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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5YVG

Crystal structure of Karyopherin beta2 in complex with FUS(full length)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006606biological_processprotein import into nucleus
A0006886biological_processintracellular protein transport
A0031267molecular_functionsmall GTPase binding
B0006606biological_processprotein import into nucleus
B0006886biological_processintracellular protein transport
B0031267molecular_functionsmall GTPase binding
X0003676molecular_functionnucleic acid binding
X0003677molecular_functionDNA binding
X0003682molecular_functionchromatin binding
X0003712molecular_functiontranscription coregulator activity
X0003713molecular_functiontranscription coactivator activity
X0003723molecular_functionRNA binding
X0003730molecular_functionmRNA 3'-UTR binding
X0005515molecular_functionprotein binding
X0005634cellular_componentnucleus
X0005654cellular_componentnucleoplasm
X0005737cellular_componentcytoplasm
X0006355biological_processregulation of DNA-templated transcription
X0006357biological_processregulation of transcription by RNA polymerase II
X0008270molecular_functionzinc ion binding
X0008380biological_processRNA splicing
X0042802molecular_functionidentical protein binding
X0043484biological_processregulation of RNA splicing
X0045893biological_processpositive regulation of DNA-templated transcription
X0046872molecular_functionmetal ion binding
X0048255biological_processmRNA stabilization
X0051260biological_processprotein homooligomerization
X0098978cellular_componentglutamatergic synapse
X0098982cellular_componentGABA-ergic synapse
X0099523cellular_componentpresynaptic cytosol
X0099524cellular_componentpostsynaptic cytosol
X0140693molecular_functionmolecular condensate scaffold activity
X0140694biological_processmembraneless organelle assembly
X1905168biological_processpositive regulation of double-strand break repair via homologous recombination
X1990000biological_processamyloid fibril formation
Y0003676molecular_functionnucleic acid binding
Y0003677molecular_functionDNA binding
Y0003682molecular_functionchromatin binding
Y0003712molecular_functiontranscription coregulator activity
Y0003713molecular_functiontranscription coactivator activity
Y0003723molecular_functionRNA binding
Y0003730molecular_functionmRNA 3'-UTR binding
Y0005515molecular_functionprotein binding
Y0005634cellular_componentnucleus
Y0005654cellular_componentnucleoplasm
Y0005737cellular_componentcytoplasm
Y0006355biological_processregulation of DNA-templated transcription
Y0006357biological_processregulation of transcription by RNA polymerase II
Y0008270molecular_functionzinc ion binding
Y0008380biological_processRNA splicing
Y0042802molecular_functionidentical protein binding
Y0043484biological_processregulation of RNA splicing
Y0045893biological_processpositive regulation of DNA-templated transcription
Y0046872molecular_functionmetal ion binding
Y0048255biological_processmRNA stabilization
Y0051260biological_processprotein homooligomerization
Y0098978cellular_componentglutamatergic synapse
Y0098982cellular_componentGABA-ergic synapse
Y0099523cellular_componentpresynaptic cytosol
Y0099524cellular_componentpostsynaptic cytosol
Y0140693molecular_functionmolecular condensate scaffold activity
Y0140694biological_processmembraneless organelle assembly
Y1905168biological_processpositive regulation of double-strand break repair via homologous recombination
Y1990000biological_processamyloid fibril formation
Functional Information from PROSITE/UniProt
site_idPS01358
Number of Residues22
DetailsZF_RANBP2_1 Zinc finger RanBP2-type signature. WkCpnptCenmNfswrneCnqC
ChainResidueDetails
XTRP426-CYS447
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues54
DetailsRepeat: {"description":"HEAT 1","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues68
DetailsDomain: {"description":"Importin N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00115","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues38
DetailsRepeat: {"description":"HEAT 2","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues33
DetailsRepeat: {"description":"HEAT 3","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues30
DetailsRepeat: {"description":"HEAT 5","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues54
DetailsRepeat: {"description":"HEAT 6","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues54
DetailsRepeat: {"description":"HEAT 7","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues56
DetailsRepeat: {"description":"HEAT 9","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues54
DetailsRepeat: {"description":"HEAT 10","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues66
DetailsRepeat: {"description":"HEAT 11","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues66
DetailsRepeat: {"description":"HEAT 12","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues76
DetailsRepeat: {"description":"HEAT 13","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues102
DetailsRepeat: {"description":"HEAT 14","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues62
DetailsRepeat: {"description":"HEAT 15","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues66
DetailsRepeat: {"description":"HEAT 16","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues70
DetailsRepeat: {"description":"HEAT 17","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues66
DetailsRepeat: {"description":"HEAT 18","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues40
DetailsRepeat: {"description":"HEAT 20","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues4
DetailsSite: {"description":"Important for interaction with cargo nuclear localization signals","evidences":[{"source":"PubMed","id":"24753571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues31
DetailsRepeat: {"description":"HEAT 19","evidences":[{"source":"PubMed","id":"10353245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues15
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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