Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nucleoprotein TPR

Gene

Tpr

Organism
Mus musculus (Mouse)
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. 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

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiR-MMU-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-MMU-4570464. SUMOylation of RNA binding 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1922066. Tpr.

Subcellular locationi

  • Nucleus By similarity
  • Nucleus membrane By similarity; Peripheral membrane protein By similarity; Nucleoplasmic side By similarity
  • Nucleus envelope 2 Publications
  • Nucleusnuclear pore complex By similarity1 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
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Chemistry

ChEMBLiCHEMBL3038516.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24312431Nucleoprotein TPRPRO_0000422100Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei326 – 3261N6-acetyllysineBy similarity
Modified residuei386 – 3861N6-acetyllysineBy similarity
Modified residuei419 – 4191N6-acetyllysineBy similarity
Modified residuei453 – 4531PhosphoserineBy similarity
Modified residuei502 – 5021N6-acetyllysineBy similarity
Modified residuei531 – 5311N6-acetyllysineBy similarity
Modified residuei551 – 5511N6-acetyllysineCombined sources
Modified residuei596 – 5961PhosphoserineBy similarity
Modified residuei597 – 5971PhosphoserineBy similarity
Modified residuei706 – 7061PhosphoserineBy similarity
Modified residuei787 – 7871N6-acetyllysineCombined sources
Modified residuei797 – 7971N6-acetyllysineBy similarity
Modified residuei822 – 8221N6-acetyllysineCombined sources
Modified residuei829 – 8291N6-acetyllysineCombined sources
Modified residuei1259 – 12591PhosphoserineCombined sources
Modified residuei1760 – 17601N6-acetyllysineCombined sources
Modified residuei1762 – 17621PhosphothreonineBy similarity
Modified residuei1963 – 19631PhosphoserineBy similarity
Modified residuei2116 – 21161PhosphoserineBy similarity
Modified residuei2118 – 21181PhosphoserineBy similarity
Modified residuei2141 – 21411PhosphoserineCombined sources
Modified residuei2184 – 21841PhosphothreonineCombined sources
Modified residuei2223 – 22231PhosphoserineCombined 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

EPDiF6ZDS4.
MaxQBiF6ZDS4.
PaxDbiF6ZDS4.
PRIDEiF6ZDS4.

PTM databases

iPTMnetiF6ZDS4.

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

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. 10 interactions.
IntActiF6ZDS4. 1 interaction.
MINTiMINT-4119134.
STRINGi10090.ENSMUSP00000117616.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni77 – 8711Sufficient for interaction with TPRBy similarityAdd
BLAST
Regioni88 – 191104Necessary for interaction with HSF1By similarityAdd
BLAST
Regioni511 – 58777Necessary for association to the NPCBy similarityAdd
BLAST
Regioni1292 – 1394103Necessary for interaction with HSF1By similarityAdd
BLAST
Regioni1882 – 193756Sufficient and essential for mediating its nuclear importBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili98 – 444347Sequence analysisAdd
BLAST
Coiled coili486 – 678193Sequence analysisAdd
BLAST
Coiled coili736 – 1246511Sequence analysisAdd
BLAST
Coiled coili1289 – 1494206Sequence analysisAdd
BLAST
Coiled coili1547 – 1700154Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi33 – 7745Ala-richAdd
BLAST
Compositional biasi2010 – 208172Asp-richAdd
BLAST

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.
OMAiNRLLHDQ.
OrthoDBiEOG7JQBMF.
TreeFamiTF350364.

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.

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.

Cross-referencesi

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.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224509. 10 interactions.
IntActiF6ZDS4. 1 interaction.
MINTiMINT-4119134.
STRINGi10090.ENSMUSP00000117616.

Chemistry

ChEMBLiCHEMBL3038516.

PTM databases

iPTMnetiF6ZDS4.

Proteomic databases

EPDiF6ZDS4.
MaxQBiF6ZDS4.
PaxDbiF6ZDS4.
PRIDEiF6ZDS4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7175.
MGIiMGI:1922066. Tpr.

Phylogenomic databases

eggNOGiKOG4674. Eukaryota.
ENOG410XSA1. LUCA.
GeneTreeiENSGT00730000111014.
HOVERGENiHBG053916.
InParanoidiF6ZDS4.
KOiK09291.
OMAiNRLLHDQ.
OrthoDBiEOG7JQBMF.
TreeFamiTF350364.

Enzyme and pathway databases

ReactomeiR-MMU-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-MMU-4570464. SUMOylation of RNA binding proteins.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5578749. Transcriptional regulation by small RNAs.

Miscellaneous databases

ChiTaRSiTpr. mouse.
NextBioi361556.
PROiF6ZDS4.
SOURCEiSearch...

Gene expression databases

ExpressionAtlasiF6ZDS4. baseline and differential.
GenevisibleiF6ZDS4. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-1274, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: 129/Ola.
  4. "The mouse interferon-inducible gene Ifi204 product interacts with the Tpr protein, a component of the nuclear pore complex."
    De Andrea M., Zannetti C., Noris E., Gariglio M., Azzimonti B., Landolfo S.
    J. Interferon Cytokine Res. 22:1113-1121(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1229-2431, INTERACTION WITH IFI203 AND IFI204, SUBCELLULAR LOCATION.
    Tissue: Fibroblast.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1259 AND SER-2223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1259; SER-2141; THR-2184 AND SER-2223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-551; LYS-787; LYS-822; LYS-829 AND LYS-1760, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTPR_MOUSE
AccessioniPrimary (citable) accession number: F6ZDS4
Secondary accession number(s): Q8R4A0, Q921B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: April 18, 2012
Last modified: May 11, 2016
This is version 42 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.