CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010397
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleolar protein 14 
Protein Synonyms/Alias
 Nucleolar complex protein 14 
Gene Name
 NOP14 
Gene Synonyms/Alias
 C4orf9; NOL14; RES4-25 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26GARGGPAKANSNPFEubiquitination[1]
35NSNPFEVKVNRQKFQubiquitination[1]
226EKLDQDWKEIQTLLSubiquitination[1]
249RDKKEKPKPDAYDMMubiquitination[1]
265RELGFEMKAQPSNRMubiquitination[2]
411GKGLISGKERAGKATacetylation[3]
535MEEMIETKGRAALPGubiquitination[1]
643HPFRALGKNSELLVVubiquitination[2]
772LFTPRLVKVLEFGRKacetylation[4]
772LFTPRLVKVLEFGRKubiquitination[2, 5]
834AERKRKVKQLFNSLAubiquitination[2, 6, 7]
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] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [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] 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]
 [6] 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]
 [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
Functional Description
 Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity). 
Sequence Annotation
 MOD_RES 96 96 Phosphoserine.
 MOD_RES 146 146 Phosphoserine.
 MOD_RES 148 148 Phosphoserine.
 MOD_RES 349 349 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ribosome biogenesis; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 857 AA 
Protein Sequence
MAKAKKVGAR RKASGAPAGA RGGPAKANSN PFEVKVNRQK FQILGRKTRH DVGLPGVSRA 60
RALRKRTQTL LKEYKERDKS NVFRDKRFGE YNSNMSPEEK MMKRFALEQQ RHHEKKSIYN 120
LNEDEELTHY GQSLADIEKH NDIVDSDSDA EDRGTLSAEL TAAHFGGGGG LLHKKTQQEG 180
EEREKPKSRK ELIEELIAKS KQEKRERQAQ REDALELTEK LDQDWKEIQT LLSHKTPKSE 240
NRDKKEKPKP DAYDMMVREL GFEMKAQPSN RMKTEAELAK EEQEHLRKLE AERLRRMLGK 300
DEDENVKKPK HMSADDLNDG FVLDKDDRRL LSYKDGKMNV EEDVQEEQSK EASDPESNEE 360
EGDSSGGEDT EESDSPDSHL DLESNVESEE ENEKPAKEQR QTPGKGLISG KERAGKATRD 420
ELPYTFAAPE SYEELRSLLL GRSMEEQLLV VERIQKCNHP SLAEGNKAKL EKLFGFLLEY 480
VGDLATDDPP DLTVIDKLVV HLYHLCQMFP ESASDAIKFV LRDAMHEMEE MIETKGRAAL 540
PGLDVLIYLK ITGLLFPTSD FWHPVVTPAL VCLSQLLTKC PILSLQDVVK GLFVCCLFLE 600
YVALSQRFIP ELINFLLGIL YIATPNKASQ GSTLVHPFRA LGKNSELLVV SAREDVATWQ 660
QSSLSLRWAS RLRAPTSTEA NHIRLSCLAV GLALLKRCVL MYGSLPSFHA IMGPLQALLT 720
DHLADCSHPQ ELQELCQSTL TEMESQKQLC RPLTCEKSKP VPLKLFTPRL VKVLEFGRKQ 780
GSSKEEQERK RLIHKHKREF KGAVREIRKD NQFLARMQLS EIMERDAERK RKVKQLFNSL 840
ATQEGEWKAL KRKKFKK 857 
Gene Ontology
 GO:0005739; C:mitochondrion; ISS:UniProtKB.
 GO:0030692; C:Noc4p-Nop14p complex; ISS:UniProtKB.
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0032040; C:small-subunit processome; ISS:UniProtKB.
 GO:0030515; F:snoRNA binding; ISS:UniProtKB.
 GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
 GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
 GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB. 
Interpro
 IPR007276; Nop14. 
Pfam
 PF04147; Nop14 
SMART
  
PROSITE
  
PRINTS