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Q9Y5L0

- TNPO3_HUMAN

UniProt

Q9Y5L0 - TNPO3_HUMAN

Protein

Transportin-3

Gene

TNPO3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (15 Jan 2008)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    2. receptor activity Source: ProtInc

    GO - Biological processi

    1. splicing factor protein import into nucleus Source: UniProtKB

    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-SubCell
    2. intracellular membrane-bounded organelle Source: HPA
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    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

    Gene expression databases

    ArrayExpressiQ9Y5L0.
    BgeeiQ9Y5L0.
    CleanExiHS_TNPO3.
    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. 31 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 – 2013
    Helixi24 – 3916
    Beta strandi40 – 423
    Helixi43 – 5311
    Helixi57 – 7317
    Helixi75 – 773
    Helixi82 – 9615
    Turni97 – 1004
    Helixi102 – 11716
    Beta strandi121 – 1233
    Helixi125 – 1339
    Beta strandi134 – 1363
    Turni137 – 1393
    Helixi140 – 15213
    Helixi153 – 1553
    Turni157 – 1593
    Helixi163 – 18826
    Helixi195 – 21117
    Helixi216 – 2205
    Helixi223 – 23311
    Helixi239 – 25416
    Turni259 – 2624
    Helixi263 – 27412
    Helixi277 – 2859
    Helixi289 – 30517
    Helixi307 – 3126
    Helixi317 – 3193
    Helixi322 – 33110
    Helixi336 – 3394
    Helixi340 – 3423
    Helixi343 – 35513
    Helixi362 – 3643
    Helixi366 – 37914
    Beta strandi392 – 3943
    Helixi395 – 41016
    Helixi411 – 4133
    Helixi416 – 42510
    Turni426 – 4305
    Helixi434 – 44714
    Turni448 – 4503
    Helixi453 – 4553
    Helixi456 – 46712
    Helixi475 – 48713
    Helixi490 – 4945
    Helixi496 – 4983
    Helixi499 – 51012
    Helixi513 – 5153
    Helixi516 – 52914
    Turni535 – 5373
    Helixi538 – 5469
    Helixi547 – 5504
    Helixi555 – 56915
    Helixi574 – 59522
    Helixi609 – 62113
    Helixi635 – 65117
    Turni652 – 6543
    Helixi656 – 67318
    Turni675 – 6806
    Helixi681 – 69414
    Helixi698 – 71114
    Beta strandi712 – 7143
    Turni715 – 7173
    Helixi718 – 73720
    Helixi741 – 7444
    Helixi746 – 76217
    Helixi764 – 7685
    Beta strandi769 – 7713
    Helixi773 – 78311
    Helixi789 – 80315
    Helixi804 – 8063
    Helixi815 – 84228
    Helixi847 – 8493
    Helixi850 – 87728
    Helixi892 – 90312
    Helixi908 – 91912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 3-922.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG237172.
    HOGENOMiHOG000273876.
    HOVERGENiHBG057505.
    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

    MEGAKPTLQL VYQAVQALYH DPDPSGKERA SFWLGELQRS VHAWEISDQL    50
    LQIRQDVESC YFAAQTMKMK IQTSFYELPT DSHASLRDSL LTHIQNLKDL 100
    SPVIVTQLAL AIADLALQMP SWKGCVQTLV EKYSNDVTSL PFLLEILTVL 150
    PEEVHSRSLR IGANRRTEII EDLAFYSSTV VSLLMTCVEK AGTDEKMLMK 200
    VFRCLGSWFN LGVLDSNFMA NNKLLALLFE VLQQDKTSSN LHEAASDCVC 250
    SALYAIENVE TNLPLAMQLF QGVLTLETAY HMAVAREDLD KVLNYCRIFT 300
    ELCETFLEKI VCTPGQGLGD LRTLELLLIC AGHPQYEVVE ISFNFWYRLG 350
    EHLYKTNDEV IHGIFKAYIQ RLLHALARHC QLEPDHEGVP EETDDFGEFR 400
    MRVSDLVKDL IFLIGSMECF AQLYSTLKEG NPPWEVTEAV LFIMAAIAKS 450
    VDPENNPTLV EVLEGVVRLP ETVHTAVRYT SIELVGEMSE VVDRNPQFLD 500
    PVLGYLMKGL CEKPLASAAA KAIHNICSVC RDHMAQHFNG LLEIARSLDS 550
    FLLSPEAAVG LLKGTALVLA RLPLDKITEC LSELCSVQVM ALKKLLSQEP 600
    SNGISSDPTV FLDRLAVIFR HTNPIVENGQ THPCQKVIQE IWPVLSETLN 650
    KHRADNRIVE RCCRCLRFAV RCVGKGSAAL LQPLVTQMVN VYHVHQHSCF 700
    LYLGSILVDE YGMEEGCRQG LLDMLQALCI PTFQLLEQQN GLQNHPDTVD 750
    DLFRLATRFI QRSPVTLLRS QVVIPILQWA IASTTLDHRD ANCSVMRFLR 800
    DLIHTGVAND HEEDFELRKE LIGQVMNQLG QQLVSQLLHT CCFCLPPYTL 850
    PDVAEVLWEI MQVDRPTFCR WLENSLKGLP KETTVGAVTV THKQLTDFHK 900
    QVTSAEECKQ VCWALRDFTR LFR 923
    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.

    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

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 3-922.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117080. 31 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 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.
    HOGENOMi HOG000273876.
    HOVERGENi HBG057505.
    KOi K15436.
    OrthoDBi EOG718KC9.
    PhylomeDBi Q9Y5L0.
    TreeFami TF314539.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi Q9Y5L0.
    Bgeei Q9Y5L0.
    CleanExi HS_TNPO3.
    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

    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].

    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: October 1, 2014
    This is version 110 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3