PRS7_HUMAN - dbPTM
PRS7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRS7_HUMAN
UniProt AC P35998
Protein Name 26S proteasome regulatory subunit 7
Gene Name PSMC2
Organism Homo sapiens (Human).
Sequence Length 433
Subcellular Localization Cytoplasm . Colocalizes with TRIM5 in cytoplasmic bodies.
Protein Description Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC2 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides..
Protein Sequence MPDYLGADQRKTKEDEKDDKPIRALDEGDIALLKTYGQSTYSRQIKQVEDDIQQLLKKINELTGIKESDTGLAPPALWDLAADKQTLQSEQPLQVARCTKIINADSEDPKYIINVKQFAKFVVDLSDQVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTVTMMQVEEKPDVTYSDVGGCKEQIEKLREVVETPLLHPERFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKIEFSLPDLEGRTHIFKIHARSMSVERDIRFELLARLCPNSTGAEIRSVCTEAGMFAIRARRKIATEKDFLEAVNKVIKSYAKFSATPRYMTYN
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
4Nitration----MPDYLGADQRK
----CCCCCCCCCCC
10.93-
4Phosphorylation----MPDYLGADQRK
----CCCCCCCCCCC
10.9319664994
9UbiquitinationPDYLGADQRKTKEDE
CCCCCCCCCCCCCCC
48.51-
11UbiquitinationYLGADQRKTKEDEKD
CCCCCCCCCCCCCCC
59.3121906983
13UbiquitinationGADQRKTKEDEKDDK
CCCCCCCCCCCCCCC
67.2321906983
17UbiquitinationRKTKEDEKDDKPIRA
CCCCCCCCCCCCCCC
81.3021906983
20UbiquitinationKEDEKDDKPIRALDE
CCCCCCCCCCCCCCH
53.1021906983
34UbiquitinationEGDIALLKTYGQSTY
HHCEEEEEHHCCCHH
40.3221890473
34UbiquitinationEGDIALLKTYGQSTY
HHCEEEEEHHCCCHH
40.3221890473
34AcetylationEGDIALLKTYGQSTY
HHCEEEEEHHCCCHH
40.3223236377
34UbiquitinationEGDIALLKTYGQSTY
HHCEEEEEHHCCCHH
40.3221906983
34UbiquitinationEGDIALLKTYGQSTY
HHCEEEEEHHCCCHH
40.3221890473
35PhosphorylationGDIALLKTYGQSTYS
HCEEEEEHHCCCHHH
32.6228152594
36PhosphorylationDIALLKTYGQSTYSR
CEEEEEHHCCCHHHH
16.1628152594
39PhosphorylationLLKTYGQSTYSRQIK
EEEHHCCCHHHHHHH
25.5829496907
44UbiquitinationGQSTYSRQIKQVEDD
CCCHHHHHHHHHHHH
41.09-
46UbiquitinationSTYSRQIKQVEDDIQ
CHHHHHHHHHHHHHH
39.7021890473
46UbiquitinationSTYSRQIKQVEDDIQ
CHHHHHHHHHHHHHH
39.7021890473
46UbiquitinationSTYSRQIKQVEDDIQ
CHHHHHHHHHHHHHH
39.7021906983
46UbiquitinationSTYSRQIKQVEDDIQ
CHHHHHHHHHHHHHH
39.7021890473
49UbiquitinationSRQIKQVEDDIQQLL
HHHHHHHHHHHHHHH
47.69-
57UbiquitinationDDIQQLLKKINELTG
HHHHHHHHHHHHHHC
61.2721890473
57UbiquitinationDDIQQLLKKINELTG
HHHHHHHHHHHHHHC
61.2721890473
57UbiquitinationDDIQQLLKKINELTG
HHHHHHHHHHHHHHC
61.2721906983
57UbiquitinationDDIQQLLKKINELTG
HHHHHHHHHHHHHHC
61.2721890473
58MalonylationDIQQLLKKINELTGI
HHHHHHHHHHHHHCC
51.2226320211
58UbiquitinationDIQQLLKKINELTGI
HHHHHHHHHHHHHCC
51.2221906983
63PhosphorylationLKKINELTGIKESDT
HHHHHHHHCCCHHCC
30.5920068231
66UbiquitinationINELTGIKESDTGLA
HHHHHCCCHHCCCCC
53.1321906983
73UbiquitinationKESDTGLAPPALWDL
CHHCCCCCCHHHHHH
14.91-
84UbiquitinationLWDLAADKQTLQSEQ
HHHHHHCHHCCCCCC
40.2221890473
84UbiquitinationLWDLAADKQTLQSEQ
HHHHHHCHHCCCCCC
40.2221890473
84UbiquitinationLWDLAADKQTLQSEQ
HHHHHHCHHCCCCCC
40.2221906983
84UbiquitinationLWDLAADKQTLQSEQ
HHHHHHCHHCCCCCC
40.2221890473
85UbiquitinationWDLAADKQTLQSEQP
HHHHHCHHCCCCCCC
48.25-
100AcetylationLQVARCTKIINADSE
HHHHEEEEEEECCCC
45.2626051181
100UbiquitinationLQVARCTKIINADSE
HHHHEEEEEEECCCC
45.2621906983
106PhosphorylationTKIINADSEDPKYII
EEEEECCCCCCCEEE
41.3029214152
110UbiquitinationNADSEDPKYIINVKQ
ECCCCCCCEEEEHHH
62.4921890473
110UbiquitinationNADSEDPKYIINVKQ
ECCCCCCCEEEEHHH
62.4921890473
110AcetylationNADSEDPKYIINVKQ
ECCCCCCCEEEEHHH
62.4927452117
110UbiquitinationNADSEDPKYIINVKQ
ECCCCCCCEEEEHHH
62.4921906983
110UbiquitinationNADSEDPKYIINVKQ
ECCCCCCCEEEEHHH
62.4921890473
111UbiquitinationADSEDPKYIINVKQF
CCCCCCCEEEEHHHH
16.66-
111PhosphorylationADSEDPKYIINVKQF
CCCCCCCEEEEHHHH
16.6628152594
116UbiquitinationPKYIINVKQFAKFVV
CCEEEEHHHHHHHHE
34.9021890473
116UbiquitinationPKYIINVKQFAKFVV
CCEEEEHHHHHHHHE
34.9021890473
116AcetylationPKYIINVKQFAKFVV
CCEEEEHHHHHHHHE
34.9019608861
116SuccinylationPKYIINVKQFAKFVV
CCEEEEHHHHHHHHE
34.9023954790
116UbiquitinationPKYIINVKQFAKFVV
CCEEEEHHHHHHHHE
34.9021890473
116UbiquitinationPKYIINVKQFAKFVV
CCEEEEHHHHHHHHE
34.9021890473
120UbiquitinationINVKQFAKFVVDLSD
EEHHHHHHHHEECCC
39.7221906983
130UbiquitinationVDLSDQVAPTDIEEG
EECCCCCCCCCHHHC
8.81-
131UbiquitinationDLSDQVAPTDIEEGM
ECCCCCCCCCHHHCC
31.57-
132PhosphorylationLSDQVAPTDIEEGMR
CCCCCCCCCHHHCCE
39.61-
138SulfoxidationPTDIEEGMRVGVDRN
CCCHHHCCEECCCCC
3.3821406390
146UbiquitinationRVGVDRNKYQIHIPL
EECCCCCCEEEECCC
39.1521890473
146UbiquitinationRVGVDRNKYQIHIPL
EECCCCCCEEEECCC
39.1521890473
146UbiquitinationRVGVDRNKYQIHIPL
EECCCCCCEEEECCC
39.1521906983
146UbiquitinationRVGVDRNKYQIHIPL
EECCCCCCEEEECCC
39.1521890473
147PhosphorylationVGVDRNKYQIHIPLP
ECCCCCCEEEECCCC
19.0927642862
156UbiquitinationIHIPLPPKIDPTVTM
EECCCCCCCCCCEEE
58.77-
160PhosphorylationLPPKIDPTVTMMQVE
CCCCCCCCEEEEEEE
25.5120860994
163SulfoxidationKIDPTVTMMQVEEKP
CCCCCEEEEEEEECC
1.2128465586
164SulfoxidationIDPTVTMMQVEEKPD
CCCCEEEEEEEECCC
2.7028465586
169AcetylationTMMQVEEKPDVTYSD
EEEEEEECCCCCHHH
32.7726051181
169UbiquitinationTMMQVEEKPDVTYSD
EEEEEEECCCCCHHH
32.77-
173PhosphorylationVEEKPDVTYSDVGGC
EEECCCCCHHHCCCH
25.3729978859
174PhosphorylationEEKPDVTYSDVGGCK
EECCCCCHHHCCCHH
11.6129978859
175PhosphorylationEKPDVTYSDVGGCKE
ECCCCCHHHCCCHHH
19.2229978859
179UbiquitinationVTYSDVGGCKEQIEK
CCHHHCCCHHHHHHH
21.12-
181UbiquitinationYSDVGGCKEQIEKLR
HHHCCCHHHHHHHHH
56.80-
186UbiquitinationGCKEQIEKLREVVET
CHHHHHHHHHHHHHC
55.24-
193PhosphorylationKLREVVETPLLHPER
HHHHHHHCCCCCHHH
13.97-
203UbiquitinationLHPERFVNLGIEPPK
CCHHHHHCCCCCCCC
29.82-
210UbiquitinationNLGIEPPKGVLLFGP
CCCCCCCCEEEEECC
72.8221890473
210UbiquitinationNLGIEPPKGVLLFGP
CCCCCCCCEEEEECC
72.8221890473
210UbiquitinationNLGIEPPKGVLLFGP
CCCCCCCCEEEEECC
72.8221906983
210UbiquitinationNLGIEPPKGVLLFGP
CCCCCCCCEEEEECC
72.8221890473
219UbiquitinationVLLFGPPGTGKTLCA
EEEECCCCCCHHHHH
50.67-
222AcetylationFGPPGTGKTLCARAV
ECCCCCCHHHHHHHH
37.8625953088
222UbiquitinationFGPPGTGKTLCARAV
ECCCCCCHHHHHHHH
37.8620639865
236GlutathionylationVANRTDACFIRVIGS
HHCCCCCEEEEHHCH
3.0322555962
243PhosphorylationCFIRVIGSELVQKYV
EEEEHHCHHHHHHHH
19.34-
248UbiquitinationIGSELVQKYVGEGAR
HCHHHHHHHHHHHHH
34.1321890473
248UbiquitinationIGSELVQKYVGEGAR
HCHHHHHHHHHHHHH
34.1321890473
248AcetylationIGSELVQKYVGEGAR
HCHHHHHHHHHHHHH
34.1326051181
248UbiquitinationIGSELVQKYVGEGAR
HCHHHHHHHHHHHHH
34.1321906983
248UbiquitinationIGSELVQKYVGEGAR
HCHHHHHHHHHHHHH
34.1321890473
249PhosphorylationGSELVQKYVGEGARM
CHHHHHHHHHHHHHH
9.1521406692
263SulfoxidationMVRELFEMARTKKAC
HHHHHHHHHHHCCEE
2.1021406390
265UbiquitinationRELFEMARTKKACLI
HHHHHHHHHCCEEEE
45.85-
267UbiquitinationLFEMARTKKACLIFF
HHHHHHHCCEEEEEE
32.59-
268UbiquitinationFEMARTKKACLIFFD
HHHHHHCCEEEEEEC
43.6621890473
270UbiquitinationMARTKKACLIFFDEI
HHHHCCEEEEEECCC
4.04-
278UbiquitinationLIFFDEIDAIGGARF
EEEECCCCCCCCCCC
30.04-
281UbiquitinationFDEIDAIGGARFDDG
ECCCCCCCCCCCCCC
25.98-
285AcetylationDAIGGARFDDGAGGD
CCCCCCCCCCCCCCC
11.28-
285UbiquitinationDAIGGARFDDGAGGD
CCCCCCCCCCCCCCC
11.28-
316SumoylationFDPRGNIKVLMATNR
CCCCCCEEEEEECCC
33.06-
316UbiquitinationFDPRGNIKVLMATNR
CCCCCCEEEEEECCC
33.0621906983
340AcetylationRPGRLDRKIEFSLPD
CCCCCCCEEEEECCC
46.3726051181
340UbiquitinationRPGRLDRKIEFSLPD
CCCCCCCEEEEECCC
46.3721906983
356UbiquitinationEGRTHIFKIHARSMS
CCCEEEEEEEECCCC
32.7421890473
356UbiquitinationEGRTHIFKIHARSMS
CCCEEEEEEEECCCC
32.7421890473
356AcetylationEGRTHIFKIHARSMS
CCCEEEEEEEECCCC
32.7425953088
356UbiquitinationEGRTHIFKIHARSMS
CCCEEEEEEEECCCC
32.7421906983
356UbiquitinationEGRTHIFKIHARSMS
CCCEEEEEEEECCCC
32.7421890473
361PhosphorylationIFKIHARSMSVERDI
EEEEEECCCCCCHHH
19.0527251275
363PhosphorylationKIHARSMSVERDIRF
EEEECCCCCCHHHHH
23.2924719451
389GlutathionylationGAEIRSVCTEAGMFA
CHHHHHHHHHHHHHH
2.7622555962
389S-nitrosylationGAEIRSVCTEAGMFA
CHHHHHHHHHHHHHH
2.762212679
394SulfoxidationSVCTEAGMFAIRARR
HHHHHHHHHHHHHHH
2.3621406390
402UbiquitinationFAIRARRKIATEKDF
HHHHHHHHCCCHHHH
31.0121906983
405PhosphorylationRARRKIATEKDFLEA
HHHHHCCCHHHHHHH
47.22-
407UbiquitinationRRKIATEKDFLEAVN
HHHCCCHHHHHHHHH
49.8021890473
407UbiquitinationRRKIATEKDFLEAVN
HHHCCCHHHHHHHHH
49.8021890473
407AcetylationRRKIATEKDFLEAVN
HHHCCCHHHHHHHHH
49.8025953088
407UbiquitinationRRKIATEKDFLEAVN
HHHCCCHHHHHHHHH
49.8021906983
407UbiquitinationRRKIATEKDFLEAVN
HHHCCCHHHHHHHHH
49.8021890473
415UbiquitinationDFLEAVNKVIKSYAK
HHHHHHHHHHHHHHC
38.4421890473
415UbiquitinationDFLEAVNKVIKSYAK
HHHHHHHHHHHHHHC
38.4421890473
415AcetylationDFLEAVNKVIKSYAK
HHHHHHHHHHHHHHC
38.4425953088
415UbiquitinationDFLEAVNKVIKSYAK
HHHHHHHHHHHHHHC
38.4421906983
415UbiquitinationDFLEAVNKVIKSYAK
HHHHHHHHHHHHHHC
38.4421890473
418UbiquitinationEAVNKVIKSYAKFSA
HHHHHHHHHHHCCCC
40.16-
422UbiquitinationKVIKSYAKFSATPRY
HHHHHHHCCCCCCCC
31.4521890473
422UbiquitinationKVIKSYAKFSATPRY
HHHHHHHCCCCCCCC
31.4521890473
422AcetylationKVIKSYAKFSATPRY
HHHHHHHCCCCCCCC
31.4519608861
422UbiquitinationKVIKSYAKFSATPRY
HHHHHHHCCCCCCCC
31.4521906983
422UbiquitinationKVIKSYAKFSATPRY
HHHHHHHCCCCCCCC
31.4521890473
424PhosphorylationIKSYAKFSATPRYMT
HHHHHCCCCCCCCCC
30.4428851738
426PhosphorylationSYAKFSATPRYMTYN
HHHCCCCCCCCCCCC
13.70-
428MethylationAKFSATPRYMTYN--
HCCCCCCCCCCCC--
29.51115492839
429PhosphorylationKFSATPRYMTYN---
CCCCCCCCCCCC---
8.6028851738
431PhosphorylationSATPRYMTYN-----
CCCCCCCCCC-----
15.8128851738
432PhosphorylationATPRYMTYN------
CCCCCCCCC------
11.4428851738

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 PRS7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRS7_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 PRS7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSMD5_HUMANPSMD5physical
16189514
PSMD5_HUMANPSMD5physical
10625621
NDC80_HUMANNDC80physical
9295362
PRS4_HUMANPSMC1physical
11361004
TBP_HUMANTBPphysical
11118327
TF2B_HUMANGTF2Bphysical
11118327
TF2H1_HUMANGTF2H1physical
11118327
T2FA_HUMANGTF2F1physical
11118327
C2TA_HUMANCIITAphysical
20351748
PSMD1_HUMANPSMD1physical
21767633
PSMD8_HUMANPSMD8physical
21767633
HSP74_HUMANHSPA4physical
21767633
PRS4_HUMANPSMC1physical
19490896
PRS6A_HUMANPSMC3physical
9464850
PRS8_HUMANPSMC5physical
9464850
PRS10_HUMANPSMC6physical
9464850
PSMD2_HUMANPSMD2physical
20810900
PAAF1_HUMANPAAF1physical
15831487
PRS4_HUMANPSMC1physical
21628461
PRS6B_HUMANPSMC4physical
21628461
PRS6A_HUMANPSMC3physical
21628461
PRS8_HUMANPSMC5physical
21628461
PSMD8_HUMANPSMD8physical
21628461
PSMD4_HUMANPSMD4physical
21628461
PSB5_HUMANPSMB5physical
21628461
PSMD6_HUMANPSMD6physical
22275368
PSMD8_HUMANPSMD8physical
22275368
PSMD2_HUMANPSMD2physical
22275368
PRS7_HUMANPSMC2physical
22275368
PRS8_HUMANPSMC5physical
22275368
PRS6A_HUMANPSMC3physical
22275368
SQSTM_HUMANSQSTM1physical
15340068
PRS4_HUMANPSMC1physical
22921402
PSMD2_HUMANPSMD2physical
22921402
PSMD4_HUMANPSMD4physical
22921402
PSMD5_HUMANPSMD5physical
22921402
PRS7_HUMANPSMC2physical
15782218
PSMD5_HUMANPSMD5physical
22939629
PSD13_HUMANPSMD13physical
22939629
PSMD7_HUMANPSMD7physical
22939629
PSMD2_HUMANPSMD2physical
22939629
PRS8_HUMANPSMC5physical
22939629
PSD10_HUMANPSMD10physical
22939629
PSDE_HUMANPSMD14physical
22939629
PSMD6_HUMANPSMD6physical
22939629
PSD11_HUMANPSMD11physical
22939629
PSD12_HUMANPSMD12physical
22939629
PSMD1_HUMANPSMD1physical
22939629
PSMD3_HUMANPSMD3physical
22939629
PSMD8_HUMANPSMD8physical
22939629
PSMD4_HUMANPSMD4physical
22939629
PSA3_HUMANPSMA3physical
22939629
PSA6_HUMANPSMA6physical
22939629
PSA7_HUMANPSMA7physical
22939629
PSB5_HUMANPSMB5physical
22939629
PSA5_HUMANPSMA5physical
22939629
PSB7_HUMANPSMB7physical
22939629
PSA2_HUMANPSMA2physical
22939629
PSB1_HUMANPSMB1physical
22939629
PSA4_HUMANPSMA4physical
22939629
PSB2_HUMANPSMB2physical
22939629
PSB3_HUMANPSMB3physical
22939629
PSA1_HUMANPSMA1physical
22939629
PSB6_HUMANPSMB6physical
22939629
PSME2_HUMANPSME2physical
22939629
PSME1_HUMANPSME1physical
22939629
PSB4_HUMANPSMB4physical
22939629
PSME3_HUMANPSME3physical
22939629
UCHL5_HUMANUCHL5physical
22939629
PSA7L_HUMANPSMA8physical
22939629
PSB8_HUMANPSMB8physical
22939629
RD23B_HUMANRAD23Bphysical
22939629
UBQL1_HUMANUBQLN1physical
22939629
XPO1_HUMANXPO1physical
22939629
TCPQ_HUMANCCT8physical
22939629
SC23A_HUMANSEC23Aphysical
22939629
ZCHC8_HUMANZCCHC8physical
22939629
TBB5_HUMANTUBBphysical
22939629
UFC1_HUMANUFC1physical
22939629
YBOX1_HUMANYBX1physical
22939629
U520_HUMANSNRNP200physical
22939629
PYR1_HUMANCADphysical
22939629
RT16_HUMANMRPS16physical
22939629
VP26A_HUMANVPS26Aphysical
22939629
TPM4_HUMANTPM4physical
22939629
PCD10_HUMANPCDH10physical
23260144
ADRM1_HUMANADRM1physical
22863883
CLIP1_HUMANCLIP1physical
22863883
PRS4_HUMANPSMC1physical
22863883
PSMD3_HUMANPSMD3physical
22863883
PSMD4_HUMANPSMD4physical
22863883
PSMD6_HUMANPSMD6physical
22863883
PSMD7_HUMANPSMD7physical
22863883
PSMD5_HUMANPSMD5physical
25416956
UBC_HUMANUBCphysical
24743594
NEUL4_HUMANNEURL4physical
26186194
SMC1A_HUMANSMC1Aphysical
26186194
SMC3_HUMANSMC3physical
26186194
PRS4_HUMANPSMC1physical
26186194
PSD10_HUMANPSMD10physical
26186194
MTMR1_HUMANMTMR1physical
26186194
CX7A2_HUMANCOX7A2physical
26186194
RAD21_HUMANRAD21physical
26186194
ADRM1_HUMANADRM1physical
26344197
PYR1_HUMANCADphysical
26344197
TCPB_HUMANCCT2physical
26344197
TCPG_HUMANCCT3physical
26344197
DNJA1_HUMANDNAJA1physical
26344197
DNJA4_HUMANDNAJA4physical
26344197
GFPT1_HUMANGFPT1physical
26344197
MCFD2_HUMANMCFD2physical
26344197
NFS1_HUMANNFS1physical
26344197
PSA1_HUMANPSMA1physical
26344197
PSA2_HUMANPSMA2physical
26344197
PSA4_HUMANPSMA4physical
26344197
PSB2_HUMANPSMB2physical
26344197
PSB4_HUMANPSMB4physical
26344197
PSB5_HUMANPSMB5physical
26344197
PSB8_HUMANPSMB8physical
26344197
PRS4_HUMANPSMC1physical
26344197
PRS6A_HUMANPSMC3physical
26344197
PRS6B_HUMANPSMC4physical
26344197
PRS8_HUMANPSMC5physical
26344197
PRS10_HUMANPSMC6physical
26344197
PSD11_HUMANPSMD11physical
26344197
PSD12_HUMANPSMD12physical
26344197
PSD13_HUMANPSMD13physical
26344197
PSDE_HUMANPSMD14physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD6_HUMANPSMD6physical
26344197
PSMD7_HUMANPSMD7physical
26344197
RD23A_HUMANRAD23Aphysical
26344197
RD23B_HUMANRAD23Bphysical
26344197
RPN1_HUMANRPN1physical
26344197
SUCB1_HUMANSUCLA2physical
26344197
UBR2_HUMANUBR2physical
26344197
UBR5_HUMANUBR5physical
26344197
PSMD5_HUMANPSMD5physical
21516116
PSD12_HUMANPSMD12physical
28514442
RAD21_HUMANRAD21physical
28514442
PRS6B_HUMANPSMC4physical
28514442
SMC3_HUMANSMC3physical
28514442
PRS4_HUMANPSMC1physical
28514442
NEUL4_HUMANNEURL4physical
28514442
MTMR1_HUMANMTMR1physical
28514442
PRS6A_HUMANPSMC3physical
28514442
SMC1A_HUMANSMC1Aphysical
28514442
UBCP1_HUMANUBLCP1physical
28539385
PSMD2_HUMANPSMD2physical
28539385
PSMD4_HUMANPSMD4physical
28539385
PSMD5_HUMANPSMD5physical
28539385
PSMD9_HUMANPSMD9physical
28539385
PSD10_HUMANPSMD10physical
28539385
PAAF1_HUMANPAAF1physical
28539385

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 PRS7_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-116 AND LYS-422, AND MASSSPECTROMETRY.

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