CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000102
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pescadillo homolog 
Protein Synonyms/Alias
  
Gene Name
 PES1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26TRNKARKKLQLSLADubiquitination[1]
41FRRLCILKGIYPHEPubiquitination[1]
68ARTFYLIKDIRFLLHubiquitination[1, 2]
81LHEPIVNKFREYKVFubiquitination[1, 2, 3, 4]
86VNKFREYKVFVRKLRubiquitination[1]
94VFVRKLRKAYGKSEWubiquitination[1]
98KLRKAYGKSEWNTVEacetylation[5]
98KLRKAYGKSEWNTVEubiquitination[1, 3]
121YKLDHIIKERYPTFIubiquitination[3]
275DSESCMEKLAALSASubiquitination[1]
325EAQEKHKKLFEGLKFubiquitination[1]
331KKLFEGLKFFLNREVubiquitination[1, 3]
441YVPPEKLKLLALQRGubiquitination[1, 2]
517RVMAGTLKLEDKQRLsumoylation[6]
521GTLKLEDKQRLAQEEacetylation[7]
533QEEESEAKRLAIMMMubiquitination[3]
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] 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]
 [3] 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]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] Pescadillo, a novel cell cycle regulatory protein abnormally expressed in malignant cells.
 Kinoshita Y, Jarell AD, Flaman JM, Foltz G, Schuster J, Sopher BL, Irvin DK, Kanning K, Kornblum HI, Nelson PS, Hieter P, Morrison RS.
 J Biol Chem. 2001 Mar 2;276(9):6656-65. [PMID: 11071894]
 [7] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. 
Sequence Annotation
 DOMAIN 322 415 BRCT.
 REGION 1 257 Sufficient for nucleolar localization.
 REGION 1 54 Required for 28S ribosomal RNA
 REGION 306 415 Sufficient for interaction with MAP1B (By
 REGION 539 588 Required for 28S ribosomal RNA
 MOD_RES 98 98 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chromosome; Complete proteome; Nucleus; Polymorphism; Reference proteome; Ribosome biogenesis; rRNA processing; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 588 AA 
Protein Sequence
MGGLEKKKYE RGSATNYITR NKARKKLQLS LADFRRLCIL KGIYPHEPKH KKKVNKGSTA 60
ARTFYLIKDI RFLLHEPIVN KFREYKVFVR KLRKAYGKSE WNTVERLKDN KPNYKLDHII 120
KERYPTFIDA LRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLTVEFMH YIIAARALRK 180
VFLSIKGIYY QAEVLGQPIV WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ 240
LLNLHYPPKL EGQAQAEAKA GEGTYALDSE SCMEKLAALS ASLARVVVPA TEEEAEVDEF 300
PTDGEMSAQE EDRRKELEAQ EKHKKLFEGL KFFLNREVPR EALAFIIRSF GGEVSWDKSL 360
CIGATYDVTD SRITHQIVDR PGQQTSVIGR CYVQPQWVFD SVNARLLLPV AEYFSGVQLP 420
PHLSPFVTEK EGDYVPPEKL KLLALQRGED PGNLNESEEE EEEDDNNEGD GDEEGENEEE 480
EEDAEAGSEK EEEARLAALE EQRMEGKKPR VMAGTLKLED KQRLAQEEES EAKRLAIMMM 540
KKREKYLYQK IMFGKRRKIR EANKLAEKRK AHDEAVRSEK KAKKARPE 588 
Gene Ontology
 GO:0000793; C:condensed chromosome; IEA:Compara.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0070545; C:PeBoW complex; IDA:UniProtKB.
 GO:0030687; C:preribosome, large subunit precursor; IDA:UniProtKB.
 GO:0008283; P:cell proliferation; IMP:UniProtKB.
 GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:UniProtKB.
 GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:UniProtKB.
 GO:0007000; P:nucleolus organization; IEA:Compara.
 GO:0033365; P:protein localization to organelle; IEA:Compara.
 GO:0051726; P:regulation of cell cycle; IMP:UniProtKB. 
Interpro
 IPR001357; BRCT_dom.
 IPR010613; Pescadillo. 
Pfam
 PF00533; BRCT
 PF06732; Pescadillo_N 
SMART
 SM00292; BRCT 
PROSITE
 PS50172; BRCT 
PRINTS