CE85L_HUMAN - dbPTM
CE85L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CE85L_HUMAN
UniProt AC Q5SZL2
Protein Name Centrosomal protein of 85 kDa-like
Gene Name CEP85L
Organism Homo sapiens (Human).
Sequence Length 805
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Subcellular experiments using a GFP-tagged system produced a weak signal, rendering it difficult to confirm centrosome association.
Protein Description
Protein Sequence MWGRFLAPEASGRDSPGGARSFPAGPDYSSAWLPANESLWQATTVPSNHRNNHIRRHSIASDSGDTGIGTSCSDSVEDHSTSSGTLSFKPSQSLITLPTAHVMPSNSSASISKLRESLTPDGSKWSTSLMQTLGNHSRGEQDSSLDMKDFRPLRKWSSLSKLTAPDNCGQGGTVCREESRNGLEKIGKAKALTSQLRTIGPSCLHDSMEMLRLEDKEINKKRSSTLDCKYKFESCSKEDFRASSSTLRRQPVDMTYSALPESKPIMTSSEAFEPPKYLMLGQQAVGGVPIQPSVRTQMWLTEQLRTNPLEGRNTEDSYSLAPWQQQQIEDFRQGSETPMQVLTGSSRQSYSPGYQDFSKWESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAQHAMLGHYVNCEDSYVASLQPQYENTSLQTPFSEESVSHSQQGEFEQKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPLFDLTVIDQLFKEMSCCLFDLKALCSILNQRAQGKEPNLSLLLGIRSMNCSAEETENDHSTETLTKKLSDVCQLRRDIDELRTTISDRYAQDMGDNCITQ
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
11PhosphorylationRFLAPEASGRDSPGG
CCCCCCCCCCCCCCC		32.4723403867
15PhosphorylationPEASGRDSPGGARSF
CCCCCCCCCCCCCCC		24.8823403867
87PhosphorylationSTSSGTLSFKPSQSL
CCCCCEECCCCCCCE		30.9424719451
113UbiquitinationNSSASISKLRESLTP
CCCCHHHHHHHHCCC		50.31-
117PhosphorylationSISKLRESLTPDGSK
HHHHHHHHCCCCCCH		30.9822199227
119PhosphorylationSKLRESLTPDGSKWS
HHHHHHCCCCCCHHH		28.7222199227
123PhosphorylationESLTPDGSKWSTSLM
HHCCCCCCHHHHHHH		38.0327307780
126PhosphorylationTPDGSKWSTSLMQTL
CCCCCHHHHHHHHHH		16.3227307780
127PhosphorylationPDGSKWSTSLMQTLG
CCCCHHHHHHHHHHC		25.4327307780
128PhosphorylationDGSKWSTSLMQTLGN
CCCHHHHHHHHHHCC		19.1427307780
132PhosphorylationWSTSLMQTLGNHSRG
HHHHHHHHHCCCCCC		23.7527307780
137PhosphorylationMQTLGNHSRGEQDSS
HHHHCCCCCCCCCCC		46.0827307780
144PhosphorylationSRGEQDSSLDMKDFR
CCCCCCCCCCHHCCC		36.3624719451
148UbiquitinationQDSSLDMKDFRPLRK
CCCCCCHHCCCCCCC		54.07-
157PhosphorylationFRPLRKWSSLSKLTA
CCCCCCCCCCCCCCC		25.1623312004
158PhosphorylationRPLRKWSSLSKLTAP
CCCCCCCCCCCCCCC		35.2323312004
160PhosphorylationLRKWSSLSKLTAPDN
CCCCCCCCCCCCCCC		27.8023312004
161UbiquitinationRKWSSLSKLTAPDNC
CCCCCCCCCCCCCCC		55.97-
164 (in isoform 4)Ubiquitination-21.64-
185UbiquitinationESRNGLEKIGKAKAL
HHHCHHHHHHHHHHH		62.90-
188 (in isoform 4)Ubiquitination-50.62-
190UbiquitinationLEKIGKAKALTSQLR
HHHHHHHHHHHHHHH		47.63-
207PhosphorylationGPSCLHDSMEMLRLE
CHHHHHHHHHHHHHC		13.0921938754
210 (in isoform 4)Phosphorylation-1.6527251275
212DimethylationHDSMEMLRLEDKEIN
HHHHHHHHHCCHHHH		34.42-
212MethylationHDSMEMLRLEDKEIN
HHHHHHHHHCCHHHH		34.42-
231UbiquitinationSTLDCKYKFESCSKE
CCCCCCHHCCCCCHH		28.31-
232 (in isoform 4)Ubiquitination-8.30-
234PhosphorylationDCKYKFESCSKEDFR
CCCHHCCCCCHHHHH		27.1630631047
236PhosphorylationKYKFESCSKEDFRAS
CHHCCCCCHHHHHCC		48.6530631047
237UbiquitinationYKFESCSKEDFRASS
HHCCCCCHHHHHCCC		66.68-
240 (in isoform 4)Ubiquitination-8.03-
243PhosphorylationSKEDFRASSSTLRRQ
CHHHHHCCCCCCCCC		22.1427251275
246 (in isoform 4)Phosphorylation-26.6527251275
246PhosphorylationDFRASSSTLRRQPVD
HHHCCCCCCCCCCCC		26.65-
280 (in isoform 4)Phosphorylation-5.3127642862
314PhosphorylationNPLEGRNTEDSYSLA
CCCCCCCCCCCCCCC		39.55-
317PhosphorylationEGRNTEDSYSLAPWQ
CCCCCCCCCCCCHHH		15.47-
351PhosphorylationGSSRQSYSPGYQDFS
CCCCCCCCCCCCCHH		19.66-
359UbiquitinationPGYQDFSKWESMLKI
CCCCCHHHHHHHHHH		55.78-
361 (in isoform 3)Ubiquitination-29.9721890473
362 (in isoform 4)Ubiquitination-28.44-
367UbiquitinationWESMLKIKEGLLRQK
HHHHHHHHHHHHHCC		44.11-
374UbiquitinationKEGLLRQKEIVIDRQ
HHHHHHCCEEEECHH		42.87-
377 (in isoform 4)Ubiquitination-3.79-
382UbiquitinationEIVIDRQKQQITHLH
EEEECHHHHHHHHHH		45.09-
453UbiquitinationQKLASTEKEVLQLNE
HHHHHCHHHHHHHHH		53.89-
456 (in isoform 4)Ubiquitination-5.13-
463UbiquitinationLQLNEFLKQRLSLFS
HHHHHHHHHHHHCCH		38.4021890473
463UbiquitinationLQLNEFLKQRLSLFS
HHHHHHHHHHHHCCH		38.4021890473
463 (in isoform 1)Ubiquitination-38.4021890473
466 (in isoform 2)Ubiquitination-4.9021890473
488PhosphorylationKTRDRYISSLKKKCQ
HHHHHHHHHHHHHHH		22.2324719451
514PhosphorylationRIETLEKYLADLPTL
HHHHHHHHHHCCCCH		9.5724043423
520PhosphorylationKYLADLPTLDDVQSQ
HHHHCCCCHHHHHHH		50.5524043423
526PhosphorylationPTLDDVQSQSLQLQI
CCHHHHHHHHHHHHH		22.9124043423
528PhosphorylationLDDVQSQSLQLQILE
HHHHHHHHHHHHHHH		24.2724043423
537UbiquitinationQLQILEEKNKNLQEA
HHHHHHHHCCCHHHH		64.94-
548PhosphorylationLQEALIDTEKKLEEI
HHHHHHHHHHHHHHH		42.5925690035
556SuccinylationEKKLEEIKKQCQDKE
HHHHHHHHHHHCCHH		39.8223954790
564PhosphorylationKQCQDKETQLICQKK
HHHCCHHHHHHHCHH		34.1228152594
586UbiquitinationTVQSLQQKVERCLED
HHHHHHHHHHHHHHC		32.86-
589 (in isoform 4)Ubiquitination-33.05-
621UbiquitinationQQNETASKIIDSQQD
HHHHHHHHHHHHHHH		41.01-
624 (in isoform 4)Ubiquitination-43.81-
646AcetylationSMQGKLSKEKLTTQK
HHCCCCCHHHHHHHH		70.1119817345
650PhosphorylationKLSKEKLTTQKMMEE
CCCHHHHHHHHHHHH		37.9428509920
651PhosphorylationLSKEKLTTQKMMEEL
CCHHHHHHHHHHHHH		36.3128509920
653AcetylationKEKLTTQKMMEELEK
HHHHHHHHHHHHHHH		37.8219817351
670UbiquitinationRNVQRLTKALLENQR
HHHHHHHHHHHHHHH		41.45-
673 (in isoform 4)Ubiquitination-7.49-
740UbiquitinationLNQRAQGKEPNLSLL
HHHHHCCCCCCHHHH		58.90-
743 (in isoform 4)Ubiquitination-43.27-
756PhosphorylationGIRSMNCSAEETEND
HHHHCCCCCCCCCCC		33.44-
772UbiquitinationSTETLTKKLSDVCQL
CHHHHHHHHHHHHHH		48.24-
775 (in isoform 4)Ubiquitination-56.50-
788PhosphorylationRDIDELRTTISDRYA
HHHHHHHHHHHHHHH		40.9029083192
789PhosphorylationDIDELRTTISDRYAQ
HHHHHHHHHHHHHHH		16.4329083192
791PhosphorylationDELRTTISDRYAQDM
HHHHHHHHHHHHHHH		17.5929083192
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 CE85L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CE85L_HUMAN !!
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 CE85L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CE85L_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CE85L_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory