CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011532
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosome biogenesis ATPase RIX7 
Protein Synonyms/Alias
  
Gene Name
 RIX7 
Gene Synonyms/Alias
 YLL034C 
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
8MVKVKSKKNSLTSSLubiquitination[1]
404DGAIDFAKLAKLTPGacetylation[2]
Reference
 [1] 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]
 [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
Functional Description
 Involved in ribosome biogenesis. Seems to be required for restructuring nucleoplasmic 60S pre-ribosomal particles to make them competent for nuclear export. 
Sequence Annotation
 NP_BIND 246 253 ATP (Potential).
 NP_BIND 574 581 ATP (Potential).
 MOD_RES 42 42 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 837 AA 
Protein Sequence
MVKVKSKKNS LTSSLDNKIV DLIYRLLEEK TLDRKRSLRQ ESQGEEGENN EGEEDEDIFE 60
SMFFAKDLTA GEIFTFCLTK DLSLQRVKKV VLQKTIDRML KDVIESELEE FGSYPGYNNE 120
EEEKPSLEEE LAKKNMMIER DTNEMNKRIT STWSKSGSVS ESITETDDPK TEEVKKSKKR 180
SKEGTCKVKR QKIKEDRSPP NSSLKSLGGM DDVVAQLMEL IGLPILHPEI FLSTGVEPPR 240
GVLLHGPPGC GKTSIANALA GELQVPFISI SAPSVVSGMS GESEKKIRDL FDEARSLAPC 300
LVFFDEIDAI TPKRDGGAQR EMERRIVAQL LTSMDELTME KTNGKPVIII GATNRPDSLD 360
AALRRAGRFD REICLNVPNE VSRLHILKKM SDNLKIDGAI DFAKLAKLTP GFVGADLKAL 420
VTAAGTCAIK RIFQTYANIK STPTTATDSS EDNMEIDETA NGDESSLKNT ANMIDPLPLS 480
VVQQFIRNYP EPLSGEQLSL LSIKYEDFLK ALPTIQPTAK REGFATVPDV TWANVGALQR 540
VRLELNMAIV QPIKRPELYE KVGISAPGGV LLWGPPGCGK TLLAKAVANE SRANFISIKG 600
PELLNKYVGE SERSIRQVFT RARASVPCVI FFDELDALVP RRDTSLSESS SRVVNTLLTE 660
LDGLNDRRGI FVIGATNRPD MIDPAMLRPG RLDKSLFIEL PNTEEKLDII KTLTKSHGTP 720
LSSDVDFEEI IRNEKCNNFS GADLAALVRE SSVLALKRKF FQSEEIQSVL DNDLDKEFED 780
LSVGVSGEEI IVTMSDFRSA LRKIKPSVSD KDRLKYDRLN KKMGLTEEMK DAEEMKQ 837 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:SGD.
 GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; ISS:SGD.
 GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
 GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR003960; ATPase_AAA_CS.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00004; AAA 
SMART
 SM00382; AAA 
PROSITE
 PS00674; AAA 
PRINTS