CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017089
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 pre-rRNA processing protein FTSJ3 
Protein Synonyms/Alias
 2'-O-ribose RNA methyltransferase SPB1 homolog; Protein ftsJ homolog 3; Putative rRNA methyltransferase 3 
Gene Name
 FTSJ3 
Gene Synonyms/Alias
 SB92 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
14VGKSRRDKFYHLAKEubiquitination[1]
20DKFYHLAKETGYRSRacetylation[2]
20DKFYHLAKETGYRSRubiquitination[1]
44RRFQFLQKARALLDLubiquitination[3]
157RGGSFITKVFRSRDYubiquitination[3, 4, 5]
214DSKFFDPKFAFKEVEubiquitination[1, 3, 4, 6]
218FDPKFAFKEVEVQAKubiquitination[1, 6]
233TVTELVTKKKPKAEGacetylation[2, 6, 7]
234VTELVTKKKPKAEGYubiquitination[1]
269NPVDFLSKASEIMVDubiquitination[5, 8]
384AQEVAELKRKKKKLLubiquitination[1, 6]
678GAVIASSKKAKRDLIubiquitination[6, 8, 9]
679AVIASSKKAKRDLIDubiquitination[1]
710EWFVQEEKQHRIRQLubiquitination[1, 5]
749VAEAKARKKRRMLKRmethylation[10]
762KRLEQTRKKAEAVVNubiquitination[1, 6]
763RLEQTRKKAEAVVNTmethylation[10]
763RLEQTRKKAEAVVNTubiquitination[1]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] 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]
 [9] 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]
 [10] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837] 
Functional Description
 Probable methyltransferase involved in the processing of the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation. 
Sequence Annotation
 ACT_SITE 157 157 Proton acceptor (By similarity).
 BINDING 56 56 S-adenosyl-L-methionine; via amide
 BINDING 58 58 S-adenosyl-L-methionine; via amide
 BINDING 76 76 S-adenosyl-L-methionine (By similarity).
 BINDING 92 92 S-adenosyl-L-methionine (By similarity).
 BINDING 117 117 S-adenosyl-L-methionine (By similarity).
 MOD_RES 333 333 Phosphoserine.
 MOD_RES 335 335 Phosphoserine.
 MOD_RES 336 336 Phosphoserine.
 MOD_RES 347 347 Phosphoserine.
 MOD_RES 356 356 Phosphoserine.
 MOD_RES 371 371 Phosphothreonine.
 MOD_RES 549 549 Phosphoserine.
 MOD_RES 584 584 Phosphoserine.
 MOD_RES 644 644 Phosphoserine.
 MOD_RES 676 676 Phosphoserine.
 MOD_RES 688 688 Phosphoserine.  
Keyword
 Coiled coil; Complete proteome; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ribosome biogenesis; rRNA processing; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 847 AA 
Protein Sequence
MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ 60
VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ QDITTERCRQ ALRKELKTWK VDVVLNDGAP 120
NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGSFITKVFR SRDYQPLLWI FQQLFRRVQA 180
TKPQASRHES AEIFVVCQGF LAPDKVDSKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG 240
YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEIMVDDEEL AQHPATTEDI RVCCQDIRVL 300
GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSGEED EGDEEDSTAG TTKQPSKEEE 360
EEEEEEQLNQ TLAEMKAQEV AELKRKKKKL LREQRKQRER VELKMDLPGV SIADEGETGM 420
FSLSTIRGHQ LLEEVTQGDM SAADTFLSDL PRDDIYVSDV EDDGDDTSLD SDLDPEELAG 480
VRGHQGLRDQ KRMRLTEVQD DKEEEEEENP LLVPLEEKAV LQEEQANLWF SKGSFAGIED 540
DADEALEISQ AQLLFENRRK GRQQQQKQQL PQTPPSCLKT EIMSPLYQDE APKGTEASSG 600
TEAATGLEGE EKDGISDSDS STSSEEEESW EPLRGKKRSR GPKSDDDGFE IVPIEDPAKH 660
RILDPEGLAL GAVIASSKKA KRDLIDNSFN RYTFNEDEGE LPEWFVQEEK QHRIRQLPVG 720
KKEVEHYRKR WREINARPIK KVAEAKARKK RRMLKRLEQT RKKAEAVVNT VDISEREKVA 780
QLRSLYKKAG LGKEKRHVTY VVAKKGVGRK VRRPAGVRGH FKVVDSRMKK DQRAQQRKEQ 840
KKKHKRK 847 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
 GO:0001510; P:RNA methylation; IEA:InterPro.
 GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. 
Interpro
 IPR015507; rRNA-MeTfrase_E.
 IPR012920; rRNA_MeTfrase_Spb1_C.
 IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
 IPR002877; rRNA_MeTrfase_FtsJ_dom. 
Pfam
 PF11861; DUF3381
 PF01728; FtsJ
 PF07780; Spb1_C 
SMART
  
PROSITE
  
PRINTS