2AYU
The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000785 | cellular_component | chromatin |
A | 0000920 | biological_process | septum digestion after cytokinesis |
A | 0000921 | biological_process | septin ring assembly |
A | 0003677 | molecular_function | DNA binding |
A | 0003682 | molecular_function | chromatin binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005935 | cellular_component | cellular bud neck |
A | 0006334 | biological_process | nucleosome assembly |
A | 0006337 | biological_process | nucleosome disassembly |
A | 0006607 | biological_process | NLS-bearing protein import into nucleus |
A | 0007117 | biological_process | budding cell bud growth |
A | 0008047 | molecular_function | enzyme activator activity |
A | 0030332 | molecular_function | cyclin binding |
A | 0031116 | biological_process | positive regulation of microtubule polymerization |
A | 0032153 | cellular_component | cell division site |
A | 0032174 | cellular_component | cellular bud neck septin collar |
A | 0032968 | biological_process | positive regulation of transcription elongation by RNA polymerase II |
A | 0042274 | biological_process | ribosomal small subunit biogenesis |
A | 0042393 | molecular_function | histone binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0051082 | molecular_function | unfolded protein binding |
A | 0098841 | biological_process | protein localization to cell division site after cytokinesis |
A | 1990317 | cellular_component | Gin4 complex |
A | 2000617 | biological_process | obsolete positive regulation of histone H3-K9 acetylation |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 26 |
Details | DNA_BIND: H-T-H motif => ECO:0000255 |
Chain | Residue | Details |
A | LEU330-ALA356 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | THR20 | |
A | THR24 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER27 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | THR53 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER69 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER76 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18086883, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER82 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18086883 |
Chain | Residue | Details |
A | SER98 | |
A | SER104 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18086883, ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER140 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:18086883 |
Chain | Residue | Details |
A | SER159 | |
A | SER397 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:18086883, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER177 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
Chain | Residue | Details |
A | LYS50 |