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Protein

Nucleoprotein TPR

Gene

Tpr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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. 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 (By similarity). Plays a role in the regulation of nuclear protein export.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiR-RNO-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-RNO-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-4570464. SUMOylation of RNA binding proteins.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5578749. Transcriptional regulation by small RNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoprotein TPR
Alternative name(s):
Megator
NPC-associated intranuclear protein
Translocated promoter region protein
Gene namesi
Name:Tpr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi1310664. Tpr.

Subcellular locationi

  • Nucleus By similarity
  • Nucleus membrane By similarity; Peripheral membrane protein By similarity; Nucleoplasmic side By similarity
  • Nucleus envelope By similarity
  • Nucleusnuclear pore complex 1 Publication
  • Cytoplasm By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Chromosomecentromerekinetochore By similarity
  • Nucleus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

  • 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 (By similarity). 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. Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore. Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic dynein complex Source: UniProtKB
  • extrinsic component of membrane Source: UniProtKB
  • kinetochore Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nuclear envelope Source: UniProtKB
  • nuclear inclusion body Source: UniProtKB
  • nuclear membrane Source: UniProtKB
  • nuclear periphery Source: UniProtKB
  • nuclear pore Source: UniProtKB
  • nuclear pore nuclear basket Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 23602359Nucleoprotein TPRPRO_0000422101Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity
Modified residuei312 – 3121N6-acetyllysineBy similarity
Modified residuei345 – 3451N6-acetyllysineBy similarity
Modified residuei379 – 3791PhosphoserineCombined sources
Modified residuei428 – 4281N6-acetyllysineBy similarity
Modified residuei457 – 4571N6-acetyllysineBy similarity
Modified residuei477 – 4771N6-acetyllysineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity
Modified residuei523 – 5231PhosphoserineBy similarity
Modified residuei632 – 6321PhosphoserineBy similarity
Modified residuei713 – 7131N6-acetyllysineBy similarity
Modified residuei723 – 7231N6-acetyllysineBy similarity
Modified residuei748 – 7481N6-acetyllysineBy similarity
Modified residuei755 – 7551N6-acetyllysineBy similarity
Modified residuei1180 – 11801PhosphoserineCombined sources
Modified residuei1185 – 11851PhosphoserineBy similarity
Modified residuei1689 – 16891N6-acetyllysineBy similarity
Modified residuei1691 – 16911PhosphothreonineBy similarity
Modified residuei1892 – 18921PhosphoserineBy similarity
Modified residuei2031 – 20311PhosphoserineBy similarity
Modified residuei2034 – 20341PhosphoserineBy similarity
Modified residuei2045 – 20451PhosphoserineBy similarity
Modified residuei2047 – 20471PhosphoserineBy similarity
Modified residuei2070 – 20701PhosphoserineBy similarity
Modified residuei2113 – 21131PhosphothreonineBy similarity
Modified residuei2134 – 21341PhosphothreonineBy similarity
Modified residuei2152 – 21521PhosphoserineCombined sources

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiF1MA98.

PTM databases

iPTMnetiF1MA98.

Expressioni

Gene expression databases

BgeeiENSRNOG00000002394.
GenevisibleiF1MA98. RN.

Interactioni

Subunit structurei

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 region and 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 IFI204 (via C-terminal region). Interacts with IFI203. Interacts with MTA1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiF1MA98. 1 interaction.
STRINGi10116.ENSRNOP00000062172.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 1311Sufficient for interaction with TPRBy similarityAdd
BLAST
Regioni14 – 117104Necessary for interaction with HSF1By similarityAdd
BLAST
Regioni437 – 51377Necessary for association to the NPCBy similarityAdd
BLAST
Regioni1218 – 1320103Necessary for interaction with HSF1By similarityAdd
BLAST
Regioni1811 – 186656Sufficient and essential for mediating its nuclear importBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili24 – 370347Sequence analysisAdd
BLAST
Coiled coili423 – 603181Sequence analysisAdd
BLAST
Coiled coili664 – 1172509Sequence analysisAdd
BLAST
Coiled coili1215 – 1420206Sequence analysisAdd
BLAST
Coiled coili1472 – 1629158Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1939 – 201072Asp-richAdd
BLAST
Compositional biasi2306 – 23094Poly-Ser

Domaini

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

Sequence similaritiesi

Belongs to the TPR family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4674. Eukaryota.
ENOG410XSA1. LUCA.
GeneTreeiENSGT00730000111014.
HOGENOMiHOG000139431.
InParanoidiF1MA98.
OMAiNRLLHDQ.
OrthoDBiEOG091G006U.

Family and domain databases

Gene3Di1.10.287.40. 1 hit.
InterProiIPR015866. Ser-tRNA-synth_1_N.
IPR012929. TPR/MLP1.
[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.

F1MA98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVLQQVLE RPELNKLPKS TQNKLEKFLA EQQSEIDCLK GRHEKFKVES
60 70 80 90 100
EQQYFEIEKR LSQSQERLVN ETRECQNLRL ELEKLNNQVK VLTEKNKELE
110 120 130 140 150
TAQDRNLGIQ SQFTRAKEEL EAEKRDLIRT NERLSQEVEY LTEDVKRLNE
160 170 180 190 200
KLKESNTTKG ELQLKLDELQ ASDVTVKYRE KRLEQEKELL HNQNSWLNTE
210 220 230 240 250
LKTKTDELLA LGREKGNEIL ELKCTLENKK EEVLRLEEQM NGLKTSNEHL
260 270 280 290 300
QKHVEDLLTK LKEAKEQQAS MEEKFHNELN AHIKLSNLYK SAADDSEAKS
310 320 330 340 350
NELTRAVDEL HKLLKEAGEA NKTIQDHLLQ VEESKDQMEK EMLEKIGKLE
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
VASLSAKLEQ AMKEIQRLQE DTDKANKHSS VLERDNQRME IQIKDLSQQI
510 520 530 540 550
RVLLMELEEA RGNHVIRDEE VSSADISSSS EVISQHLVSY RNIEELQQQN
560 570 580 590 600
QRLLFALREL GETREREEQE TTSSKIAELQ NKLENSLTEL EQLRESRQHQ
610 620 630 640 650
MQLVDSIVRQ RDMYRILLSQ TTGMAIPLQA SSLDDISLVS TPKRSSTSQT
660 670 680 690 700
VSTPAPEPII ESTETIEAKA ALKQLQEIFE NYKKEKMDSE KLQNEQLEKL
710 720 730 740 750
QEQVTDLRSQ NTKISTQLDF ASKRYEMLQD NVEGYRREIT SLQERNQKLT
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 DTEINLHLNT KELLKNAQKD
910 920 930 940 950
IATLKQHLNN MEAQLASQST QRTGKGQPGD RDDVDDLKSQ LRQAEEQVND
960 970 980 990 1000
LKERLKTSAS NVEQYRAMVT SLEDSLNKEK QVTEEVHKNI EVRLKESAEF
1010 1020 1030 1040 1050
QTQLEKKLME VEKEKQELQD DKRKAIESME QQLTELKKTL SSVQSEVQEA
1060 1070 1080 1090 1100
LQRASTALSN EQQARRDCQE QAKIAVEAQN KYERELMLHA ADVEALQAAK
1110 1120 1130 1140 1150
EQVSKMASVR QHLEETTQKA ESQLLECKAS WEERERVLKD EVSKSVSRCE
1160 1170 1180 1190 1200
DLEKQNRLLH DQIEKLSDKV VTSMKEVVQS PLNISLNEEG KSQEQILEIL
1210 1220 1230 1240 1250
RFIRREKEIA ETRFEVAQVE SLRYRQRVEL LERELQELQD SLNAEREKVQ
1260 1270 1280 1290 1300
VTAKTMAQHE ELMKKTETMN VVMETNKMLR EEKERLEQNL QQMQAKVRKL
1310 1320 1330 1340 1350
ELDILPLQEA NAELSEKSGM LQAEKKLLEE DVKRWKARNQ HLINQQKDPD
1360 1370 1380 1390 1400
TEEYRKLLSE KEIHTKRIQQ LNEEVGRLKA EIARSNASLT NNQNLIQSLK
1410 1420 1430 1440 1450
EDLSKVRTEK ESIQKDLDAK IIDIQEKVKT ITQVKKIGRR YKTQFEELKA
1460 1470 1480 1490 1500
QQKAMETSTQ SSGDHQEQHI SVQEMQELKD NLSQSETKTK SLEGQVENLQ
1510 1520 1530 1540 1550
KTLSEKETEA RSLQEQTAQL QSELSRLRQE LQDKTTKEEQ LRQQMNEKDE
1560 1570 1580 1590 1600
KTWKAITVAR SKIAHLSGVK DQLTKENEEL KQRNGALDQQ KDELDVRMTA
1610 1620 1630 1640 1650
LKSQYEGRIS RLERELREHQ ERHLEQRDEP QEPTNKAPEQ QRQITLKTTP
1660 1670 1680 1690 1700
ASGERGIAST SDPPTANIKP TPVVSTPSKV TAAAMAGNKS TPRASIRPMV
1710 1720 1730 1740 1750
TPATVTNPTT TPTATVMPTT QVESQEAMQS EGPVEHVPVF GSTSGSVRST
1760 1770 1780 1790 1800
SPNVQPSISQ PLLTVQQQTQ ATAFVQPTQQ SHPQIEPANQ ELSPNIVEVV
1810 1820 1830 1840 1850
QSSPVERPST STAVFGTVSA TPSSSLPKRA REEEEDSTIE AGDQVSDDTV
1860 1870 1880 1890 1900
EMPLPKKLKT VTPVGTEEEV MAEESTDGEA ETQTYNQDSQ DSIGEGVTQG
1910 1920 1930 1940 1950
DYTPMEDSEE TSQSLQIDLG PLQSDQQTTS SQDGQGKGDD VIVIDSDDED
1960 1970 1980 1990 2000
DDEENDGEHE DYEEDEDEDD DEEDDTGMGD EGEDSNEGTG SADGNDGYEA
2010 2020 2030 2040 2050
DDAEGGDGTD PGTETEESMG GAESNQRAAD SQNSGEGNTS AAESSFSQEV
2060 2070 2080 2090 2100
AREQQPTSAS ERQTPQAPQS PRRPPHPLPP RLTIHAPPQE LGPPVQRIQM
2110 2120 2130 2140 2150
TRRQSVGRGL QLTPGIGGMQ QHFFDDEDRT VPSTPTLVVP HRTDGFAEAI
2160 2170 2180 2190 2200
HSPQVAGVPR FRFGPPEDMP QTSSSHSDLG QLASQGGLGM YETPLFLAHE
2210 2220 2230 2240 2250
EESGGRSVPT TPLQVAAPVT VFTESTTSDA SEHASQSVPM VTTSTGTLST
2260 2270 2280 2290 2300
TNETPAGDDG DEVFVETESE GISSEAGLEI DSQQEEEPVQ ASDESDLPST
2310 2320 2330 2340 2350
SQDPPSSSSV DTSSSQPKPF RRVRLQTTLR QGVRGRQFNR QRGISHAMGG
2360
RGGINRGNIN
Length:2,360
Mass (Da):267,306
Last modified:May 3, 2011 - v1
Checksum:i8540034E08DAF079
GO

Sequence cautioni

The sequence AAI01884 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06075372 Genomic DNA. No translation available.
BC101883 mRNA. Translation: AAI01884.1. Sequence problems.
UniGeneiRn.58980.

Genome annotation databases

EnsembliENSRNOT00000063833; ENSRNOP00000062172; ENSRNOG00000002394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06075372 Genomic DNA. No translation available.
BC101883 mRNA. Translation: AAI01884.1. Sequence problems.
UniGeneiRn.58980.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiF1MA98. 1 interaction.
STRINGi10116.ENSRNOP00000062172.

PTM databases

iPTMnetiF1MA98.

Proteomic databases

PaxDbiF1MA98.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000063833; ENSRNOP00000062172; ENSRNOG00000002394.

Organism-specific databases

RGDi1310664. Tpr.

Phylogenomic databases

eggNOGiKOG4674. Eukaryota.
ENOG410XSA1. LUCA.
GeneTreeiENSGT00730000111014.
HOGENOMiHOG000139431.
InParanoidiF1MA98.
OMAiNRLLHDQ.
OrthoDBiEOG091G006U.

Enzyme and pathway databases

ReactomeiR-RNO-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-RNO-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-4570464. SUMOylation of RNA binding proteins.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5578749. Transcriptional regulation by small RNAs.

Miscellaneous databases

ChiTaRSiTpr. rat.
PROiF1MA98.

Gene expression databases

BgeeiENSRNOG00000002394.
GenevisibleiF1MA98. RN.

Family and domain databases

Gene3Di1.10.287.40. 1 hit.
InterProiIPR015866. Ser-tRNA-synth_1_N.
IPR012929. TPR/MLP1.
[Graphical view]
PfamiPF07926. TPR_MLP1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTPR_RAT
AccessioniPrimary (citable) accession number: F1MA98
Secondary accession number(s): Q3T1J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: May 3, 2011
Last modified: September 7, 2016
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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