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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1QGR

STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005643cellular_componentnuclear pore
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006404biological_processRNA import into nucleus
A0006606biological_processprotein import into nucleus
A0006607biological_processNLS-bearing protein import into nucleus
A0006610biological_processribosomal protein import into nucleus
A0006886biological_processintracellular protein transport
A0007079biological_processmitotic chromosome movement towards spindle pole
A0007080biological_processmitotic metaphase chromosome alignment
A0008139molecular_functionnuclear localization sequence binding
A0008270molecular_functionzinc ion binding
A0010494cellular_componentcytoplasmic stress granule
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0019899molecular_functionenzyme binding
A0019904molecular_functionprotein domain specific binding
A0030953biological_processastral microtubule organization
A0031267molecular_functionsmall GTPase binding
A0031965cellular_componentnuclear membrane
A0032991cellular_componentprotein-containing complex
A0035580cellular_componentspecific granule lumen
A0040001biological_processestablishment of mitotic spindle localization
A0042564cellular_componentNLS-dependent protein nuclear import complex
A0045540biological_processregulation of cholesterol biosynthetic process
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0051879molecular_functionHsp90 protein binding
A0061608molecular_functionnuclear import signal receptor activity
A0061676molecular_functionimportin-alpha family protein binding
A0070062cellular_componentextracellular exosome
A0071782cellular_componentendoplasmic reticulum tubular network
A0090307biological_processmitotic spindle assembly
A1904813cellular_componentficolin-1-rich granule lumen
B0006606biological_processprotein import into nucleus
B0061608molecular_functionnuclear import signal receptor activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues29
DetailsRepeat: {"description":"HEAT 1","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues80
DetailsDomain: {"description":"Importin N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00115","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues32
DetailsRepeat: {"description":"HEAT 2","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues38
DetailsRepeat: {"description":"HEAT 3","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues31
DetailsRepeat: {"description":"HEAT 4","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues32
DetailsRepeat: {"description":"HEAT 5","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues35
DetailsRepeat: {"description":"HEAT 6","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues49
DetailsRepeat: {"description":"HEAT 7","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues46
DetailsRepeat: {"description":"HEAT 8","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues30
DetailsRepeat: {"description":"HEAT 9","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues36
DetailsRepeat: {"description":"HEAT 10","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues36
DetailsRepeat: {"description":"HEAT 11","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues37
DetailsRepeat: {"description":"HEAT 12","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues48
DetailsRepeat: {"description":"HEAT 13","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues37
DetailsRepeat: {"description":"HEAT 15","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues38
DetailsRepeat: {"description":"HEAT 16","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues44
DetailsRepeat: {"description":"HEAT 17","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues43
DetailsRepeat: {"description":"HEAT 18","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues42
DetailsRepeat: {"description":"HEAT 19","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues176
DetailsRegion: {"description":"Essential for high affinity interaction with RPL23A","evidences":[{"source":"PubMed","id":"9687515","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues13
DetailsRegion: {"description":"IAB-binding"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues85
DetailsRegion: {"description":"Ran-GTP binding"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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PDB entries from 2025-12-03

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