TPR_MOUSE - dbPTM
TPR_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPR_MOUSE
UniProt AC F6ZDS4
Protein Name Nucleoprotein TPR
Gene Name Tpr
Organism Mus musculus (Mouse).
Sequence Length 2431
Subcellular Localization Nucleus . Nucleus membrane
Peripheral membrane protein
Nucleoplasmic side . Nucleus envelope . Nucleus, nuclear pore complex . Cytoplasm . Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . Nucleus membrane
Peripheral membrane
Protein 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)..
Protein Sequence MTSGGSASRSGHRGVPMTSRGFDGSRRGSLRRAGARETASEAADGAAPAAGLRASPCSLASPSAAAAVAAIPADMAAVLQQVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVTETRECQNLRLELEKLNNQVKVLTEKTKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVAVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVLRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQDHLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKQENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDNQRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETREREEQETTSSKIAELQHKLENSLAELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLLSTPKRSSTSQTVSTPAPEPVIDSTEAIEAKAALKQLQEIFENYKKEKIDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLNSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINLHLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSTSNVEQYRAMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLSELKKTLSTVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMTSIRQHLEETTQKAESQLLECKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKDAVQAPLNVSLNEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNVEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQQLINQQKDPDTEEYRKLLSEKEIHTKRIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLREDLSKARTEKEGIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFEELKAQQNKAMETSTQSSGDHQEQHISVQEMQELKDTLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTVQLQSELSRLRQDLQDKTTEEQLRQQMNEKTWKTLALAKSKITHLSGVKDQLTKEIEELKQRNGALDQQKDELDVRMTALKSQYEGRISRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGNASGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPTNQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTMEAGDQVSEDTVEMPLPKKLKMVTPVGTEEEVMAEESTDGEAETQAYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTSSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDDDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGAESHQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETAAGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGISHAMGGRGGINRGNIN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MTSGGSASR
------CCCCCCCCC
28576409
18PhosphorylationGHRGVPMTSRGFDGS
CCCCCCCCCCCCCCC
24719451
19PhosphorylationHRGVPMTSRGFDGSR
CCCCCCCCCCCCCCC
24719451
55PhosphorylationPAAGLRASPCSLASP
CCCCCCCCCCCCCCH
30352176
58PhosphorylationGLRASPCSLASPSAA
CCCCCCCCCCCHHHH
30352176
61PhosphorylationASPCSLASPSAAAAV
CCCCCCCCHHHHHHH
30352176
63PhosphorylationPCSLASPSAAAAVAA
CCCCCCHHHHHHHHH
30352176
209PhosphorylationIRTNERLSQEVEYLT
HHHCHHHHHHHHHHH
25338131
214PhosphorylationRLSQEVEYLTEDVKR
HHHHHHHHHHHHHHH
25293948
216PhosphorylationSQEVEYLTEDVKRLN
HHHHHHHHHHHHHHH
25293948
279PhosphorylationNTELKTKTDELLALG
HHHHHHHHHHHHHHC
25890499
326AcetylationTSNEHLQKHVEDLLT
CCHHHHHHHHHHHHH
-
364UbiquitinationIKLSNLYKSAADDSE
HHHHHHHHHHCCCHH
-
386AcetylationRAVDELHKLLKEAGE
HHHHHHHHHHHHHHH
-
419AcetylationMEKEMLEKIGKLEKE
HHHHHHHHHHHHHHH
-
438UbiquitinationNDLLSATKRKGAILS
HHHHHHHHHCCCCCC
27667366
445PhosphorylationKRKGAILSEEELAAM
HHCCCCCCHHHHHCC
26239621
453PhosphorylationEEELAAMSPTAAAVA
HHHHHCCCHHHHHHH
25521595
455PhosphorylationELAAMSPTAAAVAKI
HHHCCCHHHHHHHHH
22942356
464UbiquitinationAAVAKIVKPGMKLTE
HHHHHHHCCCCCHHH
27667366
502AcetylationKYLDEIVKEVEAKAP
HHHHHHHHHHHHHCH
-
507UbiquitinationIVKEVEAKAPILKRQ
HHHHHHHHCHHHHHH
27667366
523AcetylationEEYERAQKAVASLSA
HHHHHHHHHHHHHHH
-
531AcetylationAVASLSAKLEQAMKE
HHHHHHHHHHHHHHH
-
531UbiquitinationAVASLSAKLEQAMKE
HHHHHHHHHHHHHHH
-
548UbiquitinationRLQEDTDKANKHSSV
HHHHHHHHHHHHHHH
27667366
551AcetylationEDTDKANKHSSVLER
HHHHHHHHHHHHHHH
23806337
568UbiquitinationQRMEIQIKDLSQQIR
CCEEEEHHHHHHHHH
-
596PhosphorylationVIRDEEVSSADISSS
CCCCCCCCCCCCCCC
25777480
597PhosphorylationIRDEEVSSADISSSS
CCCCCCCCCCCCCCH
26824392
601PhosphorylationEVSSADISSSSEVIS
CCCCCCCCCCHHHHH
25521595
602PhosphorylationVSSADISSSSEVISQ
CCCCCCCCCHHHHHH
25777480
603PhosphorylationSSADISSSSEVISQH
CCCCCCCCHHHHHHH
25293948
604PhosphorylationSADISSSSEVISQHL
CCCCCCCHHHHHHHH
25777480
608PhosphorylationSSSSEVISQHLVSYR
CCCHHHHHHHHHHCC
25777480
613PhosphorylationVISQHLVSYRNIEEL
HHHHHHHHCCCHHHH
25777480
614PhosphorylationISQHLVSYRNIEELQ
HHHHHHHCCCHHHHH
25777480
693PhosphorylationDMYRILLSQTTGMAI
HHHHHHHCCCCCCCC
25777480
695PhosphorylationYRILLSQTTGMAIPL
HHHHHCCCCCCCCCC
25777480
696PhosphorylationRILLSQTTGMAIPLQ
HHHHCCCCCCCCCCC
25777480
705PhosphorylationMAIPLQASSLDDISL
CCCCCCCCCCCCCCC
25159016
706PhosphorylationAIPLQASSLDDISLL
CCCCCCCCCCCCCCC
25159016
711PhosphorylationASSLDDISLLSTPKR
CCCCCCCCCCCCCCC
25777480
714PhosphorylationLDDISLLSTPKRSST
CCCCCCCCCCCCCCC
26239621
715PhosphorylationDDISLLSTPKRSSTS
CCCCCCCCCCCCCCC
26824392
719PhosphorylationLLSTPKRSSTSQTVS
CCCCCCCCCCCCCCC
23684622
720PhosphorylationLSTPKRSSTSQTVST
CCCCCCCCCCCCCCC
23684622
721PhosphorylationSTPKRSSTSQTVSTP
CCCCCCCCCCCCCCC
22942356
722PhosphorylationTPKRSSTSQTVSTPA
CCCCCCCCCCCCCCC
23684622
724PhosphorylationKRSSTSQTVSTPAPE
CCCCCCCCCCCCCCC
25521595
726PhosphorylationSSTSQTVSTPAPEPV
CCCCCCCCCCCCCCC
23684622
727PhosphorylationSTSQTVSTPAPEPVI
CCCCCCCCCCCCCCC
26824392
736PhosphorylationAPEPVIDSTEAIEAK
CCCCCCCCHHHHHHH
28833060
737PhosphorylationPEPVIDSTEAIEAKA
CCCCCCCHHHHHHHH
28833060
756PhosphorylationLQEIFENYKKEKIDS
HHHHHHHHHHHCCCH
26824392
787AcetylationDLRSQNTKISTQLDF
HHHHCCHHHHHHHHH
23806337
797AcetylationTQLDFASKRYEMLQD
HHHHHHHHHHHHHHH
7669769
822AcetylationSLQERNQKLTATTQK
HHHHHHHHCCCHHHH
23806337
829AcetylationKLTATTQKQEQIINT
HCCCHHHHHHHHHHH
23806337
829UbiquitinationKLTATTQKQEQIINT
HCCCHHHHHHHHHHH
-
847UbiquitinationDLRGANEKLAVAEVR
HHCCCCHHHHHHHHH
27667366
994PhosphorylationAQLASQSTQRTGKGQ
HHHHHHHHCCCCCCC
22668510
1028UbiquitinationQVNDLKERLKTSTSN
HHHHHHHHHHHCCCC
27667366
1030UbiquitinationNDLKERLKTSTSNVE
HHHHHHHHHCCCCHH
27667366
1044PhosphorylationEQYRAMVTSLEDSLN
HHHHHHHHHHHHHHC
-
1115PhosphorylationSELKKTLSTVQNEVQ
HHHHHHHHHHHHHHH
28285833
1202AcetylationESQLLECKASWEERE
HHHHHHHHCCHHHHH
-
1221PhosphorylationDEVSKSVSRCEDLEK
HHHHHHHHCCHHHHH
20531401
1259PhosphorylationVQAPLNVSLNEEGKS
HHCCCCCCCCCCCCC
26824392
1340PhosphorylationHEELMKKTETMNVVM
HHHHHHHHCHHHHHH
28576409
1501UbiquitinationKIIDIQEKVKTITQV
HEEEHHHHHHHHHHH
-
1536PhosphorylationAMETSTQSSGDHQEQ
HHCHHCCCCCCCCHH
-
1546PhosphorylationDHQEQHISVQEMQEL
CCCHHHCCHHHHHHH
-
1558PhosphorylationQELKDTLSQSETKTK
HHHHHHHCCCHHHHH
27841257
1563UbiquitinationTLSQSETKTKSLEGQ
HHCCCHHHHHHHHHH
27667366
1565UbiquitinationSQSETKTKSLEGQVE
CCCHHHHHHHHHHHH
27667366
1579UbiquitinationENLQKTLSEKETEAR
HHHHHHHCHHHHHHH
27667366
1581UbiquitinationLQKTLSEKETEARSL
HHHHHCHHHHHHHHH
27667366
1623UbiquitinationRQQMNEKTWKTLALA
HHHHHHHHHHHHHHH
27667366
1625MalonylationQMNEKTWKTLALAKS
HHHHHHHHHHHHHHH
26320211
1625UbiquitinationQMNEKTWKTLALAKS
HHHHHHHHHHHHHHH
27667366
1631MalonylationWKTLALAKSKITHLS
HHHHHHHHHHCHHHH
26320211
1632PhosphorylationKTLALAKSKITHLSG
HHHHHHHHHCHHHHC
24719451
1635PhosphorylationALAKSKITHLSGVKD
HHHHHHCHHHHCCHH
24719451
1638PhosphorylationKSKITHLSGVKDQLT
HHHCHHHHCCHHHHH
24719451
1650UbiquitinationQLTKEIEELKQRNGA
HHHHHHHHHHHHCCC
27667366
1652UbiquitinationTKEIEELKQRNGALD
HHHHHHHHHHCCCHH
27667366
1654DimethylationEIEELKQRNGALDQQ
HHHHHHHHCCCHHHH
-
1654MethylationEIEELKQRNGALDQQ
HHHHHHHHCCCHHHH
54541789
1681PhosphorylationSQYEGRISRLERELR
HHHHHHHHHHHHHHH
25338131
1705UbiquitinationRDEPQEPTNKAPEQQ
CCCCCCCCCCCHHHH
27667366
1707UbiquitinationEPQEPTNKAPEQQRQ
CCCCCCCCCHHHHHC
27667366
1716UbiquitinationPEQQRQITLKTTPAS
HHHHHCEEEEECCCC
27667366
1718UbiquitinationQQRQITLKTTPASGE
HHHCEEEEECCCCCC
27667366
1719PhosphorylationQRQITLKTTPASGER
HHCEEEEECCCCCCC
22802335
1720PhosphorylationRQITLKTTPASGERG
HCEEEEECCCCCCCC
22802335
1723PhosphorylationTLKTTPASGERGIAS
EEEECCCCCCCCCCC
22802335
1730PhosphorylationSGERGIASTSDPPTA
CCCCCCCCCCCCCCC
25266776
1731PhosphorylationGERGIASTSDPPTAN
CCCCCCCCCCCCCCC
25266776
1732PhosphorylationERGIASTSDPPTANI
CCCCCCCCCCCCCCC
26643407
1736PhosphorylationASTSDPPTANIKPTP
CCCCCCCCCCCCCCC
26643407
1742PhosphorylationPTANIKPTPVVSTPS
CCCCCCCCCCCCCCC
25263469
1746PhosphorylationIKPTPVVSTPSKVTA
CCCCCCCCCCCHHHH
26239621
1747PhosphorylationKPTPVVSTPSKVTAA
CCCCCCCCCCHHHHH
22942356
1749PhosphorylationTPVVSTPSKVTAAAM
CCCCCCCCHHHHHHH
24453211
1752PhosphorylationVSTPSKVTAAAMAGN
CCCCCHHHHHHHCCC
22802335
1760AcetylationAAAMAGNKSTPRASI
HHHHCCCCCCCCCCC
23806337
1761PhosphorylationAAMAGNKSTPRASIR
HHHCCCCCCCCCCCC
26745281
1762PhosphorylationAMAGNKSTPRASIRP
HHCCCCCCCCCCCCC
26745281
1780PhosphorylationPATVTNPTTTPTATV
CCEECCCCCCCCCEE
25338131
1963PhosphorylationYNQDSQDSIGEGVTQ
CCCCCCCCCCCCCCC
-
2080PhosphorylationDAEGGDGTDPGTETE
CCCCCCCCCCCCCCC
-
2084PhosphorylationGDGTDPGTETEESMG
CCCCCCCCCCCCCCC
20531401
2086PhosphorylationGTDPGTETEESMGGA
CCCCCCCCCCCCCCH
-
2102PhosphorylationSHQRAADSQNSGEGN
HHHHHHHCCCCCCCC
26239621
2105PhosphorylationRAADSQNSGEGNTSA
HHHHCCCCCCCCCHH
23684622
2110PhosphorylationQNSGEGNTSAAESSF
CCCCCCCCHHHHHHH
26239621
2111PhosphorylationNSGEGNTSAAESSFS
CCCCCCCHHHHHHHH
25293948
2115PhosphorylationGNTSAAESSFSQEVA
CCCHHHHHHHHHHHH
28833060
2116PhosphorylationNTSAAESSFSQEVAR
CCHHHHHHHHHHHHH
28833060
2118PhosphorylationSAAESSFSQEVAREQ
HHHHHHHHHHHHHHH
28833060
2128PhosphorylationVAREQQPTSASERQT
HHHHHCCCCHHHCCC
23684622
2129PhosphorylationAREQQPTSASERQTP
HHHHCCCCHHHCCCC
29514104
2131PhosphorylationEQQPTSASERQTPQA
HHCCCCHHHCCCCCC
23684622
2135PhosphorylationTSASERQTPQAPQSP
CCHHHCCCCCCCCCC
27742792
2141PhosphorylationQTPQAPQSPRRPPHP
CCCCCCCCCCCCCCC
27087446
2174MethylationQRIQMTRRQSVGRGL
CEEECCCHHCCCCCC
24129315
2176PhosphorylationIQMTRRQSVGRGLQL
EECCCHHCCCCCCCC
23737553
2179DimethylationTRRQSVGRGLQLTPG
CCHHCCCCCCCCCCC
-
2179MethylationTRRQSVGRGLQLTPG
CCHHCCCCCCCCCCC
24129315
2184PhosphorylationVGRGLQLTPGIGGMQ
CCCCCCCCCCCCCCC
25521595
2201PhosphorylationFFDDEDRTVPSTPTL
CCCCCCCCCCCCCEE
28833060
2204PhosphorylationDEDRTVPSTPTLVVP
CCCCCCCCCCEEEEC
20469934
2205PhosphorylationEDRTVPSTPTLVVPH
CCCCCCCCCEEEECC
26824392
2207PhosphorylationRTVPSTPTLVVPHRT
CCCCCCCEEEECCCC
28833060
2214PhosphorylationTLVVPHRTDGFAEAI
EEEECCCCCCHHHHH
28833060
2223PhosphorylationGFAEAIHSPQVAGVP
CHHHHHCCCCCCCCC
27087446
2231MethylationPQVAGVPRFRFGPPE
CCCCCCCCCCCCCCC
24129315
2398PhosphorylationFRRVRLQTTLRQGVR
CCEEHHHHHHHHCCC
29514104
2411Asymmetric dimethylarginineVRGRQFNRQRGISHA
CCCCCHHHHHCCCHH
-
2411MethylationVRGRQFNRQRGISHA
CCCCCHHHHHCCCHH
24129315
2413Asymmetric dimethylarginineGRQFNRQRGISHAMG
CCCHHHHHCCCHHHC
-
2413MethylationGRQFNRQRGISHAMG
CCCHHHHHCCCHHHC
24129315
2422Asymmetric dimethylarginineISHAMGGRGGINRGN
CCHHHCCCCCCCCCC
-
2422MethylationISHAMGGRGGINRGN
CCHHHCCCCCCCCCC
24129315
2427DimethylationGGRGGINRGNIN---
CCCCCCCCCCCC---
-
2427MethylationGGRGGINRGNIN---
CCCCCCCCCCCC---
54541773

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
2184TPhosphorylationKinaseMAPK1P63085
GPS
2205TPhosphorylationKinaseMAPK1P63085
GPS
2223SPhosphorylationKinaseMAPK1P63085
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPR_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TPR_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AHNK_HUMANAHNAKphysical
20360068
TRI29_HUMANTRIM29physical
20360068
PPIA_HUMANPPIAphysical
20360068
TPR_HUMANTPRphysical
20360068
KPYM_HUMANPKMphysical
20360068
POF1B_HUMANPOF1Bphysical
20360068

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPR_MOUSE

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Related Literatures of Post-Translational Modification

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