Q92973 (TNPO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transportin-1

Alternative name(s):
Importin beta-2
Karyopherin beta-2
M9 region interaction protein
Short name=MIP

Gene names

Name:	TNPO1
Synonyms:	KPNB2, MIP1, TRN

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	898 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin 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 the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. 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 By similarity. Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a RanGTP-dependent manner. Ref.7 Ref.9 Ref.10 Ref.13
Subunit structure	Binds HNRPA1, HNRPA2, HNRPDL, RPL23A, RPS7, RPL5, RAN and SRP19. Interacts with H2A, H2B, H3 and H4 histones. Binds to HIV-1 Rev. Interacts with isoform 5 of ADAR/ADAR1 (via DRBM 3 domain). Interacts with SNAI1 (via zinc fingers); the interaction mediates SNAI1 nuclear import. Interacts with SNAI2 (via zinc fingers). Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the importin beta family. Contains 8 HEAT repeats. Contains 1 importin N-terminal domain.
Sequence caution	The sequence AAC50723.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH40340.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Host-virus interaction Protein transport Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gene expression Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome protein import into nucleus, translocation Traceable author statement Ref.2. Source: ProtInc virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear pore Inferred from electronic annotation. Source: InterPro nucleus Traceable author statement Ref.2. Source: ProtInc
Molecular_function	nuclear localization sequence binding Traceable author statement Ref.1. Source: ProtInc protein transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	2	EBI-286693,EBI-401755
RAN	P62826	2	EBI-286693,EBI-286642

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92973-1)

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.

Isoform 2 (identifier: Q92973-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MVWDRQTKM → M

Isoform 3 (identifier: Q92973-3)

The sequence of this isoform differs from the canonical sequence as follows:
     69-118: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 898

898

Transportin-1

PRO_0000120765

Regions

Domain

41 – 109

69

Importin N-terminal

Repeat

132 – 169

38

HEAT 1

Repeat

178 – 215

38

HEAT 2

Repeat

219 – 256

38

HEAT 3

Repeat

401 – 438

38

HEAT 4

Repeat

442 – 479

38

HEAT 5

Repeat

484 – 521

38

HEAT 6

Repeat

568 – 607

40

HEAT 7

Repeat

671 – 708

38

HEAT 8

Compositional bias

358 – 376

19

Asp/Glu-rich (acidic)

Natural variations

Alternative sequence

1 – 9

9

MVWDRQTKM → M in isoform 2.

VSP_038028

Alternative sequence

69 – 118

50

Missing in isoform 3.

VSP_038029

Natural variant

34

1

D → E.
Corresponds to variant rs25661 [ dbSNP | Ensembl ].

VAR_014455

Experimental info

Sequence conflict

104

1

L → S in AAB68948. Ref.3

Sequence conflict

225

1

I → T in AAC50723. Ref.1

Sequence conflict

669

1

Q → L in AAB68948. Ref.3

Sequence conflict

880

1

F → L in BAG62638. Ref.4

Secondary structure

1

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898

Helix Strand Turn

Details...

Helix

17 – 30

14

Beta strand

31 – 33

3

Helix

35 – 48

14

Beta strand

49 – 51

3

Helix

52 – 63

12

Helix

70 – 83

14

Turn

84 – 86

3

Helix

88 – 90

3

Helix

93 – 104

12

Turn

105 – 108

4

Helix

112 – 128

17

Turn

129 – 133

5

Helix

137 – 145

9

Helix

147 – 149

3

Helix

150 – 167

18

Helix

170 – 173

4

Beta strand

175 – 178

4

Helix

180 – 187

8

Turn

188 – 192

5

Helix

196 – 207

12

Turn

208 – 213

6

Helix

215 – 218

4

Helix

221 – 232

12

Helix

237 – 253

17

Helix

255 – 258

4

Helix

259 – 261

3

Helix

262 – 273

12

Beta strand

275 – 277

3

Helix

278 – 291

14

Beta strand

294 – 296

3

Helix

297 – 301

5

Turn

302 – 304

3

Helix

305 – 315

11

Helix

320 – 327

8

Helix

340 – 342

3

Helix

367 – 370

4

Helix

383 – 398

16

Helix

399 – 402

4

Helix

403 – 414

12

Beta strand

416 – 418

3

Helix

419 – 431

13

Turn

432 – 436

5

Helix

437 – 440

4

Helix

441 – 443

3

Helix

444 – 454

11

Helix

460 – 472

13

Helix

474 – 479

6

Turn

482 – 485

4

Helix

486 – 497

12

Beta strand

498 – 500

3

Helix

502 – 519

18

Helix

520 – 526

7

Helix

527 – 540

14

Helix

543 – 560

18

Helix

561 – 564

4

Helix

567 – 583

17

Helix

591 – 605

15

Helix

606 – 612

7

Helix

613 – 636

24

Turn

638 – 640

3

Helix

647 – 663

17

Helix

664 – 667

4

Helix

668 – 672

5

Helix

676 – 683

8

Helix

689 – 705

17

Helix

707 – 709

3

Helix

711 – 713

3

Helix

714 – 723

10

Helix

727 – 729

3

Helix

730 – 747

18

Helix

748 – 755

8

Helix

756 – 766

11

Beta strand

768 – 770

3

Helix

773 – 789

17

Helix

791 – 794

4

Helix

795 – 797

3

Helix

798 – 810

13

Helix

816 – 831

16

Helix

833 – 835

3

Helix

837 – 839

3

Helix

840 – 848

9

Helix

855 – 880

26

Helix

881 – 883

3

Helix

886 – 894

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: 7B880D9E7CA6798F	FASTA	898	102,355
	10 20 30 40 50 60 MVWDRQTKME YEWKPDEQGL QQILQLLKES QSPDTTIQRT VQQKLEQLNQ YPDFNNYLIF 70 80 90 100 110 120 VLTKLKSEDE PTRSLSGLIL KNNVKAHFQN FPNGVTDFIK SECLNNIGDS SPLIRATVGI 130 140 150 160 170 180 LITTIASKGE LQNWPDLLPK LCSLLDSEDY NTCEGAFGAL QKICEDSAEI LDSDVLDRPL 190 200 210 220 230 240 NIMIPKFLQF FKHSSPKIRS HAVACVNQFI ISRTQALMLH IDSFIENLFA LAGDEEPEVR 250 260 270 280 290 300 KNVCRALVML LEVRMDRLLP HMHNIVEYML QRTQDQDENV ALEACEFWLT LAEQPICKDV 310 320 330 340 350 360 LVRHLPKLIP VLVNGMKYSD IDIILLKGDV EEDETIPDSE QDIRPRFHRS RTVAQQHDED 370 380 390 400 410 420 GIEEEDDDDD EIDDDDTISD WNLRKCSAAA LDVLANVYRD ELLPHILPLL KELLFHHEWV 430 440 450 460 470 480 VKESGILVLG AIAEGCMQGM IPYLPELIPH LIQCLSDKKA LVRSITCWTL SRYAHWVVSQ 490 500 510 520 530 540 PPDTYLKPLM TELLKRILDS NKRVQEAACS AFATLEEEAC TELVPYLAYI LDTLVFAFSK 550 560 570 580 590 600 YQHKNLLILY DAIGTLADSV GHHLNKPEYI QMLMPPLIQK WNMLKDEDKD LFPLLECLSS 610 620 630 640 650 660 VATALQSGFL PYCEPVYQRC VNLVQKTLAQ AMLNNAQPDQ YEAPDKDFMI VALDLLSGLA 670 680 690 700 710 720 EGLGGNIEQL VARSNILTLM YQCMQDKMPE VRQSSFALLG DLTKACFQHV KPCIADFMPI 730 740 750 760 770 780 LGTNLNPEFI SVCNNATWAI GEISIQMGIE MQPYIPMVLH QLVEIINRPN TPKTLLENTA 790 800 810 820 830 840 ITIGRLGYVC PQEVAPMLQQ FIRPWCTSLR NIRDNEEKDS AFRGICTMIS VNPSGVIQDF 850 860 870 880 890 IFFCDAVASW INPKDDLRDM FCKILHGFKN QVGDENWRRF SDQFPLPLKE RLAAFYGV
	Isoform 2 [UniParc]. Checksum: 4762DB4895472D10	FASTA	890	101,310
	10 20 30 40 50 60 MEYEWKPDEQ GLQQILQLLK ESQSPDTTIQ RTVQQKLEQL NQYPDFNNYL IFVLTKLKSE 70 80 90 100 110 120 DEPTRSLSGL ILKNNVKAHF QNFPNGVTDF IKSECLNNIG DSSPLIRATV GILITTIASK 130 140 150 160 170 180 GELQNWPDLL PKLCSLLDSE DYNTCEGAFG ALQKICEDSA EILDSDVLDR PLNIMIPKFL 190 200 210 220 230 240 QFFKHSSPKI RSHAVACVNQ FIISRTQALM LHIDSFIENL FALAGDEEPE VRKNVCRALV 250 260 270 280 290 300 MLLEVRMDRL LPHMHNIVEY MLQRTQDQDE NVALEACEFW LTLAEQPICK DVLVRHLPKL 310 320 330 340 350 360 IPVLVNGMKY SDIDIILLKG DVEEDETIPD SEQDIRPRFH RSRTVAQQHD EDGIEEEDDD 370 380 390 400 410 420 DDEIDDDDTI SDWNLRKCSA AALDVLANVY RDELLPHILP LLKELLFHHE WVVKESGILV 430 440 450 460 470 480 LGAIAEGCMQ GMIPYLPELI PHLIQCLSDK KALVRSITCW TLSRYAHWVV SQPPDTYLKP 490 500 510 520 530 540 LMTELLKRIL DSNKRVQEAA CSAFATLEEE ACTELVPYLA YILDTLVFAF SKYQHKNLLI 550 560 570 580 590 600 LYDAIGTLAD SVGHHLNKPE YIQMLMPPLI QKWNMLKDED KDLFPLLECL SSVATALQSG 610 620 630 640 650 660 FLPYCEPVYQ RCVNLVQKTL AQAMLNNAQP DQYEAPDKDF MIVALDLLSG LAEGLGGNIE 670 680 690 700 710 720 QLVARSNILT LMYQCMQDKM PEVRQSSFAL LGDLTKACFQ HVKPCIADFM PILGTNLNPE 730 740 750 760 770 780 FISVCNNATW AIGEISIQMG IEMQPYIPMV LHQLVEIINR PNTPKTLLEN TAITIGRLGY 790 800 810 820 830 840 VCPQEVAPML QQFIRPWCTS LRNIRDNEEK DSAFRGICTM ISVNPSGVIQ DFIFFCDAVA 850 860 870 880 890 SWINPKDDLR DMFCKILHGF KNQVGDENWR RFSDQFPLPL KERLAAFYGV
	Isoform 3 [UniParc]. Checksum: 6DF034D06DC572B4	FASTA	848	96,901
	10 20 30 40 50 60 MVWDRQTKME YEWKPDEQGL QQILQLLKES QSPDTTIQRT VQQKLEQLNQ YPDFNNYLIF 70 80 90 100 110 120 VLTKLKSEGI LITTIASKGE LQNWPDLLPK LCSLLDSEDY NTCEGAFGAL QKICEDSAEI 130 140 150 160 170 180 LDSDVLDRPL NIMIPKFLQF FKHSSPKIRS HAVACVNQFI ISRTQALMLH IDSFIENLFA 190 200 210 220 230 240 LAGDEEPEVR KNVCRALVML LEVRMDRLLP HMHNIVEYML QRTQDQDENV ALEACEFWLT 250 260 270 280 290 300 LAEQPICKDV LVRHLPKLIP VLVNGMKYSD IDIILLKGDV EEDETIPDSE QDIRPRFHRS 310 320 330 340 350 360 RTVAQQHDED GIEEEDDDDD EIDDDDTISD WNLRKCSAAA LDVLANVYRD ELLPHILPLL 370 380 390 400 410 420 KELLFHHEWV VKESGILVLG AIAEGCMQGM IPYLPELIPH LIQCLSDKKA LVRSITCWTL 430 440 450 460 470 480 SRYAHWVVSQ PPDTYLKPLM TELLKRILDS NKRVQEAACS AFATLEEEAC TELVPYLAYI 490 500 510 520 530 540 LDTLVFAFSK YQHKNLLILY DAIGTLADSV GHHLNKPEYI QMLMPPLIQK WNMLKDEDKD 550 560 570 580 590 600 LFPLLECLSS VATALQSGFL PYCEPVYQRC VNLVQKTLAQ AMLNNAQPDQ YEAPDKDFMI 610 620 630 640 650 660 VALDLLSGLA EGLGGNIEQL VARSNILTLM YQCMQDKMPE VRQSSFALLG DLTKACFQHV 670 680 690 700 710 720 KPCIADFMPI LGTNLNPEFI SVCNNATWAI GEISIQMGIE MQPYIPMVLH QLVEIINRPN 730 740 750 760 770 780 TPKTLLENTA ITIGRLGYVC PQEVAPMLQQ FIRPWCTSLR NIRDNEEKDS AFRGICTMIS 790 800 810 820 830 840 VNPSGVIQDF IFFCDAVASW INPKDDLRDM FCKILHGFKN QVGDENWRRF SDQFPLPLKE RLAAFYGV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel receptor-mediated nuclear protein import pathway." Pollard V.W., Michael W.M., Nakielny S., Siomi M.C., Wang F., Dreyfuss G. Cell 86:985-994(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Karyopherin beta2 mediates nuclear import of a mRNA binding protein." Bonifaci N., Moroianu J., Radu A., Blobel G. Proc. Natl. Acad. Sci. U.S.A. 94:5055-5060(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Liver.
[3]	Fridell R.A., Thorne L.W., Benson R.E., Cullen B.R. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[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 3). Tissue: Spleen.
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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.
[7]	"Transportin: nuclear transport receptor of a novel nuclear protein import pathway." Nakielny S., Siomi M.C., Siomi H., Michael W.M., Pollard V., Dreyfuss G. Exp. Cell Res. 229:261-266(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Molecular cloning of the cDNA encoding A + U-rich element RNA binding factor." Doi A., Shiosaka T., Takaoka Y., Yanagisawa K., Fujita S. Biochim. Biophys. Acta 1396:51-56(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HNRPDL.
[9]	"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 AND RPL5.
[10]	"Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin." Dean K.A., von Ahsen O., Goerlich D., Fried H.M. J. Cell Sci. 114:3479-3485(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SRP19.
[11]	"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.
[12]	"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: INTERACTION WITH SNAI1 AND SNAI2.
[13]	"RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1." Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., Jantsch M.F. Mol. Cell. Biol. 29:1487-1497(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ADAR.
[14]	"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].
[15]	"Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp." Chook Y.M., Blobel G. Nature 399:230-237(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH RAN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U70322 mRNA. Translation: AAC50723.1. Different initiation.
U72069 mRNA. Translation: AAB58254.1.
U72395 mRNA. Translation: AAB68948.1.
AK301021 mRNA. Translation: BAG62638.1.
BC040340 mRNA. Translation: AAH40340.1. Different initiation.

IPI

IPI00024364.
IPI00843876.
IPI00908817.

RefSeq

NP_002261.3. NM_002270.3.
NP_694858.1. NM_153188.2.

UniGene

Hs.482497.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QBK	X-ray	3.00	B	9-898	[»]
2H4M	X-ray	3.05	A/B	9-898	[»]
2OT8	X-ray	3.10	A/B	9-890	[»]
2QMR	X-ray	3.00	A/B/C/D	9-898	[»]
2Z5J	X-ray	3.40	A	9-890	[»]
2Z5K	X-ray	2.60	A	9-890	[»]
2Z5M	X-ray	3.00	A	9-890	[»]
2Z5N	X-ray	3.20	A	9-890	[»]
2Z5O	X-ray	3.20	A	9-890	[»]
4FDD	X-ray	2.30	A	9-898	[»]
4JLQ	X-ray	3.04	A	9-898	[»]

ProteinModelPortal

Q92973.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29335N.

IntAct

Q92973. 11 interactions.

MINT

MINT-94165.

STRING

9606.ENSP00000336712.

PTM databases

PhosphoSite

Q92973.

Polymorphism databases

DMDM

259016171.

Proteomic databases

PaxDb

Q92973.

PRIDE

Q92973.

Protocols and materials databases

DNASU

3842.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337273; ENSP00000336712; ENSG00000083312.
ENST00000454282; ENSP00000398524; ENSG00000083312.
ENST00000506351; ENSP00000425118; ENSG00000083312.
ENST00000523768; ENSP00000428899; ENSG00000083312.

GeneID

3842.

KEGG

hsa:3842.

UCSC

uc003kcg.4. human.
uc011csj.1. human.

Organism-specific databases

CTD

3842.

GeneCards

GC05P072148.

HGNC

HGNC:6401. TNPO1.

HPA

CAB016325.

MIM

602901. gene.

neXtProt

NX_Q92973.

PharmGKB

PA30192.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5215.

HOGENOM

HOG000203940.

HOVERGEN

HBG058963.

InParanoid

Q92973.

OMA

EEDIKPR.

OrthoDB

EOG4T4CTR.

Enzyme and pathway databases

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q92973.

Bgee

Q92973.

CleanEx

HS_TNPO1.

Genevestigator

Q92973.

GermOnline

ENSG00000083312. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 2 hits.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001494. Importin-beta_N.
[Graphical view]

Pfam

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. False negative.
PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TNPO1. human.

EvolutionaryTrace

Q92973.

GenomeRNAi

3842.

NextBio

15119.

SOURCE

Search...

Entry information

Entry name

TNPO1_HUMAN

Accession

Primary (citable) accession number: Q92973
Secondary accession number(s): B4DVC6, Q92957, Q92975

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 22, 2009
Last modified:	May 29, 2013
This is version 139 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.