SENP3_HUMAN - dbPTM
SENP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP3_HUMAN
UniProt AC Q9H4L4
Protein Name Sentrin-specific protease 3
Gene Name SENP3
Organism Homo sapiens (Human).
Sequence Length 574
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm . Cytoplasm . Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress (PubMed:19680224). Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and c
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, NPM1. 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 MKETIQGTGSWGPEPPGPGIPPAYSSPRRERLRWPPPPKPRLKSGGGFGPDPGSGTTVPARRLPVPRPSFDASASEEEEEEEEEEDEDEEEEVAAWRLPPRWSQLGTSQRPRPSRPTHRKTCSQRRRRAMRAFRMLLYSKSTSLTFHWKLWGRHRGRRRGLAHPKNHLSPQQGGATPQVPSPCCRFDSPRGPPPPRLGLLGALMAEDGVRGSPPVPSGPPMEEDGLRWTPKSPLDPDSGLLSCTLPNGFGGQSGPEGERSLAPPDASILISNVCSIGDHVAQELFQGSDLGMAEEAERPGEKAGQHSPLREEHVTCVQSILDEFLQTYGSLIPLSTDEVVEKLEDIFQQEFSTPSRKGLVLQLIQSYQRMPGNAMVRGFRVAYKRHVLTMDDLGTLYGQNWLNDQVMNMYGDLVMDTVPEKVHFFNSFFYDKLRTKGYDGVKRWTKNVDIFNKELLLIPIHLEVHWSLISVDVRRRTITYFDSQRTLNRRCPKHIAKYLQAEAVKKDRLDFHQGWKGYFKMNVARQNNDSDCGAFVLQYCKHLALSQPFSFTQQDMPKLRRQIYKELCHCKLTV
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
2Methylation------MKETIQGTG
------CCCCCCCCC		64.66115981559
4Phosphorylation----MKETIQGTGSW
----CCCCCCCCCCC		17.0626074081
8PhosphorylationMKETIQGTGSWGPEP
CCCCCCCCCCCCCCC		16.2126074081
10PhosphorylationETIQGTGSWGPEPPG
CCCCCCCCCCCCCCC		28.7926074081
24PhosphorylationGPGIPPAYSSPRRER
CCCCCCCCCCCCHHH		18.5630175587
25PhosphorylationPGIPPAYSSPRRERL
CCCCCCCCCCCHHHC		35.6523401153
26PhosphorylationGIPPAYSSPRRERLR
CCCCCCCCCCHHHCC		15.1125159151
39AcetylationLRWPPPPKPRLKSGG
CCCCCCCCCCCCCCC		48.8526051181
39UbiquitinationLRWPPPPKPRLKSGG
CCCCCCCCCCCCCCC		48.8522817900
43MethylationPPPKPRLKSGGGFGP
CCCCCCCCCCCCCCC		48.6230994653
43UbiquitinationPPPKPRLKSGGGFGP
CCCCCCCCCCCCCCC		48.6222817900
44PhosphorylationPPKPRLKSGGGFGPD
CCCCCCCCCCCCCCC		47.4625159151
54PhosphorylationGFGPDPGSGTTVPAR
CCCCCCCCCCCCCCC		38.0525159151
56PhosphorylationGPDPGSGTTVPARRL
CCCCCCCCCCCCCCC		26.7323186163
57PhosphorylationPDPGSGTTVPARRLP
CCCCCCCCCCCCCCC		28.1929396449
69PhosphorylationRLPVPRPSFDASASE
CCCCCCCCCCCCCCH		36.7230576142
73PhosphorylationPRPSFDASASEEEEE
CCCCCCCCCCHHHHH		33.8823898821
75PhosphorylationPSFDASASEEEEEEE
CCCCCCCCHHHHHHH		42.9423898821
120AcetylationPSRPTHRKTCSQRRR
CCCCCCCHHHHHHHH		46.407695551
139PhosphorylationAFRMLLYSKSTSLTF
HHHHHHHCCCCCCEE		21.79-
141PhosphorylationRMLLYSKSTSLTFHW
HHHHHCCCCCCEEEE		19.79-
142PhosphorylationMLLYSKSTSLTFHWK
HHHHCCCCCCEEEEE		31.34-
143PhosphorylationLLYSKSTSLTFHWKL
HHHCCCCCCEEEEEE		32.29-
145PhosphorylationYSKSTSLTFHWKLWG
HCCCCCCEEEEEECC		17.14-
169PhosphorylationAHPKNHLSPQQGGAT
CCCCCCCCCCCCCCC		17.0819664994
176PhosphorylationSPQQGGATPQVPSPC
CCCCCCCCCCCCCCC		19.9622167270
181PhosphorylationGATPQVPSPCCRFDS
CCCCCCCCCCCCCCC		31.5419664994
188PhosphorylationSPCCRFDSPRGPPPP
CCCCCCCCCCCCCCC		17.4923401153
190MethylationCCRFDSPRGPPPPRL
CCCCCCCCCCCCCCH		74.36115493635
212PhosphorylationAEDGVRGSPPVPSGP
HHCCCCCCCCCCCCC		18.5729255136
217PhosphorylationRGSPPVPSGPPMEED
CCCCCCCCCCCCCCC		65.2523927012
229PhosphorylationEEDGLRWTPKSPLDP
CCCCCCCCCCCCCCC		17.8830266825
231UbiquitinationDGLRWTPKSPLDPDS
CCCCCCCCCCCCCCC		58.2829967540
232PhosphorylationGLRWTPKSPLDPDSG
CCCCCCCCCCCCCCC		31.7229255136
238PhosphorylationKSPLDPDSGLLSCTL
CCCCCCCCCCEEEEC		36.4130266825
242PhosphorylationDPDSGLLSCTLPNGF
CCCCCCEEEECCCCC		15.3130266825
244PhosphorylationDSGLLSCTLPNGFGG
CCCCEEEECCCCCCC		41.7030266825
253PhosphorylationPNGFGGQSGPEGERS
CCCCCCCCCCCCCCC		60.6426074081
288PhosphorylationAQELFQGSDLGMAEE
HHHHHCCCCCCCHHH		20.9123898821
307PhosphorylationGEKAGQHSPLREEHV
CCCCCCCCCCCHHHH		20.1030266825
352PhosphorylationDIFQQEFSTPSRKGL
HHHHHHCCCCCHHHH		38.3625159151
353PhosphorylationIFQQEFSTPSRKGLV
HHHHHCCCCCHHHHH		30.5125159151
355PhosphorylationQQEFSTPSRKGLVLQ
HHHCCCCCHHHHHHH		46.8722199227
357UbiquitinationEFSTPSRKGLVLQLI
HCCCCCHHHHHHHHH		62.02-
366PhosphorylationLVLQLIQSYQRMPGN
HHHHHHHHHHCCCCC		19.0827642862
367PhosphorylationVLQLIQSYQRMPGNA
HHHHHHHHHCCCCCC		5.4627642862
432AcetylationFNSFFYDKLRTKGYD
CCHHHHHHHHHCCCC		28.6126051181
436UbiquitinationFYDKLRTKGYDGVKR
HHHHHHHCCCCHHHH		49.38-
442UbiquitinationTKGYDGVKRWTKNVD
HCCCCHHHHHHCCEE		47.9829967540
446AcetylationDGVKRWTKNVDIFNK
CHHHHHHCCEEECCC		48.2726051181
446UbiquitinationDGVKRWTKNVDIFNK
CHHHHHHCCEEECCC		48.2729967540
477PhosphorylationSVDVRRRTITYFDSQ
ECCCCCCEEEEEHHH		18.83-
483PhosphorylationRTITYFDSQRTLNRR
CEEEEEHHHHHHHHH		16.21-
497AcetylationRCPKHIAKYLQAEAV
HCHHHHHHHHHHHHH		45.9826051181
497UbiquitinationRCPKHIAKYLQAEAV
HCHHHHHHHHHHHHH		45.9829967540
498PhosphorylationCPKHIAKYLQAEAVK
CHHHHHHHHHHHHHH		8.60-
505UbiquitinationYLQAEAVKKDRLDFH
HHHHHHHHHCCCCCC		56.8829967540
506UbiquitinationLQAEAVKKDRLDFHQ
HHHHHHHHCCCCCCC		41.29-
516UbiquitinationLDFHQGWKGYFKMNV
CCCCCHHCCCCHHHH		51.0229967540
520UbiquitinationQGWKGYFKMNVARQN
CHHCCCCHHHHCCCC		22.5329967540
541UbiquitinationAFVLQYCKHLALSQP
HHHHHHHHHHHHHCC		36.40-
558UbiquitinationFTQQDMPKLRRQIYK
CCHHHHHHHHHHHHH		48.2429967540
565UbiquitinationKLRRQIYKELCHCKL
HHHHHHHHHHHCCCC		45.9329967540
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
25SPhosphorylationKinaseMTORP42345
PSP
26SPhosphorylationKinaseMTORP42345
PSP
139SPhosphorylationKinaseMTORP42345
PSP
141SPhosphorylationKinaseMTORP42345
PSP
142TPhosphorylationKinaseMTORP42345
PSP
143SPhosphorylationKinaseMTORP42345
PSP
145TPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SENP3_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 SENP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PARP1_HUMANPARP1physical
19622798
HIC1_HUMANHIC1physical
17283066
PELP1_HUMANPELP1physical
20442285
CHIP_HUMANSTUB1physical
20924358
HS90A_HUMANHSP90AA1physical
20924358
MDM2_HUMANMDM2physical
21316347
P53_HUMANTP53physical
21316347
NR1H2_HUMANNR1H2physical
21331046
NPM_HUMANNPM1physical
18259216
RLA0_HUMANRPLP0physical
18259216
RS4X_HUMANRPS4Xphysical
18259216
RS8_HUMANRPS8physical
18259216
RS11_HUMANRPS11physical
18259216
RS18_HUMANRPS18physical
18259216
RBBP5_HUMANRBBP5physical
24930734
WDR5_HUMANWDR5physical
24930734
KMT2A_HUMANKMT2Aphysical
24930734
KMT2D_HUMANKMT2Dphysical
24930734
ASH2L_HUMANASH2Lphysical
24930734
MEN1_HUMANMEN1physical
24930734
EP300_HUMANEP300physical
22684029
BOREA_HUMANCDCA8physical
18946085
CUL1_HUMANCUL1physical
26511642
CUL3_HUMANCUL3physical
26511642
XRCC5_HUMANXRCC5physical
26511642
SP1_HUMANSP1physical
26511642
UBE3A_HUMANUBE3Aphysical
26511642
SYF1_HUMANXAB2physical
26511642
IMB1_HUMANKPNB1physical
26511642
MCM4_HUMANMCM4physical
26511642
NUP93_HUMANNUP93physical
26511642
CDC5L_HUMANCDC5Lphysical
26511642
RNZ2_HUMANELAC2physical
26511642
TF3C4_HUMANGTF3C4physical
26511642
NCBP1_HUMANNCBP1physical
26511642
TELO2_HUMANTELO2physical
26511642
MD1L1_HUMANMAD1L1physical
26511642
MCM3_HUMANMCM3physical
26511642
DHX15_HUMANDHX15physical
26511642
DDX27_HUMANDDX27physical
26511642
UBF1_HUMANUBTFphysical
26511642
TERA_HUMANVCPphysical
26511642
ZW10_HUMANZW10physical
26511642
TIF1B_HUMANTRIM28physical
26511642
MATR3_HUMANMATR3physical
26511642
NSUN2_HUMANNSUN2physical
26511642
HNRL1_HUMANHNRNPUL1physical
26511642
RRP1B_HUMANRRP1Bphysical
26511642
LAS1L_HUMANLAS1Lphysical
26511642
ZC3HE_HUMANZC3H14physical
26511642
MCM5_HUMANMCM5physical
26511642
CND2_HUMANNCAPHphysical
26511642
MCM7_HUMANMCM7physical
26511642
SSRP1_HUMANSSRP1physical
26511642
MRE11_HUMANMRE11Aphysical
26511642
DDX17_HUMANDDX17physical
26511642
PSMD2_HUMANPSMD2physical
26511642
COPG1_HUMANCOPG1physical
26511642
COPG2_HUMANCOPG2physical
26511642
PYGL_HUMANPYGLphysical
26511642
PYGB_HUMANPYGBphysical
26511642
GANAB_HUMANGANABphysical
26511642
PDC6I_HUMANPDCD6IPphysical
26511642
EF2_HUMANEEF2physical
26511642
ENPL_HUMANHSP90B1physical
26511642
TRRAP_HUMANTRRAPphysical
26511642
MOGS_HUMANMOGSphysical
26511642
VPS35_HUMANVPS35physical
26511642
AP1G1_HUMANAP1G1physical
26511642
UFL1_HUMANUFL1physical
26511642
RIR1_HUMANRRM1physical
26511642
CSDE1_HUMANCSDE1physical
26511642
SEC63_HUMANSEC63physical
26511642
SYQ_HUMANQARSphysical
26511642
P5CS_HUMANALDH18A1physical
26511642
MAGD1_HUMANMAGED1physical
26511642
PFKAP_HUMANPFKPphysical
26511642
TFR1_HUMANTFRCphysical
26511642
GEPH_HUMANGPHNphysical
26511642
HS90A_HUMANHSP90AA1physical
26511642
ACINU_HUMANACIN1physical
26511642
MIC60_HUMANIMMTphysical
26511642
HS90B_HUMANHSP90AB1physical
26511642
SYTC_HUMANTARSphysical
26511642
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 SENP3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-181, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-176; SER-181;SER-188 AND SER-212, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-75; SER-169;SER-181; SER-212; SER-232 AND SER-307, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-181, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-253, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-232, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353, AND MASSSPECTROMETRY.

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