SENP7_HUMAN - dbPTM
SENP7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP7_HUMAN
UniProt AC Q9BQF6
Protein Name Sentrin-specific protease 7
Gene Name SENP7
Organism Homo sapiens (Human).
Sequence Length 1050
Subcellular Localization
Protein Description Protease that deconjugates SUMO2 and SUMO3 from targeted proteins, but not SUMO1. Catalyzes the deconjugation of poly-SUMO2 and poly-SUMO3 chains. Has very low efficiency in processing full-length SUMO proteins to their mature forms..
Protein Sequence MDKRKLGRRPSSSEIITEGKRKKSSSDLSEIRKMLNAKPEDVHVQSPLSKFRSSERWTLPLQWERSLRNKVISLDHKNKKHIRGCPVTSKSSPERQLKVMLTNVLWTDLGRKFRKTLPRNDANLCDANKVQSDSLPSTSVDSLETCQKLEPLRQSLNLSERIPRVILTNVLGTELGRKYIRTPPVTEGSLSDTDNLQSEQLSSSSDGSLESYQNLNPHKSCYLSERGSQRSKTVDDNSAKQTAHNKEKRRKDDGISLLISDTQPEDLNSGSRGCDHLEQESRNKDVKYSDSKVELTLISRKTKRRLRNNLPDSQYCTSLDKSTEQTKKQEDDSTISTEFEKPSENYHQDPKLPEEITTKPTKSDFTKLSSLNSQELTLSNATKSASAGSTTETVENSNSIDIVGISSLVEKDENELNTIEKPILRGHNEGNQSLISAEPIVVSSDEEGPVEHKSSEILKLQSKQDRETTNENESTSESALLELPLITCESVQMSSELCPYNPVMENISSIMPSNEMDLQLDFIFTSVYIGKIKGASKGCVTITKKYIKIPFQVSLNEISLLVDTTHLKRFGLWKSKDDNHSKRSHAILFFWVSSDYLQEIQTQLEHSVLSQQSKSSEFIFLELHNPVSQREELKLKDIMTEISIISGELELSYPLSWVQAFPLFQNLSSKESSFIHYYCVSTCSFPAGVAVAEEMKLKSVSQPSNTDAAKPTYTFLQKQSSGCYSLSITSNPDEEWREVRHTGLVQKLIVYPPPPTKGGLGVTNEDLECLEEGEFLNDVIIDFYLKYLILEKASDELVERSHIFSSFFYKCLTRKENNLTEDNPNLSMAQRRHKRVRTWTRHINIFNKDYIFVPVNESSHWYLAVICFPWLEEAVYEDFPQTVSQQSQAQQSQNDNKTIDNDLRTTSTLSLSAEDSQSTESNMSVPKKMCKRPCILILDSLKAASVQNTVQNLREYLEVEWEVKLKTHRQFSKTNMVDLCPKVPKQDNSSDCGVYLLQYVESFFKDPIVNFELPIHLEKWFPRHVIKTKREDIRELILKLHLQQQKGSSS
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
11PhosphorylationRKLGRRPSSSEIITE
CCCCCCCCHHHHHCC		44.6925159151
12PhosphorylationKLGRRPSSSEIITEG
CCCCCCCHHHHHCCC		34.3723401153
13PhosphorylationLGRRPSSSEIITEGK
CCCCCCHHHHHCCCC		36.8330266825
17PhosphorylationPSSSEIITEGKRKKS
CCHHHHHCCCCCCCC		44.3323403867
20MethylationSEIITEGKRKKSSSD
HHHHCCCCCCCCCCC		55.61115981535
24PhosphorylationTEGKRKKSSSDLSEI
CCCCCCCCCCCHHHH		37.8025159151
25PhosphorylationEGKRKKSSSDLSEIR
CCCCCCCCCCHHHHH		36.4325159151
26PhosphorylationGKRKKSSSDLSEIRK
CCCCCCCCCHHHHHH		50.0628102081
29PhosphorylationKKSSSDLSEIRKMLN
CCCCCCHHHHHHHHC		35.6523090842
46PhosphorylationPEDVHVQSPLSKFRS
CHHHEECCCHHHCCC		27.0725159151
49PhosphorylationVHVQSPLSKFRSSER
HEECCCHHHCCCCCC		32.8828450419
55 (in isoform 4)Phosphorylation-54.1826552605
56 (in isoform 4)Phosphorylation-33.3626552605
58 (in isoform 4)Phosphorylation-25.3926552605
59 (in isoform 4)Phosphorylation-2.9426552605
64 (in isoform 4)Phosphorylation-21.3026552605
83MethylationHKNKKHIRGCPVTSK
CCCCCCCCCCCCCCC		40.14115493643
88PhosphorylationHIRGCPVTSKSSPER
CCCCCCCCCCCCHHH		18.6426552605
89PhosphorylationIRGCPVTSKSSPERQ
CCCCCCCCCCCHHHH		30.6726552605
90UbiquitinationRGCPVTSKSSPERQL
CCCCCCCCCCHHHHH		45.66-
91PhosphorylationGCPVTSKSSPERQLK
CCCCCCCCCHHHHHH		51.3928450419
92 (in isoform 5)Phosphorylation-34.22-
92PhosphorylationCPVTSKSSPERQLKV
CCCCCCCCHHHHHHH		34.2223401153
116O-linked_GlycosylationLGRKFRKTLPRNDAN
HHHHHHHHCCCCCCC		37.4330379171
132PhosphorylationCDANKVQSDSLPSTS
CCCCCCCCCCCCCCC		31.9626714015
134PhosphorylationANKVQSDSLPSTSVD
CCCCCCCCCCCCCCC		47.6426714015
148UbiquitinationDSLETCQKLEPLRQS
CCHHHHHHHHHHHHH		57.89-
155PhosphorylationKLEPLRQSLNLSERI
HHHHHHHHCCHHHHC		16.88-
159PhosphorylationLRQSLNLSERIPRVI
HHHHCCHHHHCCHHH		24.61-
182PhosphorylationLGRKYIRTPPVTEGS
HHHCCCCCCCCCCCC		23.5324247654
191PhosphorylationPVTEGSLSDTDNLQS
CCCCCCCCCCCCCCH		39.9128348404
193PhosphorylationTEGSLSDTDNLQSEQ
CCCCCCCCCCCCHHH		24.3428348404
231PhosphorylationSERGSQRSKTVDDNS
CCCCCCCCCCCCCCH		25.66-
233PhosphorylationRGSQRSKTVDDNSAK
CCCCCCCCCCCCHHH		30.34-
240AcetylationTVDDNSAKQTAHNKE
CCCCCHHHHHHHHHH		48.2625953088
269PhosphorylationTQPEDLNSGSRGCDH
CCCHHCCCCCCCCHH		45.5026714015
271PhosphorylationPEDLNSGSRGCDHLE
CHHCCCCCCCCHHHH		25.8926714015
296PhosphorylationSDSKVELTLISRKTK
CCCCEEEEEEEHHHH		14.45-
299PhosphorylationKVELTLISRKTKRRL
CEEEEEEEHHHHHHH		30.7321060948
321UbiquitinationQYCTSLDKSTEQTKK
HHHHCCCCCCHHHHC		65.65-
333PhosphorylationTKKQEDDSTISTEFE
HHCCCCCCCCCCCCC		39.7126714015
334PhosphorylationKKQEDDSTISTEFEK
HCCCCCCCCCCCCCC		26.4126714015
359AcetylationLPEEITTKPTKSDFT
CCHHHCCCCCCCCCC		41.8825953088
367UbiquitinationPTKSDFTKLSSLNSQ
CCCCCCCHHHHCCCC		46.49-
369PhosphorylationKSDFTKLSSLNSQEL
CCCCCHHHHCCCCEE		34.0427251275
370PhosphorylationSDFTKLSSLNSQELT
CCCCHHHHCCCCEEE		41.8427251275
373PhosphorylationTKLSSLNSQELTLSN
CHHHHCCCCEEECCC		30.2622817901
378PhosphorylationLNSQELTLSNATKSA
CCCCEEECCCCCCCC		6.09-
379PhosphorylationNSQELTLSNATKSAS
CCCEEECCCCCCCCC		21.1318452278
407PhosphorylationIDIVGISSLVEKDEN
EEEEEEHHHEECCCC		34.22-
421UbiquitinationNELNTIEKPILRGHN
CCCCCCCCCCCCCCC		33.24-
433PhosphorylationGHNEGNQSLISAEPI
CCCCCCCCCCCCCCE		31.5023927012
436PhosphorylationEGNQSLISAEPIVVS
CCCCCCCCCCCEEEE		31.6930108239
443PhosphorylationSAEPIVVSSDEEGPV
CCCCEEEECCCCCCC		22.6023401153
444PhosphorylationAEPIVVSSDEEGPVE
CCCEEEECCCCCCCC		37.1123927012
454PhosphorylationEGPVEHKSSEILKLQ
CCCCCCCCHHHHHHC		34.8026074081
455PhosphorylationGPVEHKSSEILKLQS
CCCCCCCHHHHHHCC		33.2026074081
459UbiquitinationHKSSEILKLQSKQDR
CCCHHHHHHCCCCCC		50.57-
468PhosphorylationQSKQDRETTNENEST
CCCCCCCCCCCCCCC		35.50-
537UbiquitinationGKIKGASKGCVTITK
HCCCCCCCCCEEEEC		56.65-
643PhosphorylationKDIMTEISIISGELE
HHHHHHHHEEECCEE		13.9822468782
698UbiquitinationVAEEMKLKSVSQPSN
HHHHHHCEECCCCCC		43.20-
699PhosphorylationAEEMKLKSVSQPSNT
HHHHHCEECCCCCCC		37.1228450419
701PhosphorylationEMKLKSVSQPSNTDA
HHHCEECCCCCCCCC		43.3928450419
704PhosphorylationLKSVSQPSNTDAAKP
CEECCCCCCCCCCCC		44.7330576142
706PhosphorylationSVSQPSNTDAAKPTY
ECCCCCCCCCCCCCE		31.2130576142
710UbiquitinationPSNTDAAKPTYTFLQ
CCCCCCCCCCEEEEE		39.34-
712PhosphorylationNTDAAKPTYTFLQKQ
CCCCCCCCEEEEECC		34.1930576142
720PhosphorylationYTFLQKQSSGCYSLS
EEEEECCCCCEEEEE		35.4224247654
721PhosphorylationTFLQKQSSGCYSLSI
EEEECCCCCEEEEEE		30.3225072903
724PhosphorylationQKQSSGCYSLSITSN
ECCCCCEEEEEEECC		19.0325072903
725PhosphorylationKQSSGCYSLSITSNP
CCCCCEEEEEEECCC		21.5125072903
727PhosphorylationSSGCYSLSITSNPDE
CCCEEEEEEECCCCH		20.2025072903
729PhosphorylationGCYSLSITSNPDEEW
CEEEEEEECCCCHHH		21.0525072903
730PhosphorylationCYSLSITSNPDEEWR
EEEEEEECCCCHHHH		44.7025072903
756PhosphorylationIVYPPPPTKGGLGVT
EEECCCCCCCCCCCC		48.3628258704
815UbiquitinationFYKCLTRKENNLTED
HHHHHHHHHHCCCCC		60.60-
916PhosphorylationLSLSAEDSQSTESNM
EEEEHHHCCCCCCCC		19.96-
973UbiquitinationKTHRQFSKTNMVDLC
CHHCCCCCCCHHHCC		45.25-
982UbiquitinationNMVDLCPKVPKQDNS
CHHHCCCCCCCCCCC		70.89-
1002PhosphorylationYLLQYVESFFKDPIV
HHHHHHHHHHCCCCC		26.41-
1039UbiquitinationDIRELILKLHLQQQK
HHHHHHHHHHHHHHC		27.20-
1046UbiquitinationKLHLQQQKGSSS---
HHHHHHHCCCCC---		57.32-
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 SENP7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SENP7_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 SENP7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUMO2_HUMANSUMO2physical
24018422
CBX5_HUMANCBX5physical
24018422
TIF1B_HUMANTRIM28physical
24018422
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 SENP7_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-25; SER-443 AND SER-444,AND MASS 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-443 AND SER-444, ANDMASS SPECTROMETRY.

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