PCNT_MOUSE - dbPTM
PCNT_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCNT_MOUSE
UniProt AC P48725
Protein Name Pericentrin
Gene Name Pcnt
Organism Mus musculus (Mouse).
Sequence Length 2898
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Centrosomal at all stages of the cell cycle. Remains associated with centrosomes following microtubule depolymerization. Colocalized with DISC1 at the centrosome.
Protein Description Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome..
Protein Sequence MEDEQEQRRRKVEAGRAKLANFRQRKTKGDCPNSKKKTAKRKGSAVHASVQEEGSVATPNSELPQGGAVFESPSCSNTLEGTRGASAAQEQEDCELDVTDLQGQQQTQPPPPQTAHSLELEALRLSLNNMHTAQLELTQANLQKEKETALTELREMLNGRRAQELALLQSRQQCELELLREQHAREKEEMALRSGQEAAELKEKLRSEMEKNAQTIETLKQDWESERELCLENLRQELSLKHQSEMEGLQSQFQKELSEQKVELEKIFQAKHEAEVSLKNLEAQHQAAIKKLQEDLQSEHCQYLQDLEQKFREKEKAKELELETLQASYEDLKAQSQEEIRLLWSQLESMKTNREELNGSWDPVLAQASHLEELEHLRSGFAQQQQQERAQHESELEHLRVYFEKKLKDAEKTYQEDLTVFQQRLQEAREDSLESTEISSSCVLPEETSGREGKEPPDPLDLQLGQPKVQESLVEDCQVKLSKAEEKIQQMKEEFQKKEAEWELSREELKREAEERLASMFLELREKAESEKLSIISRFEHRESSMRHLQDQQAAQILDLERSLMEQQGHLRQLEQELTRDDLLPCSQCGQEPAMAQEEKNGALLREKEDCALQLLMAQNRFLEERKEIMEKFAKEQDAFLRDAQEKHNHELQLLQQGHQQQLLALRMELETKHRSELTEQLASSESRRQALLETHVAELQVKHNAEISALEKRHLSNLDELESCYVADVQTIRDEHQQALELLRAELEEQLQKKESCHREMLTQELENLKRQHAEELQSVRDSLRMEMSAQHIENGKGPAADLQGAHQQDPAMALHNEGHLLVEDGDAVLRSVDAEGLLHQAGPQELGDAHTVEMQKSQAELAKPQELQASQDQVAQVRDKVFLLNRELEECRAELEQLQQRRERENQEGTTLICMLRADLELAQGEGKALRDALRRLLDLFGDTLKAAVTLKSRISERAGLLLDHEDAADTSDARLAAAALGDMWSDEGLLEIDRTLPEGAETSSVCEISSHVCESFFISPENTLDCEQPIRRVYQSLSTAVEGLLEMALDSSKQLEEARQLHRCVEREFRHRNEEMAQAMQKQQELLERLREESAAKDRLALELHTAKGLLEGFKVEKVDLQEALGKKEESEQQLILELEDLRKQLQQAARELLTLKEEKSVLWNQKETLTNEAKEREAALQEEVESLTRVQWESRKQSEKDRATLLSQMRVLESELEDQLVQHRGCAQLAEEVATLKQQLAALDKHLRSQRQFMDDQAAEREHEREEFQQEIQRLEGQLRQAARPRPPGPRDSQCVQLDEEVELLQEKLREKLDGFNELVIKKDFADQQLLIQEEEIKRLEETNASIQRQMVQLQEELEKQKKSMEELKEKEILKQENMGDLLLTTVSRSGLDEAGCPMLPQGSSSRGPEAQPDVTERALLQHENEVVHRRNSEIDELKSLIENLQENQRQLQKDKAEEIEQLHEVIEKLQSELSLMGPKVHEVSDPQAGSLHSELACLRGEGLGGQALRSELQAAQAAKEVFGQLLANQAHGHSQALEALQQRLQDAEEVAARHLAELEHCVALREAEVEAMASQIQEFAATLKAKEAIIEQRDLEIDAVNKWKVSHSLELEAILLALAHFRHALEQQTCATPDEPPELRQLRVQCARLSHQLQVLYRPFLKCRMQLDQHQPHVASIGCANPCADDELEQEGVSNRLALAPHSLAAQAKEELEDCPLGKANLMAQVRQLQEELDHRVHSVASRDTNSETCKLQQPNLSENGPRNHCCNGEESKPSPPDDVLNIAKTTWDVIDIIKNQDLLVQVEMPDFPTQEKLTSQGGPFSSQASGHSGSLLPEEAAEPQQDPVRALDLSSWSSPEVVRKDPSLEPQHSLPLTPGVGTVSLHSVDISPDWTDPLLQADVSGLLCYPGKSASGQAPLWAVAPSAGKHHAERTATEKDVEDFIVTSFDSQELLTSPSHELARRSDGSRKSDGPDIAMMLTLGSEGSETPTTDLVAAAAAAVPFSRRFVQSPGAMKEKEIHAKQMKALLQMVFDESHQILALSESQDPSSALNKGEPRDPLDGFPRDSQALSEVTTDKGEKESLETHLTWSEELLRAIQEVFAREQEKAELQPRPYGSNLGDYNSLVQRLEKVIQEQGDPQKVQDHLCLSDRSSLLAEIQALRAQLRMTHLQNQEKLQQLCAALTSTEARGSQREHQLRRQVELLAYKVEQEKCIANELQKTLSKEQETASDVRKRLVVEQNAVQDLKSELHACKQENTSLLESLDKVQQEVLRLRAVLDGKEKELKVVLEELESERGKGQALQAQQEEQQLRYLQREGQSSRALEELKLSLEKQLAQNNQLCVALKHERAAKDNLQKELQIEASRCEALLAQEKGQLSELQKSLEAERSRSLELSEALQHERLLTEQLSRNSQEACARQETQVQHALLRKLKAEKTRALELEAMLEKVQKQAAHTQQQLEAQAQERCVELRREKERELEIQRQRDEHKIEQLQRLVRELRWKEEVSGGNGPCRGSPGRGSLERDQFQEQQQELEKIRQQLLCAAGLLTSFTNHTVDRTIKDWTSSNEKAVSSLMRTLEELKSELSMPTSFQKKMTAELQVQLMNELLSDNDALTKAVGMATREKAELCRTVSRLEKTLKHHTQKGCVLNRQSKSSLKQDGTDLQSSLRHSDPEWHSQTTSGDTNTCNIKMEKLYLHYLRAESFRKALIYQKKYLLLLIGGFQDSEQETLSMIAHLGVFPSKADKKITMSRPFTKFRTAVRVVIAVLRLRFLVKKWQEVDRKGALVHPKSTRHGHRTSQRQRSPSGPRASLPTRDTSSGPTKASRHSPRSAAAGSPGKERSTSTPSSRLERSLTASQDPEHSLTEYIHHLEMIQQRLGGLPPDSTQKSCHQKIKQ
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
44PhosphorylationKTAKRKGSAVHASVQ
CCCCCCCCCCHHHHC		30.10-
239PhosphorylationENLRQELSLKHQSEM
HHHHHHHHHHHHHHH		34.3219144319
432PhosphorylationLQEAREDSLESTEIS
HHHHHHHHHHCCCCC		29.3225619855
435PhosphorylationAREDSLESTEISSSC
HHHHHHHCCCCCCCC		36.3125619855
436PhosphorylationREDSLESTEISSSCV
HHHHHHCCCCCCCCC		28.1528833060
439PhosphorylationSLESTEISSSCVLPE
HHHCCCCCCCCCCCC		15.2328833060
440PhosphorylationLESTEISSSCVLPEE
HHCCCCCCCCCCCCC		33.1628833060
441PhosphorylationESTEISSSCVLPEET
HCCCCCCCCCCCCCC		11.0628833060
563PhosphorylationQILDLERSLMEQQGH
HHHHHHHHHHHHHHH		23.7728066266
676PhosphorylationELETKHRSELTEQLA
HHHHHHHHHHHHHHH		36.36-
930UbiquitinationELAQGEGKALRDALR
HHHCCCCHHHHHHHH		39.69-
946PhosphorylationLLDLFGDTLKAAVTL
HHHHHHHHHHHHHHH		30.4518846507
952PhosphorylationDTLKAAVTLKSRISE
HHHHHHHHHHHHHHH		24.6018846507
955PhosphorylationKAAVTLKSRISERAG
HHHHHHHHHHHHHHC		37.6518846507
973PhosphorylationDHEDAADTSDARLAA
CCCHHCCCHHHHHHH		24.6328066266
974PhosphorylationHEDAADTSDARLAAA
CCHHCCCHHHHHHHH		29.8028066266
1022PhosphorylationVCESFFISPENTLDC
HHCCCCCCCCCCCCC		22.47-
1147AcetylationLELEDLRKQLQQAAR
HHHHHHHHHHHHHHH		63.767711671
1160AcetylationARELLTLKEEKSVLW
HHHHHHHHHHHHHHH		59.607711683
1174PhosphorylationWNQKETLTNEAKERE
HCCHHHHCHHHHHHH		38.13-
1350PhosphorylationRLEETNASIQRQMVQ
HHHHHCHHHHHHHHH		22.7130635358
1435PhosphorylationENEVVHRRNSEIDEL
HHHHHHHCHHHHHHH		35.8319144319
1437PhosphorylationEVVHRRNSEIDELKS
HHHHHCHHHHHHHHH		33.8327087446
1444PhosphorylationSEIDELKSLIENLQE
HHHHHHHHHHHHHHH		47.4019854140
1780PhosphorylationNGEESKPSPPDDVLN
CCCCCCCCCCHHHHH		53.4529550500
1828PhosphorylationSQGGPFSSQASGHSG
CCCCCCCCCCCCCCC		30.09-
1856PhosphorylationPVRALDLSSWSSPEV
CCHHHCCCCCCCCHH		29.4528066266
1857PhosphorylationVRALDLSSWSSPEVV
CHHHCCCCCCCCHHH		37.9728066266
1859PhosphorylationALDLSSWSSPEVVRK
HHCCCCCCCCHHHCC		37.6521743459
1860PhosphorylationLDLSSWSSPEVVRKD
HCCCCCCCCHHHCCC		20.8722942356
1931AcetylationAVAPSAGKHHAERTA
EECCCCCCCCHHCCC		31.7523806337
1953PhosphorylationFIVTSFDSQELLTSP
HEEECCCCCHHHCCC		24.4421183079
1958PhosphorylationFDSQELLTSPSHELA
CCCCHHHCCCCHHHH		51.7423984901
1959PhosphorylationDSQELLTSPSHELAR
CCCHHHCCCCHHHHH		25.1126239621
1961PhosphorylationQELLTSPSHELARRS
CHHHCCCCHHHHHCC		29.3923984901
1974PhosphorylationRSDGSRKSDGPDIAM
CCCCCCCCCCCCEEE		46.84-
1984PhosphorylationPDIAMMLTLGSEGSE
CCEEEEEECCCCCCC		15.92-
1987PhosphorylationAMMLTLGSEGSETPT
EEEEECCCCCCCCCC		41.7321183079
1990PhosphorylationLTLGSEGSETPTTDL
EECCCCCCCCCCHHH		33.9621183079
1992PhosphorylationLGSEGSETPTTDLVA
CCCCCCCCCCHHHHH		27.8622817900
2014PhosphorylationFSRRFVQSPGAMKEK
CHHHHHCCCCCCCHH		21.7225266776
2039PhosphorylationLQMVFDESHQILALS
HHHHHCCHHHHHEEE		23.6522802335
2046PhosphorylationSHQILALSESQDPSS
HHHHHEEECCCCHHH		29.6022802335
2048PhosphorylationQILALSESQDPSSAL
HHHEEECCCCHHHHC		36.1922802335
2053PhosphorylationSESQDPSSALNKGEP
ECCCCHHHHCCCCCC		42.0122802335
2128PhosphorylationSNLGDYNSLVQRLEK
CCCCCHHHHHHHHHH		24.56-
2387PhosphorylationQLSELQKSLEAERSR
CHHHHHHHHHHHHHH		20.6230635358
2393PhosphorylationKSLEAERSRSLELSE
HHHHHHHHHHCHHHH		20.0930635358
2395PhosphorylationLEAERSRSLELSEAL
HHHHHHHHCHHHHHH		27.6930635358
2399PhosphorylationRSRSLELSEALQHER
HHHHCHHHHHHHHHH		16.0830635358
2510PhosphorylationLRWKEEVSGGNGPCR
HHCCHHHCCCCCCCC		44.2423684622
2519PhosphorylationGNGPCRGSPGRGSLE
CCCCCCCCCCCCCCC		12.5823684622
2575PhosphorylationSSNEKAVSSLMRTLE
CCCHHHHHHHHHHHH		23.7130635358
2576PhosphorylationSNEKAVSSLMRTLEE
CCHHHHHHHHHHHHH		21.4230635358
2580PhosphorylationAVSSLMRTLEELKSE
HHHHHHHHHHHHHHH		25.2630635358
2586PhosphorylationRTLEELKSELSMPTS
HHHHHHHHHHCCCCH		57.2930635358
2589PhosphorylationEELKSELSMPTSFQK
HHHHHHHCCCCHHHH		20.7530635358
2592PhosphorylationKSELSMPTSFQKKMT
HHHHCCCCHHHHHHH		33.2730635358
2593PhosphorylationSELSMPTSFQKKMTA
HHHCCCCHHHHHHHH		21.5830635358
2636PhosphorylationAELCRTVSRLEKTLK
HHHHHHHHHHHHHHH		30.4529176673
2650S-nitrosocysteineKHHTQKGCVLNRQSK
HHHCCCCCCCCCCCH		3.97-
2650S-nitrosylationKHHTQKGCVLNRQSK
HHHCCCCCCCCCCCH		3.9721278135
2669PhosphorylationQDGTDLQSSLRHSDP
CCCCCHHHHHCCCCC		38.3428066266
2670PhosphorylationDGTDLQSSLRHSDPE
CCCCHHHHHCCCCCH		19.2328066266
2771PhosphorylationRVVIAVLRLRFLVKK
HHHHHHHHHHHHHHH		19.7424719451
2792AcetylationKGALVHPKSTRHGHR
CCCCCCCCCCCCCCC		49.9715612401
2806PhosphorylationRTSQRQRSPSGPRAS
CCCCCCCCCCCCCCC		18.3223737553
2808PhosphorylationSQRQRSPSGPRASLP
CCCCCCCCCCCCCCC		63.7828066266
2813PhosphorylationSPSGPRASLPTRDTS
CCCCCCCCCCCCCCC		35.8429514104
2819PhosphorylationASLPTRDTSSGPTKA
CCCCCCCCCCCCCCC		22.8525338131
2820PhosphorylationSLPTRDTSSGPTKAS
CCCCCCCCCCCCCCC		37.2725338131
2827PhosphorylationSSGPTKASRHSPRSA
CCCCCCCCCCCCCHH		31.8923375375
2830PhosphorylationPTKASRHSPRSAAAG
CCCCCCCCCCHHCCC		22.3923375375
2833PhosphorylationASRHSPRSAAAGSPG
CCCCCCCHHCCCCCC		26.1623375375
2838PhosphorylationPRSAAAGSPGKERST
CCHHCCCCCCCCCCC		26.2524453211
2855PhosphorylationPSSRLERSLTASQDP
CCHHHHHHHCCCCCC		22.2426370283
2865PhosphorylationASQDPEHSLTEYIHH
CCCCCCCCHHHHHHH		35.0126370283
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

Oops, there are no upstream regulatory protein records of PCNT_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCNT_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 PCNT_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PCNT_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCNT_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-1437, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1437, AND MASSSPECTROMETRY.

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