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Protein

Transportin-1

Gene

TNPO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. organelle organization Source: Reactome
  3. protein import into nucleus, translocation Source: ProtInc
  4. 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.
REACT_268024. Intraflagellar transport.

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 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6401. TNPO1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleus Source: ProtInc
  5. primary cilium Source: Reactome
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

Keywords - PTMi

Acetylation

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. 47 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 – 3014Combined sources
Beta strandi31 – 333Combined sources
Helixi35 – 4814Combined sources
Beta strandi49 – 513Combined sources
Helixi52 – 6312Combined sources
Helixi70 – 8314Combined sources
Turni84 – 863Combined sources
Helixi88 – 903Combined sources
Helixi93 – 10412Combined sources
Turni105 – 1084Combined sources
Helixi112 – 12817Combined sources
Turni129 – 1335Combined sources
Beta strandi134 – 1363Combined sources
Helixi137 – 1459Combined sources
Helixi147 – 1493Combined sources
Helixi150 – 16718Combined sources
Helixi170 – 1734Combined sources
Beta strandi175 – 1784Combined sources
Helixi180 – 1878Combined sources
Turni188 – 1925Combined sources
Helixi196 – 20712Combined sources
Turni208 – 2136Combined sources
Helixi215 – 2184Combined sources
Helixi221 – 23212Combined sources
Helixi237 – 25317Combined sources
Helixi255 – 2584Combined sources
Helixi259 – 2613Combined sources
Helixi262 – 27312Combined sources
Beta strandi275 – 2773Combined sources
Helixi278 – 29114Combined sources
Beta strandi294 – 2963Combined sources
Helixi297 – 3015Combined sources
Turni302 – 3043Combined sources
Helixi305 – 31511Combined sources
Helixi320 – 3278Combined sources
Helixi340 – 3423Combined sources
Helixi367 – 3704Combined sources
Helixi383 – 39816Combined sources
Helixi399 – 4024Combined sources
Helixi403 – 41412Combined sources
Beta strandi416 – 4183Combined sources
Helixi419 – 43113Combined sources
Turni432 – 4365Combined sources
Helixi437 – 4404Combined sources
Helixi441 – 4433Combined sources
Helixi444 – 45411Combined sources
Helixi460 – 47213Combined sources
Helixi474 – 4796Combined sources
Turni482 – 4854Combined sources
Helixi486 – 49712Combined sources
Beta strandi498 – 5003Combined sources
Helixi502 – 51918Combined sources
Helixi520 – 5267Combined sources
Helixi527 – 54014Combined sources
Helixi543 – 56018Combined sources
Helixi561 – 5644Combined sources
Helixi567 – 58317Combined sources
Helixi591 – 60515Combined sources
Helixi606 – 6127Combined sources
Helixi613 – 63624Combined sources
Turni638 – 6403Combined sources
Helixi647 – 66317Combined sources
Helixi664 – 6674Combined sources
Helixi668 – 6725Combined sources
Helixi676 – 6838Combined sources
Helixi689 – 70517Combined sources
Helixi707 – 7093Combined sources
Helixi711 – 7133Combined sources
Helixi714 – 72310Combined sources
Helixi727 – 7293Combined sources
Helixi730 – 74718Combined sources
Helixi748 – 7558Combined sources
Helixi756 – 76611Combined sources
Beta strandi768 – 7703Combined sources
Helixi773 – 78917Combined sources
Helixi791 – 7944Combined sources
Helixi795 – 7973Combined sources
Helixi798 – 81013Combined sources
Helixi816 – 83116Combined sources
Helixi833 – 8353Combined sources
Helixi837 – 8393Combined sources
Helixi840 – 8489Combined sources
Helixi855 – 88026Combined sources
Helixi881 – 8833Combined sources
Helixi886 – 8949Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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
Repeati19 – 4628HEAT 11 PublicationAdd
BLAST
Domaini41 – 10969Importin N-terminalPROSITE-ProRule annotationAdd
BLAST
Repeati51 – 8939HEAT 21 PublicationAdd
BLAST
Repeati98 – 13134HEAT 31 PublicationAdd
BLAST
Repeati137 – 17438HEAT 41 PublicationAdd
BLAST
Repeati181 – 21131HEAT 51 PublicationAdd
BLAST
Repeati224 – 25128HEAT 61 PublicationAdd
BLAST
Repeati263 – 29028HEAT 71 PublicationAdd
BLAST
Repeati306 – 39792HEAT 81 PublicationAdd
BLAST
Repeati405 – 43329HEAT 91 PublicationAdd
BLAST
Repeati445 – 47228HEAT 101 PublicationAdd
BLAST
Repeati486 – 51934HEAT 111 PublicationAdd
BLAST
Repeati527 – 56034HEAT 121 PublicationAdd
BLAST
Repeati568 – 60639HEAT 131 PublicationAdd
BLAST
Repeati614 – 66552HEAT 141 PublicationAdd
BLAST
Repeati676 – 70732HEAT 151 PublicationAdd
BLAST
Repeati715 – 74834HEAT 161 PublicationAdd
BLAST
Repeati756 – 79136HEAT 171 PublicationAdd
BLAST
Repeati799 – 83234HEAT 181 PublicationAdd
BLAST
Repeati841 – 87232HEAT 191 PublicationAdd
BLAST
Repeati875 – 89521HEAT 201 PublicationAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 20 HEAT repeats.1 Publication
Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5215.
GeneTreeiENSGT00550000074720.
HOGENOMiHOG000203940.
HOVERGENiHBG058963.
InParanoidiQ92973.
KOiK18752.
OMAiQQHEEDG.
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. AlignAdd to basket

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

Note: Contains a N-acetylmethionine at position 1.2 Publications

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041L → S in AAB68948 (Ref. 3) Curated
Sequence conflicti225 – 2251I → T in AAC50723 (PubMed:8808633).Curated
Sequence conflicti669 – 6691Q → L in AAB68948 (Ref. 3) Curated
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi110040. 47 interactions.
DIPiDIP-29335N.
IntActiQ92973. 18 interactions.
MINTiMINT-94165.
STRINGi9606.ENSP00000336712.

PTM databases

PhosphoSiteiQ92973.

Polymorphism databases

DMDMi259016171.

Proteomic databases

MaxQBiQ92973.
PaxDbiQ92973.
PRIDEiQ92973.

Protocols and materials databases

DNASUi3842.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi3842.
GeneCardsiGC05P072148.
HGNCiHGNC:6401. TNPO1.
HPAiCAB016325.
MIMi602901. gene.
neXtProtiNX_Q92973.
PharmGKBiPA30192.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5215.
GeneTreeiENSGT00550000074720.
HOGENOMiHOG000203940.
HOVERGENiHBG058963.
InParanoidiQ92973.
KOiK18752.
OMAiQQHEEDG.
OrthoDBiEOG7XM2X0.
PhylomeDBiQ92973.
TreeFamiTF300825.

Enzyme and pathway databases

ReactomeiREACT_25064. Tristetraprolin (TTP) destabilizes mRNA.
REACT_268024. Intraflagellar transport.

Miscellaneous databases

ChiTaRSiTNPO1. human.
EvolutionaryTraceiQ92973.
GeneWikiiTransportin_1.
GenomeRNAii3842.
NextBioi15119.
PROiQ92973.
SOURCEiSearch...

Gene expression databases

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

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]
ProtoNetiSearch...

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(1995) [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(1996) [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 (SEP-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(2003) [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(2003) [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(2003) [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(1995) [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(1997) [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(1997) [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(2000) [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(2005) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), 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(2008) [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(2008) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), 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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH RAN, REPEAT STRUCTURE.

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: April 1, 2015
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.