SENP5_HUMAN - dbPTM
SENP5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP5_HUMAN
UniProt AC Q96HI0
Protein Name Sentrin-specific protease 5
Gene Name SENP5
Organism Homo sapiens (Human).
Sequence Length 755
Subcellular Localization Nucleus, nucleolus .
Protein Description Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO3 to its mature form and deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak proteolytic activity against full-length SUMO1 or SUMO1 conjugates. Required for cell division..
Protein Sequence MKKQRKILWRKGIHLAFSEKWNTGFGGFKKFYFHQHLCILKAKLGRPVTWNRQLRHFQGRKKALQIQKTWIKDEPLCAKTKFNVATQNVSTLSSKVKRKDAKHFISSSKTLLRLQAEKLLSSAKNSDHEYCREKNLLKAVTDFPSNSALGQANGHRPRTDPQPSDFPMKFNGESQSPGESGTIVVTLNNHKRKGFCYGCCQGPEHHRNGGPLIPKKFQLNQHRRIKLSPLMMYEKLSMIRFRYRILRSQHFRTKSKVCKLRKAQRSWVQKVTGDHQETRRENGEGGSCSPFPSPEPKDPSCRHQPYFPDMDSSAVVKGTNSHVPDCHTKGSSFLGKELSLDEAFPDQQNGSATNAWDQSSCSSPKWECTELIHDIPLPEHRSNTMFISETEREIMTLGQENQTSSVSDDRVKLSVSGADTSVSSVDGPVSQKAVQNENSYQMEEDGSLKQSILSSELLDHPYCKSPLEAPLVCSGLKLENQVGGGKNSQKASPVDDEQLSVCLSGFLDEVMKKYGSLVPLSEKEVLGRLKDVFNEDFSNRKPFINREITNYRARHQKCNFRIFYNKHMLDMDDLATLDGQNWLNDQVINMYGELIMDAVPDKVHFFNSFFHRQLVTKGYNGVKRWTKKVDLFKKSLLLIPIHLEVHWSLITVTLSNRIISFYDSQGIHFKFCVENIRKYLLTEAREKNRPEFLQGWQTAVTKCIPQQKNDSDCGVFVLQYCKCLALEQPFQFSQEDMPRVRKRIYKELCECRLMD
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
3Acetylation-----MKKQRKILWR
-----CCHHHHHHHH
54.7869459
6Acetylation--MKKQRKILWRKGI
--CCHHHHHHHHCCC
39.3969463
11AcetylationQRKILWRKGIHLAFS
HHHHHHHCCCHHEEE
51.1169467
18PhosphorylationKGIHLAFSEKWNTGF
CCCHHEEECCCCCCC
32.4324719451
62UbiquitinationRHFQGRKKALQIQKT
HHHCCHHHHHHHHCC
53.63-
72UbiquitinationQIQKTWIKDEPLCAK
HHHCCCCCCCCCCCC
47.83-
79AcetylationKDEPLCAKTKFNVAT
CCCCCCCCCCCEEEC
51.7825953088
90PhosphorylationNVATQNVSTLSSKVK
EEECCCHHHHCHHCC
31.0524173317
91PhosphorylationVATQNVSTLSSKVKR
EECCCHHHHCHHCCH
26.7824173317
93PhosphorylationTQNVSTLSSKVKRKD
CCCHHHHCHHCCHHH
28.3528555341
94PhosphorylationQNVSTLSSKVKRKDA
CCHHHHCHHCCHHHH
44.5828555341
95AcetylationNVSTLSSKVKRKDAK
CHHHHCHHCCHHHHH
48.6925953088
106PhosphorylationKDAKHFISSSKTLLR
HHHHHHHHCCHHHHH
27.84-
107PhosphorylationDAKHFISSSKTLLRL
HHHHHHHCCHHHHHH
30.91-
109UbiquitinationKHFISSSKTLLRLQA
HHHHHCCHHHHHHHH
45.18-
159PhosphorylationANGHRPRTDPQPSDF
CCCCCCCCCCCCCCC
55.5020068231
164PhosphorylationPRTDPQPSDFPMKFN
CCCCCCCCCCCCCCC
46.7920068231
174PhosphorylationPMKFNGESQSPGESG
CCCCCCCCCCCCCCC
37.0425627689
176PhosphorylationKFNGESQSPGESGTI
CCCCCCCCCCCCCEE
44.1222199227
180PhosphorylationESQSPGESGTIVVTL
CCCCCCCCCEEEEEE
47.3422199227
182PhosphorylationQSPGESGTIVVTLNN
CCCCCCCEEEEEECC
21.6322199227
216UbiquitinationGGPLIPKKFQLNQHR
CCCCCCCCCCCCCCC
32.75-
228PhosphorylationQHRRIKLSPLMMYEK
CCCCCCCCHHHHHHH
15.8122199227
243PhosphorylationLSMIRFRYRILRSQH
HHHHHHHHHHHHCCC
10.17-
270UbiquitinationAQRSWVQKVTGDHQE
HHHHHHHHHHCCCHH
31.95-
270UbiquitinationAQRSWVQKVTGDHQE
HHHHHHHHHHCCCHH
31.95-
287PhosphorylationRENGEGGSCSPFPSP
HHCCCCCCCCCCCCC
23.4423663014
289PhosphorylationNGEGGSCSPFPSPEP
CCCCCCCCCCCCCCC
31.1323663014
293PhosphorylationGSCSPFPSPEPKDPS
CCCCCCCCCCCCCCC
42.1323927012
306PhosphorylationPSCRHQPYFPDMDSS
CCCCCCCCCCCCCCC
22.6029759185
312PhosphorylationPYFPDMDSSAVVKGT
CCCCCCCCCCEEECC
17.3529759185
313PhosphorylationYFPDMDSSAVVKGTN
CCCCCCCCCEEECCC
22.3328555341
332PhosphorylationDCHTKGSSFLGKELS
CCCCCCCCCCCCCCC
32.91-
339PhosphorylationSFLGKELSLDEAFPD
CCCCCCCCCCCCCCC
34.5627251275
351PhosphorylationFPDQQNGSATNAWDQ
CCCCCCCCCCCCCCC
39.2027251275
353PhosphorylationDQQNGSATNAWDQSS
CCCCCCCCCCCCCHH
27.4522210691
359PhosphorylationATNAWDQSSCSSPKW
CCCCCCCHHCCCCCE
30.7326074081
360PhosphorylationTNAWDQSSCSSPKWE
CCCCCCHHCCCCCEE
16.6325159151
362PhosphorylationAWDQSSCSSPKWECT
CCCCHHCCCCCEEEE
52.1826074081
363PhosphorylationWDQSSCSSPKWECTE
CCCHHCCCCCEEEEH
34.5225159151
369PhosphorylationSSPKWECTELIHDIP
CCCCEEEEHHHHCCC
23.4726074081
414PhosphorylationSDDRVKLSVSGADTS
CCCCEEEEECCCCCC
14.4428450419
416PhosphorylationDRVKLSVSGADTSVS
CCEEEEECCCCCCCC
25.5328450419
420PhosphorylationLSVSGADTSVSSVDG
EEECCCCCCCCCCCC
30.4128450419
421PhosphorylationSVSGADTSVSSVDGP
EECCCCCCCCCCCCC
22.1328450419
423PhosphorylationSGADTSVSSVDGPVS
CCCCCCCCCCCCCCC
25.1428450419
424PhosphorylationGADTSVSSVDGPVSQ
CCCCCCCCCCCCCCH
23.2828450419
439PhosphorylationKAVQNENSYQMEEDG
HHHCCCCCCCCCCCC
15.5728985074
449UbiquitinationMEEDGSLKQSILSSE
CCCCCCCCHHHHCHH
43.63-
454PhosphorylationSLKQSILSSELLDHP
CCCHHHHCHHHHCCC
21.7928122231
455PhosphorylationLKQSILSSELLDHPY
CCHHHHCHHHHCCCC
28.9028122231
462PhosphorylationSELLDHPYCKSPLEA
HHHHCCCCCCCCCCC
14.7526074081
465PhosphorylationLDHPYCKSPLEAPLV
HCCCCCCCCCCCCEE
31.0230266825
474PhosphorylationLEAPLVCSGLKLENQ
CCCCEEECCCEEECC
39.4128122231
477UbiquitinationPLVCSGLKLENQVGG
CEEECCCEEECCCCC
58.23-
486UbiquitinationENQVGGGKNSQKASP
ECCCCCCCCCCCCCC
57.61-
513UbiquitinationFLDEVMKKYGSLVPL
HHHHHHHHHCCCCCC
36.43-
513UbiquitinationFLDEVMKKYGSLVPL
HHHHHHHHHCCCCCC
36.43-
523UbiquitinationSLVPLSEKEVLGRLK
CCCCCCHHHHHHHHH
50.15-
523UbiquitinationSLVPLSEKEVLGRLK
CCCCCCHHHHHHHHH
50.15-
530UbiquitinationKEVLGRLKDVFNEDF
HHHHHHHHHHCCCCC
50.95-
530UbiquitinationKEVLGRLKDVFNEDF
HHHHHHHHHHCCCCC
50.95-
651PhosphorylationEVHWSLITVTLSNRI
EEEEEEEEEEECCCE
16.84-
679PhosphorylationCVENIRKYLLTEARE
HHHHHHHHHHHHHHH
9.33-
682PhosphorylationNIRKYLLTEAREKNR
HHHHHHHHHHHHHCC
25.63-
687UbiquitinationLLTEAREKNRPEFLQ
HHHHHHHHCCHHHHH
53.34-
700UbiquitinationLQGWQTAVTKCIPQQ
HHHHHHHHHHHCCCC
6.29-
746UbiquitinationRVRKRIYKELCECRL
HHHHHHHHHHHHHHC
41.67-

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 SENP5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SENP5_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 SENP5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUMO3_HUMANSUMO3physical
16608850
SUMO2_HUMANSUMO2physical
16608850
RBGP1_HUMANRABGAP1physical
16608850

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 SENP5_HUMAN

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Related Literatures of Post-Translational Modification

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