CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024791
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleoprotein TPR 
Protein Synonyms/Alias
 NPC-associated intranuclear protein; Translocated promoter region and nuclear basket protein 
Gene Name
 Tpr 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
326TSNEHLQKHVEDLLTacetylation[1]
386RAVDELHKLLKEAGEacetylation[2]
502KYLDEIVKEVEAKAPacetylation[2]
523EEYERAQKAVASLSAacetylation[1]
531AVASLSAKLEQAMKEacetylation[2]
531AVASLSAKLEQAMKEubiquitination[3]
551EDTDKANKHSSVLERacetylation[4]
568QRMEIQIKDLSQQIRubiquitination[3]
787DLRSQNTKISTQLDFacetylation[2, 4]
797TQLDFASKRYEMLQDacetylation[1, 4]
822SLQERNQKLTATTQKacetylation[1, 2, 4, 5, 6]
829KLTATTQKQEQIINTacetylation[1, 2, 4, 5]
829KLTATTQKQEQIINTubiquitination[3]
1202ESQLLECKASWEEREacetylation[2]
1625QMNEKTWKTLALAKSubiquitination[3]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
Functional Description
 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). 
Sequence Annotation
 REGION 77 87 Sufficient for interaction with TPR (By
 REGION 88 191 Necessary for interaction with HSF1 (By
 REGION 511 587 Necessary for association to the NPC (By
 REGION 1292 1394 Necessary for interaction with HSF1 (By
 REGION 1882 1937 Sufficient and essential for mediating
 MOD_RES 326 326 N6-acetyllysine (By similarity).
 MOD_RES 386 386 N6-acetyllysine (By similarity).
 MOD_RES 419 419 N6-acetyllysine (By similarity).
 MOD_RES 453 453 Phosphoserine (By similarity).
 MOD_RES 502 502 N6-acetyllysine (By similarity).
 MOD_RES 531 531 N6-acetyllysine (By similarity).
 MOD_RES 787 787 N6-acetyllysine (By similarity).
 MOD_RES 797 797 N6-acetyllysine (By similarity).
 MOD_RES 822 822 N6-acetyllysine (By similarity).
 MOD_RES 829 829 N6-acetyllysine (By similarity).
 MOD_RES 1259 1259 Phosphoserine (By similarity).
 MOD_RES 1762 1762 Phosphothreonine (By similarity).
 MOD_RES 2116 2116 Phosphoserine (By similarity).
 MOD_RES 2118 2118 Phosphoserine (By similarity).
 MOD_RES 2141 2141 Phosphoserine (By similarity).
 MOD_RES 2223 2223 Phosphoserine (By similarity).  
Keyword
 Acetylation; Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Kinetochore; Membrane; Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport; Proto-oncogene; Reference proteome; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2431 AA 
Protein Sequence
MTSGGSASRS GHRGVPMTSR GFDGSRRGSL RRAGARETAS EAADGAAPAA GLRASPCSLA 60
SPSAAAAVAA IPADMAAVLQ QVLERPELNK LPKSTQNKLE KFLAEQQSEI DCLKGRHEKF 120
KVESEQQYFE IEKRLSQSQE RLVTETRECQ NLRLELEKLN NQVKVLTEKT KELETAQDRN 180
LGIQSQFTRA KEELEAEKRD LIRTNERLSQ EVEYLTEDVK RLNEKLKESN TTKGELQLKL 240
DELQASDVAV KYREKRLEQE KELLHNQNSW LNTELKTKTD ELLALGREKG NEILELKCNL 300
ENKKEEVLRL EEQMNGLKTS NEHLQKHVED LLTKLKEAKE QQASMEEKFH NELNAHIKLS 360
NLYKSAADDS EAKSNELTRA VDELHKLLKE AGEANKTIQD HLLQVEESKD QMEKEMLEKI 420
GKLEKELENA NDLLSATKRK GAILSEEELA AMSPTAAAVA KIVKPGMKLT ELYNAYVETQ 480
DQLLLEKQEN KRINKYLDEI VKEVEAKAPI LKRQREEYER AQKAVASLSA KLEQAMKEIQ 540
RLQEDTDKAN KHSSVLERDN QRMEIQIKDL SQQIRVLLME LEEARGNHVI RDEEVSSADI 600
SSSSEVISQH LVSYRNIEEL QQQNQRLLFA LRELGETRER EEQETTSSKI AELQHKLENS 660
LAELEQLRES RQHQMQLVDS IVRQRDMYRI LLSQTTGMAI PLQASSLDDI SLLSTPKRSS 720
TSQTVSTPAP EPVIDSTEAI EAKAALKQLQ EIFENYKKEK IDSEKLQNEQ LEKLQEQVTD 780
LRSQNTKIST QLDFASKRYE MLQDNVEGYR REITSLQERN QKLTATTQKQ EQIINTMTQD 840
LRGANEKLAV AEVRAENLKK EKEMLKLSEV RLSQQRESLL AEQRGQNLLL TNLQTIQGIL 900
ERSETETKQR LNSQIEKLEH EISHLKKKLE NEVEQRHTLT RNLDVQLLDT KRQLDTEINL 960
HLNTKELLKN AQKDIATLKQ HLNNMEAQLA SQSTQRTGKG QPGDRDDVDD LKSQLRQAEE 1020
QVNDLKERLK TSTSNVEQYR AMVTSLEDSL NKEKQVTEEV HKNIEVRLKE SAEFQTQLEK 1080
KLMEVEKEKQ ELQDDKRKAI ESMEQQLSEL KKTLSTVQNE VQEALQRAST ALSNEQQARR 1140
DCQEQAKIAV EAQNKYEREL MLHAADVEAL QAAKEQVSKM TSIRQHLEET TQKAESQLLE 1200
CKASWEERER VLKDEVSKSV SRCEDLEKQN RLLHDQIEKL SDKVVTSMKD AVQAPLNVSL 1260
NEEGKSQEQI LEILRFIRRE KEIAETRFEV AQVESLRYRQ RVELLERELQ ELQDSLNVER 1320
EKVQVTAKTM AQHEELMKKT ETMNVVMETN KMLREEKERL EQNLQQMQAK VRKLELDILP 1380
LQEANAELSE KSGMLQAEKK LLEEDVKRWK ARNQQLINQQ KDPDTEEYRK LLSEKEIHTK 1440
RIQQLNEEVG RLKAEIARSN ASLTNNQNLI QSLREDLSKA RTEKEGIQKD LDAKIIDIQE 1500
KVKTITQVKK IGRRYKTQFE ELKAQQNKAM ETSTQSSGDH QEQHISVQEM QELKDTLSQS 1560
ETKTKSLEGQ VENLQKTLSE KETEARSLQE QTVQLQSELS RLRQDLQDKT TEEQLRQQMN 1620
EKTWKTLALA KSKITHLSGV KDQLTKEIEE LKQRNGALDQ QKDELDVRMT ALKSQYEGRI 1680
SRLERELREH QERHLEQRDE PQEPTNKAPE QQRQITLKTT PASGERGIAS TSDPPTANIK 1740
PTPVVSTPSK VTAAAMAGNK STPRASIRPM VTPATVTNPT TTPTATVMPT TQVESQEAMQ 1800
SEGPVEHVPV FGNASGSVRS TSPNVQPSIS QPILTVQQQT QATAFVQPTQ QSHPQIEPTN 1860
QELSPNIVEV VQSSPVERPS TSTAVFGTVS ATPSSSLPKR TREEEEDSTM EAGDQVSEDT 1920
VEMPLPKKLK MVTPVGTEEE VMAEESTDGE AETQAYNQDS QDSIGEGVTQ GDYTPMEDSE 1980
ETSQSLQIDL GPLQSDQQTT SSQDGQGKGD DVIVIDSDDE DDDEENDGEH EDYEEDEDDD 2040
DDEEDDTGMG DEGEDSNEGT GSADGNDGYE ADDAEGGDGT DPGTETEESM GGAESHQRAA 2100
DSQNSGEGNT SAAESSFSQE VAREQQPTSA SERQTPQAPQ SPRRPPHPLP PRLTIHAPPQ 2160
ELGPPVQRIQ MTRRQSVGRG LQLTPGIGGM QQHFFDDEDR TVPSTPTLVV PHRTDGFAEA 2220
IHSPQVAGVP RFRFGPPEDM PQTSSSHSDL GQLASQGGLG MYETPLFLAH EEESGGRSVP 2280
TTPLQVAAPV TVFTESTTSD ASEHASQSVP MVTTSTGTLS TTNETAAGDD GDEVFVEAES 2340
EGISSEAGLE IDSQQEEEPV QASDESDLPS TSQDPPSSSS VDTSSSQPKP FRRVRLQTTL 2400
RQGVRGRQFN RQRGISHAMG GRGGINRGNI N 2431 
Gene Ontology
 GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
 GO:0019898; C:extrinsic to membrane; ISS:UniProtKB.
 GO:0000776; C:kinetochore; ISS:UniProtKB.
 GO:0072686; C:mitotic spindle; ISS:UniProtKB.
 GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
 GO:0031965; C:nuclear membrane; ISS:UniProtKB.
 GO:0034399; C:nuclear periphery; IDA:UniProtKB.
 GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0003682; F:chromatin binding; ISS:UniProtKB.
 GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
 GO:0051019; F:mitogen-activated protein kinase binding; ISS:UniProtKB.
 GO:0003729; F:mRNA binding; ISS:UniProtKB.
 GO:0005487; F:nucleocytoplasmic transporter activity; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0004828; F:serine-tRNA ligase activity; IEA:InterPro.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0035457; P:cellular response to interferon-alpha; IDA:UniProtKB.
 GO:0000189; P:MAPK import into nucleus; ISS:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007094; P:mitotic spindle assembly checkpoint; ISS:UniProtKB.
 GO:0031990; P:mRNA export from nucleus in response to heat stress; ISS:UniProtKB.
 GO:0046832; P:negative regulation of RNA export from nucleus; ISS:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
 GO:0006999; P:nuclear pore organization; ISS:UniProtKB.
 GO:0031453; P:positive regulation of heterochromatin assembly; ISS:UniProtKB.
 GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
 GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
 GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
 GO:0010965; P:regulation of mitotic sister chromatid separation; ISS:UniProtKB.
 GO:1901673; P:regulation of spindle assembly involved in mitosis; ISS:UniProtKB.
 GO:0070849; P:response to epidermal growth factor stimulus; ISS:UniProtKB.
 GO:0006404; P:RNA import into nucleus; ISS:UniProtKB.
 GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR009053; Prefoldin.
 IPR015866; Ser-tRNA-synth_1_N.
 IPR012929; TPR_MLP1_2. 
Pfam
 PF07926; TPR_MLP1_2 
SMART
  
PROSITE
  
PRINTS