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P12270 (TPR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleoprotein TPR
Alternative name(s):
Megator
NPC-associated intranuclear protein
Translocated promoter region protein
Gene names
Name:TPR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 (Ref.39 and Ref.13). 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. Ref.10 Ref.13 Ref.15 Ref.17 Ref.20 Ref.23 Ref.25 Ref.29 Ref.32 Ref.33 Ref.36 Ref.39

Subunit structure

Interacts with IFI204 (via C-terminus 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-terminus domain) with the KPNB1; the interaction occurs in a RanGTP-dependent manner. Interacts (via C-terminus 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-terminus 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. Ref.11 Ref.15 Ref.16 Ref.17 Ref.20 Ref.23 Ref.25 Ref.28 Ref.29 Ref.33 Ref.39

Subcellular location

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 (Ref.2). 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 (Ref.23). Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore (Ref.29). Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle. Ref.3 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.23 Ref.25 Ref.29 Ref.32 Ref.33 Ref.39

Tissue specificity

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. Ref.3 Ref.12

Domain

The N-terminus domain mediates intranuclear attachment to the nuclear pore complex. The C-terminus domain mediates its nuclear import. Ref.9 Ref.10

Post-translational modification

Phosphorylated. Phosphorylation occurs on serine and threonine residues (comprised in the C-terminus region) by MAPK1/ERK2 and stabilizes the interaction between these two proteins. Ref.25

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.

Involvement in disease

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.

Sequence similarities

Belongs to the TPR family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
mRNA transport
Protein transport
Translocation
Transport
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Membrane
Nuclear pore complex
Nucleus
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK import into nucleus

Inferred from mutant phenotype Ref.25. Source: UniProtKB

RNA export from nucleus

Inferred from mutant phenotype Ref.13. Source: UniProtKB

RNA import into nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular response to heat

Inferred from direct assay Ref.20. Source: UniProtKB

cellular response to interferon-alpha

Inferred from sequence or structural similarity. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

glucose transport

Traceable author statement. Source: Reactome

hexose transport

Traceable author statement. Source: Reactome

mRNA export from nucleus in response to heat stress

Inferred from direct assay Ref.20. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

mitotic spindle assembly checkpoint

Inferred from mutant phenotype Ref.23Ref.33. Source: UniProtKB

negative regulation of RNA export from nucleus

Inferred from direct assay Ref.39. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.36. Source: UniProtKB

negative regulation of translational initiation

Inferred from mutant phenotype Ref.36. Source: UniProtKB

nuclear pore organization

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of heterochromatin assembly

Inferred from mutant phenotype Ref.32. Source: UniProtKB

positive regulation of intracellular protein transport

Inferred from mutant phenotype Ref.29. Source: UniProtKB

positive regulation of mitotic cell cycle spindle assembly checkpoint

Inferred from mutant phenotype Ref.29. Source: UniProtKB

positive regulation of protein export from nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein import into nucleus

Inferred from mutant phenotype Ref.25. Source: UniProtKB

protein import into nucleus

Traceable author statement Ref.2. Source: ProtInc

regulation of glucose transport

Traceable author statement. Source: Reactome

regulation of mitotic sister chromatid separation

Inferred from mutant phenotype Ref.33. Source: UniProtKB

regulation of spindle assembly involved in mitosis

Inferred from mutant phenotype Ref.29. Source: UniProtKB

response to epidermal growth factor

Inferred from direct assay Ref.25. Source: UniProtKB

seryl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.13Ref.15. Source: UniProtKB

cytoplasmic dynein complex

Inferred from direct assay Ref.33. Source: UniProtKB

extrinsic component of membrane

Inferred from direct assay Ref.15. Source: UniProtKB

kinetochore

Inferred from direct assay Ref.33. Source: UniProtKB

mitotic spindle

Inferred from direct assay Ref.33. Source: UniProtKB

nuclear envelope

Inferred from direct assay PubMed 17098863. Source: UniProtKB

nuclear inclusion body

Inferred from direct assay Ref.11Ref.14. Source: UniProtKB

nuclear membrane

Inferred from direct assay Ref.11Ref.14Ref.13Ref.15Ref.16Ref.25Ref.32Ref.39Ref.3Ref.9Ref.10. Source: UniProtKB

nuclear periphery

Inferred from direct assay Ref.11Ref.14Ref.13Ref.16PubMed 22401879Ref.3. Source: UniProtKB

nuclear pore

Inferred from direct assay Ref.11Ref.15Ref.23Ref.9Ref.10. Source: UniProtKB

nuclear pore nuclear basket

Inferred from direct assay Ref.14Ref.16Ref.3. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.17. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

chromatin binding

Inferred from direct assay Ref.20. Source: UniProtKB

dynein complex binding

Inferred from direct assay Ref.33. Source: UniProtKB

heat shock protein binding

Inferred from direct assay Ref.20. Source: UniProtKB

mRNA binding

Inferred from direct assay Ref.20. Source: UniProtKB

mitogen-activated protein kinase binding

Inferred from direct assay Ref.25. Source: UniProtKB

nucleocytoplasmic transporter activity

Inferred from direct assay Ref.39. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.11Ref.15. Source: UniProtKB

serine-tRNA ligase activity

Inferred from electronic annotation. Source: InterPro

tubulin binding

Inferred from direct assay Ref.33. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 23632362Nucleoprotein TPR
PRO_0000204920

Regions

Region3 – 1311Sufficient for interaction with TPR
Region14 – 117104Necessary for interaction with HSF1
Region437 – 51377Necessary for association to the NPC
Region1218 – 1320103Necessary for interaction with HSF1
Region1812 – 186756Sufficient and essential for mediating its nuclear import
Coiled coil29 – 370342 Potential
Coiled coil423 – 602180 Potential
Coiled coil661 – 1173513 Potential
Coiled coil1215 – 1630416 Potential
Compositional bias527 – 5304Poly-Ser
Compositional bias1833 – 18364Poly-Glu
Compositional bias1971 – 19788Poly-Asp
Compositional bias2309 – 23124Poly-Ser

Sites

Site1911Breakpoint for translocation to form TRK-T1

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.27 Ref.38 Ref.40
Modified residue2521N6-acetyllysine Ref.31
Modified residue3121N6-acetyllysine Ref.31
Modified residue3451N6-acetyllysine Ref.31
Modified residue3791Phosphoserine Ref.26 Ref.34
Modified residue4281N6-acetyllysine Ref.31
Modified residue4571N6-acetyllysine Ref.31
Modified residue4771N6-acetyllysine By similarity
Modified residue7131N6-acetyllysine Ref.31
Modified residue7231N6-acetyllysine Ref.31
Modified residue7481N6-acetyllysine Ref.31
Modified residue7551N6-acetyllysine Ref.31
Modified residue11851Phosphoserine Ref.19 Ref.26 Ref.30 Ref.34 Ref.37
Modified residue16901N6-acetyllysine By similarity
Modified residue16921Phosphothreonine Ref.34
Modified residue20481Phosphoserine Ref.26
Modified residue20501Phosphoserine Ref.22 Ref.30
Modified residue20731Phosphoserine Ref.18 Ref.37
Modified residue21551Phosphoserine Ref.21 Ref.24 Ref.26 Ref.30 Ref.34

Natural variations

Natural variant9601S → N.
Corresponds to variant rs3753565 [ dbSNP | Ensembl ].
VAR_020429
Natural variant14281V → G.
Corresponds to variant rs35550453 [ dbSNP | Ensembl ].
VAR_047289
Natural variant17071T → A.
Corresponds to variant rs35766045 [ dbSNP | Ensembl ].
VAR_047290

Experimental info

Mutagenesis4581L → 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. Ref.11 Ref.15
Mutagenesis4891M → 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. Ref.11 Ref.15
Sequence conflict321Q → R in CAA44719. Ref.5
Sequence conflict321Q → R in CAA68681. Ref.6
Sequence conflict7791V → I in AAB48030. Ref.3
Sequence conflict9061Q → R in AAB48030. Ref.3
Sequence conflict12391Q → E in CAA47021. Ref.2
Sequence conflict1952 – 196514Missing in CAA47021. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P12270 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 01E669CBDC496772

FASTA2,363267,293
        10         20         30         40         50         60 
MAAVLQQVLE RTELNKLPKS VQNKLEKFLA DQQSEIDGLK GRHEKFKVES EQQYFEIEKR 

        70         80         90        100        110        120 
LSHSQERLVN ETRECQSLRL ELEKLNNQLK ALTEKNKELE IAQDRNIAIQ SQFTRTKEEL 

       130        140        150        160        170        180 
EAEKRDLIRT NERLSQELEY LTEDVKRLNE KLKESNTTKG ELQLKLDELQ ASDVSVKYRE 

       190        200        210        220        230        240 
KRLEQEKELL HSQNTWLNTE LKTKTDELLA LGREKGNEIL ELKCNLENKK EEVSRLEEQM 

       250        260        270        280        290        300 
NGLKTSNEHL QKHVEDLLTK LKEAKEQQAS MEEKFHNELN AHIKLSNLYK SAADDSEAKS 

       310        320        330        340        350        360 
NELTRAVEEL HKLLKEAGEA NKAIQDHLLE VEQSKDQMEK EMLEKIGRLE KELENANDLL 

       370        380        390        400        410        420 
SATKRKGAIL SEEELAAMSP TAAAVAKIVK PGMKLTELYN AYVETQDQLL LEKLENKRIN 

       430        440        450        460        470        480 
KYLDEIVKEV EAKAPILKRQ REEYERAQKA VASLSVKLEQ AMKEIQRLQE DTDKANKQSS 

       490        500        510        520        530        540 
VLERDNRRME IQVKDLSQQI RVLLMELEEA RGNHVIRDEE VSSADISSSS EVISQHLVSY 

       550        560        570        580        590        600 
RNIEELQQQN QRLLVALREL GETREREEQE TTSSKITELQ LKLESALTEL EQLRKSRQHQ 

       610        620        630        640        650        660 
MQLVDSIVRQ RDMYRILLSQ TTGVAIPLHA SSLDDVSLAS TPKRPSTSQT VSTPAPVPVI 

       670        680        690        700        710        720 
ESTEAIEAKA ALKQLQEIFE NYKKEKAENE KIQNEQLEKL QEQVTDLRSQ NTKISTQLDF 

       730        740        750        760        770        780 
ASKRYEMLQD NVEGYRREIT SLHERNQKLT ATTQKQEQII NTMTQDLRGA NEKLAVAEVR 

       790        800        810        820        830        840 
AENLKKEKEM LKLSEVRLSQ QRESLLAEQR GQNLLLTNLQ TIQGILERSE TETKQRLSSQ 

       850        860        870        880        890        900 
IEKLEHEISH LKKKLENEVE QRHTLTRNLD VQLLDTKRQL DTETNLHLNT KELLKNAQKE 

       910        920        930        940        950        960 
IATLKQHLSN MEVQVASQSS QRTGKGQPSN KEDVDDLVSQ LRQTEEQVND LKERLKTSTS 

       970        980        990       1000       1010       1020 
NVEQYQAMVT SLEESLNKEK QVTEEVRKNI EVRLKESAEF QTQLEKKLME VEKEKQELQD 

      1030       1040       1050       1060       1070       1080 
DKRRAIESME QQLSELKKTL SSVQNEVQEA LQRASTALSN EQQARRDCQE QAKIAVEAQN 

      1090       1100       1110       1120       1130       1140 
KYERELMLHA ADVEALQAAK EQVSKMASVR QHLEETTQKA ESQLLECKAS WEERERMLKD 

      1150       1160       1170       1180       1190       1200 
EVSKCVCRCE DLEKQNRLLH DQIEKLSDKV VASVKEGVQG PLNVSLSEEG KSQEQILEIL 

      1210       1220       1230       1240       1250       1260 
RFIRREKEIA ETRFEVAQVE SLRYRQRVEL LERELQELQD SLNAEREKVQ VTAKTMAQHE 

      1270       1280       1290       1300       1310       1320 
ELMKKTETMN VVMETNKMLR EEKERLEQDL QQMQAKVRKL ELDILPLQEA NAELSEKSGM 

      1330       1340       1350       1360       1370       1380 
LQAEKKLLEE DVKRWKARNQ HLVSQQKDPD TEEYRKLLSE KEVHTKRIQQ LTEEIGRLKA 

      1390       1400       1410       1420       1430       1440 
EIARSNASLT NNQNLIQSLK EDLNKVRTEK ETIQKDLDAK IIDIQEKVKT ITQVKKIGRR 

      1450       1460       1470       1480       1490       1500 
YKTQYEELKA QQDKVMETSA QSSGDHQEQH VSVQEMQELK ETLNQAETKS KSLESQVENL 

      1510       1520       1530       1540       1550       1560 
QKTLSEKETE ARNLQEQTVQ LQSELSRLRQ DLQDRTTQEE QLRQQITEKE EKTRKAIVAA 

      1570       1580       1590       1600       1610       1620 
KSKIAHLAGV KDQLTKENEE LKQRNGALDQ QKDELDVRIT ALKSQYEGRI SRLERELREH 

      1630       1640       1650       1660       1670       1680 
QERHLEQRDE PQEPSNKVPE QQRQITLKTT PASGERGIAS TSDPPTANIK PTPVVSTPSK 

      1690       1700       1710       1720       1730       1740 
VTAAAMAGNK STPRASIRPM VTPATVTNPT TTPTATVMPT TQVESQEAMQ SEGPVEHVPV 

      1750       1760       1770       1780       1790       1800 
FGSTSGSVRS TSPNVQPSIS QPILTVQQQT QATAFVQPTQ QSHPQIEPAN QELSSNIVEV 

      1810       1820       1830       1840       1850       1860 
VQSSPVERPS TSTAVFGTVS ATPSSSLPKR TREEEEDSTI EASDQVSDDT VEMPLPKKLK 

      1870       1880       1890       1900       1910       1920 
SVTPVGTEEE VMAEESTDGE VETQVYNQDS QDSIGEGVTQ GDYTPMEDSE ETSQSLQIDL 

      1930       1940       1950       1960       1970       1980 
GPLQSDQQTT TSSQDGQGKG DDVIVIDSDD EEEDDDENDG EHEDYEEDEE DDDDDEDDTG 

      1990       2000       2010       2020       2030       2040 
MGDEGEDSNE GTGSADGNDG YEADDAEGGD GTDPGTETEE SMGGGEGNHR AADSQNSGEG 

      2050       2060       2070       2080       2090       2100 
NTGAAESSFS QEVSREQQPS SASERQAPRA PQSPRRPPHP LPPRLTIHAP PQELGPPVQR 

      2110       2120       2130       2140       2150       2160 
IQMTRRQSVG RGLQLTPGIG GMQQHFFDDE DRTVPSTPTL VVPHRTDGFA EAIHSPQVAG 

      2170       2180       2190       2200       2210       2220 
VPRFRFGPPE DMPQTSSSHS DLGQLASQGG LGMYETPLFL AHEEESGGRS VPTTPLQVAA 

      2230       2240       2250       2260       2270       2280 
PVTVFTESTT SDASEHASQS VPMVTTSTGT LSTTNETATG DDGDEVFVEA ESEGISSEAG 

      2290       2300       2310       2320       2330       2340 
LEIDSQQEEE PVQASDESDL PSTSQDPPSS SSVDTSSSQP KPFRRVRLQT TLRQGVRGRQ 

      2350       2360 
FNRQRGVSHA MGGRGGINRG NIN 

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References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]Bienvenut W.V., Glen H., Brunton V.G., Frame M.C., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (JUL-2007) to UniProtKB
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS23741.
RefSeqNP_003283.2. NM_003292.2.
UniGeneHs.279640.

3D structure databases

ProteinModelPortalP12270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113028. 63 interactions.
IntActP12270. 11 interactions.
MINTMINT-4993169.
STRING9606.ENSP00000356448.

PTM databases

PhosphoSiteP12270.

Polymorphism databases

DMDM215274208.

Proteomic databases

PaxDbP12270.
PRIDEP12270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367478; ENSP00000356448; ENSG00000047410.
GeneID7175.
KEGGhsa:7175.
UCSCuc001grv.3. human.

Organism-specific databases

CTD7175.
GeneCardsGC01M186282.
HGNCHGNC:12017. TPR.
HPAHPA019661.
HPA019663.
HPA024336.
MIM188550. phenotype.
189940. gene.
neXtProtNX_P12270.
Orphanet146. Papillary or follicular thyroid carcinoma.
PharmGKBPA36696.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000139431.
HOVERGENHBG009158.
InParanoidP12270.
KOK09291.
OMARRDCQEQ.
OrthoDBEOG7JQBMF.
PhylomeDBP12270.
TreeFamTF350364.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP12270.
BgeeP12270.
CleanExHS_TPR.
GenevestigatorP12270.

Family and domain databases

Gene3D1.10.287.40. 1 hit.
InterProIPR015866. Ser-tRNA-synth_1_N.
IPR012929. TPR_MLP1_2.
[Graphical view]
PfamPF07926. TPR_MLP1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi7175.
NextBio18907.
PMAP-CutDBP12270.
PROP12270.
SOURCESearch...

Entry information

Entry nameTPR_HUMAN
AccessionPrimary (citable) accession number: P12270
Secondary accession number(s): Q15655, Q5SWY0, Q99968
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM