IED Industry Enzyme Database

Detail Information for IndEnz0002002860
IED ID IndEnz0002002860
Enzyme Type ID protease002860
Protein Name Histone H2B.2
Gene Name HTB2 H2B2 YBL002W YBL0104
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MSSAAEKKPASKAPAEKKPAAKKTSTSVDGKKRSKVRKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA
Enzyme Length 131
Uniprot Accession Number P02294
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:14752010, ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:15632065, ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663, ECO:0000269|PubMed:16598039}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (1); Chain (1); Compositional bias (1); Cross-link (5); Helix (4); Initiator methionine (1); Modified residue (13); Mutagenesis (5); Region (1); Turn (1)
Keywords 3D-structure;Acetylation;Chromosome;DNA-binding;Direct protein sequencing;Isopeptide bond;Methylation;Nucleosome core;Nucleus;Phosphoprotein;Reference proteome;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus. Chromosome.
Modified Residue MOD_RES 7; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000269|PubMed:16598039"; MOD_RES 8; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000269|PubMed:16598039"; MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663"; MOD_RES 12; /note="N6-acetyllysine"; /evidence="ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774"; MOD_RES 17; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774, ECO:0000269|PubMed:16598039, ECO:0000269|PubMed:19113941"; MOD_RES 18; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000269|PubMed:19113941"; MOD_RES 22; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000269|PubMed:19113941"; MOD_RES 22; /note="N6-butyryllysine; alternate"; /evidence="ECO:0000269|PubMed:19113941"; MOD_RES 23; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000269|PubMed:19113941"; MOD_RES 23; /note="N6-methyllysine; alternate"; /evidence="ECO:0000269|PubMed:19113941"; MOD_RES 35; /note="N6-succinyllysine"; /evidence="ECO:0000269|PubMed:22389435"; MOD_RES 38; /note="N6,N6-dimethyllysine"; /evidence="ECO:0000269|PubMed:19113941"; MOD_RES 47; /note="N6-succinyllysine"; /evidence="ECO:0000269|PubMed:22389435"
Post Translational Modification PTM: Monoubiquitinated by the RAD6/UBC2-BRE1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation. Deubiquitination is performed by UBP8 in presence of SGF11.; PTM: Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis. {ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663}.; PTM: Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription. {ECO:0000269|PubMed:10777603, ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774, ECO:0000269|PubMed:16598039}.; PTM: Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription. {ECO:0000269|PubMed:15166219, ECO:0000269|PubMed:16598039}.
Signal Peptide
Structure 3D Electron microscopy (1); X-ray crystallography (2)
Cross Reference PDB 1ID3; 4JJN; 6QLD;
Mapped Pubmed ID 10458604; 10629113; 10642555; 10859162; 11260253; 11283351; 11305943; 11309407; 11467741; 11702777; 11805826; 11805837; 11835281; 11973294; 12070136; 12142001; 12213658; 12761051; 1312335; 1406694; 14645854; 14660704; 14673149; 14718168; 14979016; 15020048; 15171247; 15284894; 15461807; 15528187; 15632126; 15694334; 15713633; 15786493; 15843385; 15925550; 15961354; 15961637; 15978030; 15996904; 16039595; 16227579; 16429126; 16531994; 16554755; 16568953; 16675445; 16705165; 16772277; 16912715; 16936821; 17052450; 17052455; 17066037; 17082210; 17088385; 17118266; 17163647; 17184543; 17244531; 17289583; 17362199; 17392337; 17543890; 17574019; 17689491; 17700626; 17700858; 17996059; 18374642; 18385160; 18488019; 18562693; 18614047; 18671409; 18718879; 18728017; 18806472; 19037758; 19230796; 19234527; 19269973; 19317649; 19332560; 19355820; 19385041; 19482523; 19524533; 19536198; 19574230; 19620965; 19633430; 19661920; 19662160; 19667127; 19682934; 19683499; 19795076; 19805358; 19923226; 19929865; 19995894; 20005892; 20007597; 20012585; 20018700; 20020052; 20168086; 20232928; 20232933; 20347425; 20363118; 20432449; 20439497; 20460436; 20461077; 20479120; 20502685; 20508643; 20585957; 20621280; 20621284; 20668333; 20678485; 20683473; 20699646; 20713692; 20865123; 21111233; 21115484; 21115727; 21117171; 21179020; 21249157; 21310294; 21326895; 21362547; 21441211; 21467136; 21646431; 21680712; 21734642; 21772248; 21791612; 21829450; 21884933; 21893585; 21923481; 21937884; 21984211; 21998594; 22015777; 2201678; 22034500; 22081017; 22096199; 22121211; 22188810; 22199229; 22199252; 22201790; 22214660; 22252319; 22306662; 22345607; 22366340; 2247060; 22549955; 22555441; 2275823; 22982193; 23103252; 23337853; 23453808; 23481674; 23499444; 23580526; 23592332; 23650358; 23661467; 23728291; 23791651; 23818500; 23818662; 23833181; 23917692; 23934150; 23974242; 24025678; 24030711; 24034245; 24106087; 24135701; 24248595; 24459729; 24606900; 24794003; 25136098; 25228644; 25252977; 25275495; 25348398; 25480300; 25484185; 25611318; 25705722; 25897129; 26130720; 26241481; 26414936; 26416482; 26420880; 26429065; 26455391; 26498326; 26537406; 26560339; 26627840; 26644575; 26740628; 26849847; 26895087; 26912860; 27184763; 27250769; 27339085; 27458205; 27666592; 27693354; 27737893; 27769718; 27840029; 2834270; 3123916; 31578520; 3316978; 33231641; 7016339; 7026046; 8017102; 8655644; 8670902; 8849886; 9610403; 9878065;
Motif
Gene Encoded By
Mass 14,237
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda