CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006805
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleolar protein 4 
Protein Synonyms/Alias
 Nucleolar protein NOP77 
Gene Name
 NOP4 
Gene Synonyms/Alias
 NOP77; YPL043W 
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
144DGEDSMLKGKPKLIIacetylation[1]
312SLAPHFSKFGSVKYAacetylation[2]
325YALPVIDKSTGLAKGubiquitination[3]
Reference
 [1] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
 [2] 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]
 [3] 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, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Required for 60S ribosomal subunit synthesis. Probably involved in the processing of 27S rRNA to produce mature 25S rRNA. 
Sequence Annotation
 DOMAIN 26 103 RRM 1.
 DOMAIN 147 225 RRM 2.
 DOMAIN 290 383 RRM 3.
 DOMAIN 462 612 RRM 4.
 MOD_RES 247 247 Phosphoserine.  
Keyword
 Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis; RNA-binding; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 685 AA 
Protein Sequence
MEETIENVEV PSSNVSKQND DGLDMKTLFV RSIPQDVTDE QLADFFSNFA PIKHAVVVKD 60
TNKRSRGFGF VSFAVEDDTK EALAKARKTK FNGHILRVDI AKRRDRSKKT SEVVEKSTPE 120
SSEKITGQNN EDEDDADGED SMLKGKPKLI IRNMPWSCRD PVKLKKIFGR YGTVVEATIP 180
RKRDGKLCGF AFVTMKKISN CRIALENTKD LKIDGRKVAV DFAVQKNRWE DYKKAQPEMN 240
DKDDNESGNE DAEENHDDEE DENEEEDRQV DQASKNKESK RKAQNKREDF SVFVRNVPYD 300
ATEESLAPHF SKFGSVKYAL PVIDKSTGLA KGTAFVAFKD QYTYNECIKN APAAGSTSLL 360
IGDDVMPEYV YEGRVLSITP TLVREDAGRM AEKNAAKRKE ALGKAPGEKD RRNLYLLNEG 420
RVVEGSKMAD LLTNTDMEIR EKSYKLRVEQ LKKNPSLHLS MTRLAIRNLP RAMNDKALKA 480
LARKAVVEFA TEVKNKERHP LSKEEIIRST KEKYKFMGPD EIEAQKKKDK KSGVVKQAKV 540
IMEVKGSTAG RSRGYGFVEF RDHKNALMGL RWLNCHAVTS DEILEGLNDD EKKQVDNDLG 600
KGRRLCVEFA IENSNVVKRR REQLKQARTK RTRPDNEDTG DVGESENKKP KKEEATTPTN 660
PDDKKMGDDI KRIIGFKRKR KHAKK 685 
Gene Ontology
 GO:0005730; C:nucleolus; TAS:SGD.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; ISS:SGD.
 GO:0006364; P:rRNA processing; TAS:SGD. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS