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P12270

- TPR_HUMAN

UniProt

P12270 - TPR_HUMAN

Protein

Nucleoprotein TPR

Gene

TPR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:22253824 and PubMed:11952838). Plays also a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases.11 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei191 – 1911Breakpoint for translocation to form TRK-T1

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. dynein complex binding Source: UniProtKB
    3. heat shock protein binding Source: UniProtKB
    4. mitogen-activated protein kinase binding Source: UniProtKB
    5. mRNA binding Source: UniProtKB
    6. nucleocytoplasmic transporter activity Source: UniProtKB
    7. poly(A) RNA binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein homodimerization activity Source: UniProtKB
    10. tubulin binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cellular response to heat Source: UniProtKB
    3. cellular response to interferon-alpha Source: UniProtKB
    4. cytokine-mediated signaling pathway Source: Reactome
    5. glucose transport Source: Reactome
    6. hexose transport Source: Reactome
    7. MAPK import into nucleus Source: UniProtKB
    8. mitotic cell cycle Source: Reactome
    9. mitotic nuclear division Source: UniProtKB-KW
    10. mitotic nuclear envelope disassembly Source: Reactome
    11. mitotic spindle assembly checkpoint Source: UniProtKB
    12. mRNA export from nucleus in response to heat stress Source: UniProtKB
    13. negative regulation of RNA export from nucleus Source: UniProtKB
    14. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    15. negative regulation of translational initiation Source: UniProtKB
    16. nuclear pore organization Source: UniProtKB
    17. positive regulation of heterochromatin assembly Source: UniProtKB
    18. positive regulation of intracellular protein transport Source: UniProtKB
    19. positive regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
    20. positive regulation of protein export from nucleus Source: UniProtKB
    21. positive regulation of protein import into nucleus Source: UniProtKB
    22. protein import into nucleus Source: ProtInc
    23. regulation of glucose transport Source: Reactome
    24. regulation of mitotic sister chromatid separation Source: UniProtKB
    25. regulation of spindle assembly involved in mitosis Source: UniProtKB
    26. response to epidermal growth factor Source: UniProtKB
    27. RNA export from nucleus Source: UniProtKB
    28. RNA import into nucleus Source: UniProtKB
    29. small molecule metabolic process Source: Reactome
    30. transmembrane transport Source: Reactome
    31. viral process Source: Reactome

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoprotein TPR
    Alternative name(s):
    Megator
    NPC-associated intranuclear protein
    Translocated promoter region protein
    Gene namesi
    Name:TPR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12017. TPR.

    Subcellular locationi

    Nucleus. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Nucleus envelope. Nucleusnuclear pore complex. Cytoplasm. Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Detected as discrete intranuclear foci with IFI204 By similarity. In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (PubMed:7798308). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. Reorganized during mitosis in a viscous and dynamic nuclear-derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase (PubMed:18981471). Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore (PubMed:19273613). Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle.By similarity3 Publications

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic dynein complex Source: UniProtKB
    3. extrinsic component of membrane Source: UniProtKB
    4. kinetochore Source: UniProtKB
    5. mitotic spindle Source: UniProtKB
    6. nuclear envelope Source: UniProtKB
    7. nuclear inclusion body Source: UniProtKB
    8. nuclear membrane Source: UniProtKB
    9. nuclear periphery Source: UniProtKB
    10. nuclear pore Source: UniProtKB
    11. nuclear pore nuclear basket Source: UniProtKB
    12. nucleoplasm Source: Reactome
    13. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Membrane, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Thyroid papillary carcinoma (TPC) [MIM:188550]: A common tumor of the thyroid that typically arises as an irregular, solid or cystic mass from otherwise normal thyroid tissue. Papillary carcinomas are malignant neoplasm characterized by the formation of numerous, irregular, finger-like projections of fibrous stroma that is covered with a surface layer of neoplastic epithelial cells.
    Note: The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving TPR has been found in thyroid papillary carcinomas. Intrachromosomal rearrangement that links the 5'-end of the TPR gene to the protein kinase domain of NTRK1 forms the fusion protein TRK-T1. TRK-T1 is a 55 kDa protein reacting with antibodies against the carboxy terminus of the NTRK1 protein.
    Involved in tumorigenic rearrangements with the MET or RAF genes.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi458 – 4581L → P: Diminishes association to NPC but not homodimerization. Inhibits association to NPC, interaction with NUP153 and nuclear membrane localization but not homodimerization; when associated with P-489. 2 Publications
    Mutagenesisi489 – 4891M → P: Diminishes association to NPC but not homodimerization. Inhibits association to NPC, interaction with NUP153 and nuclear membrane localization but not homodimerization; when associated with P-458. 2 Publications

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    MIMi188550. phenotype.
    Orphaneti146. Papillary or follicular thyroid carcinoma.
    PharmGKBiPA36696.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 23632362Nucleoprotein TPRPRO_0000204920Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei252 – 2521N6-acetyllysine1 Publication
    Modified residuei312 – 3121N6-acetyllysine1 Publication
    Modified residuei345 – 3451N6-acetyllysine1 Publication
    Modified residuei379 – 3791Phosphoserine3 Publications
    Modified residuei428 – 4281N6-acetyllysine1 Publication
    Modified residuei457 – 4571N6-acetyllysine1 Publication
    Modified residuei477 – 4771N6-acetyllysineBy similarity
    Modified residuei713 – 7131N6-acetyllysine1 Publication
    Modified residuei723 – 7231N6-acetyllysine1 Publication
    Modified residuei748 – 7481N6-acetyllysine1 Publication
    Modified residuei755 – 7551N6-acetyllysine1 Publication
    Modified residuei1185 – 11851Phosphoserine6 Publications
    Modified residuei1690 – 16901N6-acetyllysineBy similarity
    Modified residuei1692 – 16921Phosphothreonine2 Publications
    Modified residuei2048 – 20481Phosphoserine2 Publications
    Modified residuei2050 – 20501Phosphoserine3 Publications
    Modified residuei2073 – 20731Phosphoserine3 Publications
    Modified residuei2155 – 21551Phosphoserine6 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation occurs on serine and threonine residues (comprised in the C-terminal region) by MAPK1/ERK2 and stabilizes the interaction between these two proteins.10 Publications
    Proteolytically degraded after poliovirus (PV) infection; degradation is restricted to its unfolded C-terminal tail domain whereas its coiled-coil domain containing NCP- and NUP153-binding domains withstand degradation.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP12270.
    PaxDbiP12270.
    PRIDEiP12270.

    PTM databases

    PhosphoSiteiP12270.

    Miscellaneous databases

    PMAP-CutDBP12270.

    Expressioni

    Tissue specificityi

    Expressed in esophagus, ovary, liver, skin, smooth muscles, cerebrum and fetal cerebellum (at protein level). Highest in testis, lung, thymus, spleen and brain, lower levels in heart, liver and kidney.2 Publications

    Gene expression databases

    ArrayExpressiP12270.
    BgeeiP12270.
    CleanExiHS_TPR.
    GenevestigatoriP12270.

    Organism-specific databases

    HPAiHPA019661.
    HPA019663.
    HPA024336.

    Interactioni

    Subunit structurei

    Interacts with IFI204 (via C-terminal region). Interacts with IFI203 By similarity. Homodimer. Part of the nuclear pore complex (NPC). Associates with the XPO1/CRM1-mediated nuclear export complex, the Importin alpha/Importin beta receptor and the dynein 1 complex. Interacts (via C-terminal domain) with the KPNB1; the interaction occurs in a RanGTP-dependent manner. Interacts (via C-terminal regionand phosphorylated form) with MAPK1/ERK2 (via phosphorylated form); the interaction requires dimerization of MAPK1/ERK2 and increases following EGF stimulation. Interacts with MAPK3/ERK1; the interaction increases following EGF stimulation. Interacts (via coiled coil region) with NUP153; the interaction is direct. Interacts with HSF1; the interaction increases in a stress-responsive manner and stimulates export of stress-induced HSP70 mRNA. Interacts with huntingtin/HTT; the interaction is inhibited by aggregated huntingtin/HTT forms with expanded polyglutamine stretch. Interacts with MAD1L1 (via N-terminal region), MAD2L1, and TTK; the interactions occurs in a microtubule-independent manner. Interacts (via middle region) with DYNLL1. Interacts with DCTN1, dynein, NUP153 and tubulin. Interacts with MTA1.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAD1L1Q9Y6D92EBI-1048528,EBI-742610

    Protein-protein interaction databases

    BioGridi113028. 67 interactions.
    IntActiP12270. 13 interactions.
    MINTiMINT-4993169.
    STRINGi9606.ENSP00000356448.

    Structurei

    3D structure databases

    ProteinModelPortaliP12270.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni3 – 1311Sufficient for interaction with TPRAdd
    BLAST
    Regioni14 – 117104Necessary for interaction with HSF1Add
    BLAST
    Regioni437 – 51377Necessary for association to the NPCAdd
    BLAST
    Regioni1218 – 1320103Necessary for interaction with HSF1Add
    BLAST
    Regioni1812 – 186756Sufficient and essential for mediating its nuclear importAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili29 – 370342Sequence AnalysisAdd
    BLAST
    Coiled coili423 – 602180Sequence AnalysisAdd
    BLAST
    Coiled coili661 – 1173513Sequence AnalysisAdd
    BLAST
    Coiled coili1215 – 1630416Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi527 – 5304Poly-Ser
    Compositional biasi1833 – 18364Poly-Glu
    Compositional biasi1971 – 19788Poly-Asp
    Compositional biasi2309 – 23124Poly-Ser

    Domaini

    The N-terminal domain mediates intranuclear attachment to the nuclear pore complex. The C-terminal domain mediates its nuclear import.

    Sequence similaritiesi

    Belongs to the TPR family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000139431.
    HOVERGENiHBG009158.
    InParanoidiP12270.
    KOiK09291.
    OMAiECKASWE.
    OrthoDBiEOG7JQBMF.
    PhylomeDBiP12270.
    TreeFamiTF350364.

    Family and domain databases

    Gene3Di1.10.287.40. 1 hit.
    InterProiIPR015866. Ser-tRNA-synth_1_N.
    IPR012929. TPR_MLP1_2.
    [Graphical view]
    PfamiPF07926. TPR_MLP1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P12270-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVLQQVLE RTELNKLPKS VQNKLEKFLA DQQSEIDGLK GRHEKFKVES     50
    EQQYFEIEKR LSHSQERLVN ETRECQSLRL ELEKLNNQLK ALTEKNKELE 100
    IAQDRNIAIQ SQFTRTKEEL EAEKRDLIRT NERLSQELEY LTEDVKRLNE 150
    KLKESNTTKG ELQLKLDELQ ASDVSVKYRE KRLEQEKELL HSQNTWLNTE 200
    LKTKTDELLA LGREKGNEIL ELKCNLENKK EEVSRLEEQM NGLKTSNEHL 250
    QKHVEDLLTK LKEAKEQQAS MEEKFHNELN AHIKLSNLYK SAADDSEAKS 300
    NELTRAVEEL HKLLKEAGEA NKAIQDHLLE VEQSKDQMEK EMLEKIGRLE 350
    KELENANDLL SATKRKGAIL SEEELAAMSP TAAAVAKIVK PGMKLTELYN 400
    AYVETQDQLL LEKLENKRIN KYLDEIVKEV EAKAPILKRQ REEYERAQKA 450
    VASLSVKLEQ AMKEIQRLQE DTDKANKQSS VLERDNRRME IQVKDLSQQI 500
    RVLLMELEEA RGNHVIRDEE VSSADISSSS EVISQHLVSY RNIEELQQQN 550
    QRLLVALREL GETREREEQE TTSSKITELQ LKLESALTEL EQLRKSRQHQ 600
    MQLVDSIVRQ RDMYRILLSQ TTGVAIPLHA SSLDDVSLAS TPKRPSTSQT 650
    VSTPAPVPVI ESTEAIEAKA ALKQLQEIFE NYKKEKAENE KIQNEQLEKL 700
    QEQVTDLRSQ NTKISTQLDF ASKRYEMLQD NVEGYRREIT SLHERNQKLT 750
    ATTQKQEQII NTMTQDLRGA NEKLAVAEVR AENLKKEKEM LKLSEVRLSQ 800
    QRESLLAEQR GQNLLLTNLQ TIQGILERSE TETKQRLSSQ IEKLEHEISH 850
    LKKKLENEVE QRHTLTRNLD VQLLDTKRQL DTETNLHLNT KELLKNAQKE 900
    IATLKQHLSN MEVQVASQSS QRTGKGQPSN KEDVDDLVSQ LRQTEEQVND 950
    LKERLKTSTS NVEQYQAMVT SLEESLNKEK QVTEEVRKNI EVRLKESAEF 1000
    QTQLEKKLME VEKEKQELQD DKRRAIESME QQLSELKKTL SSVQNEVQEA 1050
    LQRASTALSN EQQARRDCQE QAKIAVEAQN KYERELMLHA ADVEALQAAK 1100
    EQVSKMASVR QHLEETTQKA ESQLLECKAS WEERERMLKD EVSKCVCRCE 1150
    DLEKQNRLLH DQIEKLSDKV VASVKEGVQG PLNVSLSEEG KSQEQILEIL 1200
    RFIRREKEIA ETRFEVAQVE SLRYRQRVEL LERELQELQD SLNAEREKVQ 1250
    VTAKTMAQHE ELMKKTETMN VVMETNKMLR EEKERLEQDL QQMQAKVRKL 1300
    ELDILPLQEA NAELSEKSGM LQAEKKLLEE DVKRWKARNQ HLVSQQKDPD 1350
    TEEYRKLLSE KEVHTKRIQQ LTEEIGRLKA EIARSNASLT NNQNLIQSLK 1400
    EDLNKVRTEK ETIQKDLDAK IIDIQEKVKT ITQVKKIGRR YKTQYEELKA 1450
    QQDKVMETSA QSSGDHQEQH VSVQEMQELK ETLNQAETKS KSLESQVENL 1500
    QKTLSEKETE ARNLQEQTVQ LQSELSRLRQ DLQDRTTQEE QLRQQITEKE 1550
    EKTRKAIVAA KSKIAHLAGV KDQLTKENEE LKQRNGALDQ QKDELDVRIT 1600
    ALKSQYEGRI SRLERELREH QERHLEQRDE PQEPSNKVPE QQRQITLKTT 1650
    PASGERGIAS TSDPPTANIK PTPVVSTPSK VTAAAMAGNK STPRASIRPM 1700
    VTPATVTNPT TTPTATVMPT TQVESQEAMQ SEGPVEHVPV FGSTSGSVRS 1750
    TSPNVQPSIS QPILTVQQQT QATAFVQPTQ QSHPQIEPAN QELSSNIVEV 1800
    VQSSPVERPS TSTAVFGTVS ATPSSSLPKR TREEEEDSTI EASDQVSDDT 1850
    VEMPLPKKLK SVTPVGTEEE VMAEESTDGE VETQVYNQDS QDSIGEGVTQ 1900
    GDYTPMEDSE ETSQSLQIDL GPLQSDQQTT TSSQDGQGKG DDVIVIDSDD 1950
    EEEDDDENDG EHEDYEEDEE DDDDDEDDTG MGDEGEDSNE GTGSADGNDG 2000
    YEADDAEGGD GTDPGTETEE SMGGGEGNHR AADSQNSGEG NTGAAESSFS 2050
    QEVSREQQPS SASERQAPRA PQSPRRPPHP LPPRLTIHAP PQELGPPVQR 2100
    IQMTRRQSVG RGLQLTPGIG GMQQHFFDDE DRTVPSTPTL VVPHRTDGFA 2150
    EAIHSPQVAG VPRFRFGPPE DMPQTSSSHS DLGQLASQGG LGMYETPLFL 2200
    AHEEESGGRS VPTTPLQVAA PVTVFTESTT SDASEHASQS VPMVTTSTGT 2250
    LSTTNETATG DDGDEVFVEA ESEGISSEAG LEIDSQQEEE PVQASDESDL 2300
    PSTSQDPPSS SSVDTSSSQP KPFRRVRLQT TLRQGVRGRQ FNRQRGVSHA 2350
    MGGRGGINRG NIN 2363
    Length:2,363
    Mass (Da):267,293
    Last modified:November 25, 2008 - v3
    Checksum:i01E669CBDC496772
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321Q → R in CAA44719. 1 PublicationCurated
    Sequence conflicti32 – 321Q → R in CAA68681. (PubMed:1532241)Curated
    Sequence conflicti779 – 7791V → I in AAB48030. (PubMed:9024684)Curated
    Sequence conflicti906 – 9061Q → R in AAB48030. (PubMed:9024684)Curated
    Sequence conflicti1239 – 12391Q → E in CAA47021. (PubMed:7798308)Curated
    Sequence conflicti1952 – 196514Missing in CAA47021. (PubMed:7798308)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti960 – 9601S → N.
    Corresponds to variant rs3753565 [ dbSNP | Ensembl ].
    VAR_020429
    Natural varianti1428 – 14281V → G.
    Corresponds to variant rs35550453 [ dbSNP | Ensembl ].
    VAR_047289
    Natural varianti1707 – 17071T → A.
    Corresponds to variant rs35766045 [ dbSNP | Ensembl ].
    VAR_047290

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66397 mRNA. Translation: CAA47021.1.
    U69668 mRNA. Translation: AAB48030.1.
    AL596220, AL133553 Genomic DNA. Translation: CAI13119.1.
    AL133553, AL596220 Genomic DNA. Translation: CAI17859.1.
    CH471067 Genomic DNA. Translation: EAW91205.1.
    X62947 mRNA. Translation: CAA44719.1. Different termination.
    Y00672 mRNA. Translation: CAA68681.1.
    CCDSiCCDS41446.1.
    PIRiS23741.
    RefSeqiNP_003283.2. NM_003292.2.
    UniGeneiHs.279640.

    Genome annotation databases

    EnsembliENST00000367478; ENSP00000356448; ENSG00000047410.
    GeneIDi7175.
    KEGGihsa:7175.
    UCSCiuc001grv.3. human.

    Polymorphism databases

    DMDMi215274208.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66397 mRNA. Translation: CAA47021.1 .
    U69668 mRNA. Translation: AAB48030.1 .
    AL596220 , AL133553 Genomic DNA. Translation: CAI13119.1 .
    AL133553 , AL596220 Genomic DNA. Translation: CAI17859.1 .
    CH471067 Genomic DNA. Translation: EAW91205.1 .
    X62947 mRNA. Translation: CAA44719.1 . Different termination.
    Y00672 mRNA. Translation: CAA68681.1 .
    CCDSi CCDS41446.1.
    PIRi S23741.
    RefSeqi NP_003283.2. NM_003292.2.
    UniGenei Hs.279640.

    3D structure databases

    ProteinModelPortali P12270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113028. 67 interactions.
    IntActi P12270. 13 interactions.
    MINTi MINT-4993169.
    STRINGi 9606.ENSP00000356448.

    PTM databases

    PhosphoSitei P12270.

    Polymorphism databases

    DMDMi 215274208.

    Proteomic databases

    MaxQBi P12270.
    PaxDbi P12270.
    PRIDEi P12270.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367478 ; ENSP00000356448 ; ENSG00000047410 .
    GeneIDi 7175.
    KEGGi hsa:7175.
    UCSCi uc001grv.3. human.

    Organism-specific databases

    CTDi 7175.
    GeneCardsi GC01M186282.
    HGNCi HGNC:12017. TPR.
    HPAi HPA019661.
    HPA019663.
    HPA024336.
    MIMi 188550. phenotype.
    189940. gene.
    neXtProti NX_P12270.
    Orphaneti 146. Papillary or follicular thyroid carcinoma.
    PharmGKBi PA36696.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000139431.
    HOVERGENi HBG009158.
    InParanoidi P12270.
    KOi K09291.
    OMAi ECKASWE.
    OrthoDBi EOG7JQBMF.
    PhylomeDBi P12270.
    TreeFami TF350364.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.

    Miscellaneous databases

    GenomeRNAii 7175.
    NextBioi 18907.
    PMAP-CutDB P12270.
    PROi P12270.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12270.
    Bgeei P12270.
    CleanExi HS_TPR.
    Genevestigatori P12270.

    Family and domain databases

    Gene3Di 1.10.287.40. 1 hit.
    InterProi IPR015866. Ser-tRNA-synth_1_N.
    IPR012929. TPR_MLP1_2.
    [Graphical view ]
    Pfami PF07926. TPR_MLP1_2. 1 hit.
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    Publicationsi

    1. "The human tpr gene encodes a protein of 2094 amino acids that has extensive coiled-coil regions and an acidic C-terminal domain."
      Mitchell P.J., Cooper C.S.
      Oncogene 7:2329-2333(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex."
      Byrd D.A., Sweet D.J., Pante N., Konstantinov K.N., Guan T., Saphire A.C.S., Mitchell P.J., Cooper C.S., Aebi U., Gerace L.
      J. Cell Biol. 127:1515-1526(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION, CHARACTERIZATION.
    3. "Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments."
      Cordes V.C., Reidenbach S., Rackwitz H.R., Franke W.W.
      J. Cell Biol. 136:515-529(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Embryonic brain.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "TRK-T1 is a novel oncogene formed by the fusion of TPR and TRK genes in human papillary thyroid carcinomas."
      Greco A., Pierotti M.A., Bongarzone I., Pagliardini S., Lanzi C., Della Porta G.
      Oncogene 7:237-242(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-191, CHROMOSOMAL REARRANGEMENT WITH NTRK1.
    7. "tpr homologues activate met and raf."
      King H.W.S., Tempest P.R., Merrifield K.R., Rance A.J.
      Oncogene 2:617-619(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-142.
    8. Cited for: PROTEIN SEQUENCE OF 2-11; 502-511; 1192-1201 AND 1421-1427, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma and Osteosarcoma.
    9. "Molecular segments of protein Tpr that confer nuclear targeting and association with the nuclear pore complex."
      Cordes V.C., Hase M.E., Muller L.
      Exp. Cell Res. 245:43-56(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NPC-BINDING DOMAIN AND NUCLEAR IMPORT DOMAIN.
    10. "Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA export."
      Bangs P., Burke B., Powers C., Craig R., Purohit A., Doxsey S.
      J. Cell Biol. 143:1801-1812(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NPC-BINDING DOMAIN AND NUCLEAR IMPORT DOMAIN, SUBCELLULAR LOCATION.
    11. "Amino acid substitutions of coiled-coil protein Tpr abrogate anchorage to the nuclear pore complex but not parallel, in-register homodimerization."
      Hase M.E., Kuznetsov N.V., Cordes V.C.
      Mol. Biol. Cell 12:2433-2452(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-458 AND MET-489.
    12. "The evolutionarily conserved single-copy gene for murine Tpr encodes one prevalent isoform in somatic cells and lacks paralogs in higher eukaryotes."
      Kuznetsov N.V., Sandblad L., Hase M.E., Hunziker A., Hergt M., Cordes V.C.
      Chromosoma 111:236-255(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    13. "Nucleocytoplasmic transport of proteins and poly(A)+ RNA in reconstituted Tpr-less nuclei in living mammalian cells."
      Shibata S., Matsuoka Y., Yoneda Y.
      Genes Cells 7:421-434(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
      Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
      J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex."
      Hase M.E., Cordes V.C.
      Mol. Biol. Cell 14:1923-1940(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSENCE OF FUNCTION IN ANCHORING NUCLEOPORINS, INTERACTION WITH NUP153, HOMODIMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-458 AND MET-489.
    16. "Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket."
      Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.
      Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX.
    17. "Polyglutamine expansion of huntingtin impairs its nuclear export."
      Cornett J., Cao F., Wang C.E., Ross C.A., Bates G.P., Li S.H., Li X.J.
      Nat. Genet. 37:198-204(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NUCLEAR PROTEIN EXPORT, INTERACTION WITH HTT.
    18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2073, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA."
      Skaggs H.S., Xing H., Wilkerson D.C., Murphy L.A., Hong Y., Mayhew C.N., Sarge K.D.
      J. Biol. Chem. 282:33902-33907(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN STRESS-INDUCED NUCLEAR MRNA EXPORT, INTERACTION WITH HSF1.
    21. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2050, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    23. "Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint."
      Lee S.H., Sterling H., Burlingame A., McCormick F.
      Genes Dev. 22:2926-2931(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAD2L1 AND MAD1L1, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    24. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites and docking domain on the nuclear pore complex protein Tpr cooperatively regulate ERK2-Tpr interaction."
      Vomastek T., Iwanicki M.P., Burack W.R., Tiwari D., Kumar D., Parsons J.T., Weber M.J., Nandicoori V.K.
      Mol. Cell. Biol. 28:6954-6966(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROTEIN IMPORT, INTERACTION WITH MAPK1, PHOSPHORYLATION BY MAPK1, SUBCELLULAR LOCATION.
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-1185; SER-2048 AND SER-2155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr."
      Ben-Efraim I., Frosst P.D., Gerace L.
      BMC Cell Biol. 10:74-74(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH XPO1/CRM1 AND IMPORTIN ALPHA/IMPORTIN BETA RECEPTOR, INTERACTION WITH KPNB1.
    29. "Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator."
      Lince-Faria M., Maffini S., Orr B., Ding Y., Florindo C., Sunkel C.E., Tavares A., Johansen J., Johansen K.M., Maiato H.
      J. Cell Biol. 184:647-657(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAD1L1; MAD2L1 AND TTK, SUBCELLULAR LOCATION.
    30. "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 SER-1185; SER-2050 AND SER-2155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    31. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252; LYS-312; LYS-345; LYS-428; LYS-457; LYS-713; LYS-723; LYS-748 AND LYS-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion."
      Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., Thyberg J., Cordes V.C.
      EMBO J. 29:1659-1673(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ORGANIZATION OF PERINUCLEAR CHROMATIN, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
    33. "Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis."
      Nakano H., Funasaka T., Hashizume C., Wong R.W.
      J. Biol. Chem. 285:10841-10849(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DCTN1; DYNEIN; DYNLL1; MAD2L1; NUP153 AND TUBULIN, SUBCELLULAR LOCATION.
    34. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-1185; THR-1692 AND SER-2155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "The Tpr protein regulates export of mRNAs with retained introns that traffic through the Nxf1 pathway."
      Coyle J.H., Bor Y.C., Rekosh D., Hammarskjold M.L.
      RNA 17:1344-1356(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UNSPLICED RNA EXPORT.
    37. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185 AND SER-2073, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA."
      Rajanala K., Nandicoori V.K.
      PLoS ONE 7:E29921-E29921(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UNSPLICED RNA EXPORT, INTERACTION WITH MAPK1, SUBCELLULAR LOCATION.
    40. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "The subcellular distribution and function of MTA1 in cancer differentiation."
      Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C., Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.
      Oncotarget 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MTA1.

    Entry informationi

    Entry nameiTPR_HUMAN
    AccessioniPrimary (citable) accession number: P12270
    Secondary accession number(s): Q15655, Q5SWY0, Q99968
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 149 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3