UBP15_HUMAN - dbPTM
UBP15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP15_HUMAN
UniProt AC Q9Y4E8
Protein Name Ubiquitin carboxyl-terminal hydrolase 15
Gene Name USP15
Organism Homo sapiens (Human).
Sequence Length 981
Subcellular Localization Cytoplasm . Nucleus . Mitochondrion .
Protein Description Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways. [PubMed: 21947082]
Protein Sequence MAEGGAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKQWKKYVGFDSWDKYQMGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYTLMEGQEPIARKVVEQGMFVKHCKVEVYLTELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFSIPDEKETRLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQKNEDGTWPRGPSTPKSPGASNFSTLPKISPSSLSNNYNNMNNRNVKNSNYCLPSYTAYKNYDYSEPGRNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQLKDADGRPDKVVAEEAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERTLEVYLVRMDPLTKPMQYKVVVPKIGNILDLCTALSALSGIPADKMIVTDIYNHRFHRIFAMDENLSSIMERDDIYVFEININRTEDTEHVIIPVCLREKFRHSSYTHHTGSSLFGQPFLMAVPRNNTEDKLYNLLLLRMCRYVKISTETEETEGSLHCCKDQNINGNGPNGIHEEGSPSEMETDEPDDESSQDQELPSENENSQSEDSVGGDNDSENGLCTEDTCKGQLTGHKKRLFTFQFNNLGNTDINYIKDDTRHIRFDDRQLRLDERSFLALDWDPDLKKRYFDENAAEDFEKHESVEYKPPKKPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPINDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQRQDTFSGTGFFPLDRETKGASAATGIPLESDEDSNDNDNDIENENCMHTN
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
2Acetylation------MAEGGAADL
------CCCCCCCCC
24.9222223895
11PhosphorylationGGAADLDTQRSDIAT
CCCCCCCCCHHHHHH
32.9328348404
14PhosphorylationADLDTQRSDIATLLK
CCCCCCHHHHHHHHH
24.4528348404
14UbiquitinationADLDTQRSDIATLLK
CCCCCCHHHHHHHHH
24.4523000965
20UbiquitinationRSDIATLLKTSLRKG
HHHHHHHHHHHHCCC
5.0321890473
21UbiquitinationSDIATLLKTSLRKGD
HHHHHHHHHHHCCCC
38.9029967540
22PhosphorylationDIATLLKTSLRKGDT
HHHHHHHHHHCCCCE
32.7223312004
23PhosphorylationIATLLKTSLRKGDTW
HHHHHHHHHCCCCEE
25.2923312004
33UbiquitinationKGDTWYLVDSRWFKQ
CCCEEEEECHHHHHH
3.5421890473
42UbiquitinationSRWFKQWKKYVGFDS
HHHHHHHHHHCCCCC
31.5624816145
46UbiquitinationKQWKKYVGFDSWDKY
HHHHHHCCCCCCCCC
19.9724816145
49PhosphorylationKKYVGFDSWDKYQMG
HHHCCCCCCCCCCCC
34.6128348404
61UbiquitinationQMGDQNVYPGPIDNS
CCCCCCCCCCCCCCC
15.2622817900
78PhosphorylationLKDGDAQSLKEHLID
CCCCCHHHHHHHHHH
43.0328060719
89PhosphorylationHLIDELDYILLPTEG
HHHHHCCEEEECCCH
13.19-
102PhosphorylationEGWNKLVSWYTLMEG
CHHHHHHHHHHHHCC
25.4620068231
104PhosphorylationWNKLVSWYTLMEGQE
HHHHHHHHHHHCCCC
5.1920068231
105PhosphorylationNKLVSWYTLMEGQEP
HHHHHHHHHHCCCCC
17.2320068231
107UbiquitinationLVSWYTLMEGQEPIA
HHHHHHHHCCCCCHH
4.1321890473
108PhosphorylationVSWYTLMEGQEPIAR
HHHHHHHCCCCCHHH
61.9232645325
122SulfoxidationRKVVEQGMFVKHCKV
HHHHHCCCEEEECEE
3.3121406390
134PhosphorylationCKVEVYLTELKLCEN
CEEEEEEEEEEEECC
22.9125627689
138UbiquitinationVYLTELKLCENGNMN
EEEEEEEEECCCCCC
7.4723000965
149PhosphorylationGNMNNVVTRRFSKAD
CCCCCCEEECCCCCC
16.31-
151UbiquitinationMNNVVTRRFSKADTI
CCCCEEECCCCCCCH
30.7221963094
154UbiquitinationVVTRRFSKADTIDTI
CEEECCCCCCCHHHH
47.7921890473
154UbiquitinationVVTRRFSKADTIDTI
CEEECCCCCCCHHHH
47.7921890473
154AcetylationVVTRRFSKADTIDTI
CEEECCCCCCCHHHH
47.7926051181
154UbiquitinationVVTRRFSKADTIDTI
CEEECCCCCCCHHHH
47.7922817900
154 (in isoform 1)Ubiquitination-47.7921890473
154 (in isoform 2)Ubiquitination-47.7921890473
154 (in isoform 3)Ubiquitination-47.7921890473
160PhosphorylationSKADTIDTIEKEIRK
CCCCCHHHHHHHHHH
27.4728674419
163UbiquitinationDTIDTIEKEIRKIFS
CCHHHHHHHHHHHHC
55.3724816145
167UbiquitinationTIEKEIRKIFSIPDE
HHHHHHHHHHCCCCH
54.4824816145
170PhosphorylationKEIRKIFSIPDEKET
HHHHHHHCCCCHHHH
36.3621815630
175UbiquitinationIFSIPDEKETRLWNK
HHCCCCHHHHHHHHH
72.3029967540
182UbiquitinationKETRLWNKYMSNTFE
HHHHHHHHHHCCCCC
30.6522817900
183PhosphorylationETRLWNKYMSNTFEP
HHHHHHHHHCCCCCC
11.5422468782
185PhosphorylationRLWNKYMSNTFEPLN
HHHHHHHCCCCCCCC
29.6322468782
187PhosphorylationWNKYMSNTFEPLNKP
HHHHHCCCCCCCCCC
23.2827251275
193UbiquitinationNTFEPLNKPDSTIQD
CCCCCCCCCCCCCCC
58.8629967540
219PhosphorylationEQKNEDGTWPRGPST
EEECCCCCCCCCCCC
44.6230576142
219 (in isoform 2)Phosphorylation-44.6222199227
223 (in isoform 3)Phosphorylation-19.2122199227
225PhosphorylationGTWPRGPSTPKSPGA
CCCCCCCCCCCCCCC
61.2323927012
225 (in isoform 2)Phosphorylation-61.2322199227
225 (in isoform 4)Phosphorylation-61.2325849741
226PhosphorylationTWPRGPSTPKSPGAS
CCCCCCCCCCCCCCC
37.5625159151
226UbiquitinationTWPRGPSTPKSPGAS
CCCCCCCCCCCCCCC
37.5623000965
226 (in isoform 2)Phosphorylation-37.5622199227
226 (in isoform 4)Phosphorylation-37.5622617229
228UbiquitinationPRGPSTPKSPGASNF
CCCCCCCCCCCCCCC
70.1721890473
228UbiquitinationPRGPSTPKSPGASNF
CCCCCCCCCCCCCCC
70.1722817900
228 (in isoform 1)Ubiquitination-70.1721890473
229PhosphorylationRGPSTPKSPGASNFS
CCCCCCCCCCCCCCC
29.7519664994
229 (in isoform 3)Phosphorylation-29.7522199227
230UbiquitinationGPSTPKSPGASNFST
CCCCCCCCCCCCCCC
48.7923000965
230 (in isoform 3)Phosphorylation-48.7922199227
232UbiquitinationSTPKSPGASNFSTLP
CCCCCCCCCCCCCCC
12.5121890473
233PhosphorylationTPKSPGASNFSTLPK
CCCCCCCCCCCCCCC
44.3030266825
234 (in isoform 2)Phosphorylation-34.0625159151
234 (in isoform 4)Phosphorylation-34.0627251275
236PhosphorylationSPGASNFSTLPKISP
CCCCCCCCCCCCCCH
33.0326846344
237PhosphorylationPGASNFSTLPKISPS
CCCCCCCCCCCCCHH
42.8326846344
238 (in isoform 3)Phosphorylation-3.8425159151
242PhosphorylationFSTLPKISPSSLSNN
CCCCCCCCHHHCCCC
25.5121945579
243UbiquitinationSTLPKISPSSLSNNY
CCCCCCCHHHCCCCC
31.2621963094
244PhosphorylationTLPKISPSSLSNNYN
CCCCCCHHHCCCCCC
36.8023401153
245PhosphorylationLPKISPSSLSNNYNN
CCCCCHHHCCCCCCC
38.9221945579
247PhosphorylationKISPSSLSNNYNNMN
CCCHHHCCCCCCCCC
25.6121945579
250PhosphorylationPSSLSNNYNNMNNRN
HHHCCCCCCCCCCCC
16.5021945579
259MethylationNMNNRNVKNSNYCLP
CCCCCCCCCCCCCCC
59.2054429133
259UbiquitinationNMNNRNVKNSNYCLP
CCCCCCCCCCCCCCC
59.2023000965
261PhosphorylationNNRNVKNSNYCLPSY
CCCCCCCCCCCCCCC
24.3721945579
263PhosphorylationRNVKNSNYCLPSYTA
CCCCCCCCCCCCCCE
8.6621945579
267PhosphorylationNSNYCLPSYTAYKNY
CCCCCCCCCCEECCC
23.3628555341
268PhosphorylationSNYCLPSYTAYKNYD
CCCCCCCCCEECCCC
8.0821945579
269PhosphorylationNYCLPSYTAYKNYDY
CCCCCCCCEECCCCC
28.0528442448
271PhosphorylationCLPSYTAYKNYDYSE
CCCCCCEECCCCCCC
7.6228442448
272UbiquitinationLPSYTAYKNYDYSEP
CCCCCEECCCCCCCC
46.7123000965
274PhosphorylationSYTAYKNYDYSEPGR
CCCEECCCCCCCCCC
16.4728796482
276PhosphorylationTAYKNYDYSEPGRNN
CEECCCCCCCCCCCC
12.4628796482
277PhosphorylationAYKNYDYSEPGRNNE
EECCCCCCCCCCCCC
34.1228442448
311UbiquitinationIQCLSNTPPLTEYFL
HHHHHCCCCCHHHHH
26.5929967540
318UbiquitinationPPLTEYFLNDKYQEE
CCCHHHHHCHHHHHH
8.7423000965
324UbiquitinationFLNDKYQEELNFDNP
HHCHHHHHHHCCCCC
62.4521890473
324 (in isoform 2)Ubiquitination-62.4521890473
329 (in isoform 3)Ubiquitination-55.5621890473
340UbiquitinationGMRGEIAKSYAELIK
CHHHHHHHHHHHHHH
50.0529967540
347UbiquitinationKSYAELIKQMWSGKF
HHHHHHHHHHHCCCC
46.8823000965
353UbiquitinationIKQMWSGKFSYVTPR
HHHHHCCCCCEECCH
26.1421890473
353UbiquitinationIKQMWSGKFSYVTPR
HHHHHCCCCCEECCH
26.1423000965
353 (in isoform 1)Ubiquitination-26.1421890473
355PhosphorylationQMWSGKFSYVTPRAF
HHHCCCCCEECCHHH
23.3725348954
356PhosphorylationMWSGKFSYVTPRAFK
HHCCCCCEECCHHHH
16.1025348954
358PhosphorylationSGKFSYVTPRAFKTQ
CCCCCEECCHHHHHC
9.9925348954
363MethylationYVTPRAFKTQVGRFA
EECCHHHHHCCCCCC
36.7454429125
363UbiquitinationYVTPRAFKTQVGRFA
EECCHHHHHCCCCCC
36.74-
373UbiquitinationVGRFAPQFSGYQQQD
CCCCCCCCCCCCHHH
6.2729967540
379UbiquitinationQFSGYQQQDCQELLA
CCCCCCHHHHHHHHH
37.6129967540
387UbiquitinationDCQELLAFLLDGLHE
HHHHHHHHHHHHHHH
7.6029967540
402UbiquitinationDLNRIRKKPYIQLKD
HHHHHHCCCCEECCC
32.9529967540
408UbiquitinationKKPYIQLKDADGRPD
CCCCEECCCCCCCCC
34.2029967540
416UbiquitinationDADGRPDKVVAEEAW
CCCCCCCCCHHHHHH
41.0929967540
445PhosphorylationFHGLFKSTLVCPECA
CCCHHHCCCCCCCHH
24.65-
446UbiquitinationHGLFKSTLVCPECAK
CCHHHCCCCCCCHHE
4.8833845483
475PhosphorylationLPMKKERTLEVYLVR
CCCCCCCEEEEEEEE
28.5030622161
479PhosphorylationKERTLEVYLVRMDPL
CCCEEEEEEEECCCC
7.0730622161
480UbiquitinationERTLEVYLVRMDPLT
CCEEEEEEEECCCCC
2.0823000965
484UbiquitinationEVYLVRMDPLTKPMQ
EEEEEECCCCCCCCE
25.2121890473
487PhosphorylationLVRMDPLTKPMQYKV
EEECCCCCCCCEEEE
38.1924850871
492PhosphorylationPLTKPMQYKVVVPKI
CCCCCCEEEEEECCC
10.2530622161
530UbiquitinationTDIYNHRFHRIFAMD
EECHHCCCHHEEEEC
3.3633845483
564UbiquitinationNRTEDTEHVIIPVCL
ECCCCCCEEEEEHHH
20.4033845483
576UbiquitinationVCLREKFRHSSYTHH
HHHHHHHCCCCCCCC
39.5921890473
576 (in isoform 2)Ubiquitination-39.5921890473
578PhosphorylationLREKFRHSSYTHHTG
HHHHHCCCCCCCCCC
22.3021406692
579PhosphorylationREKFRHSSYTHHTGS
HHHHCCCCCCCCCCC
28.1121406692
580PhosphorylationEKFRHSSYTHHTGSS
HHHCCCCCCCCCCCC
17.0721406692
581PhosphorylationKFRHSSYTHHTGSSL
HHCCCCCCCCCCCCC
14.7721406692
581 (in isoform 3)Ubiquitination-14.7721890473
584PhosphorylationHSSYTHHTGSSLFGQ
CCCCCCCCCCCCCCC
31.0221406692
586PhosphorylationSYTHHTGSSLFGQPF
CCCCCCCCCCCCCCE
25.6421406692
587PhosphorylationYTHHTGSSLFGQPFL
CCCCCCCCCCCCCEE
29.1221406692
602PhosphorylationMAVPRNNTEDKLYNL
EEECCCCCHHHHHHH
49.4620068231
605UbiquitinationPRNNTEDKLYNLLLL
CCCCCHHHHHHHHHH
46.7921890473
605UbiquitinationPRNNTEDKLYNLLLL
CCCCCHHHHHHHHHH
46.7923000965
605 (in isoform 1)Ubiquitination-46.7921890473
607PhosphorylationNNTEDKLYNLLLLRM
CCCHHHHHHHHHHHH
14.9820068231
621PhosphorylationMCRYVKISTETEETE
HHCEEECCCCCCCCC
17.9323312004
622PhosphorylationCRYVKISTETEETEG
HCEEECCCCCCCCCC
50.8523312004
624PhosphorylationYVKISTETEETEGSL
EEECCCCCCCCCCCE
38.9323312004
627PhosphorylationISTETEETEGSLHCC
CCCCCCCCCCCEEEE
39.1424719451
630PhosphorylationETEETEGSLHCCKDQ
CCCCCCCCEEEECCC
14.5425849741
632PhosphorylationEETEGSLHCCKDQNI
CCCCCCEEEECCCCC
19.3433259812
658UbiquitinationGSPSEMETDEPDDES
CCCCCCCCCCCCCCC
44.3333845483
678PhosphorylationLPSENENSQSEDSVG
CCCCCCCCCCCCCCC
28.9817478428
692UbiquitinationGGDNDSENGLCTEDT
CCCCCCCCCEECCCC
53.3323000965
716PhosphorylationKRLFTFQFNNLGNTD
CEEEEEEECCCCCCC
5.9833259812
726PhosphorylationLGNTDINYIKDDTRH
CCCCCCEEECCCCCE
15.07-
728UbiquitinationNTDINYIKDDTRHIR
CCCCEEECCCCCEEE
38.91-
729UbiquitinationTDINYIKDDTRHIRF
CCCEEECCCCCEEEE
53.6129967540
750UbiquitinationLDERSFLALDWDPDL
CCCCCEECCCCCHHH
11.0633845483
753UbiquitinationRSFLALDWDPDLKKR
CCEECCCCCHHHHHH
21.6429967540
754UbiquitinationSFLALDWDPDLKKRY
CEECCCCCHHHHHHH
26.8829967540
758AcetylationLDWDPDLKKRYFDEN
CCCCHHHHHHHCCCC
42.4524471339
758UbiquitinationLDWDPDLKKRYFDEN
CCCCHHHHHHHCCCC
42.4529967540
759AcetylationDWDPDLKKRYFDENA
CCCHHHHHHHCCCCC
60.6824469783
760UbiquitinationWDPDLKKRYFDENAA
CCHHHHHHHCCCCCH
35.4529967540
769UbiquitinationFDENAAEDFEKHESV
CCCCCHHHHHHCCCC
52.8829967540
779UbiquitinationKHESVEYKPPKKPFV
HCCCCCCCCCCCCCE
41.1433845483
782UbiquitinationSVEYKPPKKPFVKLK
CCCCCCCCCCCEEHH
79.9829967540
783UbiquitinationVEYKPPKKPFVKLKD
CCCCCCCCCCEEHHH
49.8429967540
784UbiquitinationEYKPPKKPFVKLKDC
CCCCCCCCCEEHHHH
45.4423000965
789UbiquitinationKKPFVKLKDCIELFT
CCCCEEHHHHHHHHH
44.8529967540
798UbiquitinationCIELFTTKEKLGAED
HHHHHHCHHHHCCCC
50.2029967540
813UbiquitinationPWYCPNCKEHQQATK
CCCCCCHHHHHHHHH
65.9423000965
826PhosphorylationTKKLDLWSLPPVLVV
HHHCCHHHCCCEEEE
37.99-
844PhosphorylationRFSYSRYMRDKLDTL
CCCHHHHHHHHHCCC
4.3133259812
881PhosphorylationRYNLIAVSNHYGGMG
EEEEEEEECCCCCCC
14.63-
926PhosphorylationQIVSKAAYVLFYQRQ
HHHCHHEEEEEEEEC
11.5328152594
935PhosphorylationLFYQRQDTFSGTGFF
EEEEECCCCCCCCCE
16.0321406692
936PhosphorylationFYQRQDTFSGTGFFP
EEEECCCCCCCCCEE
9.4933259812
937PhosphorylationYQRQDTFSGTGFFPL
EEECCCCCCCCCEEC
37.2221406692
939PhosphorylationRQDTFSGTGFFPLDR
ECCCCCCCCCEECCC
29.6221406692
952PhosphorylationDRETKGASAATGIPL
CCCCCCCCCCCCCCC
27.4023927012
955PhosphorylationTKGASAATGIPLESD
CCCCCCCCCCCCCCC
35.0530278072
961PhosphorylationATGIPLESDEDSNDN
CCCCCCCCCCCCCCC
54.7223927012
965PhosphorylationPLESDEDSNDNDNDI
CCCCCCCCCCCCCCC
43.9923927012
980PhosphorylationENENCMHTN------
CCCCCCCCC------
0.0028450419

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
678SPhosphorylationKinaseATMQ13315
PSP
-KUbiquitinationE3 ubiquitin ligaseBRAPQ7Z569
PMID:23105109

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP15_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 UBP15_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PUR8_HUMANADSLphysical
19615732
ALDOA_HUMANALDOAphysical
19615732
CALL3_HUMANCALML3physical
19615732
KCRB_HUMANCKBphysical
19615732
CSTF1_HUMANCSTF1physical
19615732
FABP4_HUMANFABP4physical
19615732
K1H1_HUMANKRT31physical
19615732
KT33B_HUMANKRT33Bphysical
19615732
KRT34_HUMANKRT34physical
19615732
KRT35_HUMANKRT35physical
19615732
KRT81_HUMANKRT81physical
19615732
KRT85_HUMANKRT85physical
19615732
LEG7_HUMANLGALS7physical
19615732
MYH2_HUMANMYH2physical
19615732
MYH4_HUMANMYH4physical
19615732
PGAM2_HUMANPGAM2physical
19615732
PSD11_HUMANPSMD11physical
19615732
SBP1_HUMANSELENBP1physical
19615732
PRP4_HUMANPRPF4physical
19615732
PRPF3_HUMANPRPF3physical
19615732
BRE1B_HUMANRNF40physical
19615732
PPIH_HUMANPPIHphysical
19615732
LSM6_HUMANLSM6physical
19615732
LSM4_HUMANLSM4physical
19615732
PRP31_HUMANPRPF31physical
19615732
LSM8_HUMANLSM8physical
19615732
MEPCE_HUMANMEPCEphysical
19615732
LSM2_HUMANLSM2physical
19615732
STPAP_HUMANTUT1physical
19615732
LRC15_HUMANLRRC15physical
19615732
PSMD7_HUMANPSMD7physical
19615732
UBP11_HUMANUSP11physical
19615732
UBC_HUMANUBCphysical
16005295
UBP15_HUMANUSP15physical
22001210
SMAD3_HUMANSMAD3physical
21947082
UBC_HUMANUBCphysical
20622874
UBE2S_HUMANUBE2Sphysical
20622874
TRAF6_HUMANTRAF6physical
20622874
UBC_HUMANUBCphysical
19373254
FHL1_HUMANFHL1physical
21219870
SMUF2_HUMANSMURF2physical
22344298
UBP20_HUMANUSP20physical
22626734
UBP51_HUMANUSP51physical
22626734
UBP7_HUMANUSP7physical
22626734
OTUB1_HUMANOTUB1physical
22626734
JOS1_HUMANJOSD1physical
22626734
UCHL3_HUMANUCHL3physical
22626734
UBP8_HUMANUSP8physical
22626734
UBP21_HUMANUSP21physical
22626734
UBP33_HUMANUSP33physical
22626734
SENP8_HUMANSENP8physical
22626734
UBP14_HUMANUSP14physical
22626734
STAM1_HUMANSTAMphysical
22626734
BAP1_HUMANBAP1physical
22626734
OTU1_HUMANYOD1physical
22626734
UCHL1_HUMANUCHL1physical
22626734
UBC_HUMANUBCphysical
22626734
SENP3_HUMANSENP3physical
22626734
UBP4_HUMANUSP4physical
22626734
WAPL_HUMANWAPALphysical
22939629
ZC3HD_HUMANZC3H13physical
22939629
ZMYM2_HUMANZMYM2physical
22939629
RO52_HUMANTRIM21physical
23105109
BRAP_HUMANBRAPphysical
23105109
HOIL1_HUMANRBCK1physical
23105109
TRI17_HUMANTRIM17physical
23105109
PHF7_HUMANPHF7physical
23105109
RN126_HUMANRNF126physical
23105109
TRI46_HUMANTRIM46physical
23105109
TRIM5_HUMANTRIM5physical
23105109
R144B_HUMANRNF144Bphysical
23105109
TRI74_HUMANTRIM74physical
23105109
NUSAP_HUMANNUSAP1physical
22863883
PLOD2_HUMANPLOD2physical
22863883
UGPA_HUMANUGP2physical
22863883
BRE1A_HUMANRNF20physical
24526689
BRE1B_HUMANRNF40physical
24526689
SART3_HUMANSART3physical
24526689
TRI25_HUMANTRIM25physical
24399297
TRAF4_HUMANTRAF4physical
23973329
TGFR1_HUMANTGFBR1physical
24850914
BMR1A_HUMANBMPR1Aphysical
24850914
ACVR1_HUMANACVR1physical
24850914
BMR1B_HUMANBMPR1Bphysical
24850914
SMAD6_HUMANSMAD6physical
24850914
UBC_HUMANUBCphysical
24850914
PA2GA_HUMANPLA2G2Aphysical
22118674
H2B2E_HUMANHIST2H2BEphysical
24526689
SPDLY_HUMANSPDL1physical
25416956
CARD9_HUMANCARD9physical
25416956
CCD57_HUMANCCDC57physical
25416956
UBC_HUMANUBCphysical
25527291
SMAD2_HUMANSMAD2physical
26455393
SMAD3_HUMANSMAD3physical
26455393
CTNB1_HUMANCTNNB1physical
26884171
APC1_HUMANANAPC1physical
26884171
AXIN1_HUMANAXIN1physical
26884171
FBW1A_HUMANBTRCphysical
26884171
SMUF2_HUMANSMURF2physical
26435193
SART3_HUMANSART3physical
28088760
PRP31_HUMANPRPF31physical
28088760
UBP4_HUMANUSP4physical
28088760
UBC_HUMANUBCphysical
28088760
P53_HUMANTP53physical
27893708
NF2L1_HUMANNFE2L1physical
27416755
KEAP1_HUMANKEAP1physical
23727018
NS1BP_HUMANIVNS1ABPphysical
27173435
SMC1A_HUMANSMC1Aphysical
27173435
GAPD1_HUMANGAPVD1physical
27173435
ANK3_HUMANANK3physical
27173435
SBNO1_HUMANSBNO1physical
27173435
SMC3_HUMANSMC3physical
27173435
SOX4_HUMANSOX4physical
27173435
HSF1_HUMANHSF1physical
27173435
K1468_HUMANKIAA1468physical
27173435
PLK1_HUMANPLK1physical
27173435
P4R3A_HUMANSMEK1physical
27173435
RNF26_HUMANRNF26physical
27368102

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 UBP15_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-229; SER-961 AND SER-965, AND MASSSPECTROMETRY.
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-229, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-229; SER-961 AND SER-965, AND MASSSPECTROMETRY.
"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-229; SER-961 ANDSER-965, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASSSPECTROMETRY.

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