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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
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
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
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_BIND: H-T-H motif => ECO:0000255
ChainResidueDetails
ALEU330-ALA356

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR20
ATHR24

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER27

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR53

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER69

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER76

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18086883, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER82

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18086883
ChainResidueDetails
ASER98
ASER104

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18086883, ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER140

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:18086883
ChainResidueDetails
ASER159
ASER397

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:18086883, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER177

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS50

221051

PDB entries from 2024-06-12

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