CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023198
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA-binding protein NOB1 
Protein Synonyms/Alias
 Phosphorylation regulatory protein HP-10; Protein ART-4 
Gene Name
 NOB1 
Gene Synonyms/Alias
 ART4; NOB1P; PSMD8BP1; MSTP158 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
25AALQDIGKNIYTIREubiquitination[1, 2]
40VVTEIRDKATRRRLAubiquitination[2]
56LPYELRFKEPLPEYVubiquitination[2]
72LVTEFSKKTGDYPSLubiquitination[2]
133SGFHLPYKPKPPQETubiquitination[2]
275LRCHGCFKTTSDMSRubiquitination[2]
291FCSHCGNKTLKKVSVubiquitination[2]
294HCGNKTLKKVSVTVSubiquitination[2]
295CGNKTLKKVSVTVSDubiquitination[2]
315MHFSRNPKVLNPRGLubiquitination[2, 3]
333LPTPKGGKYAINPHLacetylation[4]
333LPTPKGGKYAINPHLubiquitination[1, 2, 5, 6]
358LSQKARQKTNVFAPDubiquitination[1, 2, 3, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [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] 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
Functional Description
 May play a role in mRNA degradation. 
Sequence Annotation
 DOMAIN 5 108 PINc.
 METAL 270 270 Zinc (By similarity).
 METAL 273 273 Zinc (By similarity).
 METAL 285 285 Zinc (By similarity).
 METAL 288 288 Zinc (By similarity).
 MOD_RES 184 184 Phosphoserine.
 MOD_RES 201 201 Phosphoserine.
 MOD_RES 352 352 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 412 AA 
Protein Sequence
MAPVEHVVAD AGAFLRHAAL QDIGKNIYTI REVVTEIRDK ATRRRLAVLP YELRFKEPLP 60
EYVRLVTEFS KKTGDYPSLS ATDIQVLALT YQLEAEFVGV SHLKQEPQKV KVSSSIQHPE 120
TPLHISGFHL PYKPKPPQET EKGHSACEPE NLEFSSFMFW RNPLPNIDHE LQELLIDRGE 180
DVPSEEEEEE ENGFEDRKDD SDDDGGGWIT PSNIKQIQQE LEQCDVPEDV RVGCLTTDFA 240
MQNVLLQMGL HVLAVNGMLI REARSYILRC HGCFKTTSDM SRVFCSHCGN KTLKKVSVTV 300
SDDGTLHMHF SRNPKVLNPR GLRYSLPTPK GGKYAINPHL TEDQRFPQLR LSQKARQKTN 360
VFAPDYIAGV SPFVENDISS RSATLQVRDS TLGAGRRRLN PNASRKKFVK KR 412 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 IPR017117; D-site_20S_pre-rRNA_nuclease.
 IPR014881; NOB1_Zn-bd.
 IPR006596; PINc_nuc-bd. 
Pfam
 PF08772; NOB1_Zn_bind 
SMART
 SM00670; PINc 
PROSITE
  
PRINTS