CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019199
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Molybdenum cofactor sulfurase 
Protein Synonyms/Alias
 MCS; MOS; MoCo sulfurase; hMCS 
Gene Name
 MOCOS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
220LSWIEEVKSGRLHPVubiquitination[1, 2, 3]
329FLDVIALKHGFDTLEubiquitination[1, 2]
442ISNEMVRKHFQAGHVubiquitination[2]
570TQPTPSEKAAGVLEGubiquitination[2, 3]
593NLYLYPIKSCAAFEVubiquitination[2]
629NGVCLSQKQEPRLCLubiquitination[2]
653RIMVIKAKGMEPIEVubiquitination[1, 3]
830RNQHVFQKLSESRETubiquitination[1, 2]
Reference
 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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
Functional Description
 Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime. 
Sequence Annotation
 DOMAIN 706 867 MOSC.
 ACT_SITE 424 424 By similarity.
 MOD_RES 264 264 N6-(pyridoxal phosphate)lysine (By
 MOD_RES 528 528 Phosphoserine.
 MOD_RES 530 530 Phosphoserine.  
Keyword
 Complete proteome; Disease mutation; Molybdenum cofactor biosynthesis; Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 888 AA 
Protein Sequence
MAGAAAESGR ELWTFAGSRD PSAPRLAYGY GPGSLRELRA REFSRLAGTV YLDHAGATLF 60
SQSQLESFTS DLMENTYGNP HSQNISSKLT HDTVEQVRYR ILAHFHTTAE DYTVIFTAGS 120
TAALKLVAEA FPWVSQGPES SGSRFCYLTD SHTSVVGMRN VTMAINVIST PVRPEDLWSA 180
EERSASASNP DCQLPHLFCY PAQSNFSGVR YPLSWIEEVK SGRLHPVSTP GKWFVLLDAA 240
SYVSTSPLDL SAHQADFVPI SFYKIFGFPT GLGALLVHNR AAPLLRKTYF GGGTASAYLA 300
GEDFYIPRQS VAQRFEDGTI SFLDVIALKH GFDTLERLTG GMENIKQHTF TLAQYTYVAL 360
SSLQYPNGAP VVRIYSDSEF SSPEVQGPII NFNVLDDKGN IIGYSQVDKM ASLYNIHLRT 420
GCFCNTGACQ RHLGISNEMV RKHFQAGHVC GDNMDLIDGQ PTGSVRISFG YMSTLDDVQA 480
FLRFIIDTRL HSSGDWPVPQ AHADTGETGA PSADSQADVI PAVMGRRSLS PQEDALTGSR 540
VWNNSSTVNA VPVAPPVCDV ARTQPTPSEK AAGVLEGALG PHVVTNLYLY PIKSCAAFEV 600
TRWPVGNQGL LYDRSWMVVN HNGVCLSQKQ EPRLCLIQPF IDLRQRIMVI KAKGMEPIEV 660
PLEENSERTQ IRQSRVCADR VSTYDCGEKI SSWLSTFFGR PCHLIKQSSN SQRNAKKKHG 720
KDQLPGTMAT LSLVNEAQYL LINTSSILEL HRQLNTSDEN GKEELFSLKD LSLRFRANII 780
INGKRAFEEE KWDEISIGSL RFQVLGPCHR CQMICIDQQT GQRNQHVFQK LSESRETKVN 840
FGMYLMHASL DLSSPCFLSV GSQVLPVLKE NVEGHDLPAS EKHQDVTS 888 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IMP:UniProtKB.
 GO:0030151; F:molybdenum ion binding; IEA:InterPro.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
 GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
 GO:0032324; P:molybdopterin cofactor biosynthetic process; TAS:Reactome.
 GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome. 
Interpro
 IPR000192; Aminotrans_V/Cys_dSase.
 IPR005302; MoCF_Sase_C.
 IPR005303; MOSC_N.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2.
 IPR011037; Pyrv_Knase-like_insert_dom. 
Pfam
 PF00266; Aminotran_5
 PF03473; MOSC
 PF03476; MOSC_N 
SMART
  
PROSITE
 PS00595; AA_TRANSFER_CLASS_5
 PS51340; MOSC 
PRINTS