| IED ID | IndEnz0002004219 |
| Enzyme Type ID | protease004219 |
| Protein Name |
Histone H2B.1 Suppressor of Ty protein 12 |
| Gene Name | HTB1 H2B1 SPT12 YDR224C YD9934.09C |
| 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 | MSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA |
| Enzyme Length | 131 |
| Uniprot Accession Number | P02293 |
| 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:11973294, ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:14752010, ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:15632065, ECO:0000269|PubMed:15632126, ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663, ECO:0000269|PubMed:16598039}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (2); Chain (1); Cross-link (5); Helix (4); Initiator methionine (1); Modified residue (13); Mutagenesis (8); Region (1) |
| Keywords | 3D-structure;Acetylation;Chromosome;DNA-binding;Direct protein sequencing;Isopeptide bond;Methylation;Nucleosome core;Nucleus;Phosphoprotein;Reference proteome;Ubl conjugation |
| Interact With | P32597 |
| 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 | NMR spectroscopy (1); Electron microscopy (5); X-ray crystallography (6) |
| Cross Reference PDB | 2JSS; 4KUD; 4M6B; 4WNN; 5BT1; 6AE8; 6GEJ; 6GEN; 6QLD; 7DLX; 7K78; 7K7G; |
| Mapped Pubmed ID | 10445029; 10458604; 10579938; 10629113; 10859162; 11173517; 11260253; 11283351; 11305943; 11309407; 11448992; 11467741; 11702777; 11805837; 11835281; 12070136; 12142001; 12213658; 12446762; 12697820; 12761051; 1312335; 1406694; 14645854; 14660704; 14673149; 14718168; 14967150; 14979016; 15020048; 15045029; 15171247; 15284894; 15461807; 15694334; 15713633; 15786493; 15843385; 15879519; 15925550; 15961354; 15961637; 15978030; 15996904; 16039595; 16227579; 16429126; 16455487; 16531994; 16554755; 16648479; 16675445; 16772277; 16912715; 16936821; 16971477; 17002501; 17052450; 17052455; 17082210; 17088385; 17118266; 17163647; 17184543; 17244531; 17289583; 17362199; 17392337; 17447102; 17526727; 17543890; 17574019; 17643376; 17689491; 17700626; 17700858; 17855393; 17996059; 18374642; 18385160; 18562693; 18614047; 18622391; 18671409; 18718879; 18728017; 18806472; 18998772; 19037758; 19148280; 19230796; 19234527; 19255247; 19317649; 19332560; 19355820; 19385041; 19482523; 19524533; 19536198; 19574230; 19581291; 19620965; 19633430; 19661920; 19662160; 19667127; 19682934; 19683499; 19795076; 19805358; 19929865; 19995894; 20005892; 20007597; 20012585; 20018700; 20139344; 20168086; 20232928; 20232933; 20347425; 20361019; 20363118; 20432449; 20439497; 20460436; 20461077; 20479120; 20502685; 20508643; 20585957; 20621280; 20621284; 20668333; 20678485; 20683473; 20699646; 20713692; 20865123; 21058425; 21058428; 21111233; 21115484; 21115727; 21117171; 21135121; 21179020; 21249157; 21310294; 21326895; 21362547; 21392582; 21441211; 21467136; 21487390; 21625001; 21646431; 21680712; 21701592; 21772248; 21791612; 21829450; 21884933; 21893585; 21923481; 21926967; 21937884; 21984211; 2199321; 21998594; 22015777; 2201678; 22081017; 22096199; 22121211; 22188810; 22199229; 22199252; 22201790; 22214660; 22252319; 22306662; 22345607; 22366340; 2247060; 22541333; 22555441; 22699496; 2275823; 22895177; 22977255; 22982193; 23103252; 23337853; 23453808; 23481674; 23499444; 23580526; 23592332; 23707796; 23728291; 23791651; 23818500; 23818662; 23833181; 23843746; 23917692; 23934150; 23934152; 23974242; 24025678; 24030711; 24034245; 24106087; 24135701; 24248595; 24459729; 24476359; 24507717; 25228644; 25252977; 25275495; 25326522; 25348398; 25473596; 25480300; 25484185; 25611318; 25705722; 25897129; 26130720; 26241481; 26414936; 26416482; 26420880; 26429065; 26455391; 26498326; 26537406; 26627840; 26644575; 26740628; 26787838; 26884462; 26895087; 26912860; 27143358; 27225933; 27250769; 27339085; 27458205; 27618665; 27666592; 27737893; 27769718; 28032848; 2834270; 28520954; 29038170; 29637554; 30309918; 31107867; 3123916; 31578520; 3316978; 33320380; 33602814; 33741944; 34038732; 7016339; 7026046; 8017102; 8035801; 8224824; 8417331; 8655644; 8670902; 8844144; 9055075; 9256430; 9610403; 9878065; |
| Motif | |
| Gene Encoded By | |
| Mass | 14,252 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |