Q14974 (IMB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	KPNB1
Synonyms:	NTF97

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	876 AA.
Sequence status	Complete.
Protein existence	Evidence 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.27
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.27 Ref.29 Ref.31
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 process	Host-virus interaction Protein transport Transport
Cellular component	Cytoplasm Nucleus
Domain	Repeat
PTM	ADP-ribosylation Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NLS-bearing substrate import into nucleus Traceable author statement Ref.2. Source: ProtInc apoptotic DNA fragmentation Traceable author statement. Source: Reactome cytokine-mediated signaling pathway Traceable author statement. Source: Reactome 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 viral infectious cycle Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear membrane Inferred from direct assay. Source: HPA nuclear pore Traceable author statement Ref.2. Source: ProtInc nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	nuclear localization sequence binding Traceable author statement Ref.2. Source: ProtInc protein transporter activity Inferred from electronic annotation. Source: Compara zinc ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERBB2	P04626	14	EBI-286758,EBI-641062
SMN2	Q16637-3	5	EBI-286758,EBI-395447
SMNDC1	O75940	2	EBI-286758,EBI-1052641

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 876

876

Importin subunit beta-1

PRO_0000120745

Regions

Domain

21 – 101

81

Importin N-terminal

Repeat

124 – 163

40

HEAT 1

Repeat

168 – 207

40

HEAT 2

Repeat

213 – 250

38

HEAT 3

Repeat

317 – 357

41

HEAT 4

Repeat

362 – 399

38

HEAT 5

Repeat

404 – 441

38

HEAT 6

Repeat

602 – 641

40

HEAT 7

Repeat

687 – 726

40

HEAT 8

Region

329 – 342

14

IAB-binding

Region

334 – 419

86

Ran-GTP binding

Compositional bias

337 – 341

5

Poly-Asp

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.7

Modified residue

12

1

Phosphoserine Ref.26

Modified residue

211

1

N6-acetyllysine; alternate Ref.28

Modified residue

835

1

N6-acetyllysine Ref.28

Modified residue

867

1

N6-acetyllysine Ref.28

Cross-link

206

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.24

Cross-link

211

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.24

Experimental info

Mutagenesis

178

1

I → A: Largely reduced binding to FxFG repeats and reduced nuclear import. Ref.33

Mutagenesis

178

1

I → F or D: Loss of binding to FxFG repeats and reduced nuclear import. Ref.33

Sequence conflict

97

1

Q → H in AAA82869. Ref.1

Sequence conflict

200

1

N → NA AA sequence Ref.6

Sequence conflict

863

1

T → R in AAA82869. Ref.1

Secondary structure

1

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876

Helix Strand Turn

Details...

Helix

3 – 9

7

Helix

15 – 45

31

Helix

51 – 65

15

Helix

70 – 81

12

Helix

85 – 98

14

Turn

99 – 101

3

Beta strand

104 – 106

3

Helix

109 – 120

12

Helix

121 – 123

3

Helix

129 – 138

10

Helix

144 – 160

17

Helix

163 – 165

3

Helix

167 – 169

3

Helix

170 – 181

12

Helix

188 – 201

14

Turn

202 – 205

4

Helix

206 – 209

4

Helix

212 – 225

14

Beta strand

228 – 230

3

Helix

231 – 247

17

Helix

249 – 251

3

Turn

253 – 259

7

Helix

260 – 269

10

Helix

273 – 297

25

Beta strand

303 – 305

3

Helix

314 – 329

16

Helix

330 – 332

3

Beta strand

335 – 337

3

Helix

344 – 358

15

Turn

359 – 362

4

Helix

363 – 374

12

Helix

380 – 392

13

Beta strand

394 – 397

4

Turn

399 – 402

4

Turn

404 – 408

5

Helix

409 – 415

7

Helix

416 – 418

3

Helix

422 – 438

17

Helix

439 – 442

4

Turn

446 – 448

3

Helix

449 – 457

9

Helix

464 – 483

20

Beta strand

487 – 493

7

Turn

500 – 502

3

Helix

503 – 513

11

Turn

517 – 520

4

Helix

521 – 523

3

Helix

524 – 537

14

Helix

541 – 543

3

Helix

544 – 562

19

Turn

563 – 566

4

Helix

573 – 592

20

Beta strand

593 – 595

3

Helix

597 – 601

5

Helix

604 – 614

11

Beta strand

619 – 622

4

Helix

623 – 639

17

Helix

640 – 646

7

Helix

647 – 660

14

Helix

664 – 681

18

Helix

682 – 685

4

Helix

686 – 700

15

Beta strand

703 – 705

3

Helix

707 – 709

3

Helix

710 – 724

15

Helix

725 – 731

7

Helix

732 – 743

12

Helix

752 – 777

26

Beta strand

779 – 782

4

Helix

785 – 789

5

Helix

791 – 793

3

Helix

794 – 805

12

Helix

812 – 829

18

Helix

832 – 838

7

Helix

841 – 852

12

Helix

856 – 873

18

Sequences

	Sequence		Length	Mass (Da)
	Q14974 [UniParc]. Last modified May 15, 2002. Version 2. Checksum: F3BB8B73E7E51639	FASTA	876	97,170
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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.
[28]	"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, MASS SPECTROMETRY.
[29]	"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.
[30]	"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].
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.

IPI

IPI00001639.

PIR

I52907.

RefSeq

NP_002256.2. NM_002265.5.

UniGene

Hs.532793.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q14974.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6204N.

IntAct

Q14974. 37 interactions.

MINT

MINT-94095.

STRING

9606.ENSP00000290158.

PTM databases

PhosphoSite

Q14974.

Polymorphism databases

DMDM

20981701.

Proteomic databases

PaxDb

Q14974.

PeptideAtlas

Q14974.

PRIDE

Q14974.

Protocols and materials databases

DNASU

3837.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000290158; ENSP00000290158; ENSG00000108424.

GeneID

3837.

KEGG

hsa:3837.

UCSC

uc002ilt.1. human.

Organism-specific databases

CTD

3837.

GeneCards

GC17P045727.

HGNC

HGNC:6400. KPNB1.

HPA

CAB034449.
HPA029878.

MIM

602738. gene.

neXtProt

NX_Q14974.

PharmGKB

PA30191.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5215.

HOGENOM

HOG000204108.

HOVERGEN

HBG002369.

InParanoid

Q14974.

KO

K14293.

OMA

IPEAAIN.

OrthoDB

EOG4RBQHX.

PhylomeDB

Q14974.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q14974.

Bgee

Q14974.

CleanEx

HS_KPNB1.

Genevestigator

Q14974.

GermOnline

ENSG00000108424. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 1 hit.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR021133. HEAT_type_2.
IPR001494. Importin-beta_N.
IPR027140. KPNB1.
[Graphical view]

PANTHER

PTHR10527:SF1. PTHR10527:SF1. 1 hit.

Pfam

PF00514. Arm. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view]

SMART

SM00913. IBN_N. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50077. HEAT_REPEAT. 1 hit.
PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1741199.

ChiTaRS

KPNB1. human.

EvolutionaryTrace

Q14974.

GenomeRNAi

3837.

NextBio

15083.

SOURCE

Search...

Entry information

Entry name

IMB1_HUMAN

Accession

Primary (citable) accession number: Q14974
Secondary accession number(s): D3DTT3 , Q14637, Q53XN2, Q96J27

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 15, 2002
Last modified:	May 1, 2013
This is version 146 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.