SENP_CAEEL - dbPTM
SENP_CAEEL - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP_CAEEL
UniProt AC Q09353
Protein Name Sentrin-specific protease
Gene Name ulp-1
Organism Caenorhabditis elegans.
Sequence Length 697
Subcellular Localization Nucleus envelope .
Protein Description Protease that deconjugates smo-1 from targeted proteins and may catalyze the processing of smo-1 to its mature form..
Protein Sequence MSRRSDLSDKDSQSRKRHWLTDQAVTNEEKEQSPTKRTRKTKSQGLGGLFNTFFGMFVSSNSGEKEKTEVSGEVQVQEDDEIIVEGTTRRVAENKKYMIFLNEDAPVRANAGSEENEVIIEKHVQKNVEIRNDEEKQEVQGDLVLTLSSSPKSPKNLEKSFEVQQDDEEPDVLFEKVVKTPNKQLQEARRFQNELIFLNDNPDTPDDVSVISDSRSKEFISPTPDDSVSRPITPSLSSLSNYTSNNVRDYWRRNSAKKPEVLRRVPVRHQFKHSTSVRKMNTIIDLKKIKNHLSSRDRLLQGVVASGQYEAKAISGIVEKKPKKMQRTSSTDILARAKNKIAELGGSRSNTPSLLSREPSIIIDSEESTSSSYRQHARSNSSESDSYRKLNDILSQINSLGIGSAYRGPQRYQNSYQLSKQKEDKLLEEARIREGHRSQTRGDRLEDVRKRLELQGIAIRPKVEKKKVDDFMALPDAADALVERAWSGGNPNEQFVDAFSIQICKKDLATLSGLHWLNDEIINFYLQLICDRSNGDSKYPKIYAFNTFFYSNIVSKGYASVKRWTRKVDIFAFDIVLVPVHLGMHWCMAVIDMGEKKIEFYDSLYDGNTAVLPALRGYLEAESLDKKKTAMNFSGWTIQQMTDIPRQQNGSDCGVFSCQFGEWASRRTTPRFTQKNMPYYRKRMVYEIVSKKLLATI
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
33PhosphorylationTNEEKEQSPTKRTRK
CCHHHHCCCCCCCHH
35.3121082442
35PhosphorylationEEKEQSPTKRTRKTK
HHHHCCCCCCCHHHH
38.1021082442
146PhosphorylationVQGDLVLTLSSSPKS
ECCCEEEEECCCCCC
19.6730078680
148PhosphorylationGDLVLTLSSSPKSPK
CCEEEEECCCCCCCC
24.4330078680
149PhosphorylationDLVLTLSSSPKSPKN
CEEEEECCCCCCCCC
54.4930078680
150PhosphorylationLVLTLSSSPKSPKNL
EEEEECCCCCCCCCH
32.7330078680
160PhosphorylationSPKNLEKSFEVQQDD
CCCCHHHHEECCCCC
19.7730078680
221PhosphorylationSRSKEFISPTPDDSV
CCCCCCCCCCCCCCC
28.2130078680
223PhosphorylationSKEFISPTPDDSVSR
CCCCCCCCCCCCCCC
32.3430078680
227PhosphorylationISPTPDDSVSRPITP
CCCCCCCCCCCCCCC
29.4030078680
229PhosphorylationPTPDDSVSRPITPSL
CCCCCCCCCCCCCCH
35.9730078680
233PhosphorylationDSVSRPITPSLSSLS
CCCCCCCCCCHHHHC
14.9830078680
235PhosphorylationVSRPITPSLSSLSNY
CCCCCCCCHHHHCCC
32.0330078680
237PhosphorylationRPITPSLSSLSNYTS
CCCCCCHHHHCCCCC
33.3030078680
238PhosphorylationPITPSLSSLSNYTSN
CCCCCHHHHCCCCCC
40.9030078680
328PhosphorylationKPKKMQRTSSTDILA
CCCCCCCCCHHHHHH
15.3330078680
329PhosphorylationPKKMQRTSSTDILAR
CCCCCCCCHHHHHHH
33.1730078680
330PhosphorylationKKMQRTSSTDILARA
CCCCCCCHHHHHHHH
29.5019060867
347PhosphorylationKIAELGGSRSNTPSL
HHHHHCCCCCCCHHH
30.6428854356
349PhosphorylationAELGGSRSNTPSLLS
HHHCCCCCCCHHHHC
46.9119530675
351PhosphorylationLGGSRSNTPSLLSRE
HCCCCCCCHHHHCCC
18.5919530675
353PhosphorylationGSRSNTPSLLSREPS
CCCCCCHHHHCCCCC
39.6519530675
356PhosphorylationSNTPSLLSREPSIII
CCCHHHHCCCCCEEE
39.6319530675
360PhosphorylationSLLSREPSIIIDSEE
HHHCCCCCEEECCCC
22.9730078680
381PhosphorylationRQHARSNSSESDSYR
HHHHHCCCCCCHHHH
36.4121082442

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 SENP_CAEEL !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 SENP_CAEEL !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SENP_CAEEL !!

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

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Related Literatures of Post-Translational Modification

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