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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9B3I

Cryo-EM structure of yeast (Nap1)2-H2A-H2B-Kap114-RanGTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000511molecular_functionH2A-H2B histone complex chaperone activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006334biological_processnucleosome assembly
A0006606biological_processprotein import into nucleus
A0006607biological_processNLS-bearing protein import into nucleus
A0006886biological_processintracellular protein transport
A0031267molecular_functionsmall GTPase binding
A0051170biological_processimport into nucleus
A0061608molecular_functionnuclear import signal receptor activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006281biological_processDNA repair
B0006325biological_processchromatin organization
B0006974biological_processDNA damage response
B0030527molecular_functionstructural constituent of chromatin
B0031507biological_processheterochromatin formation
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0006325biological_processchromatin organization
C0006355biological_processregulation of DNA-templated transcription
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
D0006913biological_processnucleocytoplasmic transport
E0000511molecular_functionH2A-H2B histone complex chaperone activity
E0000785cellular_componentchromatin
E0000920biological_processseptum digestion after cytokinesis
E0000921biological_processseptin ring assembly
E0003677molecular_functionDNA binding
E0003682molecular_functionchromatin binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005935cellular_componentcellular bud neck
E0005940cellular_componentseptin ring
E0006334biological_processnucleosome assembly
E0006337biological_processnucleosome disassembly
E0006607biological_processNLS-bearing protein import into nucleus
E0007117biological_processbudding cell bud growth
E0008047molecular_functionenzyme activator activity
E0030332molecular_functioncyclin binding
E0031116biological_processpositive regulation of microtubule polymerization
E0032153cellular_componentcell division site
E0032174cellular_componentcellular bud neck septin collar
E0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
E0042274biological_processribosomal small subunit biogenesis
E0042393molecular_functionhistone binding
E0042802molecular_functionidentical protein binding
E0051082molecular_functionunfolded protein binding
E0098841biological_processprotein localization to cell division site after cytokinesis
E0140597molecular_functionprotein carrier chaperone
E2000617biological_processobsolete positive regulation of histone H3-K9 acetylation
F0000511molecular_functionH2A-H2B histone complex chaperone activity
F0000785cellular_componentchromatin
F0000920biological_processseptum digestion after cytokinesis
F0000921biological_processseptin ring assembly
F0003677molecular_functionDNA binding
F0003682molecular_functionchromatin binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005935cellular_componentcellular bud neck
F0005940cellular_componentseptin ring
F0006334biological_processnucleosome assembly
F0006337biological_processnucleosome disassembly
F0006607biological_processNLS-bearing protein import into nucleus
F0007117biological_processbudding cell bud growth
F0008047molecular_functionenzyme activator activity
F0030332molecular_functioncyclin binding
F0031116biological_processpositive regulation of microtubule polymerization
F0032153cellular_componentcell division site
F0032174cellular_componentcellular bud neck septin collar
F0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
F0042274biological_processribosomal small subunit biogenesis
F0042393molecular_functionhistone binding
F0042802molecular_functionidentical protein binding
F0051082molecular_functionunfolded protein binding
F0098841biological_processprotein localization to cell division site after cytokinesis
F0140597molecular_functionprotein carrier chaperone
F2000617biological_processobsolete positive regulation of histone H3-K9 acetylation
Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. SQEL
ChainResidueDetails
BSER128-LEU131
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLtFPV
ChainResidueDetails
BALA22-VAL28
site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlILpGELaKHAVSEG
ChainResidueDetails
CARG95-GLY117
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues79
DetailsDomain: {"description":"Importin N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00115","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"12535538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12535539","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14660635","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15280549","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsRegion: {"description":"Switch-I","evidences":[{"source":"PROSITE-ProRule","id":"PRU00752","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues16
DetailsRegion: {"description":"Switch-II","evidences":[{"source":"PROSITE-ProRule","id":"PRU00752","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P62825","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues52
DetailsDNA binding: {"description":"H-T-H motif","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues438
DetailsRegion: {"description":"Interaction with NBA1","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"},{"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_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18086883","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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