CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001604
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proteasome assembly chaperone 1 
Protein Synonyms/Alias
 PAC-1; Chromosome 21 leucine-rich protein; C21-LRP; Down syndrome critical region protein 2 
Gene Name
 PSMG1 
Gene Synonyms/Alias
 C21LRP; DSCR2; PAC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11TFFGEVVKAPCRAGTubiquitination[1]
55RLLRRQTKTSLEVSLubiquitination[2]
160VFGSCPRKNMQITILubiquitination[1]
176CRHVTDYKTSESTGSubiquitination[1, 2, 3, 4]
193SPFLRALKTQNFKDSubiquitination[1, 2, 4]
198ALKTQNFKDSACCPLubiquitination[3]
251LITVEAFKPILSTRSubiquitination[1, 2, 3, 5, 6, 7]
260ILSTRSLKGLVKNIPubiquitination[1]
264RSLKGLVKNIPQSTEacetylation[8]
264RSLKGLVKNIPQSTEubiquitination[1, 4, 5, 7]
275QSTEILKKLMTTNEIubiquitination[1, 2, 3, 4]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 18 18 Phosphothreonine (By similarity).
 MOD_RES 264 264 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Endoplasmic reticulum; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 288 AA 
Protein Sequence
MAATFFGEVV KAPCRAGTED EEEEEEGRRE TPEDREVRLQ LARKREVRLL RRQTKTSLEV 60
SLLEKYPCSK FIIAIGNNAV AFLSSFVMNS GVWEEVGCAK LWNEWCRTTD TTHLSSTEAF 120
CVFYHLKSNP SVFLCQCSCY VAEDQQYQWL EKVFGSCPRK NMQITILTCR HVTDYKTSES 180
TGSLPSPFLR ALKTQNFKDS ACCPLLEQPN IVHDLPAAVL SYCQVWKIPA ILYLCYTDVM 240
KLDLITVEAF KPILSTRSLK GLVKNIPQST EILKKLMTTN EIQSNIYT 288 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0043248; P:proteasome assembly; IDA:UniProtKB. 
Interpro
 IPR016565; Proteasome_assmbl_chp_1. 
Pfam
  
SMART
  
PROSITE
  
PRINTS