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Q92973

- TNPO1_HUMAN

UniProt

Q92973 - TNPO1_HUMAN

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Protein

Transportin-1

Gene

TNPO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity4 Publications

GO - Molecular functioni

  1. nuclear localization sequence binding Source: ProtInc
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA metabolic process Source: Reactome
  3. protein import into nucleus, translocation Source: ProtInc
  4. RNA metabolic process Source: Reactome
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Transportin-1
Alternative name(s):
Importin beta-2
Karyopherin beta-2
M9 region interaction protein
Short name:
MIP
Gene namesi
Name:TNPO1
Synonyms:KPNB2, MIP1, TRN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:6401. TNPO1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30192.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 898898Transportin-1PRO_0000120765Add
BLAST

Proteomic databases

MaxQBiQ92973.
PaxDbiQ92973.
PRIDEiQ92973.

PTM databases

PhosphoSiteiQ92973.

Expressioni

Gene expression databases

BgeeiQ92973.
CleanExiHS_TNPO1.
ExpressionAtlasiQ92973. baseline and differential.
GenevestigatoriQ92973.

Organism-specific databases

HPAiCAB016325.

Interactioni

Subunit structurei

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 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).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P629932EBI-286693,EBI-401755
RANP628262EBI-286693,EBI-286642

Protein-protein interaction databases

BioGridi110040. 44 interactions.
DIPiDIP-29335N.
IntActiQ92973. 18 interactions.
MINTiMINT-94165.
STRINGi9606.ENSP00000336712.

Structurei

Secondary structure

1
898
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 3014
Beta strandi31 – 333
Helixi35 – 4814
Beta strandi49 – 513
Helixi52 – 6312
Helixi70 – 8314
Turni84 – 863
Helixi88 – 903
Helixi93 – 10412
Turni105 – 1084
Helixi112 – 12817
Turni129 – 1335
Beta strandi134 – 1363
Helixi137 – 1459
Helixi147 – 1493
Helixi150 – 16718
Helixi170 – 1734
Beta strandi175 – 1784
Helixi180 – 1878
Turni188 – 1925
Helixi196 – 20712
Turni208 – 2136
Helixi215 – 2184
Helixi221 – 23212
Helixi237 – 25317
Helixi255 – 2584
Helixi259 – 2613
Helixi262 – 27312
Beta strandi275 – 2773
Helixi278 – 29114
Beta strandi294 – 2963
Helixi297 – 3015
Turni302 – 3043
Helixi305 – 31511
Helixi320 – 3278
Helixi340 – 3423
Helixi367 – 3704
Helixi383 – 39816
Helixi399 – 4024
Helixi403 – 41412
Beta strandi416 – 4183
Helixi419 – 43113
Turni432 – 4365
Helixi437 – 4404
Helixi441 – 4433
Helixi444 – 45411
Helixi460 – 47213
Helixi474 – 4796
Turni482 – 4854
Helixi486 – 49712
Beta strandi498 – 5003
Helixi502 – 51918
Helixi520 – 5267
Helixi527 – 54014
Helixi543 – 56018
Helixi561 – 5644
Helixi567 – 58317
Helixi591 – 60515
Helixi606 – 6127
Helixi613 – 63624
Turni638 – 6403
Helixi647 – 66317
Helixi664 – 6674
Helixi668 – 6725
Helixi676 – 6838
Helixi689 – 70517
Helixi707 – 7093
Helixi711 – 7133
Helixi714 – 72310
Helixi727 – 7293
Helixi730 – 74718
Helixi748 – 7558
Helixi756 – 76611
Beta strandi768 – 7703
Helixi773 – 78917
Helixi791 – 7944
Helixi795 – 7973
Helixi798 – 81013
Helixi816 – 83116
Helixi833 – 8353
Helixi837 – 8393
Helixi840 – 8489
Helixi855 – 88026
Helixi881 – 8833
Helixi886 – 8949

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QBKX-ray3.00B9-898[»]
2H4MX-ray3.05A/B376-898[»]
A/B9-343[»]
2OT8X-ray3.10A/B9-331[»]
A/B375-898[»]
2QMRX-ray3.00A/B/C/D9-898[»]
2Z5JX-ray3.40A9-898[»]
2Z5KX-ray2.60A9-898[»]
2Z5MX-ray3.00A9-898[»]
2Z5NX-ray3.20A9-898[»]
2Z5OX-ray3.20A9-898[»]
4FDDX-ray2.30A9-331[»]
A375-898[»]
4FQ3X-ray3.00A9-898[»]
4JLQX-ray3.05A9-331[»]
A375-898[»]
4OO6X-ray2.70A375-898[»]
A9-331[»]
ProteinModelPortaliQ92973.
SMRiQ92973. Positions 11-897.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92973.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 10969Importin N-terminalPROSITE-ProRule annotationAdd
BLAST
Repeati132 – 16938HEAT 1Add
BLAST
Repeati178 – 21538HEAT 2Add
BLAST
Repeati219 – 25638HEAT 3Add
BLAST
Repeati401 – 43838HEAT 4Add
BLAST
Repeati442 – 47938HEAT 5Add
BLAST
Repeati484 – 52138HEAT 6Add
BLAST
Repeati568 – 60740HEAT 7Add
BLAST
Repeati671 – 70838HEAT 8Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi358 – 37619Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5215.
GeneTreeiENSGT00550000074720.
HOGENOMiHOG000203940.
HOVERGENiHBG058963.
InParanoidiQ92973.
OMAiEEDIKPR.
OrthoDBiEOG7XM2X0.
PhylomeDBiQ92973.
TreeFamiTF300825.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92973-1) [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
MVWDRQTKME YEWKPDEQGL QQILQLLKES QSPDTTIQRT VQQKLEQLNQ
60 70 80 90 100
YPDFNNYLIF VLTKLKSEDE PTRSLSGLIL KNNVKAHFQN FPNGVTDFIK
110 120 130 140 150
SECLNNIGDS SPLIRATVGI LITTIASKGE LQNWPDLLPK LCSLLDSEDY
160 170 180 190 200
NTCEGAFGAL QKICEDSAEI LDSDVLDRPL NIMIPKFLQF FKHSSPKIRS
210 220 230 240 250
HAVACVNQFI ISRTQALMLH IDSFIENLFA LAGDEEPEVR KNVCRALVML
260 270 280 290 300
LEVRMDRLLP HMHNIVEYML QRTQDQDENV ALEACEFWLT LAEQPICKDV
310 320 330 340 350
LVRHLPKLIP VLVNGMKYSD IDIILLKGDV EEDETIPDSE QDIRPRFHRS
360 370 380 390 400
RTVAQQHDED GIEEEDDDDD EIDDDDTISD WNLRKCSAAA LDVLANVYRD
410 420 430 440 450
ELLPHILPLL KELLFHHEWV VKESGILVLG AIAEGCMQGM IPYLPELIPH
460 470 480 490 500
LIQCLSDKKA LVRSITCWTL SRYAHWVVSQ PPDTYLKPLM TELLKRILDS
510 520 530 540 550
NKRVQEAACS AFATLEEEAC TELVPYLAYI LDTLVFAFSK YQHKNLLILY
560 570 580 590 600
DAIGTLADSV GHHLNKPEYI QMLMPPLIQK WNMLKDEDKD LFPLLECLSS
610 620 630 640 650
VATALQSGFL PYCEPVYQRC VNLVQKTLAQ AMLNNAQPDQ YEAPDKDFMI
660 670 680 690 700
VALDLLSGLA EGLGGNIEQL VARSNILTLM YQCMQDKMPE VRQSSFALLG
710 720 730 740 750
DLTKACFQHV KPCIADFMPI LGTNLNPEFI SVCNNATWAI GEISIQMGIE
760 770 780 790 800
MQPYIPMVLH QLVEIINRPN TPKTLLENTA ITIGRLGYVC PQEVAPMLQQ
810 820 830 840 850
FIRPWCTSLR NIRDNEEKDS AFRGICTMIS VNPSGVIQDF IFFCDAVASW
860 870 880 890
INPKDDLRDM FCKILHGFKN QVGDENWRRF SDQFPLPLKE RLAAFYGV
Length:898
Mass (Da):102,355
Last modified:September 22, 2009 - v2
Checksum:i7B880D9E7CA6798F
GO
Isoform 2 (identifier: Q92973-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:890
Mass (Da):101,310
Checksum:i4762DB4895472D10
GO
Isoform 3 (identifier: Q92973-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:848
Mass (Da):96,901
Checksum:i6DF034D06DC572B4
GO

Sequence cautioni

The sequence AAC50723.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAH40340.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041L → S in AAB68948. 1 PublicationCurated
Sequence conflicti225 – 2251I → T in AAC50723. (PubMed:8808633)Curated
Sequence conflicti669 – 6691Q → L in AAB68948. 1 PublicationCurated
Sequence conflicti880 – 8801F → L in BAG62638. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341D → E.
Corresponds to variant rs25661 [ dbSNP | Ensembl ].
VAR_014455

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99MVWDRQTKM → M in isoform 2. 2 PublicationsVSP_038028
Alternative sequencei69 – 11850Missing in isoform 3. 1 PublicationVSP_038029Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4016.1. [Q92973-2]
CCDS43329.1. [Q92973-1]
RefSeqiNP_002261.3. NM_002270.3. [Q92973-1]
NP_694858.1. NM_153188.2. [Q92973-2]
XP_005248557.1. XM_005248500.1. [Q92973-2]
UniGeneiHs.482497.

Genome annotation databases

EnsembliENST00000337273; ENSP00000336712; ENSG00000083312. [Q92973-1]
ENST00000506351; ENSP00000425118; ENSG00000083312. [Q92973-2]
ENST00000523768; ENSP00000428899; ENSG00000083312. [Q92973-3]
GeneIDi3842.
KEGGihsa:3842.
UCSCiuc003kcg.4. human. [Q92973-1]
uc011csj.1. human. [Q92973-3]

Polymorphism databases

DMDMi259016171.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS4016.1. [Q92973-2 ]
CCDS43329.1. [Q92973-1 ]
RefSeqi NP_002261.3. NM_002270.3. [Q92973-1 ]
NP_694858.1. NM_153188.2. [Q92973-2 ]
XP_005248557.1. XM_005248500.1. [Q92973-2 ]
UniGenei Hs.482497.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QBK X-ray 3.00 B 9-898 [» ]
2H4M X-ray 3.05 A/B 376-898 [» ]
A/B 9-343 [» ]
2OT8 X-ray 3.10 A/B 9-331 [» ]
A/B 375-898 [» ]
2QMR X-ray 3.00 A/B/C/D 9-898 [» ]
2Z5J X-ray 3.40 A 9-898 [» ]
2Z5K X-ray 2.60 A 9-898 [» ]
2Z5M X-ray 3.00 A 9-898 [» ]
2Z5N X-ray 3.20 A 9-898 [» ]
2Z5O X-ray 3.20 A 9-898 [» ]
4FDD X-ray 2.30 A 9-331 [» ]
A 375-898 [» ]
4FQ3 X-ray 3.00 A 9-898 [» ]
4JLQ X-ray 3.05 A 9-331 [» ]
A 375-898 [» ]
4OO6 X-ray 2.70 A 375-898 [» ]
A 9-331 [» ]
ProteinModelPortali Q92973.
SMRi Q92973. Positions 11-897.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110040. 44 interactions.
DIPi DIP-29335N.
IntActi Q92973. 18 interactions.
MINTi MINT-94165.
STRINGi 9606.ENSP00000336712.

PTM databases

PhosphoSitei Q92973.

Polymorphism databases

DMDMi 259016171.

Proteomic databases

MaxQBi Q92973.
PaxDbi Q92973.
PRIDEi Q92973.

Protocols and materials databases

DNASUi 3842.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337273 ; ENSP00000336712 ; ENSG00000083312 . [Q92973-1 ]
ENST00000506351 ; ENSP00000425118 ; ENSG00000083312 . [Q92973-2 ]
ENST00000523768 ; ENSP00000428899 ; ENSG00000083312 . [Q92973-3 ]
GeneIDi 3842.
KEGGi hsa:3842.
UCSCi uc003kcg.4. human. [Q92973-1 ]
uc011csj.1. human. [Q92973-3 ]

Organism-specific databases

CTDi 3842.
GeneCardsi GC05P072148.
HGNCi HGNC:6401. TNPO1.
HPAi CAB016325.
MIMi 602901. gene.
neXtProti NX_Q92973.
PharmGKBi PA30192.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5215.
GeneTreei ENSGT00550000074720.
HOGENOMi HOG000203940.
HOVERGENi HBG058963.
InParanoidi Q92973.
OMAi EEDIKPR.
OrthoDBi EOG7XM2X0.
PhylomeDBi Q92973.
TreeFami TF300825.

Enzyme and pathway databases

Reactomei REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

ChiTaRSi TNPO1. human.
EvolutionaryTracei Q92973.
GeneWikii Transportin_1.
GenomeRNAii 3842.
NextBioi 15119.
PROi Q92973.
SOURCEi Search...

Gene expression databases

Bgeei Q92973.
CleanExi HS_TNPO1.
ExpressionAtlasi Q92973. baseline and differential.
Genevestigatori Q92973.

Family and domain databases

Gene3Di 1.25.10.10. 2 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001494. Importin-beta_N.
[Graphical view ]
Pfami PF03810. IBN_N. 1 hit.
[Graphical view ]
SMARTi SM00913. IBN_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 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. 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.

Entry informationi

Entry nameiTNPO1_HUMAN
AccessioniPrimary (citable) accession number: Q92973
Secondary accession number(s): B4DVC6, Q92957, Q92975
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 22, 2009
Last modified: October 29, 2014
This is version 153 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3