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Q92973 (TNPO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length898 AA.
Sequence statusComplete.
Protein existenceEvidence 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.14

Subunit structure

Binds HNRPA1, HNRPA2, HNRNPDL, RPL23A, RPS7, RPL5, RAN and SRP19. Interacts with H2A, H2B, H3 and H4 histones. Binds to HIV-1 Rev. Interacts with isoform 5of 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.13 Ref.14

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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 898898Transportin-1
PRO_0000120765

Regions

Domain41 – 10969Importin N-terminal
Repeat132 – 16938HEAT 1
Repeat178 – 21538HEAT 2
Repeat219 – 25638HEAT 3
Repeat401 – 43838HEAT 4
Repeat442 – 47938HEAT 5
Repeat484 – 52138HEAT 6
Repeat568 – 60740HEAT 7
Repeat671 – 70838HEAT 8
Compositional bias358 – 37619Asp/Glu-rich (acidic)

Natural variations

Alternative sequence1 – 99MVWDRQTKM → M in isoform 2.
VSP_038028
Alternative sequence69 – 11850Missing in isoform 3.
VSP_038029
Natural variant341D → E.
Corresponds to variant rs25661 [ dbSNP | Ensembl ].
VAR_014455

Experimental info

Sequence conflict1041L → S in AAB68948. Ref.3
Sequence conflict2251I → T in AAC50723. Ref.1
Sequence conflict6691Q → L in AAB68948. Ref.3
Sequence conflict8801F → L in BAG62638. Ref.4

Secondary structure

.................................................................................................................................. 898
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: 7B880D9E7CA6798F

FASTA898102,355
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 4762DB4895472D10
Show »

FASTA890101,310
Isoform 3 [UniParc].

Checksum: 6DF034D06DC572B4
Show »

FASTA84896,901

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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 HNRNPDL.
[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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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.
[14]"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.
[15]"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].
[16]"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].
[17]"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.
RefSeqNP_002261.3. NM_002270.3.
NP_694858.1. NM_153188.2.
XP_005248557.1. XM_005248500.1.
UniGeneHs.482497.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QBKX-ray3.00B9-898[»]
2H4MX-ray3.05A/B9-898[»]
2OT8X-ray3.10A/B9-890[»]
2QMRX-ray3.00A/B/C/D9-898[»]
2Z5JX-ray3.40A9-890[»]
2Z5KX-ray2.60A9-890[»]
2Z5MX-ray3.00A9-890[»]
2Z5NX-ray3.20A9-890[»]
2Z5OX-ray3.20A9-890[»]
4FDDX-ray2.30A9-898[»]
4FQ3X-ray3.00A9-898[»]
4JLQX-ray3.04A9-898[»]
4OO6X-ray2.70A375-898[»]
A9-331[»]
ProteinModelPortalQ92973.
SMRQ92973. Positions 11-897.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110040. 41 interactions.
DIPDIP-29335N.
IntActQ92973. 18 interactions.
MINTMINT-94165.
STRING9606.ENSP00000336712.

PTM databases

PhosphoSiteQ92973.

Polymorphism databases

DMDM259016171.

Proteomic databases

PaxDbQ92973.
PRIDEQ92973.

Protocols and materials databases

DNASU3842.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337273; ENSP00000336712; ENSG00000083312. [Q92973-1]
ENST00000454282; ENSP00000398524; ENSG00000083312. [Q92973-3]
ENST00000506351; ENSP00000425118; ENSG00000083312. [Q92973-2]
ENST00000523768; ENSP00000428899; ENSG00000083312. [Q92973-3]
GeneID3842.
KEGGhsa:3842.
UCSCuc003kcg.4. human. [Q92973-1]
uc011csj.1. human. [Q92973-3]

Organism-specific databases

CTD3842.
GeneCardsGC05P072148.
HGNCHGNC:6401. TNPO1.
HPACAB016325.
MIM602901. gene.
neXtProtNX_Q92973.
PharmGKBPA30192.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5215.
HOGENOMHOG000203940.
HOVERGENHBG058963.
InParanoidQ92973.
OMAEEDIKPR.
OrthoDBEOG7XM2X0.
PhylomeDBQ92973.
TreeFamTF300825.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ92973.
BgeeQ92973.
CleanExHS_TNPO1.
GenevestigatorQ92973.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001494. Importin-beta_N.
[Graphical view]
PfamPF03810. IBN_N. 1 hit.
[Graphical view]
SMARTSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNPO1. human.
EvolutionaryTraceQ92973.
GeneWikiTransportin_1.
GenomeRNAi3842.
NextBio15119.
PROQ92973.
SOURCESearch...

Entry information

Entry nameTNPO1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 147 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM