SENP3_MOUSE - dbPTM
SENP3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP3_MOUSE
UniProt AC Q9EP97
Protein Name Sentrin-specific protease 3
Gene Name Senp3
Organism Mus musculus (Mouse).
Sequence Length 568
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm . Cytoplasm . Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress (By similarity). Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chr
Protein Description Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates. Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability. Deconjugates SUMO2 and SUMO3 from CDCA8. Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300. Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin. Plays a role in the regulation of sumoylation status of ZNF148. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes..
Protein Sequence MKETIQGTGSWGPEPPGPGTTYSNPRRERLRWPLPPKPRLKSGGGFGPDPGSGTTVPTRRLPAPRPSFDASASEEEEEEEEEDEEEVAAWRLPPRWGQLGASQRSRALRPSHRKTCSQRRRRAMRAFQMLLYSKSTSLTFHWKLWGRHRGRRRNLAHPKNHLSPQEGGATPQVPSPCCRFDSPRGLPPPRLGLLGALMAEDGMRGSPPVPSGPPMEEDGLRWTPKSPLDPDSGLLSCTLPNGFGGLSGPEGERSLAPPDASILISNVCSIGDHVAQELFQSSDLGIAEEADRTGEKAGQHSPLREEHVTCVQSILDEFLQTYGSLIPLSTDEVVEKLEDIFQQEFSTPSRKSLVLQLIQSYQRMPGNAMVRGFRVSYKRHVLTMDDLGTLYGQNWLNDQVMNMYGDLVMDTVPEKVHFFNSFFYDKLRTKGYDGVKRWTKNVDIFNKELLLIPIHLEVHWSLISVDVRRRTITYFDSQRTLNRRCPKHIAKYLQAEAVKKDRLDFHQGWKGYFKMNVARQNNDSDCGAFVLQYCKHLALSQPFSFTQQDMPKLRRQIYKELCHCKLTV
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
41UbiquitinationLPPKPRLKSGGGFGP
CCCCCCCCCCCCCCC		48.62-
42PhosphorylationPPKPRLKSGGGFGPD
CCCCCCCCCCCCCCC		47.4625266776
52PhosphorylationGFGPDPGSGTTVPTR
CCCCCCCCCCCCCCC		38.0529514104
67PhosphorylationRLPAPRPSFDASASE
CCCCCCCCCCCCCCH		36.7225159016
71PhosphorylationPRPSFDASASEEEEE
CCCCCCCCCCHHHHH		33.8827149854
73PhosphorylationPSFDASASEEEEEEE
CCCCCCCCHHHHHHH		42.9427149854
102PhosphorylationRWGQLGASQRSRALR
CHHHCCHHHHHHHCC		25.0722006019
104MethylationGQLGASQRSRALRPS
HHCCHHHHHHHCCHH		26.1430989305
105PhosphorylationQLGASQRSRALRPSH
HCCHHHHHHHCCHHH		17.80-
111PhosphorylationRSRALRPSHRKTCSQ
HHHHCCHHHHHHHHH		29.5022817900
163PhosphorylationAHPKNHLSPQEGGAT
CCCCCCCCCCCCCCC		19.5825521595
170PhosphorylationSPQEGGATPQVPSPC
CCCCCCCCCCCCCCC		19.9622942356
175PhosphorylationGATPQVPSPCCRFDS
CCCCCCCCCCCCCCC		31.5425521595
182PhosphorylationSPCCRFDSPRGLPPP
CCCCCCCCCCCCCCC		17.4926824392
206PhosphorylationAEDGMRGSPPVPSGP
HHCCCCCCCCCCCCC		18.7025521595
211PhosphorylationRGSPPVPSGPPMEED
CCCCCCCCCCCCCCC		65.2525619855
223PhosphorylationEEDGLRWTPKSPLDP
CCCCCCCCCCCCCCC		17.8822942356
226PhosphorylationGLRWTPKSPLDPDSG
CCCCCCCCCCCCCCC		31.7226824392
232PhosphorylationKSPLDPDSGLLSCTL
CCCCCCCCCCEEEEC		36.4125619855
236PhosphorylationDPDSGLLSCTLPNGF
CCCCCCEEEECCCCC		15.3125619855
238PhosphorylationDSGLLSCTLPNGFGG
CCCCEEEECCCCCCC		41.7025619855
293PhosphorylationIAEEADRTGEKAGQH
CCHHHHHHCCCCCCC		50.6824719451
301PhosphorylationGEKAGQHSPLREEHV
CCCCCCCCCCHHHHH		20.1025159016
309PhosphorylationPLREEHVTCVQSILD
CCHHHHHHHHHHHHH		14.6323984901
313PhosphorylationEHVTCVQSILDEFLQ
HHHHHHHHHHHHHHH		12.5323984901
321PhosphorylationILDEFLQTYGSLIPL
HHHHHHHHHHCCCCC		31.8123984901
322PhosphorylationLDEFLQTYGSLIPLS
HHHHHHHHHCCCCCC		7.5523984901
324PhosphorylationEFLQTYGSLIPLSTD
HHHHHHHCCCCCCHH		16.8323984901
329PhosphorylationYGSLIPLSTDEVVEK
HHCCCCCCHHHHHHH		28.5823984901
330PhosphorylationGSLIPLSTDEVVEKL
HCCCCCCHHHHHHHH		43.8123984901
346PhosphorylationDIFQQEFSTPSRKSL
HHHHHHCCCCCHHHH		38.3630482847
347PhosphorylationIFQQEFSTPSRKSLV
HHHHHCCCCCHHHHH		30.5125338131
471PhosphorylationSVDVRRRTITYFDSQ
ECCCCCCEEEEEHHH		18.83-
477PhosphorylationRTITYFDSQRTLNRR
CEEEEEHHHHHHHHH		16.21-
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 SENP3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SENP3_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 SENP3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SENP3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SENP3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND MASSSPECTROMETRY.

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