CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004248
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 26S proteasome non-ATPase regulatory subunit 3 
Protein Synonyms/Alias
 26S proteasome regulatory subunit RPN3; 26S proteasome regulatory subunit S3; Proteasome subunit p58; Transplantation antigen P91A; Tum-P91A antigen 
Gene Name
 Psmd3 
Gene Synonyms/Alias
 P91a; Tstap91a 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
36APQDVEMKEEAAAGSubiquitination[1]
52STGEGDGKAAATEHSubiquitination[1]
72TVTLEDIKEHVRQLEubiquitination[1]
80EHVRQLEKAVSGKEPubiquitination[1]
205ALDLVAAKCYYYHARacetylation[2]
205ALDLVAAKCYYYHARubiquitination[1]
219RVYEFLDKLDVVRSFacetylation[2]
219RVYEFLDKLDVVRSFubiquitination[1]
265SLYDQAEKLVSKSVFubiquitination[1]
269QAEKLVSKSVFPEQAubiquitination[1]
321QHTAVGFKQTVHKLLubiquitination[1]
436DAEFIVAKAIRDGVIubiquitination[1]
457EKGYVQSKEMIDIYSubiquitination[1]
499FPPKSYNKDLESAEEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. 
Sequence Annotation
 DOMAIN 354 458 PCI.  
Keyword
 Complete proteome; Proteasome; Reference proteome; Tumor antigen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 530 AA 
Protein Sequence
MKQEGSARRR GADKAKPPPG GEQEPPPPAP QDVEMKEEAA AGSGSTGEGD GKAAATEHSQ 60
RELDTVTLED IKEHVRQLEK AVSGKEPRFV LRALRMLPST SRRLNHYVLY KAVHGFFTSN 120
NATRDFLLPF LEEPMDTEAD LQFRPRTGKA ASAPLLPEVE AYLQLLMVIF LMNSKRYKEA 180
QKISDDLMQK ISTQNRRALD LVAAKCYYYH ARVYEFLDKL DVVRSFLHAR LRTATLRHDA 240
DGQATLLNLL LRNYLHYSLY DQAEKLVSKS VFPEQANNNE WARYLYYTGR IKAIQLEYSE 300
ARRTMTNALR KAPQHTAVGF KQTVHKLLIV VELLLGEIPD RLQFRQPSLK RSLMPYFLLT 360
QAVRTGNLAK FNQVLDQFGE KFQTDGTYTL IIRLRHNVIK TGVRMISLSY SRISLADIAQ 420
KLQLDSPEDA EFIVAKAIRD GVIEASINHE KGYVQSKEMI DIYSTREPQL AFHQRISFCL 480
DIHNMSVKAM RFPPKSYNKD LESAEERRER EQQDLEFAKE MAEDDDDSFP 530 
Gene Ontology
 GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
 GO:0030234; F:enzyme regulator activity; IEA:InterPro.
 GO:0050790; P:regulation of catalytic activity; IEA:GOC.
 GO:0042176; P:regulation of protein catabolic process; IEA:InterPro. 
Interpro
 IPR013586; 26S_Psome_reg_C.
 IPR013143; PAM.
 IPR000717; PCI_dom.
 IPR011990; TPR-like_helical.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF01399; PCI
 PF08375; Rpn3_C 
SMART
 SM00753; PAM
 SM00088; PINT 
PROSITE
  
PRINTS