SENP2_HUMAN - dbPTM
SENP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP2_HUMAN
UniProt AC Q9HC62
Protein Name Sentrin-specific protease 2
Gene Name SENP2
Organism Homo sapiens (Human).
Sequence Length 589
Subcellular Localization Nucleus, nuclear pore complex . Nucleus membrane
Peripheral membrane protein
Nucleoplasmic side . Cytoplasm . Shuttles between cytoplasm and nucleus.
Protein Description Protease that catalyzes two essential functions in the SUMO pathway. The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway. Deconjugates SUMO2 from MTA1. Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB. [PubMed: 20194620]
Protein Sequence MYRWLVRILGTIFRFCDRSVPPARALLKRRRSDSTLFSTVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKPMVTSACNGTRNVAPSGEVFSNSSSCELTGSGSWNNMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLNSEGCNRRPGGRRHSKGNPESSLMWKPQEQAVTEMISEESGKGLRRPHCTVEEGVQKEEREKYRKLLERLKESGHGNSVCPVTSNYHSSQRSQMDTLKTKGWGEEQNHGVKTTQFVPKQYRLVETRGPLCSLRSEKRCSKGKITDTETMVGIRFENESRRGYQLEPDLSEEVSARLRLGSGSNGLLRRKVSIIETKEKNCSGKERDRRTDDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWSLVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNSDLNLLEWTHHSMKPHEIPQQLNGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL
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
32PhosphorylationALLKRRRSDSTLFST
HHHHHHCCCCCCEEC		33.8230266825
34PhosphorylationLKRRRSDSTLFSTVD
HHHHCCCCCCEECCC		28.4030266825
35PhosphorylationKRRRSDSTLFSTVDT
HHHCCCCCCEECCCC		36.4930266825
38PhosphorylationRSDSTLFSTVDTDEI
CCCCCCEECCCCCCC		30.5430266825
39PhosphorylationSDSTLFSTVDTDEIP
CCCCCEECCCCCCCC		18.3126657352
42PhosphorylationTLFSTVDTDEIPAKR
CCEECCCCCCCCCCC		31.0629449344
122AcetylationNMLKLGNKSPNGISD
CCEECCCCCCCCCCC		66.5426051181
123PhosphorylationMLKLGNKSPNGISDY
CEECCCCCCCCCCCC		27.8321815630
128PhosphorylationNKSPNGISDYPKIRV
CCCCCCCCCCCCEEE		32.2723312004
130PhosphorylationSPNGISDYPKIRVTV
CCCCCCCCCCEEEEE		10.3021552520
168PhosphorylationRPGGRRHSKGNPESS
CCCCCCCCCCCCCCC		40.21-
216PhosphorylationQKEEREKYRKLLERL
CHHHHHHHHHHHHHH		14.2922817900
224UbiquitinationRKLLERLKESGHGNS
HHHHHHHHHCCCCCC		56.9329967540
226PhosphorylationLLERLKESGHGNSVC
HHHHHHHCCCCCCCC		34.2128555341
231PhosphorylationKESGHGNSVCPVTSN
HHCCCCCCCCCCCCC		29.68-
236PhosphorylationGNSVCPVTSNYHSSQ
CCCCCCCCCCCCCCC		9.0821945579
237PhosphorylationNSVCPVTSNYHSSQR
CCCCCCCCCCCCCCC		35.3121945579
239PhosphorylationVCPVTSNYHSSQRSQ
CCCCCCCCCCCCCCC		11.6621945579
241PhosphorylationPVTSNYHSSQRSQMD
CCCCCCCCCCCCCHH		20.1521945579
242PhosphorylationVTSNYHSSQRSQMDT
CCCCCCCCCCCCHHH		19.1221945579
253AcetylationQMDTLKTKGWGEEQN
CHHHHHCCCCCCCCC		51.597369675
261UbiquitinationGWGEEQNHGVKTTQF
CCCCCCCCCCEECEE		41.96-
264AcetylationEEQNHGVKTTQFVPK
CCCCCCCEECEECCC		50.917369685
271UbiquitinationKTTQFVPKQYRLVET
EECEECCCEEEEECC		55.44-
271AcetylationKTTQFVPKQYRLVET
EECEECCCEEEEECC		55.4420167786
284PhosphorylationETRGPLCSLRSEKRC
CCCCCCCCCCCCCCC		34.20-
287PhosphorylationGPLCSLRSEKRCSKG
CCCCCCCCCCCCCCC		53.41-
292PhosphorylationLRSEKRCSKGKITDT
CCCCCCCCCCCCCCC		48.77-
322PhosphorylationYQLEPDLSEEVSARL
EECCCCCCHHHHHHH		38.8128450419
326PhosphorylationPDLSEEVSARLRLGS
CCCCHHHHHHHCCCC		15.7928450419
333PhosphorylationSARLRLGSGSNGLLR
HHHHCCCCCCCCHHH		43.5725159151
335PhosphorylationRLRLGSGSNGLLRRK
HHCCCCCCCCHHHHC		29.4425219547
344PhosphorylationGLLRRKVSIIETKEK
CHHHHCEEEEECCHH		22.3823401153
348PhosphorylationRKVSIIETKEKNCSG
HCEEEEECCHHCCCC		33.8123403867
369PhosphorylationTDDLLELTEDMEKEI
HHHHHHHHHHHHHHH		22.14-
451PhosphorylationPKLKSGGYQAVKRWT
HHHHCCCHHHHHHHH		9.2329496907
455UbiquitinationSGGYQAVKRWTKGVN
CCCHHHHHHHHCCCC		45.2829967540
493PhosphorylationLRKKCLKYLDSMGQK
HHHHHHHHHHHCCHH		11.64-
496PhosphorylationKCLKYLDSMGQKGHR
HHHHHHHHCCHHHHH		23.40-
558PhosphorylationFTCKYADYISRDKPI
EEEHHHHHHCCCCCC		7.8227642862
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
344SPhosphorylationKinaseCHEK1O14757
GPS
369TPhosphorylationKinaseRPS6KA1Q15418
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SENP2_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 SENP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU153_HUMANNUP153physical
11896061
NU153_HUMANNUP153physical
12192048
SUMO1_HUMANSUMO1physical
12192048
SUMO3_HUMANSUMO3physical
12192048
HIPK2_HUMANHIPK2physical
15958389
DAXX_HUMANDAXXphysical
17081986
A4_HUMANAPPphysical
21832049
HNRPK_HUMANHNRNPKphysical
23092970
TPD52_HUMANTPD52physical
21988832
RAGP1_HUMANRANGAP1physical
12192048
FUND1_HUMANFUNDC1physical
25416956
KASH5_HUMANCCDC155physical
25416956
SYNE4_HUMANSYNE4physical
25416956
TM239_HUMANTMEM239physical
25416956
FZR1_HUMANFZR1physical
25483061
SUMO3_HUMANSUMO3physical
25944111
NACC1_HUMANNACC1physical
25891951
MYC_HUMANMYCphysical
25895136
UBP28_HUMANUSP28physical
28514442
PGK2_HUMANPGK2physical
28514442
IMA5_HUMANKPNA1physical
27939291
IMB1_HUMANKPNB1physical
27939291
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 SENP2_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-333, 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-333, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASSSPECTROMETRY.

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