SENP1_HUMAN - dbPTM
SENP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP1_HUMAN
UniProt AC Q9P0U3
Protein Name Sentrin-specific protease 1
Gene Name SENP1
Organism Homo sapiens (Human).
Sequence Length 644
Subcellular Localization Nucleus . Cytoplasm. Shuttles between cytoplasm and nucleus.
Protein Description Protease that catalyzes two essential functions in the SUMO pathway. [PubMed: 10652325]
Protein Sequence MDDIADRMRMDAGEVTLVNHNSVFKTHLLPQTGFPEDQLSLSDQQILSSRQGHLDRSFTCSTRSAAYNPSYYSDNPSSDSFLGSGDLRTFGQSANGQWRNSTPSSSSSLQKSRNSRSLYLETRKTSSGLSNSFAGKSNHHCHVSAYEKSFPIKPVPSPSWSGSCRRSLLSPKKTQRRHVSTAEETVQEEEREIYRQLLQMVTGKQFTIAKPTTHFPLHLSRCLSSSKNTLKDSLFKNGNSCASQIIGSDTSSSGSASILTNQEQLSHSVYSLSSYTPDVAFGSKDSGTLHHPHHHHSVPHQPDNLAASNTQSEGSDSVILLKVKDSQTPTPSSTFFQAELWIKELTSVYDSRARERLRQIEEQKALALQLQNQRLQEREHSVHDSVELHLRVPLEKEIPVTVVQETQKKGHKLTDSEDEFPEITEEMEKEIKNVFRNGNQDEVLSEAFRLTITRKDIQTLNHLNWLNDEIINFYMNMLMERSKEKGLPSVHAFNTFFFTKLKTAGYQAVKRWTKKVDVFSVDILLVPIHLGVHWCLAVVDFRKKNITYYDSMGGINNEACRILLQYLKQESIDKKRKEFDTNGWQLFSKKSQEIPQQMNGSDCGMFACKYADCITKDRPINFTQQHMPYFRKRMVWEILHRKLL
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
16PhosphorylationRMDAGEVTLVNHNSV
HCCCCCEEEECCCCH		22.2328555341
22PhosphorylationVTLVNHNSVFKTHLL
EEEECCCCHHEEEEC		22.7528555341
40PhosphorylationGFPEDQLSLSDQQIL
CCCHHHCCCCHHHHH		21.8623898821
48PhosphorylationLSDQQILSSRQGHLD
CCHHHHHHHCCCCCC		25.7124719451
49PhosphorylationSDQQILSSRQGHLDR
CHHHHHHHCCCCCCC		25.7724719451
57 (in isoform 2)Phosphorylation-25.2824719451
57PhosphorylationRQGHLDRSFTCSTRS
CCCCCCCCCEECCCC		25.2823927012
59PhosphorylationGHLDRSFTCSTRSAA
CCCCCCCEECCCCCC		13.5423403867
61PhosphorylationLDRSFTCSTRSAAYN
CCCCCEECCCCCCCC		24.6523403867
62PhosphorylationDRSFTCSTRSAAYNP
CCCCEECCCCCCCCC		30.6923403867
72PhosphorylationAAYNPSYYSDNPSSD
CCCCCHHCCCCCCCC		17.5629978859
73PhosphorylationAYNPSYYSDNPSSDS
CCCCHHCCCCCCCCC		23.7629978859
77PhosphorylationSYYSDNPSSDSFLGS
HHCCCCCCCCCCCCC		53.7029978859
78PhosphorylationYYSDNPSSDSFLGSG
HCCCCCCCCCCCCCC		38.2329978859
78 (in isoform 2)Phosphorylation-38.2324719451
80PhosphorylationSDNPSSDSFLGSGDL
CCCCCCCCCCCCCCC		25.0729978859
84PhosphorylationSSDSFLGSGDLRTFG
CCCCCCCCCCCCCCC		31.1429978859
101PhosphorylationANGQWRNSTPSSSSS
CCCCCCCCCCCCCHH		32.8722199227
102 (in isoform 2)Phosphorylation-30.6424719451
102PhosphorylationNGQWRNSTPSSSSSL
CCCCCCCCCCCCHHH		30.6425262027
104PhosphorylationQWRNSTPSSSSSLQK
CCCCCCCCCCHHHHH		42.8322199227
105PhosphorylationWRNSTPSSSSSLQKS
CCCCCCCCCHHHHHH		35.1329396449
106PhosphorylationRNSTPSSSSSLQKSR
CCCCCCCCHHHHHHC		28.4327251275
107 (in isoform 2)Phosphorylation-36.7024719451
107PhosphorylationNSTPSSSSSLQKSRN
CCCCCCCHHHHHHCC		36.7025159151
108PhosphorylationSTPSSSSSLQKSRNS
CCCCCCHHHHHHCCC		36.4525159151
111UbiquitinationSSSSSLQKSRNSRSL
CCCHHHHHHCCCCCE		57.59-
117PhosphorylationQKSRNSRSLYLETRK
HHHCCCCCEEEEEEC		22.6123401153
119PhosphorylationSRNSRSLYLETRKTS
HCCCCCEEEEEECCC		12.0727642862
124MethylationSLYLETRKTSSGLSN
CEEEEEECCCCCCCC		61.24115981575
124UbiquitinationSLYLETRKTSSGLSN
CEEEEEECCCCCCCC		61.24-
125PhosphorylationLYLETRKTSSGLSNS
EEEEEECCCCCCCCC		25.4923403867
126 (in isoform 2)Phosphorylation-25.9924719451
126PhosphorylationYLETRKTSSGLSNSF
EEEEECCCCCCCCCC		25.9930108239
127 (in isoform 2)Phosphorylation-49.3224719451
127PhosphorylationLETRKTSSGLSNSFA
EEEECCCCCCCCCCC		49.3230108239
130PhosphorylationRKTSSGLSNSFAGKS
ECCCCCCCCCCCCCC		33.6726055452
132PhosphorylationTSSGLSNSFAGKSNH
CCCCCCCCCCCCCCC		17.0725159151
132 (in isoform 2)Phosphorylation-17.0724719451
136UbiquitinationLSNSFAGKSNHHCHV
CCCCCCCCCCCEEEE		44.66-
136MethylationLSNSFAGKSNHHCHV
CCCCCCCCCCCEEEE		44.66115981581
149PhosphorylationHVSAYEKSFPIKPVP
EEEEEECCCCCCCCC		25.0623927012
153UbiquitinationYEKSFPIKPVPSPSW
EECCCCCCCCCCCCC		39.95-
153AcetylationYEKSFPIKPVPSPSW
EECCCCCCCCCCCCC		39.9526051181
157 (in isoform 2)Phosphorylation-31.6224719451
157PhosphorylationFPIKPVPSPSWSGSC
CCCCCCCCCCCCCCH		31.6222167270
159PhosphorylationIKPVPSPSWSGSCRR
CCCCCCCCCCCCHHH		37.9123401153
161PhosphorylationPVPSPSWSGSCRRSL
CCCCCCCCCCHHHHH		25.7623927012
163PhosphorylationPSPSWSGSCRRSLLS
CCCCCCCCHHHHHCC		10.0325159151
167PhosphorylationWSGSCRRSLLSPKKT
CCCCHHHHHCCCHHH		17.8223403867
167O-linked_GlycosylationWSGSCRRSLLSPKKT
CCCCHHHHHCCCHHH		17.82OGP
167 (in isoform 2)Phosphorylation-17.8224719451
170 (in isoform 2)Phosphorylation-39.7124719451
170PhosphorylationSCRRSLLSPKKTQRR
CHHHHHCCCHHHHHC		39.7123401153
180PhosphorylationKTQRRHVSTAEETVQ
HHHHCCCCCHHHHHH		18.7723312004
181PhosphorylationTQRRHVSTAEETVQE
HHHCCCCCHHHHHHH		36.6823312004
185PhosphorylationHVSTAEETVQEEERE
CCCCHHHHHHHHHHH		20.9923312004
194PhosphorylationQEEEREIYRQLLQMV
HHHHHHHHHHHHHHH		6.3820068231
202PhosphorylationRQLLQMVTGKQFTIA
HHHHHHHHCCCEEEE		33.0620068231
210UbiquitinationGKQFTIAKPTTHFPL
CCCEEEECCCCCCCH		38.76-
224PhosphorylationLHLSRCLSSSKNTLK
HHHHHHHHCCCCHHH		35.8724719451
224 (in isoform 2)Phosphorylation-35.8724719451
226PhosphorylationLSRCLSSSKNTLKDS
HHHHHHCCCCHHHHH		26.92-
227UbiquitinationSRCLSSSKNTLKDSL
HHHHHCCCCHHHHHH		56.77-
231UbiquitinationSSSKNTLKDSLFKNG
HCCCCHHHHHHHHCC		43.14-
233PhosphorylationSKNTLKDSLFKNGNS
CCCHHHHHHHHCCCC		33.8325159151
328PhosphorylationLKVKDSQTPTPSSTF
EEEECCCCCCCCCHH		32.84-
330PhosphorylationVKDSQTPTPSSTFFQ
EECCCCCCCCCHHEE		38.91-
349PhosphorylationIKELTSVYDSRARER
HHHHHHHHHHHHHHH		14.1526434552
351PhosphorylationELTSVYDSRARERLR
HHHHHHHHHHHHHHH		15.3426434552
364AcetylationLRQIEEQKALALQLQ
HHHHHHHHHHHHHHH		48.9623954790
364UbiquitinationLRQIEEQKALALQLQ
HHHHHHHHHHHHHHH		48.96-
381PhosphorylationRLQEREHSVHDSVEL
HHHHHHCCCCCCEEE		19.1828555341
385PhosphorylationREHSVHDSVELHLRV
HHCCCCCCEEEEEEC		11.5628555341
396UbiquitinationHLRVPLEKEIPVTVV
EEECCCCCCCCEEEE		69.49-
396AcetylationHLRVPLEKEIPVTVV
EEECCCCCCCCEEEE		69.4923749302
408UbiquitinationTVVQETQKKGHKLTD
EEEEHHHHCCCCCCC		69.05-
414PhosphorylationQKKGHKLTDSEDEFP
HHCCCCCCCCCCCCH		42.1325159151
416PhosphorylationKGHKLTDSEDEFPEI
CCCCCCCCCCCCHHH		41.5325159151
424PhosphorylationEDEFPEITEEMEKEI
CCCCHHHHHHHHHHH		25.0026074081
429UbiquitinationEITEEMEKEIKNVFR
HHHHHHHHHHHHHHH		64.53-
429AcetylationEITEEMEKEIKNVFR
HHHHHHHHHHHHHHH		64.5319829161
432UbiquitinationEEMEKEIKNVFRNGN
HHHHHHHHHHHHCCC		48.42-
500AcetylationFNTFFFTKLKTAGYQ
HCCHHHHHHHHHCHH		42.7126051181
502UbiquitinationTFFFTKLKTAGYQAV
CHHHHHHHHHCHHHH		37.57-
510UbiquitinationTAGYQAVKRWTKKVD
HHCHHHHHHHHCCCC		45.28-
577 (in isoform 2)Ubiquitination-72.1621890473
577UbiquitinationESIDKKRKEFDTNGW
HCHHHHHHCCCCCHH		72.1621890473
577 (in isoform 1)Ubiquitination-72.1621890473
588PhosphorylationTNGWQLFSKKSQEIP
CCHHHHHCHHHHCCC		48.0024719451
590UbiquitinationGWQLFSKKSQEIPQQ
HHHHHCHHHHCCCHH		57.06-
609UbiquitinationDCGMFACKYADCITK
CCCCHHHHHHHHCCC		39.79-
616UbiquitinationKYADCITKDRPINFT
HHHHHCCCCCCCCCH		31.65-
629PhosphorylationFTQQHMPYFRKRMVW
CHHHCCHHHHHHHHH		14.4029083192
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 SENP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SENP1_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 SENP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SENP1_HUMANSENP1physical
17704192
PARP1_HUMANPARP1physical
19622798
RUVB2_HUMANRUVBL2physical
16699503
GCM1_HUMANGCM1physical
21791615
RBP2_HUMANRANBP2physical
22194619
HIPK2_HUMANHIPK2physical
16253240
A4_HUMANAPPphysical
21832049
RAGP1_HUMANRANGAP1physical
17099698
SUMO1_HUMANSUMO1physical
17099698
SUMO2_HUMANSUMO2physical
17099698
SUMO2_HUMANSUMO2physical
16553580
PRDM1_HUMANPRDM1physical
21722636
RAGP1_HUMANRANGAP1physical
25027693
UBP25_HUMANUSP25physical
18538659
SUMO1_HUMANSUMO1physical
16553580
SUMO3_HUMANSUMO3physical
16553580
SUMO2_HUMANSUMO2physical
17000875
SUMO1_HUMANSUMO1physical
17000875
SUMO1_HUMANSUMO1physical
16608850
SUMO3_HUMANSUMO3physical
16608850
RBGP1_HUMANRABGAP1physical
16608850
SUMO1_HUMANSUMO1physical
22878415
SUMO3_HUMANSUMO3physical
22878415
SUMO2_HUMANSUMO2physical
22878415
SP100_HUMANSP100physical
22878415
CAV3_HUMANCAV3physical
21362625
RAGP1_HUMANRANGAP1physical
16553580
UBE2K_HUMANUBE2Kphysical
21098080
PML_HUMANPMLphysical
21098080
ZN420_HUMANZNF420physical
25691462
ARRB2_HUMANARRB2physical
25425640
NACC1_HUMANNACC1physical
25891951
BLK_HUMANBLKphysical
28514442
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 SENP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-157, AND MASSSPECTROMETRY.

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