for the
RT   silencing of tandemly repeated transgenes in Chlamydomonas.";
RL   Nucleic Acids Res. 35:939-950(2007).
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   -!- PTM: Acetylation is generally linked to gene activation. Acetylated to
CC       form H3K9ac (11%), H3K14ac (17%), H3K18ac (11%), H3K23ac (16%) and
CC       H3K27ac (7%). H3K4, H3K35 and H3K36 are not acetylated. H3K4me prevents
CC       acetylation. 32% of the histone H3 are acetylated with, on average, 2.4
CC       acetyl-Lys. They are all continuously deacatylated and re-acetylated
CC       with a half-life of approximately 2 min. {ECO:0000269|PubMed:7480339,
CC       ECO:0000269|PubMed:9765294}.
CC   -!- PTM: Monomethylated to form H3K4me1 (81%), H3K9me1 (16%), H3K27me1
CC       (25%), H3K35me1 (25%) and H3K36me1 (5%). No methylation at H3K14, H3K18
CC       and H3K23. Methylated by a protein complex that includes Mut11. Set1
CC       methylates specifically H3K4. H3K4me1 is associated with silenced
CC       euchromatin. Set3 forms H3K9me1, while H3K9me2 is undetected. H3K9me1
CC       is specifically associated with silent, multi-copy transgenes.
CC       {ECO:0000269|PubMed:16100335, ECO:0000269|PubMed:17251191,
CC       ECO:0000269|PubMed:7480339}.
CC   -!- PTM: No phosphorylation detected.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow the
CC       'Brno' nomenclature for histone modifications, with positions referring
CC       to those used in the literature for the 'closest' model organism. Due
CC       to slight variations in histone sequences between organisms and to the
CC       presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC       actual positions of modified amino acids in the sequence generally
CC       differ. In this entry the following conventions are used: H3K4 = Lys-5;
CC       H3K4me = methylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me =
CC       methylated Lys-10; H3S10ph = phosphorylated Ser-11; H3T11ph =
CC       phosphorylated Thr-12; H3K14 = Lys-15; H3K14ac = acetylated Lys-15;
CC       H3K18 = Lys-19; H3K18ac = acetylated Lys-19; H3K23 = Lys-24; H3K23ac =
CC       acetylated Lys-24; H3K27ac = acetylated Lys-28; H3K27me = methylated
CC       Lys-28; H3K35 = Lys-36; H3K35me = methylated Lys-36; H3K36 = Lys-37;
CC       H3K36me = methylated Lys-37. {ECO:0000305}.
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DR   EMBL; U16725; AAA98448.1; -; Genomic_DNA.
DR   EMBL; U16724; AAA98444.1; -; Genomic_DNA.
DR   RefSeq; XP_001690671.1; XM_001690619.1.
DR   RefSeq; XP_001690683.1; XM_001690631.1.
DR   RefSeq; XP_001690723.1; XM_001690671.1.
DR   RefSeq; XP_001690808.1; XM_001690756.1.
DR   RefSeq; XP_001690819.1; XM_001690767.1.
DR   RefSeq; XP_001690829.1; XM_001690777.1.
DR   RefSeq; XP_001690998.1; XM_001690946.1.
DR   RefSeq; XP_001691008.1; XM_001690956.1.
DR   RefSeq; XP_001691548.1; XM_001691496.1.
DR   RefSeq; XP_001691674.1; XM_001691622.1.
DR   RefSeq; XP_001691692.1; XM_001691640.1.
DR   RefSeq; XP_001692371.1; XM_001692319.1.
DR   RefSeq; XP_001693721.1; XM_001693669.1.
DR   RefSeq; XP_001696185.1; XM_001696133.1.
DR   RefSeq; XP_001696188.1; XM_001696136.1.
DR   RefSeq; XP_001696189.1; XM_001696137.1.
DR   RefSeq; XP_001696219.1; XM_001696167.1.
DR   RefSeq; XP_001696244.1; XM_001696192.1.
DR   RefSeq; XP_001696249.1; XM_001696197.1.
DR   RefSeq; XP_001696281.1; XM_001696229.1.
DR   RefSeq; XP_001696445.1; XM_001696393.1.
DR   RefSeq; XP_001696460.1; XM_001696408.1.
DR   RefSeq; XP_001696539.1; XM_001696487.1.
DR   RefSeq; XP_001696548.1; XM_001696496.1.
DR   RefSeq; XP_001696551.1; XM_001696499.1.
DR   RefSeq; XP_001698170.1; XM_001698118.1.
DR   RefSeq; XP_001698249.1; XM_001698197.1.
DR   RefSeq; XP_001698957.1; XM_001698905.1.
DR   RefSeq; XP_001700404.1; XM_001700352.1.
DR   RefSeq; XP_001700449.1; XM_001700397.1.
DR   RefSeq; XP_001700460.1; XM_001700408.1.
DR   RefSeq; XP_001700474.1; XM_001700422.1.
DR   RefSeq; XP_001702089.1; XM_001702037.1.
DR   RefSeq; XP_001702224.1; XM_001702172.1.
DR   RefSeq; XP_001702965.1; XM_001702913.1.
DR   RefSeq; XP_001703062.1; XM_001703010.1.
DR   AlphaFoldDB; Q6LCW8; -.
DR   SMR; Q6LCW8; -.
DR   iPTMnet; Q6LCW8; -.
DR   EnsemblPlants; PNW70159; PNW70159; CHLRE_17g708150v5.
DR   EnsemblPlants; PNW70171; PNW70171; CHLRE_17g708700v5.
DR   EnsemblPlants; PNW70178; PNW70178; CHLRE_17g709050v5.
DR   EnsemblPlants; PNW70211; PNW70211; CHLRE_17g710550v5.
DR   EnsemblPlants; PNW70246; PNW70246; CHLRE_17g711850v5.
DR   EnsemblPlants; PNW70286; PNW70286; CHLRE_17g713550v5.
DR   EnsemblPlants; PNW70297; PNW70297; CHLRE_17g713950v5.
DR   EnsemblPlants; PNW70312; PNW70312; CHLRE_17g714650v5.
DR   EnsemblPlants; PNW71334; PNW71334; CHLRE_16g649900v5.
DR   EnsemblPlants; PNW71342; PNW71342; CHLRE_16g650300v5.
DR   EnsemblPlants; PNW73722; PNW73722; CHLRE_13g569950v5.
DR   EnsemblPlants; PNW74879; PNW74879; CHLRE_12g506500v5.
DR   EnsemblPlants; PNW74883; PNW74883; CHLRE_12g506300v5.
DR   EnsemblPlants; PNW74897; PNW74897; CHLRE_12g505500v5.
DR   EnsemblPlants; PNW74912; PNW74912; CHLRE_12g504800v5.
DR   EnsemblPlants; PNW74915; PNW74915; CHLRE_12g504650v5.
DR   EnsemblPlants; PNW81886; PNW81886; CHLRE_06g264650v5.
DR   EnsemblPlants; PNW81898; PNW81898; CHLRE_06g265250v5.
DR   EnsemblPlants; PNW81903; PNW81903; CHLRE_06g265500v5.
DR   EnsemblPlants; PNW81929; PNW81929; CHLRE_06g266650v5.
DR   EnsemblPlants; PNW81958; PNW81958; CHLRE_06g267950v5.
DR   EnsemblPlants; PNW81967; PNW81967; CHLRE_06g268350v5.
DR   EnsemblPlants; PNW82039; PNW82039; CHLRE_06g271250v5.
DR   EnsemblPlants; PNW82103; PNW82103; CHLRE_06g274000v5.
DR   EnsemblPlants; PNW82105; PNW82105; CHLRE_06g274101v5.
DR   EnsemblPlants; PNW82110; PNW82110; CHLRE_06g274350v5.
DR   EnsemblPlants; PNW82120; PNW82120; CHLRE_06g274850v5.
DR   EnsemblPlants; PNW82139; PNW82139; CHLRE_06g275750v5.
DR   EnsemblPlants; PNW82162; PNW82162; CHLRE_06g276600v5.
DR   EnsemblPlants; PNW82169; PNW82169; CHLRE_06g276850v5.
DR   GeneID; 5716276; -.
DR   GeneID; 5716278; -.
DR   GeneID; 5716320; -.
DR   GeneID; 5716453; -.
DR   GeneID; 5716467; -.
DR   GeneID; 5716481; -.
DR   GeneID; 5717132; -.
DR   GeneID; 5717178; -.
DR   GeneID; 5717958; -.
DR   GeneID; 5719118; -.
DR   GeneID; 5721748; -.
DR   GeneID; 5721780; -.
DR   GeneID; 5721836; -.
DR   GeneID; 5721893; -.
DR   GeneID; 5721902; -.
DR   GeneID; 5721929; -.
DR   GeneID; 5721953; -.
DR   GeneID; 5721963; -.
DR   GeneID; 5723811; -.
DR   GeneID; 5724508; -.
DR   GeneID; 5725949; -.
DR   GeneID; 5725959; -.
DR   GeneID; 5725975; -.
DR   GeneID; 5727630; -.
DR   GeneID; 5727766; -.
DR   GeneID; 5728604; -.
DR   Gramene; PNW70159; PNW70159; CHLRE_17g708150v5.
DR   Gramene; PNW70171; PNW70171; CHLRE_17g708700v5.
DR   Gramene; PNW70178; PNW70178; CHLRE_17g709050v5.
DR   Gramene; PNW70211; PNW70211; CHLRE_17g710550v5.
DR   Gramene; PNW70246; PNW70246; CHLRE_17g711850v5.
DR   Gramene; PNW70286; PNW70286; CHLRE_17g713550v5.
DR   Gramene; PNW70297; PNW70297; CHLRE_17g713950v5.
DR   Gramene; PNW70312; PNW70312; CHLRE_17g714650v5.
DR   Gramene; PNW71334; PNW71334; CHLRE_16g649900v5.
DR   Gramene; PNW71342; PNW71342; CHLRE_16g650300v5.
DR   Gramene; PNW73722; PNW73722; CHLRE_13g569950v5.
DR   Gramene; PNW74879; PNW74879; CHLRE_12g506500v5.
DR   Gramene; PNW74883; PNW74883; CHLRE_12g506300v5.
DR   Gramene; PNW74897; PNW74897; CHLRE_12g505500v5.
DR   Gramene; PNW74912; PNW74912; CHLRE_12g504800v5.
DR   Gramene; PNW74915; PNW74915; CHLRE_12g504650v5.
DR   Gramene; PNW81886; PNW81886; CHLRE_06g264650v5.
DR   Gramene; PNW81898; PNW81898; CHLRE_06g265250v5.
DR   Gramene; PNW81903; PNW81903; CHLRE_06g265500v5.
DR   Gramene; PNW81929; PNW81929; CHLRE_06g266650v5.
DR   Gramene; PNW81958; PNW81958; CHLRE_06g267950v5.
DR   Gramene; PNW81967; PNW81967; CHLRE_06g268350v5.
DR   Gramene; PNW82039; PNW82039; CHLRE_06g271250v5.
DR   Gramene; PNW82103; PNW82103; CHLRE_06g274000v5.
DR   Gramene; PNW82105; PNW82105; CHLRE_06g274101v5.
DR   Gramene; PNW82110; PNW82110; CHLRE_06g274350v5.
DR   Gramene; PNW82120; PNW82120; CHLRE_06g274850v5.
DR   Gramene; PNW82139; PNW82139; CHLRE_06g275750v5.
DR   Gramene; PNW82162; PNW82162; CHLRE_06g276600v5.
DR   Gramene; PNW82169; PNW82169; CHLRE_06g276850v5.
DR   KEGG; cre:CHLRE_06g264650v5; -.
DR   KEGG; cre:CHLRE_06g265000v5; -.
DR   KEGG; cre:CHLRE_06g265500v5; -.
DR   KEGG; cre:CHLRE_06g266650v5; -.
DR   KEGG; cre:CHLRE_06g267950v5; -.
DR   KEGG; cre:CHLRE_06g268350v5; -.
DR   KEGG; cre:CHLRE_06g271250v5; -.
DR   KEGG; cre:CHLRE_06g274000v5; -.
DR   KEGG; cre:CHLRE_06g274350v5; -.
DR   KEGG; cre:CHLRE_06g274850v5; -.
DR   KEGG; cre:CHLRE_06g275750v5; -.
DR   KEGG; cre:CHLRE_06g276600v5; -.
DR   KEGG; cre:CHLRE_06g276850v5; -.
DR   KEGG; cre:CHLRE_12g504650v5; -.
DR   KEGG; cre:CHLRE_12g504800v5; -.
DR   KEGG; cre:CHLRE_12g505500v5; -.
DR   KEGG; cre:CHLRE_12g506300v5; -.
DR   KEGG; cre:CHLRE_13g569950v5; -.
DR   KEGG; cre:CHLRE_16g649900v5; -.
DR   KEGG; cre:CHLRE_17g708150v5; -.
DR   KEGG; cre:CHLRE_17g709050v5; -.
DR   KEGG; cre:CHLRE_17g710550v5; -.
DR   KEGG; cre:CHLRE_17g711850v5; -.
DR   KEGG; cre:CHLRE_17g713550v5; -.
DR   KEGG; cre:CHLRE_17g713950v5; -.
DR   KEGG; cre:CHLRE_17g714650v5; -.
DR   HOGENOM; CLU_078295_4_0_1; -.
DR   OrthoDB; 1564596at2759; -.
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   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; PTHR11426; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Methylation; Nucleosome core; Nucleus; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:16100335,
FT                   ECO:0000269|PubMed:7480339"
FT   CHAIN           2..135
FT                   /note="Histone H3 type 2"
FT                   /id="PRO_0000278189"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            5
FT                   /note="Not N6-acetylated"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   SITE            15
FT                   /note="Not N6-methylated"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   SITE            19
FT                   /note="Not N6-methylated"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   SITE            24
FT                   /note="Not N6-methylated"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   SITE            36
FT                   /note="Not N6-acetylated"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   SITE            37
FT                   /note="Not N6-acetylated"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   MOD_RES         5
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:16100335,
FT                   ECO:0000269|PubMed:7480339"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   MOD_RES         10
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:17251191,
FT                   ECO:0000269|PubMed:7480339"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   MOD_RES         28
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   MOD_RES         28
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   MOD_RES         36
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:7480339"
FT   MOD_RES         37
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:7480339"
SQ   SEQUENCE   135 AA;  15310 MW;  1748F7FEC8E680EC CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKTP ATGGVKKPHR YRPGTVALRE IRKYQKSTEL
     LIRKLPFQRL VREIAQDFKT DLRFQSQAVL ALQEAAEAYL VGLFEDTNLC AIHAKRVTIM
     PKDIQLARRI RGERA
 
 
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