UBP7_HUMAN - dbPTM
UBP7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP7_HUMAN
UniProt AC Q93009
Protein Name Ubiquitin carboxyl-terminal hydrolase 7
Gene Name USP7 {ECO:0000312|HGNC:HGNC:12630}
Organism Homo sapiens (Human).
Sequence Length 1102
Subcellular Localization Nucleus . Cytoplasm . Nucleus, PML body . Chromosome . Present in a minority of ND10 nuclear bodies. Association with ICP0/VMW110 at early times of infection leads to an increased proportion of USP7-containing ND10. Colocalizes with ATXN1 in the nucl
Protein Description Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX. [PubMed: 11923872]
Protein Sequence MNHQQQQQQQKAGEQQLSEPEDMEMEAGDTDDPPRITQNPVINGNVALSDGHNTAEEDMEDDTSWRSEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRFYPDRPHQKSVGFFLQCNAESDSTSWSCHAQAVLKIINYRDDEKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKGFIDDDKVTFEVFVQADAPHGVAWDSKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDDLSVRHCTNAYMLVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQKRKERQEAHLYMQVQIVAEDQFCGHQGNDMYDEEKVKYTVFKVLKNSSLAEFVQSLSQTMGFPQDQIRLWPMQARSNGTKRPAMLDNEADGNKTMIELSDNENPWTIFLETVDPELAASGATLPKFDKDHDVMLFLKMYDPKTRSLNYCGHIYTPISCKIRDLLPVMCDRAGFIQDTSLILYEEVKPNLTERIQDYDVSLDKALDELMDGDIIVFQKDDPENDNSELPTAKEYFRDLYHRVDVIFCDKTIPNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRHNYEGTLRDLLQFFKPRQPKKLYYQQLKMKITDFENRRSFKCIWLNSQFREEEITLYPDKHGCVRDLLEECKKAVELGEKASGKLRLLEIVSYKIIGVHQEDELLECLSPATSRTFRIEEIPLDQVDIDKENEMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEKEFEKFKFAIVMMGRHQYINEDEYEVNLKDFEPQPGNMSHPRPWLGLDHFNKAPKRSRYTYLEKAIKIHN
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
18PhosphorylationKAGEQQLSEPEDMEM
HHHHHHCCCHHHCCC
46.9329255136
30PhosphorylationMEMEAGDTDDPPRIT
CCCCCCCCCCCCCCC
41.1923927012
37PhosphorylationTDDPPRITQNPVING
CCCCCCCCCCCEECC
24.4730576142
49PhosphorylationINGNVALSDGHNTAE
ECCCEEECCCCCCCC
31.6328348404
54PhosphorylationALSDGHNTAEEDMED
EECCCCCCCCHHCCC
29.7628348404
63PhosphorylationEEDMEDDTSWRSEAT
CHHCCCCCCCCCCEE
42.3829978859
64PhosphorylationEDMEDDTSWRSEATF
HHCCCCCCCCCCEEE
27.7329978859
79PhosphorylationQFTVERFSRLSESVL
EEEHHHHHHHCHHCC
38.2328348404
82UbiquitinationVERFSRLSESVLSPP
HHHHHHHCHHCCCCC
27.0721890473
82PhosphorylationVERFSRLSESVLSPP
HHHHHHHCHHCCCCC
27.0724719451
84PhosphorylationRFSRLSESVLSPPCF
HHHHHCHHCCCCCEE
25.6128348404
98UbiquitinationFVRNLPWKIMVMPRF
EECCCCEEEEEECCC
20.9821906983
106PhosphorylationIMVMPRFYPDRPHQK
EEEECCCCCCCCCCC
12.9028152594
132UbiquitinationSDSTSWSCHAQAVLK
CCCCCCEEEHHHHHH
2.2221890473
143PhosphorylationAVLKIINYRDDEKSF
HHHHHHCCCCCCCCH
12.6628152594
148UbiquitinationINYRDDEKSFSRRIS
HCCCCCCCCHHHHHH
64.8921906983
149PhosphorylationNYRDDEKSFSRRISH
CCCCCCCCHHHHHHH
26.8023882029
151PhosphorylationRDDEKSFSRRISHLF
CCCCCCHHHHHHHHH
27.9517081983
155PhosphorylationKSFSRRISHLFFHKE
CCHHHHHHHHHHCCC
16.6023882029
209UbiquitinationGVAWDSKKHTGYVGL
CEEECCCCCCCCCCC
50.80-
211PhosphorylationAWDSKKHTGYVGLKN
EECCCCCCCCCCCCC
38.8028152594
213PhosphorylationDSKKHTGYVGLKNQG
CCCCCCCCCCCCCCC
7.7828152594
224UbiquitinationKNQGATCYMNSLLQT
CCCCCCCHHHHHHHH
8.58-
238UbiquitinationTLFFTNQLRKAVYMM
HHHHHHHHHHEEEEC
7.0421890473
240UbiquitinationFFTNQLRKAVYMMPT
HHHHHHHHEEEECCC
51.28-
254AcetylationTEGDDSSKSVPLALQ
CCCCCCCCCHHHHHH
60.4726051181
254UbiquitinationTEGDDSSKSVPLALQ
CCCCCCCCCHHHHHH
60.4721906983
256AcetylationGDDSSKSVPLALQRV
CCCCCCCHHHHHHHH
5.31-
256UbiquitinationGDDSSKSVPLALQRV
CCCCCCCHHHHHHHH
5.31-
272AcetylationYELQHSDKPVGTKKL
HHHHCCCCCCCCCCH
44.6223954790
272MalonylationYELQHSDKPVGTKKL
HHHHCCCCCCCCCCH
44.6226320211
272UbiquitinationYELQHSDKPVGTKKL
HHHHCCCCCCCCCCH
44.62-
2772-HydroxyisobutyrylationSDKPVGTKKLTKSFG
CCCCCCCCCHHHHHC
39.60-
277AcetylationSDKPVGTKKLTKSFG
CCCCCCCCCHHHHHC
39.6025953088
281AcetylationVGTKKLTKSFGWETL
CCCCCHHHHHCHHHH
54.9826051181
296UbiquitinationDSFMQHDVQELCRVL
HHHHHHCHHHHHHHH
4.46-
3102-HydroxyisobutyrylationLLDNVENKMKGTCVE
HHHCCCHHCCCCCEE
28.60-
310AcetylationLLDNVENKMKGTCVE
HHHCCCHHCCCCCEE
28.6025953088
312AcetylationDNVENKMKGTCVEGT
HCCCHHCCCCCEECC
53.3226051181
312UbiquitinationDNVENKMKGTCVEGT
HCCCHHCCCCCEECC
53.32-
319UbiquitinationKGTCVEGTIPKLFRG
CCCCEECCHHHHHCC
22.17-
322AcetylationCVEGTIPKLFRGKMV
CEECCHHHHHCCCEE
57.3025953088
322UbiquitinationCVEGTIPKLFRGKMV
CEECCHHHHHCCCEE
57.30-
3272-HydroxyisobutyrylationIPKLFRGKMVSYIQC
HHHHHCCCEEEEEEE
31.69-
327AcetylationIPKLFRGKMVSYIQC
HHHHHCCCEEEEEEE
31.6925953088
327MalonylationIPKLFRGKMVSYIQC
HHHHHCCCEEEEEEE
31.6926320211
331PhosphorylationFRGKMVSYIQCKEVD
HCCCEEEEEEEEECC
5.43-
335UbiquitinationMVSYIQCKEVDYRSD
EEEEEEEEECCCCCC
44.38-
339UbiquitinationIQCKEVDYRSDRRED
EEEEECCCCCCCCCC
19.7221890473
355UbiquitinationYDIQLSIKGKKNIFE
EEEEEEECCCCCHHH
62.3921906983
357UbiquitinationIQLSIKGKKNIFESF
EEEEECCCCCHHHHH
37.33-
358AcetylationQLSIKGKKNIFESFV
EEEECCCCCHHHHHC
65.0426051181
358UbiquitinationQLSIKGKKNIFESFV
EEEECCCCCHHHHHC
65.04-
379PhosphorylationQLDGDNKYDAGEHGL
ECCCCCCCCCCHHHH
19.78-
3912-HydroxyisobutyrylationHGLQEAEKGVKFLTL
HHHHHHHHCCCEEEC
75.86-
391UbiquitinationHGLQEAEKGVKFLTL
HHHHHHHHCCCEEEC
75.86-
404UbiquitinationTLPPVLHLQLMRFMY
ECCCHHHHHHHHHHH
3.5121890473
420UbiquitinationPQTDQNIKINDRFEF
CCCCCCCEECCCCCC
42.9021906983
423UbiquitinationDQNIKINDRFEFPEQ
CCCCEECCCCCCCCC
61.1821890473
424MethylationQNIKINDRFEFPEQL
CCCEECCCCCCCCCC
28.62115919673
439UbiquitinationPLDEFLQKTDPKDPA
CHHHHHHHCCCCCHH
57.9821906983
460UbiquitinationVLVHSGDNHGGHYVV
EEEECCCCCCCEEEE
38.95-
463UbiquitinationHSGDNHGGHYVVYLN
ECCCCCCCEEEEEEC
11.0321890473
474UbiquitinationVYLNPKGDGKWCKFD
EEECCCCCCCCCCCC
62.72-
476AcetylationLNPKGDGKWCKFDDD
ECCCCCCCCCCCCHH
54.9126051181
476UbiquitinationLNPKGDGKWCKFDDD
ECCCCCCCCCCCCHH
54.91-
479AcetylationKGDGKWCKFDDDVVS
CCCCCCCCCCHHHHH
51.1925953088
479UbiquitinationKGDGKWCKFDDDVVS
CCCCCCCCCCHHHHH
51.1921906983
490AcetylationDVVSRCTKEEAIEHN
HHHHHCCHHHHHHHC
58.1226051181
490UbiquitinationDVVSRCTKEEAIEHN
HHHHHCCHHHHHHHC
58.12-
507UbiquitinationGHDDDLSVRHCTNAY
CCCCCCHHHHHCCEE
6.69-
523UbiquitinationLVYIRESKLSEVLQA
EEEEEHHHHHHHHHH
51.81-
579UbiquitinationEDQFCGHQGNDMYDE
CCCCCCCCCCCCCCH
37.35-
595AcetylationKVKYTVFKVLKNSSL
HHHHHHHHHHCCCCH
42.1819608861
595UbiquitinationKVKYTVFKVLKNSSL
HHHHHHHHHHCCCCH
42.1819608861
665UbiquitinationWTIFLETVDPELAAS
EEEEEEECCHHHHHC
9.37-
672PhosphorylationVDPELAASGATLPKF
CCHHHHHCCCCCCCC
24.2921406692
675PhosphorylationELAASGATLPKFDKD
HHHHCCCCCCCCCCC
47.3121406692
679UbiquitinationSGATLPKFDKDHDVM
CCCCCCCCCCCCCEE
15.49-
6812-HydroxyisobutyrylationATLPKFDKDHDVMLF
CCCCCCCCCCCEEEE
61.16-
681AcetylationATLPKFDKDHDVMLF
CCCCCCCCCCCEEEE
61.1626051181
681UbiquitinationATLPKFDKDHDVMLF
CCCCCCCCCCCEEEE
61.16-
695UbiquitinationFLKMYDPKTRSLNYC
EEEECCCCCCCCCCC
54.39-
696UbiquitinationLKMYDPKTRSLNYCG
EEECCCCCCCCCCCC
30.77-
701PhosphorylationPKTRSLNYCGHIYTP
CCCCCCCCCCCEECC
12.7128152594
706PhosphorylationLNYCGHIYTPISCKI
CCCCCCEECCCCCCH
10.7828152594
707PhosphorylationNYCGHIYTPISCKIR
CCCCCEECCCCCCHH
17.3428152594
710PhosphorylationGHIYTPISCKIRDLL
CCEECCCCCCHHHHH
15.5728152594
712UbiquitinationIYTPISCKIRDLLPV
EECCCCCCHHHHHHH
33.70-
730PhosphorylationRAGFIQDTSLILYEE
CCCCCCCCCEEEEEE
14.7327251275
731PhosphorylationAGFIQDTSLILYEEV
CCCCCCCCEEEEEEC
23.0028348404
735PhosphorylationQDTSLILYEEVKPNL
CCCCEEEEEECCCCH
11.7527273156
739SumoylationLILYEEVKPNLTERI
EEEEEECCCCHHHHH
31.31-
743PhosphorylationEEVKPNLTERIQDYD
EECCCCHHHHHHHCC
29.83-
749PhosphorylationLTERIQDYDVSLDKA
HHHHHHHCCCCHHHH
11.2327642862
752PhosphorylationRIQDYDVSLDKALDE
HHHHCCCCHHHHHHH
28.1420873877
755UbiquitinationDYDVSLDKALDELMD
HCCCCHHHHHHHHCC
57.02-
761SulfoxidationDKALDELMDGDIIVF
HHHHHHHCCCCEEEE
5.2121406390
770UbiquitinationGDIIVFQKDDPENDN
CCEEEEECCCCCCCC
53.27-
782PhosphorylationNDNSELPTAKEYFRD
CCCCCCCCHHHHHHH
64.0924719451
784UbiquitinationNSELPTAKEYFRDLY
CCCCCCHHHHHHHHH
56.26-
791PhosphorylationKEYFRDLYHRVDVIF
HHHHHHHHHHCCEEE
7.5928152594
801AcetylationVDVIFCDKTIPNDPG
CCEEEECCCCCCCCC
49.9226051181
802O-linked_GlycosylationDVIFCDKTIPNDPGF
CEEEECCCCCCCCCE
28.5423301498
808UbiquitinationKTIPNDPGFVVTLSN
CCCCCCCCEEEEECC
30.7421890473
824AcetylationMNYFQVAKTVAQRLN
CCHHHHHHHHHHHHC
44.6825953088
824UbiquitinationMNYFQVAKTVAQRLN
CCHHHHHHHHHHHHC
44.6821906983
825UbiquitinationNYFQVAKTVAQRLNT
CHHHHHHHHHHHHCC
16.0121890473
832PhosphorylationTVAQRLNTDPMLLQF
HHHHHHCCCHHHHHH
46.1827174698
835SulfoxidationQRLNTDPMLLQFFKS
HHHCCCHHHHHHHHH
6.9421406390
841AcetylationPMLLQFFKSQGYRDG
HHHHHHHHHCCCCCC
43.0625953088
841MethylationPMLLQFFKSQGYRDG
HHHHHHHHHCCCCCC
43.0666726983
841UbiquitinationPMLLQFFKSQGYRDG
HHHHHHHHHCCCCCC
43.0621906983
842PhosphorylationMLLQFFKSQGYRDGP
HHHHHHHHCCCCCCC
24.5527174698
845PhosphorylationQFFKSQGYRDGPGNP
HHHHHCCCCCCCCCC
9.6328152594
853AcetylationRDGPGNPLRHNYEGT
CCCCCCCCCCCCCCH
11.45-
853UbiquitinationRDGPGNPLRHNYEGT
CCCCCCCCCCCCCCH
11.4521890473
859UbiquitinationPLRHNYEGTLRDLLQ
CCCCCCCCHHHHHHH
21.49-
866UbiquitinationGTLRDLLQFFKPRQP
CHHHHHHHHHCCCCC
49.3721890473
869AcetylationRDLLQFFKPRQPKKL
HHHHHHHCCCCCCCH
40.3519608861
869SumoylationRDLLQFFKPRQPKKL
HHHHHHHCCCCCCCH
40.3528112733
869UbiquitinationRDLLQFFKPRQPKKL
HHHHHHHCCCCCCCH
40.3521906983
875UbiquitinationFKPRQPKKLYYQQLK
HCCCCCCCHHHHHHH
48.7021906983
877PhosphorylationPRQPKKLYYQQLKMK
CCCCCCHHHHHHHHH
14.2230576142
878PhosphorylationRQPKKLYYQQLKMKI
CCCCCHHHHHHHHHC
10.5430576142
882SumoylationKLYYQQLKMKITDFE
CHHHHHHHHHCCCCC
33.5328112733
882UbiquitinationKLYYQQLKMKITDFE
CHHHHHHHHHCCCCC
33.5321906983
884UbiquitinationYYQQLKMKITDFENR
HHHHHHHHCCCCCCC
40.65-
886PhosphorylationQQLKMKITDFENRRS
HHHHHHCCCCCCCCC
29.1730576142
891MethylationKITDFENRRSFKCIW
HCCCCCCCCCEEEEE
28.55115919677
893PhosphorylationTDFENRRSFKCIWLN
CCCCCCCCEEEEEEC
26.3127067055
895AcetylationFENRRSFKCIWLNSQ
CCCCCCEEEEEECCC
26.5126051181
898AcetylationRRSFKCIWLNSQFRE
CCCEEEEEECCCCCC
10.04-
898UbiquitinationRRSFKCIWLNSQFRE
CCCEEEEEECCCCCC
10.04-
910UbiquitinationFREEEITLYPDKHGC
CCCEEECCCCCCCCH
7.79-
911UbiquitinationREEEITLYPDKHGCV
CCEEECCCCCCCCHH
10.75-
9142-HydroxyisobutyrylationEITLYPDKHGCVRDL
EECCCCCCCCHHHHH
37.08-
914AcetylationEITLYPDKHGCVRDL
EECCCCCCCCHHHHH
37.0823749302
914UbiquitinationEITLYPDKHGCVRDL
EECCCCCCCCHHHHH
37.08-
918AcetylationYPDKHGCVRDLLEEC
CCCCCCHHHHHHHHH
6.72-
918UbiquitinationYPDKHGCVRDLLEEC
CCCCCCHHHHHHHHH
6.72-
926AcetylationRDLLEECKKAVELGE
HHHHHHHHHHHHHHH
47.2326051181
926UbiquitinationRDLLEECKKAVELGE
HHHHHHHHHHHHHHH
47.23-
927UbiquitinationDLLEECKKAVELGEK
HHHHHHHHHHHHHHH
70.13-
934AcetylationKAVELGEKASGKLRL
HHHHHHHHHCCCCHH
46.1623749302
934UbiquitinationKAVELGEKASGKLRL
HHHHHHHHHCCCCHH
46.1621906983
946PhosphorylationLRLLEIVSYKIIGVH
CHHHHHEEEEEEEEC
26.7720860994
963PhosphorylationDELLECLSPATSRTF
HHHHHHCCCCCCCEE
24.9330266825
966PhosphorylationLECLSPATSRTFRIE
HHHCCCCCCCEEEEE
23.3330266825
967PhosphorylationECLSPATSRTFRIEE
HHCCCCCCCEEEEEE
31.2830266825
1017UbiquitinationRIHQGEHFREVMKRI
EHHCCHHHHHHHHHH
6.5721890473
1023UbiquitinationHFREVMKRIQSLLDI
HHHHHHHHHHHHHHH
17.68-
1026PhosphorylationEVMKRIQSLLDIQEK
HHHHHHHHHHHHCHH
28.6427050516
1033AcetylationSLLDIQEKEFEKFKF
HHHHHCHHHHHHHHE
51.8625953088
1033UbiquitinationSLLDIQEKEFEKFKF
HHHHHCHHHHHHHHE
51.8621906983
1037AcetylationIQEKEFEKFKFAIVM
HCHHHHHHHHEEEEE
60.2125953088
1039UbiquitinationEKEFEKFKFAIVMMG
HHHHHHHHEEEEECC
44.98-
1050PhosphorylationVMMGRHQYINEDEYE
EECCCCCCCCCCCEE
10.29-
1056PhosphorylationQYINEDEYEVNLKDF
CCCCCCCEEEECCCC
37.18-
1068AcetylationKDFEPQPGNMSHPRP
CCCCCCCCCCCCCCC
36.91-
1080UbiquitinationPRPWLGLDHFNKAPK
CCCCCCCCCCCCCCC
42.4021890473
1084AcetylationLGLDHFNKAPKRSRY
CCCCCCCCCCCCHHH
66.1919608861
1084MalonylationLGLDHFNKAPKRSRY
CCCCCCCCCCCCHHH
66.1926320211
1084UbiquitinationLGLDHFNKAPKRSRY
CCCCCCCCCCCCHHH
66.1919608861
1089PhosphorylationFNKAPKRSRYTYLEK
CCCCCCCHHHHHHHH
35.4524719451
1091PhosphorylationKAPKRSRYTYLEKAI
CCCCCHHHHHHHHHH
10.8623312004
1092PhosphorylationAPKRSRYTYLEKAIK
CCCCHHHHHHHHHHH
22.1123312004
1093PhosphorylationPKRSRYTYLEKAIKI
CCCHHHHHHHHHHHC
12.1523312004
1096AcetylationSRYTYLEKAIKIHN-
HHHHHHHHHHHCCC-
53.4619608861
1096UbiquitinationSRYTYLEKAIKIHN-
HHHHHHHHHHHCCC-
53.4621906983

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
18SPhosphorylationKinaseCSNK2A1P68400
GPS
-KUbiquitinationE3 ubiquitin ligaseICP0P08393
PMID:32416261

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
18SPhosphorylation

17651432
869Kubiquitylation

17651432
963SPhosphorylation

17651432

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 UBP7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
11923872
TRAF1_HUMANTRAF1physical
11279055
TRAF2_HUMANTRAF2physical
11279055
TRAF3_HUMANTRAF3physical
11279055
TRAF4_HUMANTRAF4physical
11279055
TRAF5_HUMANTRAF5physical
11279055
TRAF6_HUMANTRAF6physical
11279055
CLSPN_HUMANCLSPNphysical
19124652
MDM2_HUMANMDM2physical
17936559
PDC6I_HUMANPDCD6IPphysical
17927229
GUAA_HUMANGMPSphysical
15749019
H2B3B_HUMANHIST3H2BBphysical
15749019
P53_HUMANTP53physical
17525743
CRKL_HUMANCRKLphysical
19615732
DNMT1_HUMANDNMT1physical
19615732
IF4B_HUMANEIF4Bphysical
19615732
GTF2I_HUMANGTF2Iphysical
19615732
MCM4_HUMANMCM4physical
19615732
MCM5_HUMANMCM5physical
19615732
MCM6_HUMANMCM6physical
19615732
NUP98_HUMANNUP98physical
19615732
PPM1G_HUMANPPM1Gphysical
19615732
HLTF_HUMANHLTFphysical
19615732
SRP68_HUMANSRP68physical
19615732
ZN207_HUMANZNF207physical
19615732
CCDC6_HUMANCCDC6physical
19615732
AKAP1_HUMANAKAP1physical
19615732
RAE1L_HUMANRAE1physical
19615732
GUAA_HUMANGMPSphysical
19615732
UBP14_HUMANUSP14physical
19615732
BUB3_HUMANBUB3physical
19615732
TRIPC_HUMANTRIP12physical
19615732
BABA2_HUMANBREphysical
19615732
HUWE1_HUMANHUWE1physical
19615732
SCML2_HUMANSCML2physical
19615732
UBP19_HUMANUSP19physical
19615732
KIF3A_HUMANKIF3Aphysical
19615732
ABRX2_HUMANFAM175Bphysical
19615732
DCAF4_HUMANDCAF4physical
19615732
BABA1_HUMANBABAM1physical
19615732
RN220_HUMANRNF220physical
19615732
YLPM1_HUMANYLPM1physical
19615732
BRCC3_HUMANBRCC3physical
19615732
MCMBP_HUMANMCMBPphysical
19615732
FBX38_HUMANFBXO38physical
19615732
PPIL4_HUMANPPIL4physical
19615732
DOCK7_HUMANDOCK7physical
19615732
CHFR_HUMANCHFRphysical
17442268
UBP11_HUMANUSP11physical
19615732
P53_HUMANTP53physical
17380154
MDM2_HUMANMDM2physical
16943424
P53_HUMANTP53physical
16402859
MDM2_HUMANMDM2physical
16402859
PCGF2_HUMANPCGF2physical
20601937
BMI1_HUMANBMI1physical
20601937
RING1_HUMANRING1physical
20601937
RING2_HUMANRNF2physical
20601937
CBX8_HUMANCBX8physical
20601937
UBP11_HUMANUSP11physical
20601937
RING2_HUMANRNF2physical
20800574
RING1_HUMANRING1physical
20800574
BMI1_HUMANBMI1physical
20800574
EZH2_HUMANEZH2physical
20800574
SUZ12_HUMANSUZ12physical
20800574
EED_HUMANEEDphysical
20800574
GUAA_HUMANGMPSphysical
19834552
MDM4_HUMANMDM4physical
20713061
UHRF1_HUMANUHRF1physical
21745816
DNMT1_HUMANDNMT1physical
21745816
DNMT1_HUMANDNMT1physical
21268065
UHRF1_HUMANUHRF1physical
21268065
FOXN2_HUMANFOXN2physical
21845734
P53_HUMANTP53physical
21845734
CHK1_HUMANCHEK1physical
21845734
DAXX_HUMANDAXXphysical
16845383
MDM2_HUMANMDM2physical
16845383
P53_HUMANTP53physical
16845383
DNMT1_HUMANDNMT1physical
21045206
UBC_HUMANUBCphysical
20622874
UBE2S_HUMANUBE2Sphysical
20622874
TRAF6_HUMANTRAF6physical
20622874
UBP7_HUMANUSP7physical
16111684
UVSSA_HUMANUVSSAphysical
22466611
UHRF1_HUMANUHRF1physical
22411829
P53_HUMANTP53physical
14506283
P53_HUMANTP53physical
16474402
MDM2_HUMANMDM2physical
16474402
EBNA1_EBVB9BKRF1physical
16474402
ORF73_HHV8PHHV8GK18_gp81physical
22514345
UBC_HUMANUBCphysical
22195557
PSA5_HUMANPSMA5physical
19193609
PSA3_HUMANPSMA3physical
19193609
PSB6_HUMANPSMB6physical
19193609
PSB5_HUMANPSMB5physical
19193609
PSB8_HUMANPSMB8physical
19193609
PSB4_HUMANPSMB4physical
19193609
PML_HUMANPMLphysical
20719947
PML_HUMANPMLphysical
21305000
TBCB_HUMANTBCBphysical
16713569
TRI22_HUMANTRIM22physical
16713569
WWP2_HUMANWWP2physical
16713569
ACD_HUMANACDphysical
16713569
ARNT2_HUMANARNT2physical
16713569
PKHO1_HUMANPLEKHO1physical
16713569
CR3L3_HUMANCREB3L3physical
16713569
DNJA3_HUMANDNAJA3physical
16713569
EWS_HUMANEWSR1physical
16713569
RADIL_HUMANRADILphysical
16713569
RN220_HUMANRNF220physical
16713569
BEND5_HUMANBEND5physical
16713569
HECW1_HUMANHECW1physical
16713569
HERP1_HUMANHERPUD1physical
16713569
KLHL8_HUMANKLHL8physical
16713569
MAGE1_HUMANMAGEE1physical
16713569
MARH7_HUMANMARCH7physical
16713569
PEG3_HUMANPEG3physical
16713569
PICK1_HUMANPICK1physical
16713569
PKCB1_HUMANZMYND8physical
16713569
HTRA2_HUMANHTRA2physical
16713569
SYVN1_HUMANSYVN1physical
16713569
LAP2A_HUMANTMPOphysical
16713569
LAP2B_HUMANTMPOphysical
16713569
TROP_HUMANTROphysical
16713569
ZN423_HUMANZNF423physical
16713569
BCOR_HUMANBCORphysical
16713569
NECA2_HUMANNECAB2physical
16713569
PEPL_HUMANPPLphysical
16713569
UCRI_HUMANUQCRFS1physical
22939629
VAMP2_HUMANVAMP2physical
22939629
XPOT_HUMANXPOTphysical
22939629
ZCHC8_HUMANZCCHC8physical
22939629
WDR74_HUMANWDR74physical
22939629
XRCC4_HUMANXRCC4physical
22939629
VPS53_HUMANVPS53physical
22939629
TF65_HUMANRELAphysical
23267096
RARA_HUMANRARAphysical
23208507
TRI27_HUMANTRIM27physical
23105109
HOIL1_HUMANRBCK1physical
23105109
TRI31_HUMANTRIM31physical
23105109
MARH7_HUMANMARCH7physical
23105109
TRIM8_HUMANTRIM8physical
23105109
UHRF2_HUMANUHRF2physical
23105109
UBC_HUMANUBCphysical
23287719
DAXX_HUMANDAXXphysical
23348568
TRAF4_HUMANTRAF4physical
23388826
P53_HUMANTP53physical
23388826
DAXX_HUMANDAXXphysical
23536002
UB2E1_HUMANUBE2E1physical
23603909
KAT5_HUMANKAT5physical
23775119
PPARG_HUMANPPARGphysical
24072712
MCMBP_HUMANMCMBPphysical
24190967
CDC37_HUMANCDC37physical
22863883
CSN6_HUMANCOPS6physical
22863883
FKBP5_HUMANFKBP5physical
22863883
MAGD2_HUMANMAGED2physical
22863883
MMS19_HUMANMMS19physical
22863883
PPP6_HUMANPPP6Cphysical
22863883
PP6R3_HUMANPPP6R3physical
22863883
TRAP1_HUMANTRAP1physical
22863883
ABL1_HUMANABL1physical
24317448
PTEN_HUMANPTENphysical
24270891
RB_HUMANRB1physical
24823443
XPC_HUMANXPCphysical
25118285
PEPD_HUMANPEPDphysical
18330356
TPP1_HUMANTPP1physical
25172512
HUWE1_HUMANHUWE1physical
25147182
ABRX2_HUMANFAM175Bphysical
25283148
RN220_HUMANRNF220physical
25266658
PA2GA_HUMANPLA2G2Aphysical
22118674
ZEB1_HUMANZEB1physical
25086746
CHK1_HUMANCHEK1physical
25086746
SVIL_HUMANSVILphysical
23382381
ING1_HUMANING1physical
21731648
RL40_HUMANUBA52physical
14506283
UBC_HUMANUBCphysical
14506283
TRRAP_HUMANTRRAPphysical
25925205
SYDC_HUMANDARSphysical
25925205
CE112_HUMANCEP112physical
25925205
SF3B3_HUMANSF3B3physical
25925205
TM87A_HUMANTMEM87Aphysical
25925205
LMNA_HUMANLMNAphysical
25925205
GIN1_HUMANGIN1physical
25925205
MYNN_HUMANMYNNphysical
25925205
CWC22_HUMANCWC22physical
25925205
TNIP2_HUMANTNIP2physical
25925205
ZFP2_HUMANZFP2physical
25925205
ZN394_HUMANZNF394physical
25925205
ZN594_HUMANZNF594physical
25925205
FBF1_HUMANFBF1physical
25925205
ZC11A_HUMANZC3H11Aphysical
25925205
MTCH1_HUMANMTCH1physical
25925205
CA2D1_HUMANCACNA2D1physical
25925205
DDX4_HUMANDDX4physical
25925205
PIPNB_HUMANPITPNBphysical
25925205
SP110_HUMANSP110physical
25925205
DICER_HUMANDICER1physical
25925205
FA7_HUMANF7physical
25925205
KLC1_HUMANKLC1physical
25925205
GOGB1_HUMANGOLGB1physical
25925205
K2C1_HUMANKRT1physical
25925205
UTRO_HUMANUTRNphysical
25925205
MYO3A_HUMANMYO3Aphysical
25925205
MYH9_HUMANMYH9physical
25925205
MACF1_HUMANMACF1physical
25925205
DREB_HUMANDBN1physical
25925205
DYHC1_HUMANDYNC1H1physical
25925205
ZN169_HUMANZNF169physical
25925205
POLH_HUMANPOLHphysical
25435364
HNRPF_HUMANHNRNPFphysical
26344197
SMD1_HUMANSNRPD1physical
26344197
SCML2_HUMANSCML2physical
25605328
RING2_HUMANRNF2physical
25605328
BMI1_HUMANBMI1physical
25605328
H2A2C_HUMANHIST2H2ACphysical
25605328
H2B2E_HUMANHIST2H2BEphysical
25605328
BCL6_HUMANBCL6physical
26496610
BLMH_HUMANBLMHphysical
26496610
DNMT1_HUMANDNMT1physical
26496610
ETV6_HUMANETV6physical
26496610
PML_HUMANPMLphysical
26496610
TRI27_HUMANTRIM27physical
26496610
RING1_HUMANRING1physical
26496610
STIL_HUMANSTILphysical
26496610
TCF20_HUMANTCF20physical
26496610
TMF1_HUMANTMF1physical
26496610
LAP2A_HUMANTMPOphysical
26496610
LAP2B_HUMANTMPOphysical
26496610
PKP4_HUMANPKP4physical
26496610
YBOX3_HUMANYBX3physical
26496610
GUAA_HUMANGMPSphysical
26496610
KIF23_HUMANKIF23physical
26496610
WDR1_HUMANWDR1physical
26496610
SCML2_HUMANSCML2physical
26496610
FAKD2_HUMANFASTKD2physical
26496610
ZN609_HUMANZNF609physical
26496610
UHRF1_HUMANUHRF1physical
26496610
VATD_HUMANATP6V1Dphysical
26496610
BCOR_HUMANBCORphysical
26496610
BCORL_HUMANBCORL1physical
26496610
DHX40_HUMANDHX40physical
26496610
TCAL4_HUMANTCEAL4physical
26496610
FBX38_HUMANFBXO38physical
26496610
ACTL8_HUMANACTL8physical
26496610
PCGF1_HUMANPCGF1physical
26496610
PPIL4_HUMANPPIL4physical
26496610
PHLB2_HUMANPHLDB2physical
26496610
K2013_HUMANKIAA2013physical
26496610
RN169_HUMANRNF169physical
26496610
ANDR_HUMANARphysical
26175158
CI_DROMEciphysical
26120032
GLI1_HUMANGLI1physical
26120032
GLI2_HUMANGLI2physical
26120032
GLI3_HUMANGLI3physical
26120032
H2A2C_HUMANHIST2H2ACphysical
26507658
NUCL_HUMANNCLphysical
25695607
KPYM_HUMANPKMphysical
25695607
PP2AA_HUMANPPP2CAphysical
25695607
ANXA1_HUMANANXA1physical
25695607
RAD18_HUMANRAD18physical
25961918
CRY1_HUMANCRY1physical
25756610
VIRF1_HHV8PvIRF-1physical
26786098
OTUD4_HUMANOTUD4physical
25944111
PTEN_HUMANPTENphysical
26280536
RN168_HUMANRNF168physical
25894431
UHRF1_HUMANUHRF1physical
26299963
UB2D3_HUMANUBE2D3physical
26299963
TFP11_HUMANTFIP11physical
26460617
P53_HUMANTP53physical
26460617
MDM2_HUMANMDM2physical
26460617
KAT5_HUMANKAT5physical
25865756
KMT2E_HUMANKMT2Ephysical
26678539
OGT1_HUMANOGTphysical
26678539
GUAA_HUMANGMPSphysical
26046769
UHRF1_HUMANUHRF1physical
26046769
NUCL_HUMANNCLphysical
26238070
P53_HUMANTP53physical
26238070
MDM2_HUMANMDM2physical
26238070
MCM4_HUMANMCM4physical
26950370
SUMO2_HUMANSUMO2physical
26950370
DNMT1_HUMANDNMT1physical
25960197
GUAA_HUMANGMPSphysical
24462112
MDM2_HUMANMDM2physical
24462112
P53_HUMANTP53physical
24462112
UVSSA_HUMANUVSSAphysical
27129218
SYUA_HUMANSNCAphysical
27444016
MYC_HUMANMYCphysical
27618649
TRIPC_HUMANTRIP12physical
27800609
UBB_HUMANUBBphysical
27452404
UBP7_HUMANUSP7physical
27452404
PHF8_HUMANPHF8physical
27183383
MARH7_HUMANMARCH7physical
27302477
MDM2_HUMANMDM2physical
28196907
CHK1_HUMANCHEK1physical
25483066
CTNB1_HUMANCTNNB1physical
29045831
ZEB1_HUMANZEB1physical
29119051
SUV91_HUMANSUV39H1physical
26971997
MDM2_HUMANMDM2physical
26971997
INAR1_HUMANIFNAR1physical
28656291
SIR7_HUMANSIRT7physical
28655758
RN169_HUMANRNF169physical
28325877

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-595; LYS-869; LYS-1084 ANDLYS-1096, AND MASS SPECTROMETRY.
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-18; SER-49 AND THR-54,AND MASS SPECTROMETRY.
"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-18, 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-18 AND SER-963, AND MASSSPECTROMETRY.
"Biochemical characterization of USP7 reveals post-translationalmodification sites and structural requirements for substrateprocessing and subcellular localization.";
Fernandez-Montalvan A., Bouwmeester T., Joberty G., Mader R.,Mahnke M., Pierrat B., Schlaeppi J.M., Worpenberg S., Gerhartz B.;
FEBS J. 274:4256-4270(2007).
Cited for: SUBUNIT, PHOSPHORYLATION AT SER-18 AND SER-963, UBIQUITINATION ATLYS-869, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Biochemical characterization of USP7 reveals post-translationalmodification sites and structural requirements for substrateprocessing and subcellular localization.";
Fernandez-Montalvan A., Bouwmeester T., Joberty G., Mader R.,Mahnke M., Pierrat B., Schlaeppi J.M., Worpenberg S., Gerhartz B.;
FEBS J. 274:4256-4270(2007).
Cited for: SUBUNIT, PHOSPHORYLATION AT SER-18 AND SER-963, UBIQUITINATION ATLYS-869, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.

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