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 | 0000511 | molecular_function | H2A-H2B histone complex chaperone activity |
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 | 0005940 | cellular_component | septin ring |
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 | 0140597 | molecular_function | protein carrier chaperone |
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 binding: {"description":"H-T-H motif","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15665377","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |