PSB5_HUMAN - dbPTM
PSB5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSB5_HUMAN
UniProt AC P28074
Protein Name Proteasome subunit beta type-5
Gene Name PSMB5
Organism Homo sapiens (Human).
Sequence Length 263
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity..
Protein Sequence MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP
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
84PhosphorylationSRATAGAYIASQTVK
CCCCCCHHHHCHHHH		8.9728152594
87PhosphorylationTAGAYIASQTVKKVI
CCCHHHHCHHHHHHH		19.4728152594
89PhosphorylationGAYIASQTVKKVIEI
CHHHHCHHHHHHHHC		31.6228152594
91UbiquitinationYIASQTVKKVIEINP
HHHCHHHHHHHHCCH		44.7221890473
91UbiquitinationYIASQTVKKVIEINP
HHHCHHHHHHHHCCH		44.7221890473
91AcetylationYIASQTVKKVIEINP
HHHCHHHHHHHHCCH		44.7225953088
91UbiquitinationYIASQTVKKVIEINP
HHHCHHHHHHHHCCH		44.7221890473
91MalonylationYIASQTVKKVIEINP
HHHCHHHHHHHHCCH		44.7226320211
912-HydroxyisobutyrylationYIASQTVKKVIEINP
HHHCHHHHHHHHCCH		44.72-
92UbiquitinationIASQTVKKVIEINPY
HHCHHHHHHHHCCHH		44.07-
99PhosphorylationKVIEINPYLLGTMAG
HHHHCCHHHHCCCCC		15.2920090780
134PhosphorylationLRNKERISVAAASKL
HCCCHHHHHHHHHHH		16.3622210691
139PhosphorylationRISVAAASKLLANMV
HHHHHHHHHHHHHHH		21.0720068231
140UbiquitinationISVAAASKLLANMVY
HHHHHHHHHHHHHHH		42.67-
147PhosphorylationKLLANMVYQYKGMGL
HHHHHHHHHCCCCCC		8.7129496907
149PhosphorylationLANMVYQYKGMGLSM
HHHHHHHCCCCCCCC		7.57-
158PhosphorylationGMGLSMGTMICGWDK
CCCCCCCCEECCCCC		8.50-
158 (in isoform 2)Phosphorylation-8.50-
165UbiquitinationTMICGWDKRGPGLYY
CEECCCCCCCCCEEE		53.39-
171PhosphorylationDKRGPGLYYVDSEGN
CCCCCCEEEECCCCC		13.8320090780
172PhosphorylationKRGPGLYYVDSEGNR
CCCCCEEEECCCCCE		11.6528152594
175PhosphorylationPGLYYVDSEGNRISG
CCEEEECCCCCEEEC		37.0428152594
179 (in isoform 2)Phosphorylation-34.9920068231
181PhosphorylationDSEGNRISGATFSVG
CCCCCEEECEEEEEC		21.0927251275
184PhosphorylationGNRISGATFSVGSGS
CCEEECEEEEECCCE		21.7027251275
186PhosphorylationRISGATFSVGSGSVY
EEECEEEEECCCEEE		22.6323090842
189PhosphorylationGATFSVGSGSVYAYG
CEEEEECCCEEEEEE		26.2423090842
191PhosphorylationTFSVGSGSVYAYGVM
EEEECCCEEEEEEEE		17.4123090842
193PhosphorylationSVGSGSVYAYGVMDR
EECCCEEEEEEEECC		8.8723090842
195PhosphorylationGSGSVYAYGVMDRGY
CCCEEEEEEEECCCC		7.8023090842
202PhosphorylationYGVMDRGYSYDLEVE
EEEECCCCCEEEEHH		12.6428152594
203PhosphorylationGVMDRGYSYDLEVEQ
EEECCCCCEEEEHHH		18.2628152594
204PhosphorylationVMDRGYSYDLEVEQA
EECCCCCEEEEHHHH		18.9628152594
212PhosphorylationDLEVEQAYDLARRAI
EEEHHHHHHHHHHHH		15.93-
220PhosphorylationDLARRAIYQATYRDA
HHHHHHHHHHHHCCH		7.3628152594
223PhosphorylationRRAIYQATYRDAYSG
HHHHHHHHHCCHHCC		11.9928152594
224PhosphorylationRAIYQATYRDAYSGG
HHHHHHHHCCHHCCC		14.9828152594
228PhosphorylationQATYRDAYSGGAVNL
HHHHCCHHCCCCEEE		16.4928152594
229PhosphorylationATYRDAYSGGAVNLY
HHHCCHHCCCCEEEE		32.2628152594
236PhosphorylationSGGAVNLYHVREDGW
CCCCEEEEEECCCCE		7.9628152594
247PhosphorylationEDGWIRVSSDNVADL
CCCEEEECCCCCHHH		23.3328857561
248PhosphorylationDGWIRVSSDNVADLH
CCEEEECCCCCHHHH		30.2828857561
257AcetylationNVADLHEKYSGSTP-
CCHHHHHHHCCCCC-		33.6923954790
257UbiquitinationNVADLHEKYSGSTP-
CCHHHHHHHCCCCC-		33.692190698
258PhosphorylationVADLHEKYSGSTP--
CHHHHHHHCCCCC--		18.4523927012
259PhosphorylationADLHEKYSGSTP---
HHHHHHHCCCCC---		37.0223927012
261PhosphorylationLHEKYSGSTP-----
HHHHHCCCCC-----		31.4028985074
262PhosphorylationHEKYSGSTP------
HHHHCCCCC------		36.2223401153
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 PSB5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSB5_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 PSB5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSA1_HUMANPSMA1physical
14733938
PSA2_HUMANPSMA2physical
14733938
PSA3_HUMANPSMA3physical
14733938
PSB3_HUMANPSMB3physical
14733938
PSB7_HUMANPSMB7physical
14733938
POMP_HUMANPOMPphysical
14733938
PSA2_HUMANPSMA2physical
20980621
POMP_HUMANPOMPphysical
20980621
RND1_HUMANRND1physical
20980621
POMP_HUMANPOMPphysical
15944226
PSB1_HUMANPSMB1physical
17948026
PSB3_HUMANPSMB3physical
17948026
PSB4_HUMANPSMB4physical
17948026
PSB6_HUMANPSMB6physical
17948026
PSB7_HUMANPSMB7physical
17948026
PSA3_HUMANPSMA3physical
17948026
POMP_HUMANPOMPphysical
17948026
PSB7_HUMANPSMB7physical
22939629
PSMD6_HUMANPSMD6physical
22939629
PSB6_HUMANPSMB6physical
22939629
PSD12_HUMANPSMD12physical
22939629
PSD13_HUMANPSMD13physical
22939629
PSMD7_HUMANPSMD7physical
22939629
PSMD1_HUMANPSMD1physical
22939629
PSMD3_HUMANPSMD3physical
22939629
PSB8_HUMANPSMB8physical
22939629
PSD11_HUMANPSMD11physical
22939629
PSMD2_HUMANPSMD2physical
22939629
PSMD4_HUMANPSMD4physical
22939629
PSMD8_HUMANPSMD8physical
22939629
PSME2_HUMANPSME2physical
22939629
PSMD5_HUMANPSMD5physical
22939629
PSB9_HUMANPSMB9physical
22939629
RU2A_HUMANSNRPA1physical
22939629
VIME_HUMANVIMphysical
22939629
YBOX1_HUMANYBX1physical
22939629
ICAL_HUMANCASTphysical
22863883
PSA5_HUMANPSMA5physical
22863883
PSB2_HUMANPSMB2physical
22863883
P5CR3_HUMANPYCRLphysical
22863883
ACTN2_HUMANACTN2physical
26344197
ACTN4_HUMANACTN4physical
26344197
ASNA_HUMANASNA1physical
26344197
CPSF2_HUMANCPSF2physical
26344197
ELP6_HUMANELP6physical
26344197
HS105_HUMANHSPH1physical
26344197
PSA3_HUMANPSMA3physical
26344197
PSA4_HUMANPSMA4physical
26344197
PSB2_HUMANPSMB2physical
26344197
PSB3_HUMANPSMB3physical
26344197
PSB6_HUMANPSMB6physical
26344197
PRS8_HUMANPSMC5physical
26344197
PSD11_HUMANPSMD11physical
26344197
PSD13_HUMANPSMD13physical
26344197
PSDE_HUMANPSMD14physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD3_HUMANPSMD3physical
26344197
PSMD7_HUMANPSMD7physical
26344197
PSMG2_HUMANPSMG2physical
26344197
PYGL_HUMANPYGLphysical
26344197
RAN_HUMANRANphysical
26344197
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
DB00188Bortezomib
DB08889Carfilzomib
Regulatory Network of PSB5_HUMAN

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Related Literatures of Post-Translational Modification

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