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Protein

Importin subunit beta-1

Gene

Kpnb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Imports SNAI1 and PRKCI into the nucleus (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-MMU-211227. Activation of DNA fragmentation factor.
R-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit beta-1
Alternative name(s):
Karyopherin subunit beta-1
Nuclear factor p97
Pore targeting complex 97 kDa subunit
Short name:
PTAC97
SCG
Gene namesi
Name:Kpnb1
Synonyms:Impnb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107532. Kpnb1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001207461 – 876Importin subunit beta-1Add BLAST876

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei12PhosphoserineBy similarity1
Modified residuei211N6-acetyllysineBy similarity1
Modified residuei835N6-acetyllysineBy similarity1
Modified residuei867N6-acetyllysineBy similarity1

Post-translational modificationi

Mono-ADP-ribosylated by PARP16.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

EPDiP70168.
MaxQBiP70168.
PaxDbiP70168.
PeptideAtlasiP70168.
PRIDEiP70168.

PTM databases

iPTMnetiP70168.
PhosphoSitePlusiP70168.
SwissPalmiP70168.

Expressioni

Gene expression databases

BgeeiENSMUSG00000001440.
CleanExiMM_KPNB1.
GenevisibleiP70168. MM.

Interactioni

Subunit structurei

Forms a complex with an importin alpha subunit. Forms a heterodimer with IPO7. Interacts with IPO7, SNUPN, RPL23A and XPO1. The KPNB1/IPO7 heterodimer interacts with H1 histone. Interacts with H2A, H2B, H3 and H4 histones (By similarity). Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Component of a nuclear export receptor complex composed of KPNB1, Ran, SNUPN and XPO1. Interacts with SRY. Interacts with PRKCI/atypical protein kinase C iota (By similarity). Interacts with KPNA7. Interacts with SNAI1 (via zinc fingers) and SNAI2 (via zinc fingers) (By similarity). Interacts with SLC35G1 and STIM1 (By similarity). Interacts with DCAF8. Interacts with RAN (PubMed:25946333).By similarity1 Publication

GO - Molecular functioni

  • enzyme binding Source: MGI
  • Hsp90 protein binding Source: MGI
  • protein domain specific binding Source: MGI

Protein-protein interaction databases

BioGridi200654. 10 interactors.
DIPiDIP-33404N.
IntActiP70168. 15 interactors.
MINTiMINT-6478527.
STRINGi10090.ENSMUSP00000001479.

Structurei

Secondary structure

1876
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 7Combined sources7
Turni8 – 11Combined sources4
Helixi15 – 45Combined sources31
Beta strandi47 – 49Combined sources3
Helixi51 – 62Combined sources12
Turni63 – 65Combined sources3
Helixi70 – 82Combined sources13
Helixi85 – 98Combined sources14
Beta strandi104 – 106Combined sources3
Helixi108 – 120Combined sources13
Helixi121 – 123Combined sources3
Helixi129 – 138Combined sources10
Helixi144 – 160Combined sources17
Helixi163 – 166Combined sources4
Helixi167 – 169Combined sources3
Helixi170 – 181Combined sources12
Helixi188 – 201Combined sources14
Turni202 – 204Combined sources3
Helixi206 – 209Combined sources4
Helixi212 – 225Combined sources14
Helixi231 – 247Combined sources17
Helixi249 – 254Combined sources6
Turni255 – 259Combined sources5
Helixi260 – 268Combined sources9
Helixi273 – 302Combined sources30
Helixi314 – 329Combined sources16
Helixi330 – 332Combined sources3
Beta strandi338 – 340Combined sources3
Helixi344 – 359Combined sources16
Helixi360 – 362Combined sources3
Helixi363 – 374Combined sources12
Helixi380 – 392Combined sources13
Beta strandi394 – 397Combined sources4
Helixi399 – 416Combined sources18
Helixi422 – 438Combined sources17
Helixi440 – 444Combined sources5
Beta strandi447 – 449Combined sources3
Helixi464 – 485Combined sources22
Helixi486 – 488Combined sources3
Beta strandi491 – 495Combined sources5
Helixi500 – 514Combined sources15
Turni517 – 520Combined sources4
Helixi521 – 523Combined sources3
Helixi524 – 537Combined sources14
Helixi544 – 563Combined sources20
Helixi564 – 567Combined sources4
Helixi571 – 592Combined sources22
Helixi597 – 616Combined sources20
Helixi625 – 639Combined sources15
Turni640 – 643Combined sources4
Helixi644 – 648Combined sources5
Helixi651 – 659Combined sources9
Helixi661 – 663Combined sources3
Helixi664 – 680Combined sources17
Helixi682 – 685Combined sources4
Helixi686 – 701Combined sources16
Beta strandi703 – 705Combined sources3
Helixi709 – 724Combined sources16
Helixi725 – 728Combined sources4
Helixi729 – 743Combined sources15
Helixi753 – 777Combined sources25
Beta strandi779 – 782Combined sources4
Helixi785 – 790Combined sources6
Helixi793 – 806Combined sources14
Helixi812 – 828Combined sources17
Helixi834 – 838Combined sources5
Helixi841 – 849Combined sources9
Helixi856 – 871Combined sources16
Helixi872 – 875Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GCJX-ray2.60A/B1-449[»]
1UKLX-ray3.00A/B1-876[»]
ProteinModelPortaliP70168.
SMRiP70168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70168.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati3 – 29HEAT 11 PublicationAdd BLAST27
Domaini21 – 101Importin N-terminalPROSITE-ProRule annotationAdd BLAST81
Repeati32 – 62HEAT 21 PublicationAdd BLAST31
Repeati85 – 120HEAT 31 PublicationAdd BLAST36
Repeati129 – 160HEAT 41 PublicationAdd BLAST32
Repeati170 – 201HEAT 51 PublicationAdd BLAST32
Repeati212 – 247HEAT 61 PublicationAdd BLAST36
Repeati260 – 302HEAT 71 PublicationAdd BLAST43
Repeati314 – 359HEAT 81 PublicationAdd BLAST46
Repeati363 – 392HEAT 91 PublicationAdd BLAST30
Repeati399 – 438HEAT 101 PublicationAdd BLAST40
Repeati449 – 485HEAT 111 PublicationAdd BLAST37
Repeati500 – 537HEAT 121 PublicationAdd BLAST38
Repeati544 – 592HEAT 131 PublicationAdd BLAST49
Repeati597 – 639HEAT 141 PublicationAdd BLAST43
Repeati644 – 680HEAT 151 PublicationAdd BLAST37
Repeati686 – 724HEAT 161 PublicationAdd BLAST39
Repeati729 – 777HEAT 171 PublicationAdd BLAST49
Repeati785 – 828HEAT 181 PublicationAdd BLAST44
Repeati834 – 875HEAT 191 PublicationAdd BLAST42

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni329 – 342IAB-bindingAdd BLAST14
Regioni334 – 419Ran-GTP bindingBy similarityAdd BLAST86

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi337 – 341Poly-Asp5

Sequence similaritiesi

Contains 19 HEAT repeats.1 Publication
Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1241. Eukaryota.
COG5215. LUCA.
GeneTreeiENSGT00550000074898.
HOGENOMiHOG000204108.
HOVERGENiHBG002369.
InParanoidiP70168.
KOiK14293.
OMAiMSNILPY.
OrthoDBiEOG091G01XQ.
TreeFamiTF105655.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR021133. HEAT_type_2.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00185. ARM. 3 hits.
SM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS
60 70 80 90 100
QVARVAAGLQ IKNSLTSKDP DIKAQYQQRW LAIDANARRE VKNYVLQTLG
110 120 130 140 150
TETYRPSSAS QCVAGIACAE IPVSQWPELI PQLVANVTNP NSTEHMKEST
160 170 180 190 200
LEAIGYICQD IDPEQLQDKS NEILTAIIQG MRKEEPSNNV KLAATNALLN
210 220 230 240 250
SLEFTKANFD KESERHFIMQ VVCEATQCPD TRVRVAALQN LVKIMSLYYQ
260 270 280 290 300
YMETYMGPAL FAITIEAMKS DIDEVALQGI EFWSNVCDEE MDLAIEASEA
310 320 330 340 350
AEQGRPPEHT SKFYAKGALQ YLVPILTQTL TKQDENDDDD DWNPCKAAGV
360 370 380 390 400
CLMLLSTCCE DDIVPHVLPF IKEHIKNPDW RYRDAAVMAF GSILEGPEPN
410 420 430 440 450
QLKPLVIQAM PTLIELMKDP SVVVRDTTAW TVGRICELLP EAAINDVYLA
460 470 480 490 500
PLLQCLIEGL SAEPRVASNV CWAFSSLAEA AYEAADVADD QEEPATYCLS
510 520 530 540 550
SSFELIVQKL LETTDRPDGH QNNLRSSAYE SLMEIVKNSA KDCYPAVQKT
560 570 580 590 600
TLVIMERLQQ VLQMESHIQS TSDRIQFNDL QSLLCATLQN VLRKVQHQDA
610 620 630 640 650
LQISDVVMAS LLRMFQSTAG SGGVQEDALM AVSTLVEVLG GEFLKYMEAF
660 670 680 690 700
KPFLGIGLKN YAEYQVCLAA VGLVGDLCRA LQSNILPFCD EVMQLLLENL
710 720 730 740 750
GNENVHRSVK PQILSVFGDI ALAIGGEFKK YLEVVLNTLQ QASQAQVDKS
760 770 780 790 800
DFDMVDYLNE LRESCLEAYT GIVQGLKGDQ ENVHPDVMLV QPRVEFILSF
810 820 830 840 850
IDHIAGDEDH TDGVVACAAG LIGDLCTAFG KDVLKLVEAR PMIHELLTEG
860 870
RRSKTNKAKT LATWATKELR KLKNQA
Length:876
Mass (Da):97,184
Last modified:July 27, 2011 - v2
Checksum:i00D6B15023A30598
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti388M → V in BAA11034 (PubMed:8812441).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D67015 mRNA. Translation: BAA11034.1.
D45836 mRNA. Translation: BAA08273.1.
AL627445 Genomic DNA. Translation: CAM26994.1.
CH466556 Genomic DNA. Translation: EDL16074.1.
BC052438 mRNA. Translation: AAH52438.1.
BC055115 mRNA. Translation: AAH55115.1.
CCDSiCCDS25316.1.
PIRiS66288.
RefSeqiNP_032405.3. NM_008379.3.
UniGeneiMm.251013.

Genome annotation databases

EnsembliENSMUST00000001479; ENSMUSP00000001479; ENSMUSG00000001440.
GeneIDi16211.
KEGGimmu:16211.
UCSCiuc007ldu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D67015 mRNA. Translation: BAA11034.1.
D45836 mRNA. Translation: BAA08273.1.
AL627445 Genomic DNA. Translation: CAM26994.1.
CH466556 Genomic DNA. Translation: EDL16074.1.
BC052438 mRNA. Translation: AAH52438.1.
BC055115 mRNA. Translation: AAH55115.1.
CCDSiCCDS25316.1.
PIRiS66288.
RefSeqiNP_032405.3. NM_008379.3.
UniGeneiMm.251013.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GCJX-ray2.60A/B1-449[»]
1UKLX-ray3.00A/B1-876[»]
ProteinModelPortaliP70168.
SMRiP70168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200654. 10 interactors.
DIPiDIP-33404N.
IntActiP70168. 15 interactors.
MINTiMINT-6478527.
STRINGi10090.ENSMUSP00000001479.

PTM databases

iPTMnetiP70168.
PhosphoSitePlusiP70168.
SwissPalmiP70168.

Proteomic databases

EPDiP70168.
MaxQBiP70168.
PaxDbiP70168.
PeptideAtlasiP70168.
PRIDEiP70168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001479; ENSMUSP00000001479; ENSMUSG00000001440.
GeneIDi16211.
KEGGimmu:16211.
UCSCiuc007ldu.1. mouse.

Organism-specific databases

CTDi3837.
MGIiMGI:107532. Kpnb1.

Phylogenomic databases

eggNOGiKOG1241. Eukaryota.
COG5215. LUCA.
GeneTreeiENSGT00550000074898.
HOGENOMiHOG000204108.
HOVERGENiHBG002369.
InParanoidiP70168.
KOiK14293.
OMAiMSNILPY.
OrthoDBiEOG091G01XQ.
TreeFamiTF105655.

Enzyme and pathway databases

ReactomeiR-MMU-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-MMU-211227. Activation of DNA fragmentation factor.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiKpnb1. mouse.
EvolutionaryTraceiP70168.
PROiP70168.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000001440.
CleanExiMM_KPNB1.
GenevisibleiP70168. MM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR021133. HEAT_type_2.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00185. ARM. 3 hits.
SM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIMB1_MOUSE
AccessioniPrimary (citable) accession number: P70168
Secondary accession number(s): Q62117, Q6GTI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.