PRS10_HUMAN - dbPTM
PRS10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRS10_HUMAN
UniProt AC P62333
Protein Name 26S proteasome regulatory subunit 10B
Gene Name PSMC6
Organism Homo sapiens (Human).
Sequence Length 389
Subcellular Localization Cytoplasm. Nucleus.
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. PSMC6 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 MADPRDKALQDYRKKLLEHKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVADSKKLESKLDYKPV
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------MADPRDKAL
------CCCHHHHHH		35.20-
7Ubiquitination-MADPRDKALQDYRK
-CCCHHHHHHHHHHH		52.8821906983
7Acetylation-MADPRDKALQDYRK
-CCCHHHHHHHHHHH		52.8825953088
15AcetylationALQDYRKKLLEHKEI
HHHHHHHHHHHCHHH		49.6788589
15UbiquitinationALQDYRKKLLEHKEI
HHHHHHHHHHHCHHH		49.67-
20AcetylationRKKLLEHKEIDGRLK
HHHHHHCHHHHHHHH		47.1719608861
20UbiquitinationRKKLLEHKEIDGRLK
HHHHHHCHHHHHHHH		47.1721906983
29UbiquitinationIDGRLKELREQLKEL
HHHHHHHHHHHHHHH		7.54-
34UbiquitinationKELREQLKELTKQYE
HHHHHHHHHHHHHHH		50.8221906983
34AcetylationKELREQLKELTKQYE
HHHHHHHHHHHHHHH		50.8219608861
38UbiquitinationEQLKELTKQYEKSEN
HHHHHHHHHHHHCHH		64.60-
41UbiquitinationKELTKQYEKSENDLK
HHHHHHHHHCHHHHH		47.84-
42UbiquitinationELTKQYEKSENDLKA
HHHHHHHHCHHHHHH		59.12-
48UbiquitinationEKSENDLKALQSVGQ
HHCHHHHHHHHHHHH		50.3321906983
52UbiquitinationNDLKALQSVGQIVGE
HHHHHHHHHHHHHHH		29.12-
52PhosphorylationNDLKALQSVGQIVGE
HHHHHHHHHHHHHHH		29.1220068231
62UbiquitinationQIVGEVLKQLTEEKF
HHHHHHHHHHCCCCE		48.73-
66PhosphorylationEVLKQLTEEKFIVKA
HHHHHHCCCCEEEEC		68.7120068231
68AcetylationLKQLTEEKFIVKATN
HHHHCCCCEEEECCC		33.8723236377
72UbiquitinationTEEKFIVKATNGPRY
CCCCEEEECCCCCEE		44.68-
72MalonylationTEEKFIVKATNGPRY
CCCCEEEECCCCCEE		44.6826320211
72AcetylationTEEKFIVKATNGPRY
CCCCEEEECCCCCEE		44.6819608861
76UbiquitinationFIVKATNGPRYVVGC
EEEECCCCCEEEEEE		12.05-
82UbiquitinationNGPRYVVGCRRQLDK
CCCEEEEEECHHCCH		6.81-
86UbiquitinationYVVGCRRQLDKSKLK
EEEEECHHCCHHHCC		34.3619608861
86AcetylationYVVGCRRQLDKSKLK
EEEEECHHCCHHHCC		34.3619608861
91UbiquitinationRRQLDKSKLKPGTRV
CHHCCHHHCCCCCEE		67.29-
93SumoylationQLDKSKLKPGTRVAL
HCCHHHCCCCCEEEE		45.17-
96PhosphorylationKSKLKPGTRVALDMT
HHHCCCCCEEEEECC		30.4224043423
102SulfoxidationGTRVALDMTTLTIMR
CCEEEEECCHHHHHH		2.9921406390
103PhosphorylationTRVALDMTTLTIMRY
CEEEEECCHHHHHHH		20.5120860994
104PhosphorylationRVALDMTTLTIMRYL
EEEEECCHHHHHHHC		18.4420860994
106PhosphorylationALDMTTLTIMRYLPR
EEECCHHHHHHHCCC		15.6120860994
117PhosphorylationYLPREVDPLVYNMSH
HCCCCCCCCEECCCC		28.97-
118PhosphorylationLPREVDPLVYNMSHE
CCCCCCCCEECCCCC		5.74-
120PhosphorylationREVDPLVYNMSHEDP
CCCCCCEECCCCCCC		16.9030624053
122SulfoxidationVDPLVYNMSHEDPGN
CCCCEECCCCCCCCC		2.0730846556
123PhosphorylationDPLVYNMSHEDPGNV
CCCEECCCCCCCCCC		21.7830624053
131PhosphorylationHEDPGNVSYSEIGGL
CCCCCCCCHHHCCCH		27.2630576142
132PhosphorylationEDPGNVSYSEIGGLS
CCCCCCCHHHCCCHH		13.1630624053
133PhosphorylationDPGNVSYSEIGGLSE
CCCCCCHHHCCCHHH		18.4130624053
145PhosphorylationLSEQIRELREVIELP
HHHHHHHHHHHHCCC		3.98-
168UbiquitinationRVGIIPPKGCLLYGP
HCCEECCCCEEEECC		57.8321906983
173PhosphorylationPPKGCLLYGPPGTGK
CCCCEEEECCCCCCH		18.0320090780
178PhosphorylationLLYGPPGTGKTLLAR
EEECCCCCCHHHHHH		41.0828152594
180UbiquitinationYGPPGTGKTLLARAV
ECCCCCCHHHHHHHH		35.5221906983
181PhosphorylationGPPGTGKTLLARAVA
CCCCCCHHHHHHHHH		28.48-
182UbiquitinationPPGTGKTLLARAVAS
CCCCCHHHHHHHHHH		3.92-
187PhosphorylationKTLLARAVASQLDCN
HHHHHHHHHHHCCCC		4.37-
189PhosphorylationLLARAVASQLDCNFL
HHHHHHHHHCCCCHH		25.3630622161
193S-nitrosylationAVASQLDCNFLKVVS
HHHHHCCCCHHHHHC		5.4319483679
193GlutathionylationAVASQLDCNFLKVVS
HHHHHCCCCHHHHHC		5.4322555962
193S-nitrosocysteineAVASQLDCNFLKVVS
HHHHHCCCCHHHHHC		5.43-
194UbiquitinationVASQLDCNFLKVVSS
HHHHCCCCHHHHHCH		44.97-
197UbiquitinationQLDCNFLKVVSSSIV
HCCCCHHHHHCHHHH		36.1321906983
200PhosphorylationCNFLKVVSSSIVDKY
CCHHHHHCHHHHHHH		22.7326356563
201PhosphorylationNFLKVVSSSIVDKYI
CHHHHHCHHHHHHHH		16.6928152594
202PhosphorylationFLKVVSSSIVDKYIG
HHHHHCHHHHHHHHH		21.0828152594
206UbiquitinationVSSSIVDKYIGESAR
HCHHHHHHHHHHHHH		28.0721890473
206AcetylationVSSSIVDKYIGESAR
HCHHHHHHHHHHHHH		28.0719608861
206MalonylationVSSSIVDKYIGESAR
HCHHHHHHHHHHHHH		28.0726320211
207PhosphorylationSSSIVDKYIGESARL
CHHHHHHHHHHHHHH		15.0827273156
211PhosphorylationVDKYIGESARLIREM
HHHHHHHHHHHHHHH		17.3028152594
211UbiquitinationVDKYIGESARLIREM
HHHHHHHHHHHHHHH		17.30-
218SulfoxidationSARLIREMFNYARDH
HHHHHHHHHHHHHCC		1.5730846556
220UbiquitinationRLIREMFNYARDHQP
HHHHHHHHHHHCCCC		28.3919608861
220AcetylationRLIREMFNYARDHQP
HHHHHHHHHHHCCCC		28.3919608861
221PhosphorylationLIREMFNYARDHQPC
HHHHHHHHHHCCCCE		7.5518083107
228GlutathionylationYARDHQPCIIFMDEI
HHHCCCCEEEEECCC		2.7622555962
232SulfoxidationHQPCIIFMDEIDAIG
CCCEEEEECCCCCCC		2.9630846556
244PhosphorylationAIGGRRFSEGTSADR
CCCCCCCCCCCCHHH		33.0529255136
247PhosphorylationGRRFSEGTSADREIQ
CCCCCCCCCHHHHHH		19.3823403867
248PhosphorylationRRFSEGTSADREIQR
CCCCCCCCHHHHHHH		38.7423403867
258PhosphorylationREIQRTLMELLNQMD
HHHHHHHHHHHHHCC		3.1827251275
274UbiquitinationFDTLHRVKMIMATNR
CCHHHHHHHHHHCCC		23.7521906983
288UbiquitinationRPDTLDPALLRPGRL
CCCCCCHHHCCCCCC		20.92-
298UbiquitinationRPGRLDRKIHIDLPN
CCCCCCCEEECCCCC		38.0021906983
298SumoylationRPGRLDRKIHIDLPN
CCCCCCCEEECCCCC		38.00-
312UbiquitinationNEQARLDILKIHAGP
CHHHHCCEEEECCCC		5.10-
314AcetylationQARLDILKIHAGPIT
HHHCCEEEECCCCCC		32.5525953088
314UbiquitinationQARLDILKIHAGPIT
HHHCCEEEECCCCCC		32.55-
322UbiquitinationIHAGPITKHGEIDYE
ECCCCCCCCCCCCHH		50.7821906983
328UbiquitinationTKHGEIDYEAIVKLS
CCCCCCCHHHEEECC		16.96-
328PhosphorylationTKHGEIDYEAIVKLS
CCCCCCCHHHEEECC		16.9628152594
333UbiquitinationIDYEAIVKLSDGFNG
CCHHHEEECCCCCCH		35.84-
336UbiquitinationEAIVKLSDGFNGADL
HHEEECCCCCCHHHH		75.93-
342PhosphorylationSDGFNGADLRNVCTE
CCCCCHHHHHHHHHH		47.78-
347UbiquitinationGADLRNVCTEAGMFA
HHHHHHHHHHHHCEE		3.04-
347GlutathionylationGADLRNVCTEAGMFA
HHHHHHHHHHHHCEE		3.0422555962
352SulfoxidationNVCTEAGMFAIRADH
HHHHHHHCEEEECCC		2.3621406390
368SulfoxidationFVVQEDFMKAVRKVA
EECCHHHHHHHHHHH		4.1621406390
369UbiquitinationVVQEDFMKAVRKVAD
ECCHHHHHHHHHHHC		43.66-
383UbiquitinationDSKKLESKLDYKPV-
CHHHHHHHCCCCCC-		35.6821906983
386PhosphorylationKLESKLDYKPV----
HHHHHCCCCCC----		27.85-
397Ubiquitination---------------
---------------		-
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 PRS10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRS10_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 PRS10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
CA216_HUMANC1orf216physical
16189514
PSMD9_HUMANPSMD9physical
16189514
PRS6A_HUMANPSMC3physical
19490896
PAAF1_HUMANPAAF1physical
15831487
PSMD6_HUMANPSMD6physical
22275368
PSMD8_HUMANPSMD8physical
22275368
PRS10_HUMANPSMC6physical
15782218
PRS8_HUMANPSMC5physical
22939629
PSD13_HUMANPSMD13physical
22939629
PRS4_HUMANPSMC1physical
22939629
PRS6A_HUMANPSMC3physical
22939629
PRS7_HUMANPSMC2physical
22939629
PSD12_HUMANPSMD12physical
22939629
PSMD7_HUMANPSMD7physical
22939629
PSMD1_HUMANPSMD1physical
22939629
PSMD2_HUMANPSMD2physical
22939629
PSMD6_HUMANPSMD6physical
22939629
PSD10_HUMANPSMD10physical
22939629
PRS6B_HUMANPSMC4physical
22939629
PSD11_HUMANPSMD11physical
22939629
PSDE_HUMANPSMD14physical
22939629
PSMD8_HUMANPSMD8physical
22939629
PSMD4_HUMANPSMD4physical
22939629
PSMD3_HUMANPSMD3physical
22939629
PSA1_HUMANPSMA1physical
22939629
PSA6_HUMANPSMA6physical
22939629
PSA7_HUMANPSMA7physical
22939629
PSA5_HUMANPSMA5physical
22939629
PSA3_HUMANPSMA3physical
22939629
PSB1_HUMANPSMB1physical
22939629
PSB2_HUMANPSMB2physical
22939629
PSB3_HUMANPSMB3physical
22939629
PSB5_HUMANPSMB5physical
22939629
PSA4_HUMANPSMA4physical
22939629
PSB6_HUMANPSMB6physical
22939629
RD23B_HUMANRAD23Bphysical
22939629
UBP14_HUMANUSP14physical
22939629
PSA7L_HUMANPSMA8physical
22939629
UBE2C_HUMANUBE2Cphysical
22939629
RUVB1_HUMANRUVBL1physical
22939629
UFM1_HUMANUFM1physical
22939629
SEPT2_HUMANSEPT2physical
22939629
STIP1_HUMANSTIP1physical
22939629
ADRM1_HUMANADRM1physical
22863883
PRS4_HUMANPSMC1physical
22863883
PRS7_HUMANPSMC2physical
22863883
PSMD3_HUMANPSMD3physical
22863883
PSMD4_HUMANPSMD4physical
22863883
PRS10_HUMANPSMC6physical
25416956
PSMD9_HUMANPSMD9physical
25416956
SDCB1_HUMANSDCBPphysical
25416956
NB5R2_HUMANCYB5R2physical
25416956
CC146_HUMANCCDC146physical
25416956
ACACA_HUMANACACAphysical
26344197
BASP1_HUMANBASP1physical
26344197
DNJA4_HUMANDNAJA4physical
26344197
EF1A1_HUMANEEF1A1physical
26344197
ECM29_HUMANKIAA0368physical
26344197
MTCH1_HUMANMTCH1physical
26344197
PSA1_HUMANPSMA1physical
26344197
PSA2_HUMANPSMA2physical
26344197
PSA3_HUMANPSMA3physical
26344197
PSA5_HUMANPSMA5physical
26344197
PSA6_HUMANPSMA6physical
26344197
PSA7_HUMANPSMA7physical
26344197
PSB2_HUMANPSMB2physical
26344197
PSB3_HUMANPSMB3physical
26344197
PSB4_HUMANPSMB4physical
26344197
PSB5_HUMANPSMB5physical
26344197
PSB6_HUMANPSMB6physical
26344197
PSB7_HUMANPSMB7physical
26344197
PSB8_HUMANPSMB8physical
26344197
PRS4_HUMANPSMC1physical
26344197
PRS6A_HUMANPSMC3physical
26344197
PRS6B_HUMANPSMC4physical
26344197
PRS8_HUMANPSMC5physical
26344197
PSD10_HUMANPSMD10physical
26344197
PSD11_HUMANPSMD11physical
26344197
PSD13_HUMANPSMD13physical
26344197
PSDE_HUMANPSMD14physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD3_HUMANPSMD3physical
26344197
PSMD6_HUMANPSMD6physical
26344197
PSMD7_HUMANPSMD7physical
26344197
PSMD8_HUMANPSMD8physical
26344197
PSMD9_HUMANPSMD9physical
26344197
RD23B_HUMANRAD23Bphysical
26344197
RCC2_HUMANRCC2physical
26344197
RFC2_HUMANRFC2physical
26344197
S61A1_HUMANSEC61A1physical
26344197
UBP14_HUMANUSP14physical
26344197
PSMD9_HUMANPSMD9physical
21516116
INTU_HUMANINTUphysical
27173435
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 PRS10_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Mass spectrometric characterization of the affinity-purified human26S proteasome complex.";
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
Biochemistry 46:3553-3565(2007).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-20; LYS-72 AND LYS-206, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207, AND MASSSPECTROMETRY.

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