CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012375
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosome biogenesis protein BMS1 homolog 
Protein Synonyms/Alias
 Ribosome assembly protein BMS1 homolog 
Gene Name
 BMS1 
Gene Synonyms/Alias
 BMS1L; KIAA0187 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
95MGPPKVGKSTLIQCLubiquitination[1]
124PVTIVSGKKRRLTIIubiquitination[2]
795TGDVHKGKSGPNTQNubiquitination[2]
852STYFDDLKGEMQKQAubiquitination[2]
857DLKGEMQKQAQLNRAubiquitination[2]
933LKKHRWYKKILKSRDacetylation[3]
1035KLTGFPYKIFKNTSFubiquitination[4]
1144LAHGVRLKANKDSLYmethylation[5]
1152ANKDSLYKPILRQKKacetylation[6, 7]
1152ANKDSLYKPILRQKKubiquitination[1]
1275RNQKSSLKGAEGQLQubiquitination[2]
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] 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]
 [3] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [4] 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]
 [5] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [6] 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]
 [7] 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
Functional Description
 May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus (By similarity). 
Sequence Annotation
 NP_BIND 89 96 ATP (Potential).
 MOD_RES 552 552 Phosphoserine.
 MOD_RES 625 625 Phosphoserine.
 MOD_RES 639 639 Phosphoserine.
 MOD_RES 708 708 Phosphothreonine.  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ribosome biogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1282 AA 
Protein Sequence
MEAKDQKKHR KKNSGPKAAK KKKRLLQDLQ LGDEEDARKR NPKAFAVQSA VRMARSFHRT 60
QDLKTKKHHI PVVDRTPLEP PPIVVVVMGP PKVGKSTLIQ CLIRNFTRQK LTEIRGPVTI 120
VSGKKRRLTI IECGCDINMM IDLAKVADLV LMLIDASFGF EMETFEFLNI CQVHGFPKIM 180
GVLTHLDSFK HNKQLKKTKK RLKHRFWTEV YPGAKLFYLS GMVHGEYQNQ EIHNLGRFIT 240
VMKFRPLTWQ TSHPYILADR MEDLTNPEDI RTNIKCDRKV SLYGYLRGAH LKNKSQIHMP 300
GVGDFAVSDI SFLPDPCALP EQQKKRCLNE KEKLVYAPLS GVGGVLYDKD AVYVDLGGSH 360
VFQDEVGPTH ELVQSLISTH STIDAKMASS RVTLFSDSKP LGSEDIDNQG LMMPKEEKQM 420
DLNTGRMRRK AIFGDEDESG DSDDEEDDEM SEDDGLENGS SDEEAEEEEN AEMTDQYMAV 480
KGIKRRKLEL EEDSEMDLPA FADSDDDLER SSAEEGEAEE ADESSEEEDC TAGEKGISGS 540
KAAGEGSKAG LSPANCQSDR VNLEKSLLMK KAALPTFDSG HCTAEEVFAS EDESEESSSL 600
SAEEEDSENE EAIRKKLSKP SQVSSGQKLG PQNFIDETSD IENLLKEEED YKEENNDSKE 660
TSGALKWKED LSRKAAEAFL RQQQAAPNLR KLIYGTVTED NEEEDDDTLE ELGGLFRVNQ 720
PDRECKHKAD SLDCSRFLVE APHDWDLEEV MNSIRDCFVT GKWEDDKDAA KVLAEDEELY 780
GDFEDLETGD VHKGKSGPNT QNEDIEKEVK EEIDPDEEES AKKKHLDKKR KLKEMFDAEY 840
DEGESTYFDD LKGEMQKQAQ LNRAEFEDQD DEARVQYEGF RPGMYVRIEI ENVPCEFVQN 900
FDPHYPIILG GLGNSEGNVG YVQMRLKKHR WYKKILKSRD PIIFSVGWRR FQTIPLYYIE 960
DHNGRQRLLK YTPQHMHCGA AFWGPITPQG TGFLAIQSVS GIMPDFRIAA TGVVLDLDKS 1020
IKIVKKLKLT GFPYKIFKNT SFIKGMFNSA LEVAKFEGAV IRTVSGIRGQ IKKALRAPEG 1080
AFRASFEDKL LMSDIVFMRT WYPVSIPAFY NPVTSLLKPV GEKDTWSGMR TTGQLRLAHG 1140
VRLKANKDSL YKPILRQKKH FNSLHIPKAL QKALPFKNKP KTQAKAGKVP KDRRRPAVIR 1200
EPHERKILAL LDALSTVHSQ KMKKAKEQRH LHNKEHFRAK QKEEEEKLKR QKDLRKKLFR 1260
IQGQKERRNQ KSSLKGAEGQ LQ 1282 
Gene Ontology
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042255; P:ribosome assembly; ISS:UniProtKB. 
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