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Protein

Nucleoprotein TPR

Gene

TPR

Organism
Homo sapiens (Human)
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. 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

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • dynein complex binding Source: UniProtKB
  • heat shock protein binding Source: UniProtKB
  • mitogen-activated protein kinase binding Source: UniProtKB
  • mRNA binding Source: UniProtKB
  • nucleocytoplasmic transporter activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • tubulin binding Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cellular response to heat Source: UniProtKB
  • cellular response to interferon-alpha Source: UniProtKB
  • gene silencing by RNA Source: Reactome
  • intracellular transport of virus Source: Reactome
  • MAPK import into nucleus Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • mitotic nuclear envelope disassembly Source: Reactome
  • mitotic spindle assembly checkpoint Source: UniProtKB
  • mRNA export from nucleus Source: Reactome
  • mRNA export from nucleus in response to heat stress Source: UniProtKB
  • negative regulation of RNA export from nucleus Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of translational initiation Source: UniProtKB
  • nuclear pore organization Source: UniProtKB
  • positive regulation of heterochromatin assembly Source: UniProtKB
  • positive regulation of intracellular protein transport Source: UniProtKB
  • positive regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
  • positive regulation of protein export from nucleus Source: UniProtKB
  • positive regulation of protein import into nucleus Source: UniProtKB
  • protein import into nucleus Source: ProtInc
  • protein sumoylation Source: Reactome
  • regulation of cellular response to heat Source: Reactome
  • regulation of glucose transport Source: Reactome
  • regulation of mitotic sister chromatid separation Source: UniProtKB
  • regulation of mitotic spindle assembly Source: UniProtKB
  • response to epidermal growth factor Source: UniProtKB
  • RNA export from nucleus Source: UniProtKB
  • RNA import into nucleus Source: UniProtKB
  • tRNA export from nucleus Source: Reactome
  • viral process Source: Reactome
  • viral transcription Source: Reactome
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000047410-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.
SIGNORiP12270.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:12017. TPR.

Subcellular locationi

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
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TPR has been found in papillary thyroid carcinomas (PTCs). 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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi458L → 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 Publications1
Mutagenesisi489M → 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 Publications1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei191Breakpoint for translocation to form TRK-T11

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi7175.
MalaCardsiTPR.
OpenTargetsiENSG00000047410.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA36696.

Polymorphism and mutation databases

BioMutaiTPR.
DMDMi215274208.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002049202 – 2363Nucleoprotein TPRAdd BLAST2362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei252N6-acetyllysineCombined sources1
Modified residuei312N6-acetyllysineCombined sources1
Modified residuei345N6-acetyllysineCombined sources1
Modified residuei379PhosphoserineCombined sources1
Modified residuei428N6-acetyllysineCombined sources1
Modified residuei457N6-acetyllysineCombined sources1
Modified residuei477N6-acetyllysineBy similarity1
Modified residuei522PhosphoserineCombined sources1
Modified residuei523PhosphoserineCombined sources1
Modified residuei632PhosphoserineCombined sources1
Modified residuei713N6-acetyllysineCombined sources1
Modified residuei723N6-acetyllysineCombined sources1
Modified residuei748N6-acetyllysineCombined sources1
Modified residuei755N6-acetyllysineCombined sources1
Modified residuei1185PhosphoserineCombined sources1
Modified residuei1690N6-acetyllysineBy similarity1
Modified residuei1692PhosphothreonineCombined sources1
Modified residuei1893PhosphoserineCombined sources1
Modified residuei2034PhosphoserineCombined sources1
Modified residuei2037PhosphoserineCombined sources1
Modified residuei2048PhosphoserineCombined sources1
Modified residuei2050PhosphoserineCombined sources1
Modified residuei2073PhosphoserineCombined sources1
Modified residuei2106Omega-N-methylarginineBy similarity1
Modified residuei2111Omega-N-methylarginineCombined sources1
Modified residuei2116PhosphothreonineBy similarity1
Modified residuei2137PhosphothreonineCombined sources1
Modified residuei2155PhosphoserineCombined sources1
Modified residuei2163Omega-N-methylarginineBy similarity1
Modified residuei2343Asymmetric dimethylarginineBy similarity1
Modified residuei2345Asymmetric dimethylarginineBy similarity1
Modified residuei2354Asymmetric dimethylarginineBy similarity1

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.1 Publication
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, Methylation, Phosphoprotein

Proteomic databases

EPDiP12270.
MaxQBiP12270.
PaxDbiP12270.
PeptideAtlasiP12270.
PRIDEiP12270.

PTM databases

iPTMnetiP12270.
PhosphoSitePlusiP12270.

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

BgeeiENSG00000047410.
CleanExiHS_TPR.
ExpressionAtlasiP12270. baseline and differential.
GenevisibleiP12270. HS.

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

GO - Molecular functioni

  • dynein complex binding Source: UniProtKB
  • heat shock protein binding Source: UniProtKB
  • mitogen-activated protein kinase binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113028. 84 interactors.
DIPiDIP-50405N.
IntActiP12270. 25 interactors.
MINTiMINT-4993169.
STRINGi9606.ENSP00000356448.

Structurei

3D structure databases

ProteinModelPortaliP12270.
SMRiP12270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni3 – 13Sufficient for interaction with TPRAdd BLAST11
Regioni14 – 117Necessary for interaction with HSF11 PublicationAdd BLAST104
Regioni437 – 513Necessary for association to the NPCAdd BLAST77
Regioni1218 – 1320Necessary for interaction with HSF11 PublicationAdd BLAST103
Regioni1812 – 1867Sufficient and essential for mediating its nuclear importAdd BLAST56

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili29 – 370Sequence analysisAdd BLAST342
Coiled coili423 – 602Sequence analysisAdd BLAST180
Coiled coili661 – 1173Sequence analysisAdd BLAST513
Coiled coili1215 – 1630Sequence analysisAdd BLAST416

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi527 – 530Poly-Ser4
Compositional biasi1833 – 1836Poly-Glu4
Compositional biasi1971 – 1978Poly-Asp8
Compositional biasi2309 – 2312Poly-Ser4

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

eggNOGiKOG4674. Eukaryota.
ENOG410XSA1. LUCA.
GeneTreeiENSGT00730000111014.
HOGENOMiHOG000139431.
HOVERGENiHBG009158.
InParanoidiP12270.
KOiK09291.
OMAiNRLLHDQ.
OrthoDBiEOG091G006U.
PhylomeDBiP12270.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P12270-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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
Isoform 2 (identifier: P12270-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     726-726: E → L
     727-2363: Missing.

Show »
Length:726
Mass (Da):83,979
Checksum:iE6351C8CC59B6C67
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32Q → R in CAA44719 (PubMed:16710414).Curated1
Sequence conflicti32Q → R in CAA68681 (Ref. 6) Curated1
Sequence conflicti779V → I in AAB48030 (PubMed:9024684).Curated1
Sequence conflicti906Q → R in AAB48030 (PubMed:9024684).Curated1
Sequence conflicti1239Q → E in CAA47021 (PubMed:7798308).Curated1
Sequence conflicti1952 – 1965Missing in CAA47021 (PubMed:7798308).CuratedAdd BLAST14

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020429960S → N.Corresponds to variant rs3753565dbSNPEnsembl.1
Natural variantiVAR_0472891428V → G.Corresponds to variant rs35550453dbSNPEnsembl.1
Natural variantiVAR_0472901707T → A.Corresponds to variant rs35766045dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_057406726E → L in isoform 2. 1 Publication1
Alternative sequenceiVSP_057407727 – 2363Missing in isoform 2. 1 PublicationAdd BLAST1637

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63105 mRNA. Translation: CAA44819.1.
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. [P12270-1]
PIRiS23741.
RefSeqiNP_003283.2. NM_003292.2. [P12270-1]
UniGeneiHs.279640.

Genome annotation databases

EnsembliENST00000367478; ENSP00000356448; ENSG00000047410. [P12270-1]
ENST00000613151; ENSP00000483425; ENSG00000047410. [P12270-2]
GeneIDi7175.
KEGGihsa:7175.
UCSCiuc001grv.4. human. [P12270-1]
uc057nyz.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63105 mRNA. Translation: CAA44819.1.
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. [P12270-1]
PIRiS23741.
RefSeqiNP_003283.2. NM_003292.2. [P12270-1]
UniGeneiHs.279640.

3D structure databases

ProteinModelPortaliP12270.
SMRiP12270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113028. 84 interactors.
DIPiDIP-50405N.
IntActiP12270. 25 interactors.
MINTiMINT-4993169.
STRINGi9606.ENSP00000356448.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiP12270.
PhosphoSitePlusiP12270.

Polymorphism and mutation databases

BioMutaiTPR.
DMDMi215274208.

Proteomic databases

EPDiP12270.
MaxQBiP12270.
PaxDbiP12270.
PeptideAtlasiP12270.
PRIDEiP12270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367478; ENSP00000356448; ENSG00000047410. [P12270-1]
ENST00000613151; ENSP00000483425; ENSG00000047410. [P12270-2]
GeneIDi7175.
KEGGihsa:7175.
UCSCiuc001grv.4. human. [P12270-1]
uc057nyz.1. human.

Organism-specific databases

CTDi7175.
DisGeNETi7175.
GeneCardsiTPR.
HGNCiHGNC:12017. TPR.
HPAiHPA019661.
HPA019663.
HPA024336.
MalaCardsiTPR.
MIMi189940. gene.
neXtProtiNX_P12270.
OpenTargetsiENSG00000047410.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA36696.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4674. Eukaryota.
ENOG410XSA1. LUCA.
GeneTreeiENSGT00730000111014.
HOGENOMiHOG000139431.
HOVERGENiHBG009158.
InParanoidiP12270.
KOiK09291.
OMAiNRLLHDQ.
OrthoDBiEOG091G006U.
PhylomeDBiP12270.
TreeFamiTF350364.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000047410-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.
SIGNORiP12270.

Miscellaneous databases

GenomeRNAii7175.
PMAP-CutDBP12270.
PROiP12270.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000047410.
CleanExiHS_TPR.
ExpressionAtlasiP12270. baseline and differential.
GenevisibleiP12270. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P12270
Secondary accession number(s): Q15624
, Q15655, Q5SWY0, Q99968
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 173 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

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.