CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023718
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleolar protein 58 
Protein Synonyms/Alias
 Nucleolar protein 5 
Gene Name
 NOP58 
Gene Synonyms/Alias
 NOL5; NOP5; HSPC120 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30QEVDSLWKEFETPEKubiquitination[1]
67FTALMEGKINKQLKKubiquitination[1, 2, 3]
70LMEGKINKQLKKVLKubiquitination[1]
78QLKKVLKKIVKEAHEubiquitination[4]
81KVLKKIVKEAHEPLAubiquitination[1, 2, 4]
93PLAVADAKLGGVIKEubiquitination[1, 2, 3, 4]
99AKLGGVIKEKLNLSCubiquitination[1, 3, 4]
101LGGVIKEKLNLSCIHubiquitination[1, 4]
206SDNLTYCKCLQKVGDubiquitination[1, 5]
215LQKVGDRKNYASAKLubiquitination[1]
221RKNYASAKLSELLPEubiquitination[1, 2, 3, 6]
310GSLLNLAKHAASTVQubiquitination[1, 3, 4, 7]
323VQILGAEKALFRALKubiquitination[1, 3, 4, 5, 8]
337KSRRDTPKYGLIYHAubiquitination[8]
365ISRMLAAKTVLAIRYubiquitination[1, 4, 6]
411RKISGTGKALAKTEKubiquitination[4]
426YEHKSEVKTYDPSGDubiquitination[1, 4, 7]
442TLPTCSKKRKIEQVDubiquitination[1]
460EITEKKAKKAKIKVKacetylation[9]
463EKKAKKAKIKVKVEEacetylation[9]
467KKAKIKVKVEEEEEEsumoylation[10, 11, 12, 13]
497RGKKKHIKEEPLSEEsumoylation[10, 11, 12, 13]
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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58.
 Westman BJ, Verheggen C, Hutten S, Lam YW, Bertrand E, Lamond AI.
 Mol Cell. 2010 Aug 27;39(4):618-31. [PMID: 20797632]
 [11] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [12] A role for SUMOylation in snoRNP biogenesis revealed by quantitative proteomics.
 Westman BJ, Lamond AI.
 Nucleus. 2011 Jan-Feb;2(1):30-7. [PMID: 21647297]
 [13] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026
Functional Description
 Required for 60S ribosomal subunit biogenesis (By similarity). 
Sequence Annotation
 DOMAIN 282 400 Nop.
 MOD_RES 109 109 Phosphoserine.
 MOD_RES 351 351 Phosphoserine.
 MOD_RES 483 483 Phosphoserine.
 MOD_RES 502 502 Phosphoserine.
 MOD_RES 514 514 Phosphoserine.
 CROSSLNK 467 467 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 497 497 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ribosome biogenesis; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 529 AA 
Protein Sequence
MLVLFETSVG YAIFKVLNEK KLQEVDSLWK EFETPEKANK IVKLKHFEKF QDTAEALAAF 60
TALMEGKINK QLKKVLKKIV KEAHEPLAVA DAKLGGVIKE KLNLSCIHSP VVNELMRGIR 120
SQMDGLIPGV EPREMAAMCL GLAHSLSRYR LKFSADKVDT MIVQAISLLD DLDKELNNYI 180
MRCREWYGWH FPELGKIISD NLTYCKCLQK VGDRKNYASA KLSELLPEEV EAEVKAAAEI 240
SMGTEVSEED ICNILHLCTQ VIEISEYRTQ LYEYLQNRMM AIAPNVTVMV GELVGARLIA 300
HAGSLLNLAK HAASTVQILG AEKALFRALK SRRDTPKYGL IYHASLVGQT SPKHKGKISR 360
MLAAKTVLAI RYDAFGEDSS SAMGVENRAK LEARLRTLED RGIRKISGTG KALAKTEKYE 420
HKSEVKTYDP SGDSTLPTCS KKRKIEQVDK EDEITEKKAK KAKIKVKVEE EEEEKVAEEE 480
ETSVKKKKKR GKKKHIKEEP LSEEEPCTST AIASPEKKKK KKKKRENED 529 
Gene Ontology
 GO:0031428; C:box C/D snoRNP complex; NAS:BHF-UCL.
 GO:0015030; C:Cajal body; IDA:BHF-UCL.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0070761; C:pre-snoRNP complex; IDA:BHF-UCL.
 GO:0030515; F:snoRNA binding; IDA:BHF-UCL.
 GO:0016049; P:cell growth; TAS:UniProtKB.
 GO:0006364; P:rRNA processing; TAS:UniProtKB.
 GO:0006608; P:snRNP protein import into nucleus; ISS:UniProtKB. 
Interpro
 IPR012974; NOP5_N.
 IPR002687; Nop_dom.
 IPR012976; NOSIC. 
Pfam
 PF01798; Nop
 PF08156; NOP5NT
 PF08060; NOSIC 
SMART
 SM00931; NOSIC 
PROSITE
 PS51358; NOP 
PRINTS