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Protein

Nucleoprotein TPR

Gene

Tpr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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. Plays a limited role in the regulation of nuclear protein export. 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).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-MMU-170822 Regulation of Glucokinase by Glucokinase Regulatory Protein
R-MMU-191859 snRNP Assembly
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-3301854 Nuclear Pore Complex (NPC) Disassembly
R-MMU-3371453 Regulation of HSF1-mediated heat shock response
R-MMU-4551638 SUMOylation of chromatin organization proteins
R-MMU-4615885 SUMOylation of DNA replication proteins
R-MMU-5578749 Transcriptional regulation by small RNAs

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoprotein TPR
Alternative name(s):
NPC-associated intranuclear protein
Translocated promoter region and nuclear basket protein
Gene namesi
Name:Tpr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1922066 Tpr

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004221001 – 2431Nucleoprotein TPRAdd BLAST2431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei326N6-acetyllysineBy similarity1
Modified residuei386N6-acetyllysineBy similarity1
Modified residuei419N6-acetyllysineBy similarity1
Modified residuei453PhosphoserineBy similarity1
Modified residuei502N6-acetyllysineBy similarity1
Modified residuei531N6-acetyllysineBy similarity1
Modified residuei551N6-acetyllysineCombined sources1
Modified residuei596PhosphoserineBy similarity1
Modified residuei597PhosphoserineBy similarity1
Modified residuei706PhosphoserineBy similarity1
Modified residuei787N6-acetyllysineCombined sources1
Modified residuei797N6-acetyllysineBy similarity1
Modified residuei822N6-acetyllysineCombined sources1
Modified residuei829N6-acetyllysineCombined sources1
Modified residuei1259PhosphoserineCombined sources1
Modified residuei1760N6-acetyllysineCombined sources1
Modified residuei1762PhosphothreonineBy similarity1
Modified residuei1963PhosphoserineBy similarity1
Modified residuei2102PhosphoserineBy similarity1
Modified residuei2105PhosphoserineBy similarity1
Modified residuei2116PhosphoserineBy similarity1
Modified residuei2118PhosphoserineBy similarity1
Modified residuei2141PhosphoserineCombined sources1
Modified residuei2174Omega-N-methylarginineCombined sources1
Modified residuei2179Omega-N-methylarginineCombined sources1
Modified residuei2184PhosphothreonineCombined sources1
Modified residuei2205PhosphothreonineBy similarity1
Modified residuei2223PhosphoserineCombined sources1
Modified residuei2231Omega-N-methylarginineCombined sources1
Modified residuei2411Asymmetric dimethylarginineCombined sources1
Modified residuei2413Asymmetric dimethylarginineCombined sources1
Modified residuei2422Asymmetric dimethylarginineCombined sources1

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, Methylation, Phosphoprotein

Proteomic databases

EPDiF6ZDS4
MaxQBiF6ZDS4
PaxDbiF6ZDS4
PeptideAtlasiF6ZDS4
PRIDEiF6ZDS4

PTM databases

iPTMnetiF6ZDS4
PhosphoSitePlusiF6ZDS4

Expressioni

Tissue specificityi

Expressed in the heart, liver, kidney, spleen, lung and skeletal muscles.1 Publication

Developmental stagei

Expressed both maternally and zygotically. Expressed at the mid two-cell stage and in the embryo at 7, 11, 15 and 17 dpc.1 Publication

Gene expression databases

BgeeiENSMUSG00000006005
ExpressionAtlasiF6ZDS4 baseline and differential
GenevisibleiF6ZDS4 MM

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 MTA1 (By similarity). Interacts with IFI204 (via C-terminal region). Interacts with IFI203.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi224509, 12 interactors
IntActiF6ZDS4, 3 interactors
MINTiF6ZDS4
STRINGi10090.ENSMUSP00000117616

Chemistry databases

BindingDBiF6ZDS4

Structurei

3D structure databases

SMRiF6ZDS4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni77 – 87Sufficient for interaction with TPRBy similarityAdd BLAST11
Regioni88 – 191Necessary for interaction with HSF1By similarityAdd BLAST104
Regioni511 – 587Necessary for association to the NPCBy similarityAdd BLAST77
Regioni1292 – 1394Necessary for interaction with HSF1By similarityAdd BLAST103
Regioni1882 – 1937Sufficient and essential for mediating its nuclear importBy similarityAdd BLAST56

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili98 – 444Sequence analysisAdd BLAST347
Coiled coili486 – 678Sequence analysisAdd BLAST193
Coiled coili736 – 1246Sequence analysisAdd BLAST511
Coiled coili1289 – 1494Sequence analysisAdd BLAST206
Coiled coili1547 – 1700Sequence analysisAdd BLAST154

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi33 – 77Ala-richAdd BLAST45
Compositional biasi2010 – 2081Asp-richAdd BLAST72

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
HOVERGENiHBG053916
InParanoidiF6ZDS4
KOiK09291
OMAiSENTRFR
OrthoDBiEOG091G006U
TreeFamiTF350364

Family and domain databases

InterProiView protein in InterPro
IPR012929 TPR/MLP1
PfamiView protein in Pfam
PF07926 TPR_MLP1_2, 1 hit

Sequencei

Sequence statusi: Complete.

F6ZDS4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSGGSASRS GHRGVPMTSR GFDGSRRGSL RRAGARETAS EAADGAAPAA
60 70 80 90 100
GLRASPCSLA SPSAAAAVAA IPADMAAVLQ QVLERPELNK LPKSTQNKLE
110 120 130 140 150
KFLAEQQSEI DCLKGRHEKF KVESEQQYFE IEKRLSQSQE RLVTETRECQ
160 170 180 190 200
NLRLELEKLN NQVKVLTEKT KELETAQDRN LGIQSQFTRA KEELEAEKRD
210 220 230 240 250
LIRTNERLSQ EVEYLTEDVK RLNEKLKESN TTKGELQLKL DELQASDVAV
260 270 280 290 300
KYREKRLEQE KELLHNQNSW LNTELKTKTD ELLALGREKG NEILELKCNL
310 320 330 340 350
ENKKEEVLRL EEQMNGLKTS NEHLQKHVED LLTKLKEAKE QQASMEEKFH
360 370 380 390 400
NELNAHIKLS NLYKSAADDS EAKSNELTRA VDELHKLLKE AGEANKTIQD
410 420 430 440 450
HLLQVEESKD QMEKEMLEKI GKLEKELENA NDLLSATKRK GAILSEEELA
460 470 480 490 500
AMSPTAAAVA KIVKPGMKLT ELYNAYVETQ DQLLLEKQEN KRINKYLDEI
510 520 530 540 550
VKEVEAKAPI LKRQREEYER AQKAVASLSA KLEQAMKEIQ RLQEDTDKAN
560 570 580 590 600
KHSSVLERDN QRMEIQIKDL SQQIRVLLME LEEARGNHVI RDEEVSSADI
610 620 630 640 650
SSSSEVISQH LVSYRNIEEL QQQNQRLLFA LRELGETRER EEQETTSSKI
660 670 680 690 700
AELQHKLENS LAELEQLRES RQHQMQLVDS IVRQRDMYRI LLSQTTGMAI
710 720 730 740 750
PLQASSLDDI SLLSTPKRSS TSQTVSTPAP EPVIDSTEAI EAKAALKQLQ
760 770 780 790 800
EIFENYKKEK IDSEKLQNEQ LEKLQEQVTD LRSQNTKIST QLDFASKRYE
810 820 830 840 850
MLQDNVEGYR REITSLQERN QKLTATTQKQ EQIINTMTQD LRGANEKLAV
860 870 880 890 900
AEVRAENLKK EKEMLKLSEV RLSQQRESLL AEQRGQNLLL TNLQTIQGIL
910 920 930 940 950
ERSETETKQR LNSQIEKLEH EISHLKKKLE NEVEQRHTLT RNLDVQLLDT
960 970 980 990 1000
KRQLDTEINL HLNTKELLKN AQKDIATLKQ HLNNMEAQLA SQSTQRTGKG
1010 1020 1030 1040 1050
QPGDRDDVDD LKSQLRQAEE QVNDLKERLK TSTSNVEQYR AMVTSLEDSL
1060 1070 1080 1090 1100
NKEKQVTEEV HKNIEVRLKE SAEFQTQLEK KLMEVEKEKQ ELQDDKRKAI
1110 1120 1130 1140 1150
ESMEQQLSEL KKTLSTVQNE VQEALQRAST ALSNEQQARR DCQEQAKIAV
1160 1170 1180 1190 1200
EAQNKYEREL MLHAADVEAL QAAKEQVSKM TSIRQHLEET TQKAESQLLE
1210 1220 1230 1240 1250
CKASWEERER VLKDEVSKSV SRCEDLEKQN RLLHDQIEKL SDKVVTSMKD
1260 1270 1280 1290 1300
AVQAPLNVSL NEEGKSQEQI LEILRFIRRE KEIAETRFEV AQVESLRYRQ
1310 1320 1330 1340 1350
RVELLERELQ ELQDSLNVER EKVQVTAKTM AQHEELMKKT ETMNVVMETN
1360 1370 1380 1390 1400
KMLREEKERL EQNLQQMQAK VRKLELDILP LQEANAELSE KSGMLQAEKK
1410 1420 1430 1440 1450
LLEEDVKRWK ARNQQLINQQ KDPDTEEYRK LLSEKEIHTK RIQQLNEEVG
1460 1470 1480 1490 1500
RLKAEIARSN ASLTNNQNLI QSLREDLSKA RTEKEGIQKD LDAKIIDIQE
1510 1520 1530 1540 1550
KVKTITQVKK IGRRYKTQFE ELKAQQNKAM ETSTQSSGDH QEQHISVQEM
1560 1570 1580 1590 1600
QELKDTLSQS ETKTKSLEGQ VENLQKTLSE KETEARSLQE QTVQLQSELS
1610 1620 1630 1640 1650
RLRQDLQDKT TEEQLRQQMN EKTWKTLALA KSKITHLSGV KDQLTKEIEE
1660 1670 1680 1690 1700
LKQRNGALDQ QKDELDVRMT ALKSQYEGRI SRLERELREH QERHLEQRDE
1710 1720 1730 1740 1750
PQEPTNKAPE QQRQITLKTT PASGERGIAS TSDPPTANIK PTPVVSTPSK
1760 1770 1780 1790 1800
VTAAAMAGNK STPRASIRPM VTPATVTNPT TTPTATVMPT TQVESQEAMQ
1810 1820 1830 1840 1850
SEGPVEHVPV FGNASGSVRS TSPNVQPSIS QPILTVQQQT QATAFVQPTQ
1860 1870 1880 1890 1900
QSHPQIEPTN QELSPNIVEV VQSSPVERPS TSTAVFGTVS ATPSSSLPKR
1910 1920 1930 1940 1950
TREEEEDSTM EAGDQVSEDT VEMPLPKKLK MVTPVGTEEE VMAEESTDGE
1960 1970 1980 1990 2000
AETQAYNQDS QDSIGEGVTQ GDYTPMEDSE ETSQSLQIDL GPLQSDQQTT
2010 2020 2030 2040 2050
SSQDGQGKGD DVIVIDSDDE DDDEENDGEH EDYEEDEDDD DDEEDDTGMG
2060 2070 2080 2090 2100
DEGEDSNEGT GSADGNDGYE ADDAEGGDGT DPGTETEESM GGAESHQRAA
2110 2120 2130 2140 2150
DSQNSGEGNT SAAESSFSQE VAREQQPTSA SERQTPQAPQ SPRRPPHPLP
2160 2170 2180 2190 2200
PRLTIHAPPQ ELGPPVQRIQ MTRRQSVGRG LQLTPGIGGM QQHFFDDEDR
2210 2220 2230 2240 2250
TVPSTPTLVV PHRTDGFAEA IHSPQVAGVP RFRFGPPEDM PQTSSSHSDL
2260 2270 2280 2290 2300
GQLASQGGLG MYETPLFLAH EEESGGRSVP TTPLQVAAPV TVFTESTTSD
2310 2320 2330 2340 2350
ASEHASQSVP MVTTSTGTLS TTNETAAGDD GDEVFVEAES EGISSEAGLE
2360 2370 2380 2390 2400
IDSQQEEEPV QASDESDLPS TSQDPPSSSS VDTSSSQPKP FRRVRLQTTL
2410 2420 2430
RQGVRGRQFN RQRGISHAMG GRGGINRGNI N
Length:2,431
Mass (Da):273,990
Last modified:April 18, 2012 - v1
Checksum:iD21CEA4F9C2C27C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC161432 Genomic DNA No translation available.
CH466520 Genomic DNA Translation: EDL39478.1
AJ298076 Genomic DNA Translation: CAC40701.1
AF490392 mRNA Translation: AAM03151.1
CCDSiCCDS35734.2
RefSeqiNP_598541.3, NM_133780.3
UniGeneiMm.174256

Genome annotation databases

EnsembliENSMUST00000124973; ENSMUSP00000117616; ENSMUSG00000006005
GeneIDi108989
KEGGimmu:108989
UCSCiuc007cyb.2 mouse

Similar proteinsi

Entry informationi

Entry nameiTPR_MOUSE
AccessioniPrimary (citable) accession number: F6ZDS4
Secondary accession number(s): Q8R4A0, Q921B9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: April 18, 2012
Last modified: May 23, 2018
This is version 58 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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