CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013866
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Molybdenum cofactor biosynthesis protein 1 
Protein Synonyms/Alias
 Cyclic pyranopterin monophosphate synthase; Molybdenum cofactor biosynthesis protein A; Cyclic pyranopterin monophosphate synthase accessory protein; Molybdenum cofactor biosynthesis protein C 
Gene Name
 Mocs1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
265FKKMVSYKEMLDTIRubiquitination[1]
520LLGPVAFKLVQQNQLacetylation[2]
528LVQQNQLKKGDALVVacetylation[2, 3, 4, 5]
625TEVKLISKTGGQRGDacetylation[6]
625TEVKLISKTGGQRGDsuccinylation[6]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 Isoform Mocs1a and isoform Mocs1b probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z) (By similarity). 
Sequence Annotation
 REGION 1 383 Molybdenum cofactor biosynthesis protein
 REGION 317 319 GTP binding (By similarity).
 REGION 414 636 Molybdenum cofactor biosynthesis protein
 ACT_SITE 606 606 For molybdenum cofactor biosynthesis
 METAL 80 80 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By
 METAL 84 84 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By
 METAL 87 87 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By
 METAL 312 312 Iron-sulfur 2 (4Fe-4S-substrate) (By
 METAL 315 315 Iron-sulfur 2 (4Fe-4S-substrate) (By
 METAL 329 329 Iron-sulfur 2 (4Fe-4S-substrate) (By
 BINDING 73 73 GTP (By similarity).
 BINDING 86 86 S-adenosyl-L-methionine (By similarity).
 BINDING 123 123 GTP (By similarity).
 BINDING 127 127 S-adenosyl-L-methionine; via carbonyl
 BINDING 154 154 GTP (By similarity).
 BINDING 178 178 S-adenosyl-L-methionine (By similarity).
 BINDING 215 215 GTP (By similarity).
 BINDING 249 249 S-adenosyl-L-methionine; via amide
 MOD_RES 198 198 N6-acetyllysine (By similarity).  
Keyword
 4Fe-4S; Acetylation; Alternative splicing; Complete proteome; GTP-binding; Iron; Iron-sulfur; Lyase; Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome; S-adenosyl-L-methionine. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 636 AA 
Protein Sequence
MAARPAFGIV RQLLRSNARG CSSGAPVTQP RPGEPSRPTR EGLSLRLQFL QEHAAPFSAF 60
LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAD LLTTEEILTL ARLFVKEGVD 120
KIRLTGGEPL IRPDVVDIVA RLHGLEGLRT IGLTTNGINL ARLLPRLQQA GLNAVNISLD 180
TLVPAKFEFI VRRKGFHKVM EGIHKAIELG YKPVKVNCVV MRGLNEDELL DFVALTEGLP 240
LDVRFIEYMP FDGNKWNFKK MVSYKEMLDT IRQRWPGLEK LPEEDSSTAK AFKIPGFQGQ 300
ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEEE LLRIIGAAVG 360
RKKRQHAGMF NIAQMKNRPM ILIGVLLMLQ DSPPARWSNF SWDPLRVRNP SARQCLSDQM 420
ASLWKRHCIP KALPLSQQCL GSGSPQRHYS SYPDPDTHSK CLSTGSQAPD APSGPGPTSN 480
QLTHVDSAGR ASMVDVGGKP ETERVAVASA MVLLGPVAFK LVQQNQLKKG DALVVAQLAG 540
VQAAKLTSQL IPLCHHVALS HVQVHLELDS TRHAVLIQAS CRARGPTGVE MEALTSAAMA 600
ALTVYDMCKA VSRDIVVTEV KLISKTGGQR GDFHRA 636 
Gene Ontology
 GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
 GO:0032324; P:molybdopterin cofactor biosynthetic process; IMP:MGI. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR006638; Elp3/MiaB/NifB.
 IPR023045; Mo_CF_biosynth-C.
 IPR023046; Mo_CF_biosynth-C_bac.
 IPR013483; MoaA.
 IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
 IPR010505; Mob_synth_C.
 IPR002820; Mopterin_CF_biosynth-C_dom.
 IPR007197; rSAM. 
Pfam
 PF01967; MoaC
 PF06463; Mob_synth_C
 PF04055; Radical_SAM 
SMART
 SM00729; Elp3 
PROSITE
 PS01305; MOAA_NIFB_PQQE 
PRINTS