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Q9Y5L0

- TNPO3_HUMAN

UniProt

Q9Y5L0 - TNPO3_HUMAN

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Protein

Transportin-3

Gene

TNPO3

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

Functioni

Seems to function in nuclear protein import as nuclear transport receptor. In vitro, mediates the nuclear import of splicing factor SR proteins RBM4, SFRS1 and SFRS2, by recognizing phosphorylated RS domains.4 Publications

GO - Molecular functioni

  1. receptor activity Source: ProtInc

GO - Biological processi

  1. splicing factor protein import into nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Transportin-3
Alternative name(s):
Importin-12
Short name:
Imp12
Transportin-SR
Short name:
TRN-SR
Gene namesi
Name:TNPO3
Synonyms:IPO12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:17103. TNPO3.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. intracellular membrane-bounded organelle Source: HPA
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Limb-girdle muscular dystrophy 1F (LGMD1F) [MIM:608423]: An autosomal dominant myopathy characterized by proximal muscle weakness primarily affecting the lower limbs, but also affecting the upper limbs in most patients. Affected individuals also have distal muscle weakness of the hands and lower leg muscles. The disease has generally a benign clinical course but some individuals with childhood or juvenile onset manifest severe widespread myopathy, leading to wheelchair dependency and respiratory insufficiency. Muscle biopsy shows dystrophic changes with abnormal nuclei, rimmed vacuoles, and filamentous inclusions.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti818 – 8181R → P in LGMD1F. 1 Publication
VAR_071822

Keywords - Diseasei

Disease mutation, Limb-girdle muscular dystrophy

Organism-specific databases

MIMi608423. phenotype.
Orphaneti55595. Autosomal dominant limb-girdle muscular dystrophy type 1F.
186. Primary biliary cirrhosis.
PharmGKBiPA134888159.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 923923Transportin-3PRO_0000120781Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei896 – 8961Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y5L0.
PaxDbiQ9Y5L0.
PRIDEiQ9Y5L0.

PTM databases

PhosphoSiteiQ9Y5L0.

Expressioni

Tissue specificityi

Expressed in skeletal muscle.1 Publication

Gene expression databases

BgeeiQ9Y5L0.
CleanExiHS_TNPO3.
ExpressionAtlasiQ9Y5L0. baseline and differential.
GenevestigatoriQ9Y5L0.

Organism-specific databases

HPAiHPA039555.
HPA041537.

Interactioni

Subunit structurei

Interacts with phosphorylated SFRS1 and SFRS2. Interacts with NUP62 and RBM4.4 Publications

Protein-protein interaction databases

BioGridi117080. 46 interactions.
IntActiQ9Y5L0. 6 interactions.
MINTiMINT-1194798.
STRINGi9606.ENSP00000265388.

Structurei

Secondary structure

1
923
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2013Combined sources
Helixi24 – 3916Combined sources
Beta strandi40 – 423Combined sources
Helixi43 – 5311Combined sources
Helixi57 – 7317Combined sources
Helixi75 – 773Combined sources
Helixi82 – 9615Combined sources
Turni97 – 1004Combined sources
Helixi102 – 11716Combined sources
Beta strandi121 – 1233Combined sources
Helixi125 – 1339Combined sources
Beta strandi134 – 1363Combined sources
Turni137 – 1393Combined sources
Helixi140 – 15213Combined sources
Helixi153 – 1553Combined sources
Turni157 – 1593Combined sources
Helixi163 – 18826Combined sources
Helixi195 – 21117Combined sources
Helixi216 – 2205Combined sources
Helixi223 – 23311Combined sources
Helixi239 – 25416Combined sources
Turni259 – 2624Combined sources
Helixi263 – 27412Combined sources
Helixi277 – 2859Combined sources
Helixi289 – 30517Combined sources
Helixi307 – 3126Combined sources
Helixi317 – 3193Combined sources
Helixi322 – 33110Combined sources
Helixi336 – 3394Combined sources
Helixi340 – 3423Combined sources
Helixi343 – 35513Combined sources
Helixi362 – 3643Combined sources
Helixi366 – 37914Combined sources
Beta strandi392 – 3943Combined sources
Helixi395 – 41016Combined sources
Helixi411 – 4133Combined sources
Helixi416 – 42510Combined sources
Turni426 – 4305Combined sources
Helixi434 – 44714Combined sources
Turni448 – 4503Combined sources
Helixi453 – 4553Combined sources
Helixi456 – 46712Combined sources
Helixi475 – 48713Combined sources
Helixi490 – 4945Combined sources
Helixi496 – 4983Combined sources
Helixi499 – 51012Combined sources
Helixi513 – 5153Combined sources
Helixi516 – 52914Combined sources
Turni535 – 5373Combined sources
Helixi538 – 5469Combined sources
Helixi547 – 5504Combined sources
Helixi555 – 56915Combined sources
Helixi574 – 59522Combined sources
Helixi609 – 62113Combined sources
Helixi635 – 65117Combined sources
Turni652 – 6543Combined sources
Helixi656 – 67318Combined sources
Turni675 – 6806Combined sources
Helixi681 – 69414Combined sources
Helixi698 – 71114Combined sources
Beta strandi712 – 7143Combined sources
Turni715 – 7173Combined sources
Helixi718 – 73720Combined sources
Helixi741 – 7444Combined sources
Helixi746 – 76217Combined sources
Helixi764 – 7685Combined sources
Beta strandi769 – 7713Combined sources
Helixi773 – 78311Combined sources
Helixi789 – 80315Combined sources
Helixi804 – 8063Combined sources
Helixi815 – 84228Combined sources
Helixi847 – 8493Combined sources
Helixi850 – 87728Combined sources
Helixi892 – 90312Combined sources
Helixi908 – 91912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C0OX-ray2.56A/B1-923[»]
4C0PX-ray2.95A/B/C/D1-923[»]
4C0QX-ray3.42A/B1-923[»]
4OL0X-ray2.90B3-923[»]
ProteinModelPortaliQ9Y5L0.
SMRiQ9Y5L0. Positions 4-923.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiNOG237172.
GeneTreeiENSGT00530000063347.
HOGENOMiHOG000273876.
HOVERGENiHBG057505.
InParanoidiQ9Y5L0.
KOiK15436.
OrthoDBiEOG718KC9.
PhylomeDBiQ9Y5L0.
TreeFamiTF314539.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013598. Exportin-1/Importin-b-like.
[Graphical view]
PfamiPF08389. Xpo1. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: Q9Y5L0-2) [UniParc]FASTAAdd to Basket

Also known as: TRN-SR2

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
MEGAKPTLQL VYQAVQALYH DPDPSGKERA SFWLGELQRS VHAWEISDQL
60 70 80 90 100
LQIRQDVESC YFAAQTMKMK IQTSFYELPT DSHASLRDSL LTHIQNLKDL
110 120 130 140 150
SPVIVTQLAL AIADLALQMP SWKGCVQTLV EKYSNDVTSL PFLLEILTVL
160 170 180 190 200
PEEVHSRSLR IGANRRTEII EDLAFYSSTV VSLLMTCVEK AGTDEKMLMK
210 220 230 240 250
VFRCLGSWFN LGVLDSNFMA NNKLLALLFE VLQQDKTSSN LHEAASDCVC
260 270 280 290 300
SALYAIENVE TNLPLAMQLF QGVLTLETAY HMAVAREDLD KVLNYCRIFT
310 320 330 340 350
ELCETFLEKI VCTPGQGLGD LRTLELLLIC AGHPQYEVVE ISFNFWYRLG
360 370 380 390 400
EHLYKTNDEV IHGIFKAYIQ RLLHALARHC QLEPDHEGVP EETDDFGEFR
410 420 430 440 450
MRVSDLVKDL IFLIGSMECF AQLYSTLKEG NPPWEVTEAV LFIMAAIAKS
460 470 480 490 500
VDPENNPTLV EVLEGVVRLP ETVHTAVRYT SIELVGEMSE VVDRNPQFLD
510 520 530 540 550
PVLGYLMKGL CEKPLASAAA KAIHNICSVC RDHMAQHFNG LLEIARSLDS
560 570 580 590 600
FLLSPEAAVG LLKGTALVLA RLPLDKITEC LSELCSVQVM ALKKLLSQEP
610 620 630 640 650
SNGISSDPTV FLDRLAVIFR HTNPIVENGQ THPCQKVIQE IWPVLSETLN
660 670 680 690 700
KHRADNRIVE RCCRCLRFAV RCVGKGSAAL LQPLVTQMVN VYHVHQHSCF
710 720 730 740 750
LYLGSILVDE YGMEEGCRQG LLDMLQALCI PTFQLLEQQN GLQNHPDTVD
760 770 780 790 800
DLFRLATRFI QRSPVTLLRS QVVIPILQWA IASTTLDHRD ANCSVMRFLR
810 820 830 840 850
DLIHTGVAND HEEDFELRKE LIGQVMNQLG QQLVSQLLHT CCFCLPPYTL
860 870 880 890 900
PDVAEVLWEI MQVDRPTFCR WLENSLKGLP KETTVGAVTV THKQLTDFHK
910 920
QVTSAEECKQ VCWALRDFTR LFR
Length:923
Mass (Da):104,203
Last modified:January 15, 2008 - v3
Checksum:iCF7CDC14CDBA56AB
GO
Isoform 1 (identifier: Q9Y5L0-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     453-453: P → PKKPFSNAACHHSLLFGQNITSEISNCEYLPPVLR

Show »
Length:957
Mass (Da):108,001
Checksum:i6CDFAD0922CBA87F
GO
Isoform 3 (identifier: Q9Y5L0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     904-923: SAEECKQVCWALRDFTRLFR → RNVFFN

Note: No experimental confirmation available.

Show »
Length:909
Mass (Da):102,541
Checksum:i03F2BCEFA4FAA203
GO
Isoform 4 (identifier: Q9Y5L0-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     500-563: Missing.

Note: No experimental confirmation available.

Show »
Length:859
Mass (Da):97,372
Checksum:i52D04D72633709DC
GO

Sequence cautioni

The sequence AAD38537.1 differs from that shown. Reason: Frameshift at position 920. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871R → W in AAD38537. (PubMed:10366588)Curated
Sequence conflicti265 – 2651L → S in AK225999. 1 PublicationCurated
Sequence conflicti358 – 3581D → G in AK225999. 1 PublicationCurated
Sequence conflicti480 – 4801T → A in AK225999. 1 PublicationCurated
Sequence conflicti624 – 6241P → L in AK225999. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti818 – 8181R → P in LGMD1F. 1 Publication
VAR_071822

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei453 – 4531P → PKKPFSNAACHHSLLFGQNI TSEISNCEYLPPVLR in isoform 1. 1 PublicationVSP_030174
Alternative sequencei500 – 56364Missing in isoform 4. 1 PublicationVSP_045494Add
BLAST
Alternative sequencei904 – 92320SAEEC…TRLFR → RNVFFN in isoform 3. 1 PublicationVSP_011178Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF145029 mRNA. Translation: AAD38537.1. Frameshift.
AJ133769 mRNA. Translation: CAB42643.1.
AK225999 mRNA. No translation available.
AC018639 Genomic DNA. No translation available.
AC025594 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24106.1.
BC009221 mRNA. Translation: AAH09221.2.
CCDSiCCDS55162.1. [Q9Y5L0-5]
CCDS5809.1. [Q9Y5L0-2]
RefSeqiNP_001177957.2. NM_001191028.2. [Q9Y5L0-5]
NP_036602.1. NM_012470.3. [Q9Y5L0-2]
UniGeneiHs.193613.

Genome annotation databases

EnsembliENST00000265388; ENSP00000265388; ENSG00000064419. [Q9Y5L0-2]
ENST00000471234; ENSP00000418646; ENSG00000064419. [Q9Y5L0-5]
GeneIDi23534.
KEGGihsa:23534.
UCSCiuc003vol.2. human. [Q9Y5L0-2]

Polymorphism databases

DMDMi166215035.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF145029 mRNA. Translation: AAD38537.1 . Frameshift.
AJ133769 mRNA. Translation: CAB42643.1 .
AK225999 mRNA. No translation available.
AC018639 Genomic DNA. No translation available.
AC025594 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24106.1 .
BC009221 mRNA. Translation: AAH09221.2 .
CCDSi CCDS55162.1. [Q9Y5L0-5 ]
CCDS5809.1. [Q9Y5L0-2 ]
RefSeqi NP_001177957.2. NM_001191028.2. [Q9Y5L0-5 ]
NP_036602.1. NM_012470.3. [Q9Y5L0-2 ]
UniGenei Hs.193613.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4C0O X-ray 2.56 A/B 1-923 [» ]
4C0P X-ray 2.95 A/B/C/D 1-923 [» ]
4C0Q X-ray 3.42 A/B 1-923 [» ]
4OL0 X-ray 2.90 B 3-923 [» ]
ProteinModelPortali Q9Y5L0.
SMRi Q9Y5L0. Positions 4-923.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117080. 46 interactions.
IntActi Q9Y5L0. 6 interactions.
MINTi MINT-1194798.
STRINGi 9606.ENSP00000265388.

PTM databases

PhosphoSitei Q9Y5L0.

Polymorphism databases

DMDMi 166215035.

Proteomic databases

MaxQBi Q9Y5L0.
PaxDbi Q9Y5L0.
PRIDEi Q9Y5L0.

Protocols and materials databases

DNASUi 23534.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265388 ; ENSP00000265388 ; ENSG00000064419 . [Q9Y5L0-2 ]
ENST00000471234 ; ENSP00000418646 ; ENSG00000064419 . [Q9Y5L0-5 ]
GeneIDi 23534.
KEGGi hsa:23534.
UCSCi uc003vol.2. human. [Q9Y5L0-2 ]

Organism-specific databases

CTDi 23534.
GeneCardsi GC07M128594.
HGNCi HGNC:17103. TNPO3.
HPAi HPA039555.
HPA041537.
MIMi 608423. phenotype.
610032. gene.
neXtProti NX_Q9Y5L0.
Orphaneti 55595. Autosomal dominant limb-girdle muscular dystrophy type 1F.
186. Primary biliary cirrhosis.
PharmGKBi PA134888159.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG237172.
GeneTreei ENSGT00530000063347.
HOGENOMi HOG000273876.
HOVERGENi HBG057505.
InParanoidi Q9Y5L0.
KOi K15436.
OrthoDBi EOG718KC9.
PhylomeDBi Q9Y5L0.
TreeFami TF314539.

Miscellaneous databases

ChiTaRSi TNPO3. human.
GeneWikii Transportin-3.
GenomeRNAii 23534.
NextBioi 46030.
PROi Q9Y5L0.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5L0.
CleanExi HS_TNPO3.
ExpressionAtlasi Q9Y5L0. baseline and differential.
Genevestigatori Q9Y5L0.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013598. Exportin-1/Importin-b-like.
[Graphical view ]
Pfami PF08389. Xpo1. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Transportin-SR, a nuclear import receptor for SR proteins."
    Kataoka N., Bachorik J.L., Dreyfuss G.
    J. Cell Biol. 145:1145-1152(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SFRS1 AND SFRS2.
  2. "A human homologue of yeast Mtr10p and its role in nuclear protein import."
    Kutay U., Izaurralde E., Hartmann E., Goerlich D.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Colon.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-923 (ISOFORM 3).
    Tissue: Ovary.
  7. "A human importin-beta family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins."
    Lai M.-C., Lin R.-I., Huang S.-Y., Tsai C.-W., Tarn W.-Y.
    J. Biol. Chem. 275:7950-7957(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SFRS1, SUBCELLULAR LOCATION.
  8. "Transportin-SR2 mediates nuclear import of phosphorylated SR proteins."
    Lai M.-C., Lin R.-I., Tarn W.-Y.
    Proc. Natl. Acad. Sci. U.S.A. 98:10154-10159(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SFRS1 AND NUP62.
  9. "A novel splicing regulator shares a nuclear import pathway with SR proteins."
    Lai M.-C., Kuo H.-W., Chang W.-C., Tarn W.-Y.
    EMBO J. 22:1359-1369(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RBM4.
  10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-896, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: INVOLVEMENT IN LGMD1F, TISSUE SPECIFICITY, VARIANT LGMD1F PRO-818.

Entry informationi

Entry nameiTNPO3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5L0
Secondary accession number(s): A4D1K9
, C9IZM0, Q6NUM1, Q96G71, Q96GU9, Q9Y3R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 15, 2008
Last modified: November 26, 2014
This is version 112 of the entry and version 3 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 7
    Human chromosome 7: 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

External Data

Dasty 3