CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015406
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DBH-like monooxygenase protein 1 
Protein Synonyms/Alias
 Monooxygenase X 
Gene Name
 MOXD1 
Gene Synonyms/Alias
 MOX; UNQ2493/PRO5780 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36TLLDSEGKYWLGWSQubiquitination[1, 2]
Reference
 [1] 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]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
  
Sequence Annotation
 DOMAIN 35 148 DOMON.
 ACT_SITE 203 203 Potential.
 ACT_SITE 389 389 Potential.
 METAL 235 235 Copper A (By similarity).
 METAL 236 236 Copper A (By similarity).
 METAL 307 307 Copper A (By similarity).
 METAL 389 389 Copper B (By similarity).
 METAL 391 391 Copper B (By similarity).
 METAL 464 464 Copper B (By similarity).
 CARBOHYD 114 114 N-linked (GlcNAc...) (Potential).
 CARBOHYD 247 247 N-linked (GlcNAc...) (Potential).
 CARBOHYD 476 476 N-linked (GlcNAc...) (Potential).
 CARBOHYD 517 517 N-linked (GlcNAc...) (Potential).
 DISULFID 205 257 By similarity.
 DISULFID 242 269 By similarity.
 DISULFID 364 480 By similarity.
 DISULFID 368 550 By similarity.
 DISULFID 443 465 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Copper; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Polymorphism; Reference proteome; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 613 AA 
Protein Sequence
MCCWPLLLLW GLLPGTAAGG SGRTYPHRTL LDSEGKYWLG WSQRGSQIAF RLQVRTAGYV 60
GFGFSPTGAM ASADIVVGGV AHGRPYLQDY FTNANRELKK DAQQDYHLEY AMENSTHTII 120
EFTRELHTCD INDKSITDST VRVIWAYHHE DAGEAGPKYH DSNRGTKSLR LLNPEKTSVL 180
STALPYFDLV NQDVPIPNKD TTYWCQMFKI PVFQEKHHVI KVEPVIQRGH ESLVHHILLY 240
QCSNNFNDSV LESGHECYHP NMPDAFLTCE TVIFAWAIGG EGFSYPPHVG LSLGTPLDPH 300
YVLLEVHYDN PTYEEGLIDN SGLRLFYTMD IRKYDAGVIE AGLWVSLFHT IPPGMPEFQS 360
EGHCTLECLE EALEAEKPSG IHVFAVLLHA HLAGRGIRLR HFRKGKEMKL LAYDDDFDFN 420
FQEFQYLKEE QTILPGDNLI TECRYNTKDR AEMTWGGLST RSEMCLSYLL YYPRINLTRC 480
ASIPDIMEQL QFIGVKEIYR PVTTWPFIIK SPKQYKNLSF MDAMNKFKWT KKEGLSFNKL 540
VLSLPVNVRC SKTDNAEWSI QGMTALPPDI ERPYKAEPLV CGTSSSSSLH RDFSINLLVC 600
LLLLSCTLST KSL 613 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005507; F:copper ion binding; IEA:InterPro.
 GO:0004500; F:dopamine beta-monooxygenase activity; IEA:InterPro.
 GO:0006584; P:catecholamine metabolic process; IEA:InterPro. 
Interpro
 IPR014784; Cu2_ascorb_mOase-like_C.
 IPR000323; Cu2_ascorb_mOase_N.
 IPR005018; DOMON_domain.
 IPR000945; Dopamine_b_mOase.
 IPR008977; PHM/PNGase_F_dom. 
Pfam
 PF01082; Cu2_monooxygen
 PF03351; DOMON 
SMART
 SM00664; DoH 
PROSITE
 PS00084; CU2_MONOOXYGENASE_1
 PS00085; CU2_MONOOXYGENASE_2
 PS50836; DOMON 
PRINTS
 PR00767; DBMONOXGNASE.