CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019683
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleolar complex protein 14 
Protein Synonyms/Alias
 U three protein 2; U3 small nucleolar RNA-associated protein 2; U3 snoRNA-associated protein 2 
Gene Name
 NOP14 
Gene Synonyms/Alias
 UTP2; YDL148C; D1566 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
88VGKPGISKQIGEEQRacetylation[1]
680SKYSDFEKPRNILNKubiquitination[2]
693NKVEKLTKFTEHIPLacetylation[1]
716SIPTHAPKYEENFNPacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
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. 
Sequence Annotation
  
Keyword
 Complete proteome; Nucleus; Reference proteome; Ribonucleoprotein; Ribosome biogenesis; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 810 AA 
Protein Sequence
MAGSQLKNLK AALKARGLTG QTNVKSKNKK NSKRQAKEYD REEKKKAIAE IREEFNPFEI 60
KAARNKRRDG LPSKTADRIA VGKPGISKQI GEEQRKRAFE ARKMMKNKRG GVIDKRFGER 120
DKLLTEEEKM LERFTRERQS QSKRNANLFN LEDDEDDGDM FGDGLTHLGQ SLSLEDELAN 180
DEEDFLASKR FNEDDAELQQ PQRKKTKAEV MKEVIAKSKF YKQERQKAQG IMEDQIDNLD 240
DNFEDVMSEL MMTQPKKNPM EPKTDLDKEY DIKVKELQLD KRAAPSDRTK TEEEKNAEAE 300
EKKRELEQQR LDRMNGMIEL EEGEERGVED LDDGFWENEE DYEDDNDGIA DSDDDIKFED 360
QGRDEGFSQI LKKKNISISC PRTHDALLDQ VKKLDLDDHP KIVKNIIKAY QPKLAEGNKE 420
KLGKFTAVLL RHIIFLSNQN YLKNVQSFKR TQNALISILK SLSEKYNREL SEECRDYINE 480
MQARYKKNHF DALSNGDLVF FSIIGILFST SDQYHLVITP ALILMSQFLE QIKFNSLKRI 540
AFGAVLVRIV SQYQRISKRY IPEVVYFFQK ILLTFIVEKE NQEKPLDFEN IRLDSYELGL 600
PLDVDFTKKR STIIPLHTLS TMDTEAHPVD QCVSVLLNVM ESLDATISTV WKSLPAFNEI 660
ILPIQQLLSA YTSKYSDFEK PRNILNKVEK LTKFTEHIPL ALQNHKPVSI PTHAPKYEEN 720
FNPDKKSYDP DRTRSEINKM KAQLKKERKF TMKEIRKDAK FEARQRIEEK NKESSDYHAK 780
MAHIVNTINT EEGAEKNKYE RERKLRGGKK 810 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0030692; C:Noc4p-Nop14p complex; IPI:SGD.
 GO:0005730; C:nucleolus; IDA:SGD.
 GO:0032040; C:small-subunit processome; IDA:SGD.
 GO:0030515; F:snoRNA binding; IPI:SGD.
 GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
 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); IMP:SGD.
 GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. 
Interpro
 IPR007276; Nop14. 
Pfam
 PF04147; Nop14 
SMART
  
PROSITE
  
PRINTS