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2AYU

The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling

Functional Information from GO Data
ChainGOidnamespacecontents
A0000511molecular_functionH2A-H2B histone complex chaperone activity
A0000785cellular_componentchromatin
A0000920biological_processseptum digestion after cytokinesis
A0000921biological_processseptin ring assembly
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005935cellular_componentcellular bud neck
A0005940cellular_componentseptin ring
A0006334biological_processnucleosome assembly
A0006337biological_processnucleosome disassembly
A0006607biological_processNLS-bearing protein import into nucleus
A0007117biological_processbudding cell bud growth
A0008047molecular_functionenzyme activator activity
A0030332molecular_functioncyclin binding
A0031116biological_processpositive regulation of microtubule polymerization
A0032153cellular_componentcell division site
A0032174cellular_componentcellular bud neck septin collar
A0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
A0042274biological_processribosomal small subunit biogenesis
A0042393molecular_functionhistone binding
A0042802molecular_functionidentical protein binding
A0051082molecular_functionunfolded protein binding
A0098841biological_processprotein localization to cell division site after cytokinesis
A0140597molecular_functionprotein carrier chaperone
A1990317cellular_componentGin4 complex
A2000617biological_processobsolete positive regulation of histone H3-K9 acetylation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsDNA binding: {"description":"H-T-H motif","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified 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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-09-24

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