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P12270

- TPR_HUMAN

UniProt

P12270 - TPR_HUMAN

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Protein

Nucleoprotein TPR

Gene

TPR

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

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 homodimerization activity Source: UniProtKB
  9. 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
Complete GO annotation...

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
Complete GO annotation...

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 – 3791Phosphoserine2 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 – 11851Phosphoserine5 Publications
Modified residuei1690 – 16901N6-acetyllysineBy similarity
Modified residuei1692 – 16921Phosphothreonine1 Publication
Modified residuei2048 – 20481Phosphoserine1 Publication
Modified residuei2050 – 20501Phosphoserine2 Publications
Modified residuei2073 – 20731Phosphoserine2 Publications
Modified residuei2155 – 21551Phosphoserine5 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

BgeeiP12270.
CleanExiHS_TPR.
ExpressionAtlasiP12270. baseline and differential.
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. 68 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.
GeneTreeiENSGT00730000111014.
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

        10         20         30         40         50
MAAVLQQVLE RTELNKLPKS VQNKLEKFLA DQQSEIDGLK GRHEKFKVES
60 70 80 90 100
EQQYFEIEKR LSHSQERLVN ETRECQSLRL ELEKLNNQLK ALTEKNKELE
110 120 130 140 150
IAQDRNIAIQ SQFTRTKEEL EAEKRDLIRT NERLSQELEY LTEDVKRLNE
160 170 180 190 200
KLKESNTTKG ELQLKLDELQ ASDVSVKYRE KRLEQEKELL HSQNTWLNTE
210 220 230 240 250
LKTKTDELLA LGREKGNEIL ELKCNLENKK EEVSRLEEQM NGLKTSNEHL
260 270 280 290 300
QKHVEDLLTK LKEAKEQQAS MEEKFHNELN AHIKLSNLYK SAADDSEAKS
310 320 330 340 350
NELTRAVEEL HKLLKEAGEA NKAIQDHLLE VEQSKDQMEK EMLEKIGRLE
360 370 380 390 400
KELENANDLL SATKRKGAIL SEEELAAMSP TAAAVAKIVK PGMKLTELYN
410 420 430 440 450
AYVETQDQLL LEKLENKRIN KYLDEIVKEV EAKAPILKRQ REEYERAQKA
460 470 480 490 500
VASLSVKLEQ AMKEIQRLQE DTDKANKQSS VLERDNRRME IQVKDLSQQI
510 520 530 540 550
RVLLMELEEA RGNHVIRDEE VSSADISSSS EVISQHLVSY RNIEELQQQN
560 570 580 590 600
QRLLVALREL GETREREEQE TTSSKITELQ LKLESALTEL EQLRKSRQHQ
610 620 630 640 650
MQLVDSIVRQ RDMYRILLSQ TTGVAIPLHA SSLDDVSLAS TPKRPSTSQT
660 670 680 690 700
VSTPAPVPVI ESTEAIEAKA ALKQLQEIFE NYKKEKAENE KIQNEQLEKL
710 720 730 740 750
QEQVTDLRSQ NTKISTQLDF ASKRYEMLQD NVEGYRREIT SLHERNQKLT
760 770 780 790 800
ATTQKQEQII NTMTQDLRGA NEKLAVAEVR AENLKKEKEM LKLSEVRLSQ
810 820 830 840 850
QRESLLAEQR GQNLLLTNLQ TIQGILERSE TETKQRLSSQ IEKLEHEISH
860 870 880 890 900
LKKKLENEVE QRHTLTRNLD VQLLDTKRQL DTETNLHLNT KELLKNAQKE
910 920 930 940 950
IATLKQHLSN MEVQVASQSS QRTGKGQPSN KEDVDDLVSQ LRQTEEQVND
960 970 980 990 1000
LKERLKTSTS NVEQYQAMVT SLEESLNKEK QVTEEVRKNI EVRLKESAEF
1010 1020 1030 1040 1050
QTQLEKKLME VEKEKQELQD DKRRAIESME QQLSELKKTL SSVQNEVQEA
1060 1070 1080 1090 1100
LQRASTALSN EQQARRDCQE QAKIAVEAQN KYERELMLHA ADVEALQAAK
1110 1120 1130 1140 1150
EQVSKMASVR QHLEETTQKA ESQLLECKAS WEERERMLKD EVSKCVCRCE
1160 1170 1180 1190 1200
DLEKQNRLLH DQIEKLSDKV VASVKEGVQG PLNVSLSEEG KSQEQILEIL
1210 1220 1230 1240 1250
RFIRREKEIA ETRFEVAQVE SLRYRQRVEL LERELQELQD SLNAEREKVQ
1260 1270 1280 1290 1300
VTAKTMAQHE ELMKKTETMN VVMETNKMLR EEKERLEQDL QQMQAKVRKL
1310 1320 1330 1340 1350
ELDILPLQEA NAELSEKSGM LQAEKKLLEE DVKRWKARNQ HLVSQQKDPD
1360 1370 1380 1390 1400
TEEYRKLLSE KEVHTKRIQQ LTEEIGRLKA EIARSNASLT NNQNLIQSLK
1410 1420 1430 1440 1450
EDLNKVRTEK ETIQKDLDAK IIDIQEKVKT ITQVKKIGRR YKTQYEELKA
1460 1470 1480 1490 1500
QQDKVMETSA QSSGDHQEQH VSVQEMQELK ETLNQAETKS KSLESQVENL
1510 1520 1530 1540 1550
QKTLSEKETE ARNLQEQTVQ LQSELSRLRQ DLQDRTTQEE QLRQQITEKE
1560 1570 1580 1590 1600
EKTRKAIVAA KSKIAHLAGV KDQLTKENEE LKQRNGALDQ QKDELDVRIT
1610 1620 1630 1640 1650
ALKSQYEGRI SRLERELREH QERHLEQRDE PQEPSNKVPE QQRQITLKTT
1660 1670 1680 1690 1700
PASGERGIAS TSDPPTANIK PTPVVSTPSK VTAAAMAGNK STPRASIRPM
1710 1720 1730 1740 1750
VTPATVTNPT TTPTATVMPT TQVESQEAMQ SEGPVEHVPV FGSTSGSVRS
1760 1770 1780 1790 1800
TSPNVQPSIS QPILTVQQQT QATAFVQPTQ QSHPQIEPAN QELSSNIVEV
1810 1820 1830 1840 1850
VQSSPVERPS TSTAVFGTVS ATPSSSLPKR TREEEEDSTI EASDQVSDDT
1860 1870 1880 1890 1900
VEMPLPKKLK SVTPVGTEEE VMAEESTDGE VETQVYNQDS QDSIGEGVTQ
1910 1920 1930 1940 1950
GDYTPMEDSE ETSQSLQIDL GPLQSDQQTT TSSQDGQGKG DDVIVIDSDD
1960 1970 1980 1990 2000
EEEDDDENDG EHEDYEEDEE DDDDDEDDTG MGDEGEDSNE GTGSADGNDG
2010 2020 2030 2040 2050
YEADDAEGGD GTDPGTETEE SMGGGEGNHR AADSQNSGEG NTGAAESSFS
2060 2070 2080 2090 2100
QEVSREQQPS SASERQAPRA PQSPRRPPHP LPPRLTIHAP PQELGPPVQR
2110 2120 2130 2140 2150
IQMTRRQSVG RGLQLTPGIG GMQQHFFDDE DRTVPSTPTL VVPHRTDGFA
2160 2170 2180 2190 2200
EAIHSPQVAG VPRFRFGPPE DMPQTSSSHS DLGQLASQGG LGMYETPLFL
2210 2220 2230 2240 2250
AHEEESGGRS VPTTPLQVAA PVTVFTESTT SDASEHASQS VPMVTTSTGT
2260 2270 2280 2290 2300
LSTTNETATG DDGDEVFVEA ESEGISSEAG LEIDSQQEEE PVQASDESDL
2310 2320 2330 2340 2350
PSTSQDPPSS SSVDTSSSQP KPFRRVRLQT TLRQGVRGRQ FNRQRGVSHA
2360
MGGRGGINRG NIN
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. 68 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 GC01M186286.
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.
GeneTreei ENSGT00730000111014.
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

Bgeei P12270.
CleanExi HS_TPR.
ExpressionAtlasi P12270. baseline and differential.
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

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  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 5:5153-5164(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 29, 2014
This is version 150 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

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