PRS6B_MOUSE - dbPTM
PRS6B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRS6B_MOUSE
UniProt AC P54775
Protein Name 26S proteasome regulatory subunit 6B
Gene Name Psmc4
Organism Mus musculus (Mouse).
Sequence Length 418
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. PSMC4 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 MEEIGILVEKIQDEIPALSVSRPQTGLSFLGPEPEDLEDLYSRYKKLQQELEFLEVQEEYIKDEQKNLKKEFLHAQEEVKRIQSIPLVIGQFLEAVDQNTAIVGSTTGSNYYVRILSTIDRELLKPNASVALHKHSNALVDVLPPEADSSIMMLTSDQKPDVMYADIGGMDIQKQEVREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTAAFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQNVNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFSTITSKMNLSEEVDLEDYVARPDKISGADINSICQESGMLAVRENRYIVLAKDFEKAYKTVIKKDEQEHEFYK
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
1Acetylation-------MEEIGILV
-------CCCCCHHH
10.6016857966
19PhosphorylationQDEIPALSVSRPQTG
HHHCCCCCCCCCCCC
21.8326239621
21PhosphorylationEIPALSVSRPQTGLS
HCCCCCCCCCCCCCC
34.5626239621
25PhosphorylationLSVSRPQTGLSFLGP
CCCCCCCCCCCCCCC
42.6526239621
28PhosphorylationSRPQTGLSFLGPEPE
CCCCCCCCCCCCCCC
21.5526239621
41PhosphorylationPEDLEDLYSRYKKLQ
CCCHHHHHHHHHHHH
11.9222817900
70UbiquitinationDEQKNLKKEFLHAQE
HHHHHHHHHHHHHHH
57.7922790023
80AcetylationLHAQEEVKRIQSIPL
HHHHHHHHHHHHHCC
47.257744061
159AcetylationMMLTSDQKPDVMYAD
EEEECCCCCCEEEEE
48.4522733758
238AcetylationVGSEFVQKYLGEGPR
HCHHHHHHHHCCCCH
36.8223236377
238UbiquitinationVGSEFVQKYLGEGPR
HCHHHHHHHHCCCCH
36.8222790023
255UbiquitinationRDVFRLAKENAPAII
HHHHHHHHHCCCEEE
56.9722790023
272PhosphorylationDEIDAIATKRFDAQT
ECCCHHHHCCCCCCC
19.3522871156
273UbiquitinationEIDAIATKRFDAQTG
CCCHHHHCCCCCCCC
41.8822790023
346PhosphorylationRQKRLIFSTITSKMN
HHHHHHHHHHHHCCC
16.3522006019
347PhosphorylationQKRLIFSTITSKMNL
HHHHHHHHHHHCCCC
19.9522817900
397AcetylationNRYIVLAKDFEKAYK
CEEEEEECCHHHHHH
59.8122826441
397SuccinylationNRYIVLAKDFEKAYK
CEEEEEECCHHHHHH
59.8123954790
401AcetylationVLAKDFEKAYKTVIK
EEECCHHHHHHHHHC
57.94-
404MalonylationKDFEKAYKTVIKKDE
CCHHHHHHHHHCHHH
40.9726320211
418AcetylationEQEHEFYK-------
HHHCCCCC-------
60.2268815

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 PRS6B_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRS6B_MOUSE !!

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 PRS6B_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PRS6B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRS6B_MOUSE

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Related Literatures of Post-Translational Modification

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