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Q14974 (IMB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KPNB1
Synonyms:NTF97
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length876 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.12 Ref.17 Ref.28

Subunit structure

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). Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.28 Ref.30 Ref.33

Subcellular location

Cytoplasm. Nucleus envelope Ref.17.

Post-translational modification

Mono-ADP-ribosylated by PARP16.

Sequence similarities

Belongs to the importin beta family.

Contains 8 HEAT repeats.

Contains 1 importin N-terminal domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Protein transport
Transport
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   PTMAcetylation
ADP-ribosylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNLS-bearing protein import into nucleus

Traceable author statement Ref.2. Source: ProtInc

apoptotic DNA fragmentation

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

protein import into nucleus

Inferred from direct assay PubMed 15964792. Source: MGI

protein import into nucleus, translocation

Traceable author statement Ref.1. Source: ProtInc

ribosomal protein import into nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum tubular network

Inferred from direct assay Ref.33. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

nuclear envelope

Inferred from direct assay Ref.33. Source: UniProt

nuclear membrane

Inferred from direct assay. Source: HPA

nuclear pore

Traceable author statement Ref.2. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.33. Source: UniProt

nuclear localization sequence binding

Traceable author statement Ref.2. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 11984006. Source: UniProtKB

protein transporter activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 876876Importin subunit beta-1
PRO_0000120745

Regions

Domain21 – 10181Importin N-terminal
Repeat124 – 16340HEAT 1
Repeat168 – 20740HEAT 2
Repeat213 – 25038HEAT 3
Repeat317 – 35741HEAT 4
Repeat362 – 39938HEAT 5
Repeat404 – 44138HEAT 6
Repeat602 – 64140HEAT 7
Repeat687 – 72640HEAT 8
Region329 – 34214IAB-binding
Region334 – 41986Ran-GTP binding
Compositional bias337 – 3415Poly-Asp

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.27 Ref.34
Modified residue121Phosphoserine Ref.26
Modified residue2111N6-acetyllysine; alternate Ref.29
Modified residue8351N6-acetyllysine Ref.29
Modified residue8671N6-acetyllysine Ref.29
Cross-link206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.24
Cross-link211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.24

Experimental info

Mutagenesis1781I → A: Largely reduced binding to FxFG repeats and reduced nuclear import. Ref.36
Mutagenesis1781I → F or D: Loss of binding to FxFG repeats and reduced nuclear import. Ref.36
Sequence conflict971Q → H in AAA82869. Ref.1
Sequence conflict2001N → NA AA sequence Ref.6
Sequence conflict8631T → R in AAA82869. Ref.1

Secondary structure

............................................................................................................................ 876
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14974 [UniParc].

Last modified May 15, 2002. Version 2.
Checksum: F3BB8B73E7E51639

FASTA87697,170
        10         20         30         40         50         60 
MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS QVARVAAGLQ 

        70         80         90        100        110        120 
IKNSLTSKDP DIKAQYQQRW LAIDANARRE VKNYVLQTLG TETYRPSSAS QCVAGIACAE 

       130        140        150        160        170        180 
IPVNQWPELI PQLVANVTNP NSTEHMKEST LEAIGYICQD IDPEQLQDKS NEILTAIIQG 

       190        200        210        220        230        240 
MRKEEPSNNV KLAATNALLN SLEFTKANFD KESERHFIMQ VVCEATQCPD TRVRVAALQN 

       250        260        270        280        290        300 
LVKIMSLYYQ YMETYMGPAL FAITIEAMKS DIDEVALQGI EFWSNVCDEE MDLAIEASEA 

       310        320        330        340        350        360 
AEQGRPPEHT SKFYAKGALQ YLVPILTQTL TKQDENDDDD DWNPCKAAGV CLMLLATCCE 

       370        380        390        400        410        420 
DDIVPHVLPF IKEHIKNPDW RYRDAAVMAF GCILEGPEPS QLKPLVIQAM PTLIELMKDP 

       430        440        450        460        470        480 
SVVVRDTAAW TVGRICELLP EAAINDVYLA PLLQCLIEGL SAEPRVASNV CWAFSSLAEA 

       490        500        510        520        530        540 
AYEAADVADD QEEPATYCLS SSFELIVQKL LETTDRPDGH QNNLRSSAYE SLMEIVKNSA 

       550        560        570        580        590        600 
KDCYPAVQKT TLVIMERLQQ VLQMESHIQS TSDRIQFNDL QSLLCATLQN VLRKVQHQDA 

       610        620        630        640        650        660 
LQISDVVMAS LLRMFQSTAG SGGVQEDALM AVSTLVEVLG GEFLKYMEAF KPFLGIGLKN 

       670        680        690        700        710        720 
YAEYQVCLAA VGLVGDLCRA LQSNIIPFCD EVMQLLLENL GNENVHRSVK PQILSVFGDI 

       730        740        750        760        770        780 
ALAIGGEFKK YLEVVLNTLQ QASQAQVDKS DYDMVDYLNE LRESCLEAYT GIVQGLKGDQ 

       790        800        810        820        830        840 
ENVHPDVMLV QPRVEFILSF IDHIAGDEDH TDGVVACAAG LIGDLCTAFG KDVLKLVEAR 

       850        860        870 
PMIHELLTEG RRSKTNKAKT LATWATKELR KLKNQA 

« Hide

References

« Hide 'large scale' references
[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].
[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].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Brain and Eye.
[6]"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.
[7]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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"CRM1-mediated recycling of snurportin 1 to the cytoplasm."
Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U., Hartmann E., Luehrmann R., Goerlich D.
J. Cell Biol. 145:255-264(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, INTERACTION WITH IPO7; SNUPN AND XPO1.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"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].
[28]"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.
[29]"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].
[30]"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.
[31]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"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].
[33]"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.
[34]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"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.
[36]"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.
[37]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L39793 Genomic DNA. Translation: AAA82869.1.
L38951 mRNA. Translation: AAC41763.1.
BT009797 mRNA. Translation: AAP88799.1.
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.
PIRI52907.
RefSeqNP_001263382.1. NM_001276453.1.
NP_002256.2. NM_002265.5.
UniGeneHs.532793.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ14974.
SMRQ14974. Positions 1-873.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110035. 133 interactions.
DIPDIP-6204N.
IntActQ14974. 53 interactions.
MINTMINT-94095.
STRING9606.ENSP00000290158.

PTM databases

PhosphoSiteQ14974.

Polymorphism databases

DMDM20981701.

Proteomic databases

PaxDbQ14974.
PeptideAtlasQ14974.
PRIDEQ14974.

Protocols and materials databases

DNASU3837.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290158; ENSP00000290158; ENSG00000108424.
GeneID3837.
KEGGhsa:3837.
UCSCuc002ilt.2. human.

Organism-specific databases

CTD3837.
GeneCardsGC17P045727.
HGNCHGNC:6400. KPNB1.
HPACAB034449.
HPA029878.
HPA050302.
MIM602738. gene.
neXtProtNX_Q14974.
PharmGKBPA30191.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5215.
HOGENOMHOG000204108.
HOVERGENHBG002369.
InParanoidQ14974.
KOK14293.
OMAHQKQASL.
OrthoDBEOG7GN2KZ.
PhylomeDBQ14974.
TreeFamTF105655.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_578. Apoptosis.
REACT_6900. Immune System.
SignaLinkQ14974.

Gene expression databases

ArrayExpressQ14974.
BgeeQ14974.
CleanExHS_KPNB1.
GenevestigatorQ14974.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR021133. HEAT_type_2.
IPR001494. Importin-beta_N.
IPR027140. KPNB1.
[Graphical view]
PANTHERPTHR10527:SF8. PTHR10527:SF8. 1 hit.
PfamPF00514. Arm. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view]
SMARTSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50077. HEAT_REPEAT. 1 hit.
PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKPNB1. human.
EvolutionaryTraceQ14974.
GeneWikiKPNB1.
GenomeRNAi3837.
NextBio15083.
PROQ14974.
SOURCESearch...

Entry information

Entry nameIMB1_HUMAN
AccessionPrimary (citable) accession number: Q14974
Secondary accession number(s): D3DTT3 expand/collapse secondary AC list , Q14637, Q53XN2, Q96J27
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 15, 2002
Last modified: April 16, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM