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Q14974

- IMB1_HUMAN

UniProt

Q14974 - IMB1_HUMAN

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Protein

Importin subunit beta-1

Gene

KPNB1

Organism
Homo sapiens (Human)
Status
Reviewed - 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. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus.4 Publications

GO - Molecular functioni

  1. enzyme binding Source: UniProt
  2. nuclear localization sequence binding Source: ProtInc
  3. poly(A) RNA binding Source: UniProtKB
  4. protein domain specific binding Source: UniProtKB
  5. protein transporter activity Source: Ensembl
  6. zinc ion binding Source: ProtInc

GO - Biological processi

  1. apoptotic DNA fragmentation Source: Reactome
  2. apoptotic process Source: Reactome
  3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  4. cytokine-mediated signaling pathway Source: Reactome
  5. intracellular transport of virus Source: Reactome
  6. NLS-bearing protein import into nucleus Source: ProtInc
  7. protein import into nucleus Source: MGI
  8. protein import into nucleus, translocation Source: ProtInc
  9. ribosomal protein import into nucleus Source: UniProtKB
  10. small molecule metabolic process Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_13462. Activation of DNA fragmentation factor.
REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
REACT_9395. Nuclear import of Rev protein.
SignaLinkiQ14974.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit beta-1
Alternative name(s):
Importin-90
Karyopherin subunit beta-1
Nuclear factor p97
Pore targeting complex 97 kDa subunit
Short name:
PTAC97
Gene namesi
Name:KPNB1
Synonyms:NTF97
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:6400. KPNB1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus envelope 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. endoplasmic reticulum tubular network Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
  5. membrane Source: UniProtKB
  6. nuclear envelope Source: UniProt
  7. nuclear membrane Source: HPA
  8. nuclear pore Source: ProtInc
  9. nucleoplasm Source: Reactome
  10. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi178 – 1781I → A: Largely reduced binding to FxFG repeats and reduced nuclear import. 1 Publication
Mutagenesisi178 – 1781I → F or D: Loss of binding to FxFG repeats and reduced nuclear import. 1 Publication

Organism-specific databases

PharmGKBiPA30191.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 876876Importin subunit beta-1PRO_0000120745Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei12 – 121Phosphoserine1 Publication
Cross-linki206 – 206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei211 – 2111N6-acetyllysine; alternate1 Publication
Cross-linki211 – 211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei835 – 8351N6-acetyllysine1 Publication
Modified residuei867 – 8671N6-acetyllysine1 Publication

Post-translational modificationi

Mono-ADP-ribosylated by PARP16.

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14974.
PaxDbiQ14974.
PeptideAtlasiQ14974.
PRIDEiQ14974.

PTM databases

PhosphoSiteiQ14974.

Expressioni

Gene expression databases

BgeeiQ14974.
CleanExiHS_KPNB1.
ExpressionAtlasiQ14974. baseline and differential.
GenevestigatoriQ14974.

Organism-specific databases

HPAiCAB034449.
HPA029878.
HPA050302.

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. Binds to HIV-1 Rev and Tat. Interacts with HTLV-1 Rex. Interacts with SRY. Interacts with PRKCI/atypical protein kinase C iota. Interacts with human respiratory syncytial virus (HRSV) protein M. Interacts with KPNA7. Interacts with SNAI1 (via zinc fingers) and SNAI2 (via zinc fingers). Interacts with SLC35G1 and STIM1. Interacts with DCAF8.By similarity21 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2P0462614EBI-286758,EBI-641062
L1P031012EBI-286758,EBI-7362698From a different organism.
L2P031072EBI-286758,EBI-7362531From a different organism.
Mkl1Q8K4J65EBI-286758,EBI-8291665From a different organism.
NSP1P149072EBI-286758,EBI-12265From a different organism.
SMN2Q16637-35EBI-286758,EBI-395447
SMNDC1O759402EBI-286758,EBI-1052641

Protein-protein interaction databases

BioGridi110035. 138 interactions.
DIPiDIP-6204N.
IntActiQ14974. 54 interactions.
MINTiMINT-94095.
STRINGi9606.ENSP00000290158.

Structurei

Secondary structure

1
876
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97
Helixi15 – 4531
Helixi51 – 6515
Helixi70 – 8112
Helixi85 – 9814
Turni99 – 1013
Beta strandi104 – 1063
Helixi109 – 12012
Helixi121 – 1233
Helixi129 – 13810
Helixi144 – 16017
Helixi163 – 1653
Helixi167 – 1693
Helixi170 – 18112
Helixi188 – 20114
Turni202 – 2054
Helixi206 – 2094
Helixi212 – 22514
Beta strandi228 – 2303
Helixi231 – 24717
Helixi249 – 2513
Turni253 – 2597
Helixi260 – 26910
Helixi273 – 29725
Beta strandi303 – 3053
Helixi314 – 32916
Helixi330 – 3323
Beta strandi335 – 3373
Helixi344 – 35815
Turni359 – 3624
Helixi363 – 37412
Helixi380 – 39213
Beta strandi394 – 3974
Turni399 – 4024
Turni404 – 4085
Helixi409 – 4157
Helixi416 – 4183
Helixi422 – 43817
Helixi439 – 4424
Turni446 – 4483
Helixi449 – 4579
Helixi464 – 48320
Beta strandi487 – 4937
Turni500 – 5023
Helixi503 – 51311
Turni517 – 5204
Helixi521 – 5233
Helixi524 – 53714
Helixi541 – 5433
Helixi544 – 56219
Turni563 – 5664
Helixi573 – 59220
Beta strandi593 – 5953
Helixi597 – 6015
Helixi604 – 61411
Beta strandi619 – 6224
Helixi623 – 63917
Helixi640 – 6467
Helixi647 – 66014
Helixi664 – 68118
Helixi682 – 6854
Helixi686 – 70015
Beta strandi703 – 7053
Helixi707 – 7093
Helixi710 – 72415
Helixi725 – 7317
Helixi732 – 74312
Helixi752 – 77726
Beta strandi779 – 7824
Helixi785 – 7895
Helixi791 – 7933
Helixi794 – 80512
Helixi812 – 82918
Helixi832 – 8387
Helixi841 – 85212
Helixi856 – 87318

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F59X-ray2.80A/B1-442[»]
1IBRX-ray2.30B/D1-462[»]
1M5NX-ray2.90S1-485[»]
1O6OX-ray2.80A/B/C1-442[»]
1O6PX-ray2.80A/B1-442[»]
1QGKX-ray2.50A1-876[»]
1QGRX-ray2.30A1-876[»]
2P8QX-ray2.35A1-876[»]
2Q5DX-ray3.20A/B1-876[»]
2QNAX-ray2.84A127-875[»]
3LWWX-ray3.15A/C1-876[»]
3W5KX-ray2.60A1-876[»]
ProteinModelPortaliQ14974.
SMRiQ14974. Positions 1-873.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14974.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 10181Importin N-terminalPROSITE-ProRule annotationAdd
BLAST
Repeati124 – 16340HEAT 1Add
BLAST
Repeati168 – 20740HEAT 2Add
BLAST
Repeati213 – 25038HEAT 3Add
BLAST
Repeati317 – 35741HEAT 4Add
BLAST
Repeati362 – 39938HEAT 5Add
BLAST
Repeati404 – 44138HEAT 6Add
BLAST
Repeati602 – 64140HEAT 7Add
BLAST
Repeati687 – 72640HEAT 8Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni329 – 34214IAB-bindingAdd
BLAST
Regioni334 – 41986Ran-GTP bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi337 – 3415Poly-Asp

Sequence similaritiesi

Belongs to the importin beta family.Curated
Contains 8 HEAT repeats.PROSITE-ProRule annotation
Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5215.
GeneTreeiENSGT00550000074898.
HOGENOMiHOG000204108.
HOVERGENiHBG002369.
InParanoidiQ14974.
KOiK14293.
OMAiGLTIMGM.
OrthoDBiEOG7GN2KZ.
PhylomeDBiQ14974.
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.
IPR027140. KPNB1.
[Graphical view]
PANTHERiPTHR10527:SF1. PTHR10527:SF1. 1 hit.
PfamiPF00514. Arm. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14974-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 IPVNQWPELI 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
CLMLLATCCE DDIVPHVLPF IKEHIKNPDW RYRDAAVMAF GCILEGPEPS
410 420 430 440 450
QLKPLVIQAM PTLIELMKDP SVVVRDTAAW 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 LQSNIIPFCD EVMQLLLENL
710 720 730 740 750
GNENVHRSVK PQILSVFGDI ALAIGGEFKK YLEVVLNTLQ QASQAQVDKS
760 770 780 790 800
DYDMVDYLNE LRESCLEAYT GIVQGLKGDQ ENVHPDVMLV QPRVEFILSF
810 820 830 840 850
IDHIAGDEDH TDGVVACAAG LIGDLCTAFG KDVLKLVEAR PMIHELLTEG
860 870
RRSKTNKAKT LATWATKELR KLKNQA
Length:876
Mass (Da):97,170
Last modified:May 15, 2002 - v2
Checksum:iF3BB8B73E7E51639
GO
Isoform 2 (identifier: Q14974-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-145: Missing.

Note: No experimental confirmation available.

Show »
Length:731
Mass (Da):81,179
Checksum:i03F6C311DF096541
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971Q → H in AAA82869. (PubMed:7615630)Curated
Sequence conflicti200 – 2001N → NA AA sequence (PubMed:8617227)Curated
Sequence conflicti863 – 8631T → R in AAA82869. (PubMed:7615630)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 145145Missing in isoform 2. 1 PublicationVSP_054612Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L39793 Genomic DNA. Translation: AAA82869.1.
L38951 mRNA. Translation: AAC41763.1.
BT009797 mRNA. Translation: AAP88799.1.
AK316421 mRNA. Translation: BAH14792.1.
AC015674 Genomic DNA. No translation available.
AC025682 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94807.1.
CH471109 Genomic DNA. Translation: EAW94808.1.
CH471109 Genomic DNA. Translation: EAW94810.1.
BC003572 mRNA. Translation: AAH03572.1.
BC024045 mRNA. Translation: AAH24045.1.
BC036703 mRNA. Translation: AAH36703.1.
CCDSiCCDS11513.1. [Q14974-1]
CCDS62228.1. [Q14974-2]
PIRiI52907.
RefSeqiNP_001263382.1. NM_001276453.1. [Q14974-2]
NP_002256.2. NM_002265.5. [Q14974-1]
UniGeneiHs.532793.

Genome annotation databases

EnsembliENST00000290158; ENSP00000290158; ENSG00000108424. [Q14974-1]
ENST00000535458; ENSP00000438253; ENSG00000108424. [Q14974-2]
ENST00000540627; ENSP00000438964; ENSG00000108424. [Q14974-2]
GeneIDi3837.
KEGGihsa:3837.
UCSCiuc002ilt.2. human. [Q14974-1]

Polymorphism databases

DMDMi20981701.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L39793 Genomic DNA. Translation: AAA82869.1 .
L38951 mRNA. Translation: AAC41763.1 .
BT009797 mRNA. Translation: AAP88799.1 .
AK316421 mRNA. Translation: BAH14792.1 .
AC015674 Genomic DNA. No translation available.
AC025682 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94807.1 .
CH471109 Genomic DNA. Translation: EAW94808.1 .
CH471109 Genomic DNA. Translation: EAW94810.1 .
BC003572 mRNA. Translation: AAH03572.1 .
BC024045 mRNA. Translation: AAH24045.1 .
BC036703 mRNA. Translation: AAH36703.1 .
CCDSi CCDS11513.1. [Q14974-1 ]
CCDS62228.1. [Q14974-2 ]
PIRi I52907.
RefSeqi NP_001263382.1. NM_001276453.1. [Q14974-2 ]
NP_002256.2. NM_002265.5. [Q14974-1 ]
UniGenei Hs.532793.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F59 X-ray 2.80 A/B 1-442 [» ]
1IBR X-ray 2.30 B/D 1-462 [» ]
1M5N X-ray 2.90 S 1-485 [» ]
1O6O X-ray 2.80 A/B/C 1-442 [» ]
1O6P X-ray 2.80 A/B 1-442 [» ]
1QGK X-ray 2.50 A 1-876 [» ]
1QGR X-ray 2.30 A 1-876 [» ]
2P8Q X-ray 2.35 A 1-876 [» ]
2Q5D X-ray 3.20 A/B 1-876 [» ]
2QNA X-ray 2.84 A 127-875 [» ]
3LWW X-ray 3.15 A/C 1-876 [» ]
3W5K X-ray 2.60 A 1-876 [» ]
ProteinModelPortali Q14974.
SMRi Q14974. Positions 1-873.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110035. 138 interactions.
DIPi DIP-6204N.
IntActi Q14974. 54 interactions.
MINTi MINT-94095.
STRINGi 9606.ENSP00000290158.

PTM databases

PhosphoSitei Q14974.

Polymorphism databases

DMDMi 20981701.

Proteomic databases

MaxQBi Q14974.
PaxDbi Q14974.
PeptideAtlasi Q14974.
PRIDEi Q14974.

Protocols and materials databases

DNASUi 3837.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290158 ; ENSP00000290158 ; ENSG00000108424 . [Q14974-1 ]
ENST00000535458 ; ENSP00000438253 ; ENSG00000108424 . [Q14974-2 ]
ENST00000540627 ; ENSP00000438964 ; ENSG00000108424 . [Q14974-2 ]
GeneIDi 3837.
KEGGi hsa:3837.
UCSCi uc002ilt.2. human. [Q14974-1 ]

Organism-specific databases

CTDi 3837.
GeneCardsi GC17P045727.
HGNCi HGNC:6400. KPNB1.
HPAi CAB034449.
HPA029878.
HPA050302.
MIMi 602738. gene.
neXtProti NX_Q14974.
PharmGKBi PA30191.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5215.
GeneTreei ENSGT00550000074898.
HOGENOMi HOG000204108.
HOVERGENi HBG002369.
InParanoidi Q14974.
KOi K14293.
OMAi GLTIMGM.
OrthoDBi EOG7GN2KZ.
PhylomeDBi Q14974.
TreeFami TF105655.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_13462. Activation of DNA fragmentation factor.
REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
REACT_9395. Nuclear import of Rev protein.
SignaLinki Q14974.

Miscellaneous databases

ChiTaRSi KPNB1. human.
EvolutionaryTracei Q14974.
GeneWikii KPNB1.
GenomeRNAii 3837.
NextBioi 15083.
PROi Q14974.
SOURCEi Search...

Gene expression databases

Bgeei Q14974.
CleanExi HS_KPNB1.
ExpressionAtlasi Q14974. baseline and differential.
Genevestigatori Q14974.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR021133. HEAT_type_2.
IPR001494. Importin-beta_N.
IPR027140. KPNB1.
[Graphical view ]
PANTHERi PTHR10527:SF1. PTHR10527:SF1. 1 hit.
Pfami PF00514. Arm. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view ]
SMARTi SM00913. IBN_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50077. HEAT_REPEAT. 1 hit.
PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and characterization of cytoplasmic nuclear protein import factor p97."
    Chi N.C., Adam E.J.H., Adam S.A.
    J. Cell Biol. 130:265-274(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Tissue: Brain.
  2. "Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope."
    Goerlich D., Kostka S., Kraft R., Dingwall C., Laskey R.A., Hartmann E., Prehn S.
    Curr. Biol. 5:383-392(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Eye.
  8. "The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import."
    Weis K., Ryder U., Lamond A.I.
    EMBO J. 15:1818-1825(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH AN IMPORTIN ALPHA SUBUNIT.
  9. Bienvenut W.V.
    Submitted (MAY-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-9; 55-62 AND 192-206, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  10. "Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta."
    Moroianu J., Blobel G., Radu A.
    Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: RAN-GTP AND ALPHA SUBUNIT BINDING SITES.
  11. "Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta."
    Henderson B.R., Percipalle P.
    J. Mol. Biol. 274:693-707(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 REV AND TAT.
  12. "Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure."
    Huber J., Cronshagen U., Kadokura M., Marshallsay C., Wada T., Sekine M., Luehrmann R.
    EMBO J. 17:4114-4126(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNUPN.
  13. "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells."
    Jaekel S., Goerlich D.
    EMBO J. 17:4491-4502(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPL23A; RPS7; RPL5 AND IPO7.
  14. "The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1."
    Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K., Doenecke D., Goerlich D.
    EMBO J. 18:2411-2423(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH H1 HISTONE AND IPO7.
  15. Cited for: IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, INTERACTION WITH IPO7; SNUPN AND XPO1.
  16. "The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals."
    Truant R., Cullen B.R.
    Mol. Cell. Biol. 19:1210-1217(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 REV.
  17. "Importin beta can mediate the nuclear import of an arginine-rich nuclear localization signal in the absence of importin alpha."
    Palmeri D., Malim M.H.
    Mol. Cell. Biol. 19:1218-1225(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 REX.
  18. "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta."
    Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.
    Hum. Mol. Genet. 11:1785-1795(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN AN IMPORT SNRNP COMPLEX.
  19. "Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C."
    White W.O., Seibenhener M.L., Wooten M.W.
    J. Cell. Biochem. 85:42-53(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKCI, FUNCTION, SUBCELLULAR LOCATION.
  20. "Defective importin beta recognition and nuclear import of the sex-determining factor SRY are associated with XY sex-reversing mutations."
    Harley V.R., Layfield S., Mitchell C.L., Forwood J.K., John A.P., Briggs L.J., McDowall S.G., Jans D.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:7045-7050(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRY.
  21. "Regulation of human SRY subcellular distribution by its acetylation/deacetylation."
    Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N., Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B.
    EMBO J. 23:3336-3345(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRY.
  22. "Nuclear import of the respiratory syncytial virus matrix protein is mediated by importin beta1 independent of importin alpha."
    Ghildyal R., Ho A., Wagstaff K.M., Dias M.M., Barton C.L., Jans P., Bardin P.G., Jans D.A.
    Biochemistry 44:12887-12895(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRSV PROTEIN M.
  23. "Zinc finger domain of Snail functions as a nuclear localization signal for importin beta-mediated nuclear import pathway."
    Yamasaki H., Sekimoto T., Ohkubo T., Douchi T., Nagata Y., Ozawa M., Yoneda Y.
    Genes Cells 10:455-464(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAI1.
  24. "Respiratory syncytial virus M2-1 protein induces the activation of nuclear factor kappa B."
    Reimers K., Buchholz K., Werchau H.
    Virology 331:260-268(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRSV PROTEIN M2-1.
  25. "Multiple importins function as nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1."
    Arnold M., Nath A., Hauber J., Kehlenbach R.H.
    J. Biol. Chem. 281:20883-20890(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 REV.
  26. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-211.
    Tissue: Mammary cancer.
  27. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Characterization of Snail nuclear import pathways as representatives of C2H2 zinc finger transcription factors."
    Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.
    J. Cell Sci. 122:1452-1460(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNAI1 AND SNAI2.
  31. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211; LYS-835 AND LYS-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Karyopherin alpha7 (KPNA7), a divergent member of the importin alpha family of nuclear import receptors."
    Kelley J.B., Talley A.M., Spencer A., Gioeli D., Paschal B.M.
    BMC Cell Biol. 11:63-63(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KPNA7.
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Characterization of nuclear import and export signals determining the subcellular localization of WD repeat-containing protein 42A (WDR42A)."
    Wu F., Wang S., Xing J., Li M., Zheng C.
    FEBS Lett. 586:1079-1085(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCAF8.
  35. "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters."
    Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.
    Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC35G1 AND STIM1.
  36. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-beta1."
    Di Paola S., Micaroni M., Di Tullio G., Buccione R., Di Girolamo M.
    PLoS ONE 7:E37352-E37352(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION, INTERACTION WITH PARP16.
  38. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "Structural view of the Ran-Importin beta interaction at 2.3 A resolution."
    Vetter I.R., Arndt A., Kutay U., Goerlich D., Wittinghofer A.
    Cell 97:635-646(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-459.
  40. "Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking."
    Bayliss R., Littlewood T., Stewart M.
    Cell 102:99-108(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-442, MUTAGENESIS OF ILE-178.
  41. "Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta."
    Cingolani G., Bednenko J., Gillespie M.T., Gerace L.
    Mol. Cell 10:1345-1353(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-485.

Entry informationi

Entry nameiIMB1_HUMAN
AccessioniPrimary (citable) accession number: Q14974
Secondary accession number(s): B7ZAV6
, D3DTT3, Q14637, Q53XN2, Q96J27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 15, 2002
Last modified: October 29, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3