UBP25_HUMAN - dbPTM
UBP25_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP25_HUMAN
UniProt AC Q9UHP3
Protein Name Ubiquitin carboxyl-terminal hydrolase 25
Gene Name USP25
Organism Homo sapiens (Human).
Sequence Length 1055
Subcellular Localization Cytoplasm .
Isoform USP25m: Cytoplasm. Nucleus. Some transient punctuate nuclear location in myotubes during myocyte development..
Protein Description Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains.; The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function..
Protein Sequence MTVEQNVLQQSAAQKHQQTFLNQLREITGINDTQILQQALKDSNGNLELAVAFLTAKNAKTPQQEETTYYQTALPGNDRYISVGSQADTNVIDLTGDDKDDLQRAIALSLAESNRAFRETGITDEEQAISRVLEASIAENKACLKRTPTEVWRDSRNPYDRKRQDKAPVGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNAQDLPRNQKEHRNLPFMRELRYLFALLVGTKRKYVDPSRAVEILKDAFKSNDSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNGFKDLHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQALGRPEKIHNKLEFPQVLYLDRYMHRNREITRIKREEIKRLKDYLTVLQQRLERYLSYGSGPKRFPLVDVLQYALEFASSKPVCTSPVDDIDASSPPSGSIPSQTLPSTTEQQGALSSELPSTSPSSVAAISSRSVIHKPFTQSRIPPDLPMHPAPRHITEEELSVLESCLHRWRTEIENDTRDLQESISRIHRTIELMYSDKSMIQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASAYCLMYINDKAQFLIQEEFNKETGQPLVGIETLPPDLRDFVEEDNQRFEKELEEWDAQLAQKALQEKLLASQKLRESETSVTTAQAAGDPEYLEQPSRSDFSKHLKEETIQIITKASHEHEDKSPETVLQSAIKLEYARLVKLAQEDTPPETDYRLHHVVVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVAQAKLEMIKPEEVNLEEYEEWHQDYRKFRETTMYLIIGLENFQRESYIDSLLFLICAYQNNKELLSKGLYRGHDEELISHYRRECLLKLNEQAAELFESGEDREVNNGLIIMNEFIVPFLPLLLVDEMEEKDILAVEDMRNRWCSYLGQEMEPHLQEKLTDFLPKLLDCSMEIKSFHEPPKLPSYSTHELCERFARIMLSLSRTPADGR
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
2Phosphorylation------MTVEQNVLQ
------CCHHHHHHH
44.0124043423
11PhosphorylationEQNVLQQSAAQKHQQ
HHHHHHHHHHHHHHH
16.7724043423
14UbiquitinationVLQQSAAQKHQQTFL
HHHHHHHHHHHHHHH
43.4021890473
15UbiquitinationLQQSAAQKHQQTFLN
HHHHHHHHHHHHHHH
38.3621890473
15UbiquitinationLQQSAAQKHQQTFLN
HHHHHHHHHHHHHHH
38.3632015554
19PhosphorylationAAQKHQQTFLNQLRE
HHHHHHHHHHHHHHH
24.4224043423
29UbiquitinationNQLREITGINDTQIL
HHHHHHHCCCHHHHH
23.5123000965
33UbiquitinationEITGINDTQILQQAL
HHHCCCHHHHHHHHH
17.0223000965
40UbiquitinationTQILQQALKDSNGNL
HHHHHHHHHCCCCCH
5.7123000965
47UbiquitinationLKDSNGNLELAVAFL
HHCCCCCHHHEEEHH
6.3821890473
48UbiquitinationKDSNGNLELAVAFLT
HCCCCCHHHEEEHHH
38.3922817900
49UbiquitinationDSNGNLELAVAFLTA
CCCCCHHHEEEHHHH
5.3821890473
50UbiquitinationSNGNLELAVAFLTAK
CCCCHHHEEEHHHHC
4.9221963094
57UbiquitinationAVAFLTAKNAKTPQQ
EEEHHHHCCCCCCCC
52.8021890473
57UbiquitinationAVAFLTAKNAKTPQQ
EEEHHHHCCCCCCCC
52.8021906983
57 (in isoform 1)Ubiquitination-52.8021890473
57 (in isoform 2)Ubiquitination-52.8021890473
60UbiquitinationFLTAKNAKTPQQEET
HHHHCCCCCCCCCCC
70.8621906983
60 (in isoform 1)Ubiquitination-70.8621890473
60 (in isoform 2)Ubiquitination-70.8621890473
61PhosphorylationLTAKNAKTPQQEETT
HHHCCCCCCCCCCCC
24.7429978859
67PhosphorylationKTPQQEETTYYQTAL
CCCCCCCCCEEEECC
21.2428796482
67 (in isoform 3)Phosphorylation-21.2427642862
68PhosphorylationTPQQEETTYYQTALP
CCCCCCCCEEEECCC
24.4228796482
68 (in isoform 3)Phosphorylation-24.4227642862
69PhosphorylationPQQEETTYYQTALPG
CCCCCCCEEEECCCC
10.8628796482
69 (in isoform 3)Phosphorylation-10.8627642862
70PhosphorylationQQEETTYYQTALPGN
CCCCCCEEEECCCCC
9.4128796482
70 (in isoform 3)Phosphorylation-9.4127642862
71UbiquitinationQEETTYYQTALPGND
CCCCCEEEECCCCCC
15.1933845483
72PhosphorylationEETTYYQTALPGNDR
CCCCEEEECCCCCCC
17.6528796482
80PhosphorylationALPGNDRYISVGSQA
CCCCCCCEEEECCCC
10.6228674151
80 (in isoform 3)Phosphorylation-10.6227642862
82PhosphorylationPGNDRYISVGSQADT
CCCCCEEEECCCCCC
16.1023186163
85PhosphorylationDRYISVGSQADTNVI
CCEEEECCCCCCCEE
21.7523186163
89UbiquitinationSVGSQADTNVIDLTG
EECCCCCCCEEECCC
34.1122817900
91UbiquitinationGSQADTNVIDLTGDD
CCCCCCCEEECCCCC
3.8033845483
92UbiquitinationSQADTNVIDLTGDDK
CCCCCCEEECCCCCH
3.7921890473
93UbiquitinationQADTNVIDLTGDDKD
CCCCCEEECCCCCHH
33.6221890473
99SumoylationIDLTGDDKDDLQRAI
EECCCCCHHHHHHHH
58.86-
99SumoylationIDLTGDDKDDLQRAI
EECCCCCHHHHHHHH
58.8619440361
99UbiquitinationIDLTGDDKDDLQRAI
EECCCCCHHHHHHHH
58.8622817900
99 (in isoform 1)Ubiquitination-58.8621890473
99 (in isoform 2)Ubiquitination-58.8621890473
113PhosphorylationIALSLAESNRAFRET
HHHHHHHHHHHHHHH
26.4727251275
116UbiquitinationSLAESNRAFRETGIT
HHHHHHHHHHHHCCC
16.4621890473
128UbiquitinationGITDEEQAISRVLEA
CCCCHHHHHHHHHHH
12.6621890473
136PhosphorylationISRVLEASIAENKAC
HHHHHHHHHHCCHHH
16.9826270265
141SumoylationEASIAENKACLKRTP
HHHHHCCHHHHHCCC
31.79-
141SumoylationEASIAENKACLKRTP
HHHHHCCHHHHHCCC
31.79-
145UbiquitinationAENKACLKRTPTEVW
HCCHHHHHCCCHHHH
54.8521890473
147PhosphorylationNKACLKRTPTEVWRD
CHHHHHCCCHHHHHC
32.7325159151
149PhosphorylationACLKRTPTEVWRDSR
HHHHCCCHHHHHCCC
42.4228450419
166UbiquitinationYDRKRQDKAPVGLKN
CCCCCCCCCCCCCCC
46.3729967540
171UbiquitinationQDKAPVGLKNVGNTC
CCCCCCCCCCCCCCH
3.5721890473
180UbiquitinationNVGNTCWFSAVIQSL
CCCCCHHHHHHHHHH
3.5023000965
191UbiquitinationIQSLFNLLEFRRLVL
HHHHHHHHHHHHHHH
6.4922053931
200PhosphorylationFRRLVLNYKPPSNAQ
HHHHHHHCCCCCCCC
22.2526074081
201UbiquitinationRRLVLNYKPPSNAQD
HHHHHHCCCCCCCCC
49.7521890473
201UbiquitinationRRLVLNYKPPSNAQD
HHHHHHCCCCCCCCC
49.7522053931
201 (in isoform 1)Ubiquitination-49.7521890473
201 (in isoform 2)Ubiquitination-49.7521890473
204PhosphorylationVLNYKPPSNAQDLPR
HHHCCCCCCCCCCCC
54.0126074081
221UbiquitinationKEHRNLPFMRELRYL
HHHCCCHHHHHHHHH
8.9821890473
223UbiquitinationHRNLPFMRELRYLFA
HCCCHHHHHHHHHHH
39.9323000965
226UbiquitinationLPFMRELRYLFALLV
CHHHHHHHHHHHHHH
22.7323000965
239PhosphorylationLVGTKRKYVDPSRAV
HHCCCCCCCCHHHHH
17.7030576142
240UbiquitinationVGTKRKYVDPSRAVE
HCCCCCCCCHHHHHH
11.0721890473
244UbiquitinationRKYVDPSRAVEILKD
CCCCCHHHHHHHHHH
48.3023000965
250UbiquitinationSRAVEILKDAFKSND
HHHHHHHHHHHHCCC
53.3121890473
250UbiquitinationSRAVEILKDAFKSND
HHHHHHHHHHHHCCC
53.3123000965
250 (in isoform 1)Ubiquitination-53.3121890473
250 (in isoform 2)Ubiquitination-53.3121890473
250 (in isoform 3)Ubiquitination-53.31-
254UbiquitinationEILKDAFKSNDSQQQ
HHHHHHHHCCCHHCC
50.5021890473
254UbiquitinationEILKDAFKSNDSQQQ
HHHHHHHHCCCHHCC
50.5023000965
254 (in isoform 1)Ubiquitination-50.5021890473
254 (in isoform 2)Ubiquitination-50.5021890473
256UbiquitinationLKDAFKSNDSQQQDV
HHHHHHCCCHHCCCH
54.2521890473
265UbiquitinationSQQQDVSEFTHKLLD
HHCCCHHHHHHHHHH
55.1822053931
281UbiquitinationLEDAFQMKAEEETDE
HHHHHHHHHHHCCCC
41.6932015554
285UbiquitinationFQMKAEEETDEEKPK
HHHHHHHCCCCCCCC
53.7321890473
292UbiquitinationETDEEKPKNPMVELF
CCCCCCCCCCCHHHH
82.0833845483
294UbiquitinationDEEKPKNPMVELFYG
CCCCCCCCCHHHHHH
34.0321890473
299UbiquitinationKNPMVELFYGRFLAV
CCCCHHHHHHCHHHH
3.7321890473
302UbiquitinationMVELFYGRFLAVGVL
CHHHHHHCHHHHEEE
16.4222817900
303UbiquitinationVELFYGRFLAVGVLE
HHHHHHCHHHHEEEC
4.4521890473
306UbiquitinationFYGRFLAVGVLEGKK
HHHCHHHHEEECCCC
6.2321963094
311UbiquitinationLAVGVLEGKKFENTE
HHHEEECCCCEECCC
34.0021963094
312UbiquitinationAVGVLEGKKFENTEM
HHEEECCCCEECCCC
44.9321906983
312 (in isoform 1)Ubiquitination-44.9321890473
312 (in isoform 2)Ubiquitination-44.9321890473
313UbiquitinationVGVLEGKKFENTEMF
HEEECCCCEECCCCC
69.6221890473
313UbiquitinationVGVLEGKKFENTEMF
HEEECCCCEECCCCC
69.6221890473
313 (in isoform 1)Ubiquitination-69.6221890473
313 (in isoform 2)Ubiquitination-69.6221890473
317UbiquitinationEGKKFENTEMFGQYP
CCCCEECCCCCCCCC
22.9421890473
320UbiquitinationKFENTEMFGQYPLQV
CEECCCCCCCCCCEE
4.4921890473
331UbiquitinationPLQVNGFKDLHECLE
CCEECCCCCHHHHHH
61.8623000965
363UbiquitinationKSGQEHWFTELPPVL
CCCCCEECCCCCCEE
4.0322053931
366UbiquitinationQEHWFTELPPVLTFE
CCEECCCCCCEEEEE
5.4423000965
370UbiquitinationFTELPPVLTFELSRF
CCCCCCEEEEEEEHH
5.8322053931
378UbiquitinationTFELSRFEFNQALGR
EEEEEHHHHHHHHCC
42.4532015554
382UbiquitinationSRFEFNQALGRPEKI
EHHHHHHHHCCCHHH
17.0621890473
388UbiquitinationQALGRPEKIHNKLEF
HHHCCCHHHHCCCCC
52.5329967540
392UbiquitinationRPEKIHNKLEFPQVL
CCHHHHCCCCCCCHH
34.9221890473
392UbiquitinationRPEKIHNKLEFPQVL
CCHHHHCCCCCCCHH
34.9221890473
392 (in isoform 1)Ubiquitination-34.9221890473
392 (in isoform 2)Ubiquitination-34.9221890473
399UbiquitinationKLEFPQVLYLDRYMH
CCCCCCHHHHHHHHH
2.7121890473
404PhosphorylationQVLYLDRYMHRNREI
CHHHHHHHHHHCCCC
9.28-
405UbiquitinationVLYLDRYMHRNREIT
HHHHHHHHHHCCCCH
2.2022053931
409UbiquitinationDRYMHRNREITRIKR
HHHHHHCCCCHHHCH
36.3323000965
411UbiquitinationYMHRNREITRIKREE
HHHHCCCCHHHCHHH
2.5721890473
416UbiquitinationREITRIKREEIKRLK
CCCHHHCHHHHHHHH
44.3921890473
422UbiquitinationKREEIKRLKDYLTVL
CHHHHHHHHHHHHHH
4.1521890473
425PhosphorylationEIKRLKDYLTVLQQR
HHHHHHHHHHHHHHH
11.5924719451
427PhosphorylationKRLKDYLTVLQQRLE
HHHHHHHHHHHHHHH
16.9724719451
434UbiquitinationTVLQQRLERYLSYGS
HHHHHHHHHHHHCCC
41.2821890473
444UbiquitinationLSYGSGPKRFPLVDV
HHCCCCCCCCCHHHH
70.9221890473
444UbiquitinationLSYGSGPKRFPLVDV
HHCCCCCCCCCHHHH
70.9223000965
444 (in isoform 1)Ubiquitination-70.9221890473
444 (in isoform 2)Ubiquitination-70.9221890473
444 (in isoform 3)Ubiquitination-70.92-
446UbiquitinationYGSGPKRFPLVDVLQ
CCCCCCCCCHHHHHH
7.3821890473
448UbiquitinationSGPKRFPLVDVLQYA
CCCCCCCHHHHHHHH
4.7722053931
451UbiquitinationKRFPLVDVLQYALEF
CCCCHHHHHHHHHHH
2.5321890473
457UbiquitinationDVLQYALEFASSKPV
HHHHHHHHHHHCCCC
30.8721890473
469UbiquitinationKPVCTSPVDDIDASS
CCCCCCCCCCCCCCC
11.7823503661
477UbiquitinationDDIDASSPPSGSIPS
CCCCCCCCCCCCCCC
25.2821890473
489UbiquitinationIPSQTLPSTTEQQGA
CCCCCCCCCCCCCCC
51.5821963094
494UbiquitinationLPSTTEQQGALSSEL
CCCCCCCCCCCCCCC
32.6621963094
500UbiquitinationQQGALSSELPSTSPS
CCCCCCCCCCCCCHH
62.4121890473
510UbiquitinationSTSPSSVAAISSRSV
CCCHHHHHHHHCCCC
10.8821890473
520UbiquitinationSSRSVIHKPFTQSRI
HCCCCCCCCCCCCCC
30.6021890473
520UbiquitinationSSRSVIHKPFTQSRI
HCCCCCCCCCCCCCC
30.6021890473
520 (in isoform 1)Ubiquitination-30.6021890473
520 (in isoform 2)Ubiquitination-30.6021890473
539UbiquitinationPMHPAPRHITEEELS
CCCCCCCCCCHHHHH
30.2023503661
561UbiquitinationRWRTEIENDTRDLQE
HHHHHHHHCCHHHHH
62.7132015554
574UbiquitinationQESISRIHRTIELMY
HHHHHHHHHHHHHHH
21.5221890473
582PhosphorylationRTIELMYSDKSMIQV
HHHHHHHCCCCCCCC
25.2923663014
584UbiquitinationIELMYSDKSMIQVPY
HHHHHCCCCCCCCCE
35.6621890473
584UbiquitinationIELMYSDKSMIQVPY
HHHHHCCCCCCCCCE
35.6622053931
584 (in isoform 1)Ubiquitination-35.6621890473
584 (in isoform 2)Ubiquitination-35.6621890473
585PhosphorylationELMYSDKSMIQVPYR
HHHHCCCCCCCCCEE
26.5523663014
591PhosphorylationKSMIQVPYRLHAVLV
CCCCCCCEEEEEEEE
27.2723663014
620UbiquitinationFDHRESRWMKYNDIA
EECCCCCCCCCCCEE
9.2623000965
622UbiquitinationHRESRWMKYNDIAVT
CCCCCCCCCCCEEEE
33.66-
630UbiquitinationYNDIAVTKSSWEELV
CCCEEEEHHHHHHHH
35.5721890473
630UbiquitinationYNDIAVTKSSWEELV
CCCEEEEHHHHHHHH
35.5723000965
630 (in isoform 1)Ubiquitination-35.5721890473
630 (in isoform 2)Ubiquitination-35.5721890473
630 (in isoform 3)Ubiquitination-35.57-
644UbiquitinationVRDSFGGYRNASAYC
HHHHCCCCCCCCEEE
10.9023503661
652UbiquitinationRNASAYCLMYINDKA
CCCCEEEEEHHCHHH
1.5823503661
659UbiquitinationLMYINDKAQFLIQEE
EEHHCHHHHHHHHHH
14.2822053931
669UbiquitinationLIQEEFNKETGQPLV
HHHHHHHHCCCCCCE
63.0721906983
669 (in isoform 1)Ubiquitination-63.0721890473
669 (in isoform 2)Ubiquitination-63.0721890473
679UbiquitinationGQPLVGIETLPPDLR
CCCCEEEEECCCCHH
38.0623503661
680PhosphorylationQPLVGIETLPPDLRD
CCCEEEEECCCCHHH
42.52-
688UbiquitinationLPPDLRDFVEEDNQR
CCCCHHHHHHHHHHH
6.3521890473
698UbiquitinationEDNQRFEKELEEWDA
HHHHHHHHHHHHHHH
65.9621890473
698UbiquitinationEDNQRFEKELEEWDA
HHHHHHHHHHHHHHH
65.966983
698 (in isoform 1)Ubiquitination-65.9621890473
698 (in isoform 2)Ubiquitination-65.9621890473
700UbiquitinationNQRFEKELEEWDAQL
HHHHHHHHHHHHHHH
12.2321890473
705UbiquitinationKELEEWDAQLAQKAL
HHHHHHHHHHHHHHH
13.8321890473
710UbiquitinationWDAQLAQKALQEKLL
HHHHHHHHHHHHHHH
45.5221890473
710UbiquitinationWDAQLAQKALQEKLL
HHHHHHHHHHHHHHH
45.5221906983
710 (in isoform 1)Ubiquitination-45.5221890473
710 (in isoform 2)Ubiquitination-45.5221890473
711UbiquitinationDAQLAQKALQEKLLA
HHHHHHHHHHHHHHH
11.4621890473
715UbiquitinationAQKALQEKLLASQKL
HHHHHHHHHHHCHHH
35.5221890473
715UbiquitinationAQKALQEKLLASQKL
HHHHHHHHHHHCHHH
35.5221963094
715 (in isoform 1)Ubiquitination-35.5221890473
715 (in isoform 2)Ubiquitination-35.5221890473
715 (in isoform 3)Ubiquitination-35.52-
721UbiquitinationEKLLASQKLRESETS
HHHHHCHHHHHCCCC
47.2021890473
721UbiquitinationEKLLASQKLRESETS
HHHHHCHHHHHCCCC
47.2027667366
721 (in isoform 1)Ubiquitination-47.2021890473
721 (in isoform 2)Ubiquitination-47.2021890473
722UbiquitinationKLLASQKLRESETSV
HHHHCHHHHHCCCCH
5.9523503661
725PhosphorylationASQKLRESETSVTTA
HCHHHHHCCCCHHHH
39.4829978859
727PhosphorylationQKLRESETSVTTAQA
HHHHHCCCCHHHHHH
37.4629978859
728PhosphorylationKLRESETSVTTAQAA
HHHHCCCCHHHHHHH
17.2629978859
730PhosphorylationRESETSVTTAQAAGD
HHCCCCHHHHHHHCC
19.0429978859
731PhosphorylationESETSVTTAQAAGDP
HCCCCHHHHHHHCCH
18.0229978859
740PhosphorylationQAAGDPEYLEQPSRS
HHHCCHHHHCCCCCC
22.4129978859
745PhosphorylationPEYLEQPSRSDFSKH
HHHHCCCCCCHHHHH
44.0729978859
772 (in isoform 1)Phosphorylation-40.0524043423
775 (in isoform 1)Phosphorylation-29.8724043423
779 (in isoform 1)Phosphorylation-28.0024043423
782UbiquitinationTVLQSAIKLEYARLV
HHHHHHHHHHHHHHH
34.6832015554
783 (in isoform 1)Phosphorylation-5.0724043423
835PhosphorylationQFGDRNLSFDERCHN
HHCCCCCCHHHHHHH
33.9128857561
845UbiquitinationERCHNIMKVAQAKLE
HHHHHHHHHHHHHHH
30.5329967540
850UbiquitinationIMKVAQAKLEMIKPE
HHHHHHHHHHHCCHH
32.6629967540
873UbiquitinationEWHQDYRKFRETTMY
HHHHHHHHHHHHHHH
42.4123503661
877UbiquitinationDYRKFRETTMYLIIG
HHHHHHHHHHHHEEC
16.7729967540
882UbiquitinationRETTMYLIIGLENFQ
HHHHHHHEECCCHHC
0.9829967540
905UbiquitinationLFLICAYQNNKELLS
HHHHHHHHCCHHHHH
28.6123503661
905 (in isoform 1)Ubiquitination-28.61-
912PhosphorylationQNNKELLSKGLYRGH
HCCHHHHHCCCCCCC
36.98-
915UbiquitinationKELLSKGLYRGHDEE
HHHHHCCCCCCCCHH
2.7929967540
916PhosphorylationELLSKGLYRGHDEEL
HHHHCCCCCCCCHHH
24.1817924679
920UbiquitinationKGLYRGHDEELISHY
CCCCCCCCHHHHHHH
54.6229967540
933UbiquitinationHYRRECLLKLNEQAA
HHHHHHHHHHHHHHH
10.0423503661
943UbiquitinationNEQAAELFESGEDRE
HHHHHHHHHCCCCCC
5.4523503661
948PhosphorylationELFESGEDREVNNGL
HHHHCCCCCCCCCCE
56.4117924679
1006PhosphorylationPHLQEKLTDFLPKLL
HHHHHHHHHHHHHHH
35.4522210691
1011UbiquitinationKLTDFLPKLLDCSME
HHHHHHHHHHHCCCH
64.9229967540
1043UbiquitinationLCERFARIMLSLSRT
HHHHHHHHHHHHHCC
2.6729967540
1046PhosphorylationRFARIMLSLSRTPAD
HHHHHHHHHHCCCCC
13.6124719451
1048PhosphorylationARIMLSLSRTPADGR
HHHHHHHHCCCCCCC
30.6317081983
1081Ubiquitination---------------------------------
---------------------------------
29967540

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
680TPhosphorylationKinaseVRK2Q86Y07
PSP
727TPhosphorylationKinaseVRK2Q86Y07
PSP
745SPhosphorylationKinaseVRK2Q86Y07
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP25_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 UBP25_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANXA1_HUMANANXA1physical
19615732
LYSC_HUMANLYZphysical
19615732
MYO6_HUMANMYO6physical
19615732
NEDD8_HUMANNEDD8physical
19615732
PIP_HUMANPIPphysical
19615732
KLHL9_HUMANKLHL9physical
19615732
WRIP1_HUMANWRNIP1physical
19615732
UBP28_HUMANUSP28physical
19615732
BACD3_HUMANKCTD10physical
19615732
BTBD9_HUMANBTBD9physical
19615732
ZG16B_HUMANZG16Bphysical
19615732
BACD1_HUMANKCTD13physical
19615732
MT2_HUMANMT2Aphysical
16501887
G3P_HUMANGAPDHphysical
16501887
MYPC1_HUMANMYBPC1physical
16501887
ACTS_HUMANACTA1physical
16501887
FLNC_HUMANFLNCphysical
16501887
UBP25_HUMANUSP25physical
19440361
KSYK_HUMANSYKphysical
19909739
SUMO1_HUMANSUMO1physical
18538659
SUMO3_HUMANSUMO3physical
18538659
SUMO2_HUMANSUMO2physical
18538659
UBC_HUMANUBCphysical
22195557
K1468_HUMANKIAA1468physical
22863883
UBC_HUMANUBCphysical
18538659
ZN426_HUMANZNF426physical
25416956
A4_HUMANAPPphysical
25740315
KSYK_HUMANSYKphysical
21516116
BACD1_HUMANKCTD13physical
28514442
BACD2_HUMANTNFAIP1physical
28514442
BTBD9_HUMANBTBD9physical
28514442
UBB_HUMANUBBphysical
28514442
BACD3_HUMANKCTD10physical
28514442
UBP28_HUMANUSP28physical
28514442
APBP2_HUMANAPPBP2physical
28514442
SUMO1_HUMANSUMO1physical
28538147
UBC_HUMANUBCphysical
28538147
UBC_HUMANUBCphysical
29131570
UBC_HUMANUBCphysical
28327663

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 UBP25_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-916, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"The UBA-UIM domains of the USP25 regulate the enzyme ubiquitinationstate and modulate substrate recognition.";
Denuc A., Bosch-Comas A., Gonzalez-Duarte R., Marfany G.;
PLoS ONE 4:E5571-E5571(2009).
Cited for: UBIQUITINATION AT LYS-99, DEUBIQUITINATION, ACTIVE SITE AT CYS-178,ACETYLATION, PHOSPHORYLATION, SUMOYLATION, FUNCTION, SUBCELLULARLOCATION, SUBUNIT, AND MUTAGENESIS OF LYS-99 AND CYS-178.
"Mechanism and consequences for paralog-specific sumoylation ofubiquitin-specific protease 25.";
Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.;
Mol. Cell 30:610-619(2008).
Cited for: SUMOYLATION AT LYS-99, FUNCTION, INTERACTION WITH SUMO1; SUMO3 ANDUBIQUITIN, MASS SPECTROMETRY, AND MUTAGENESIS OF VAL-91; ILE-92 ANDLYS-99.

TOP