CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014094
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MOSC domain-containing protein 1, mitochondrial 
Protein Synonyms/Alias
 Mitochondrial amidoxime reducing component 1; mARC1; Moco sulfurase C-terminal domain-containing protein 1; Molybdenum cofactor sulfurase C-terminal domain-containing protein 1 
Gene Name
 MARC1 
Gene Synonyms/Alias
 MOSC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67QLWIYPVKSCKGVPVubiquitination[1]
174QWITSFLKSQPYRLVubiquitination[2]
265LIGDVELKRVMACSRubiquitination[1]
327LENPGTIKVGDPVYLubiquitination[3]
Reference
 [1] 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]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473
Functional Description
 As a component of an N-hydroxylated prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively. 
Sequence Annotation
 DOMAIN 187 335 MOSC.  
Keyword
 Alternative splicing; Complete proteome; Membrane; Mitochondrion; Mitochondrion outer membrane; Molybdenum; Oxidoreductase; Polymorphism; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 337 AA 
Protein Sequence
MGAAGSSALA RFVLLAQSRP GWLGVAALGL TAVALGAVAW RRAWPTRRRR LLQQVGTVAQ 60
LWIYPVKSCK GVPVSEAECT AMGLRSGNLR DRFWLVINQE GNMVTARQEP RLVLISLTCD 120
GDTLTLSAAY TKDLLLPIKT PTTNAVHKCR VHGLEIEGRD CGEATAQWIT SFLKSQPYRL 180
VHFEPHMRPR RPHQIADLFR PKDQIAYSDT SPFLILSEAS LADLNSRLEK KVKATNFRPN 240
IVISGCDVYA EDSWDELLIG DVELKRVMAC SRCILTTVDP DTGVMSRKEP LETLKSYRQC 300
DPSERKLYGK SPLFGQYFVL ENPGTIKVGD PVYLLGQ 337 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; ISS:UniProtKB.
 GO:0030151; F:molybdenum ion binding; IDA:UniProtKB.
 GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
 GO:0008940; F:nitrate reductase activity; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0051410; P:detoxification of nitrogen compound; NAS:UniProtKB.
 GO:0042126; P:nitrate metabolic process; IDA:UniProtKB. 
Interpro
 IPR005302; MoCF_Sase_C.
 IPR005303; MOSC_N.
 IPR011037; Pyrv_Knase-like_insert_dom. 
Pfam
 PF03473; MOSC
 PF03476; MOSC_N 
SMART
  
PROSITE
 PS51340; MOSC 
PRINTS