CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011651
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosome biogenesis protein BMS1 
Protein Synonyms/Alias
  
Gene Name
 BMS1 
Gene Synonyms/Alias
 YPL217C 
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
967RFEGAQIKTVSGIRGubiquitination[1]
1068ERHFNGLKVPKAVQKacetylation[2]
1075KVPKAVQKELPFKSQacetylation[2]
1115KARSFIQKVLTISKAacetylation[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, Villén 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
 May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. The depletion of BMS1 interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. 
Sequence Annotation
 NP_BIND 76 83 ATP (Potential).
 MOD_RES 438 438 Phosphoserine.
 MOD_RES 478 478 Phosphoserine.
 MOD_RES 492 492 Phosphoserine.
 MOD_RES 504 504 Phosphothreonine.
 MOD_RES 516 516 Phosphothreonine.
 MOD_RES 518 518 Phosphoserine.
 MOD_RES 523 523 Phosphoserine.
 MOD_RES 574 574 Phosphoserine.
 MOD_RES 578 578 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1183 AA 
Protein Sequence
MEQSNKQHRK AKEKNTAKKK LHTQGHNAKA FAVAAPGKMA RTMQRSSDVN ERKLHVPMVD 60
RTPEDDPPPF IVAVVGPPGT GKTTLIRSLV RRMTKSTLND IQGPITVVSG KHRRLTFLEC 120
PADDLNAMID IAKIADLVLL LIDGNFGFEM ETMEFLNIAQ HHGMPRVLGV ATHLDLFKSQ 180
STLRASKKRL KHRFWTEVYQ GAKLFYLSGV INGRYPDREI LNLSRFISVM KFRPLKWRNE 240
HPYMLADRFT DLTHPELIET QGLQIDRKVA IYGYLHGTPL PSAPGTRVHI AGVGDFSVAQ 300
IEKLPDPCPT PFYQQKLDDF EREKMKEEAK ANGEITTAST TRRRKRLDDK DKLIYAPMSD 360
VGGVLMDKDA VYIDIGKKNE EPSFVPGQER GEGEKLMTGL QSVEQSIAEK FDGVGLQLFS 420
NGTELHEVAD HEGMDVESGE ESIEDDEGKS KGRTSLRKPR IYGKPVQEED ADIDNLPSDE 480
EPYTNDDDVQ DSEPRMVEID FNNTGEQGAE KLALETDSEF EESEDEFSWE RTAANKLKKT 540
ESKKRTWNIG KLIYMDNISP EECIRRWRGE DDDSKDESDI EEDVDDDFFR KKDGTVTKEG 600
NKDHAVDLEK FVPYFDTFEK LAKKWKSVDA IKERFLGAGI LGNDNKTKSD SNEGGEELYG 660
DFEDLEDGNP SEQAEDNSDK ESEDEDENED TNGDDDNSFT NFDAEEKKDL TMEQEREMNA 720
AKKEKLRAQF EIEEGENFKE DDENNEYDTW YELQKAKISK QLEINNIEYQ EMTPEQRQRI 780
EGFKAGSYVR IVFEKVPMEF VKNFNPKFPI VMGGLLPTEI KFGIVKARLR RHRWHKKILK 840
TNDPLVLSLG WRRFQTLPIY TTTDSRTRTR MLKYTPEHTY CNAAFYGPLC SPNTPFCGVQ 900
IVANSDTGNG FRIAATGIVE EIDVNIEIVK KLKLVGFPYK IFKNTAFIKD MFSSAMEVAR 960
FEGAQIKTVS GIRGEIKRAL SKPEGHYRAA FEDKILMSDI VILRSWYPVR VKKFYNPVTS 1020
LLLKEKTEWK GLRLTGQIRA AMNLETPSNP DSAYHKIERV ERHFNGLKVP KAVQKELPFK 1080
SQIHQMKPQK KKTYMAKRAV VLGGDEKKAR SFIQKVLTIS KAKDSKRKEQ KASQRKERLK 1140
KLAKMEEEKS QRDKEKKKEY FAQNGKRTTM GGDDESRPRK MRR 1183 
Gene Ontology
 GO:0030686; C:90S preribosome; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005730; C:nucleolus; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005525; F:GTP binding; IDA:SGD.
 GO:0003924; F:GTPase activity; IDA:SGD.
 GO:0034511; F:U3 snoRNA binding; IDA:SGD.
 GO:0042255; P:ribosome assembly; IDA:SGD.
 GO:0006364; P:rRNA processing; IDA:SGD. 
Interpro
 IPR012948; AARP2CN.
 IPR007034; BMS1_TSR1_C.
 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase. 
Pfam
 PF08142; AARP2CN
 PF04950; DUF663
 PF00009; GTP_EFTU 
SMART
 SM00785; AARP2CN 
PROSITE
  
PRINTS