CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041794
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aldehyde oxidase 
Protein Synonyms/Alias
 Aldehyde oxidase 1 
Gene Name
 Aox1 
Gene Synonyms/Alias
 mCG_117465 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
18NGQKVVEKNVDPEMMubiquitination[1]
227ELMRIAEKQPPKTRVubiquitination[1]
249WISPVTLKELVEAKFubiquitination[1]
257ELVEAKFKYPQAPIVubiquitination[1]
324ILADIVQKLPEEKTQubiquitination[1]
952VRTINMYKHVDTTHYubiquitination[1]
960HVDTTHYKQEFSAKAubiquitination[1]
1095DLNGLAVKDACQTLLubiquitination[1]
1103DACQTLLKRLEPIISubiquitination[1]
1111RLEPIISKNPQGTWKubiquitination[1]
1296RGISGPWKLNSPLTPubiquitination[1]
1305NSPLTPEKIRMACEDubiquitination[1]
1316ACEDKFTKMIPRDEPubiquitination[1]
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
Functional Description
  
Sequence Annotation
  
Keyword
 2Fe-2S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1333 AA 
Protein Sequence
MDPIQLLFYV NGQKVVEKNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA CTVMISRYNP 60
STKAIRHHPV NACLTPICSL HGTAVTTVEG LGNTRTRLHP IQERIAKCHG TQCGFCTPGM 120
VMSMYALLRN HPEPTLDQLT DALGGNLCRC TGYRPIIDAC KTFCKASGCC QSKENGVCCL 180
DQEINGLAES QEEDKTSPEL FSEEEFLPLD PTQELIFPPE LMRIAEKQPP KTRVFYGERV 240
TWISPVTLKE LVEAKFKYPQ APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELGVISQAR 300
DGLTLGAGLS LDQVKDILAD IVQKLPEEKT QTYRALLKHL RTLAGSQIRN MASLGGHIVS 360
RHLDSDLNPL LAVGNCTLNL LSKDGERRIP LSEEFLRKCP EADLKPQEVL VSVNIPWSRK 420
WEFVSAFRQA QRQQNALAIV NSGMRVLFRE GGGVIEELSI LYGGVGSTII SAKNSCQRLI 480
GRPWNEGMLD TACRLVLDEV TLAASAPGGK VEFKRTLIIS FLFKFYLEVS QGLKREDPGH 540
SPSLAGNHES ALDDLHSKHP WRTLTHQNVD PAQLPQDPIG RPIMHLSGIK HATGEAIYCD 600
DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQEAN TFGTETFLAT 660
DEVHCVGHLV CAVIADSETR AKQAAKQVKV VYQDLAPLIL TIEEAIQHKS FFKSERKLEC 720
GNVDEAFKIV DQILEGEIHI GGQEHFYMET QSMLVVPKGE DGEIDIYVST QFPKYIQDIV 780
AATLKLSANK VMCHVRRVGG AFGGKVGKTS ILAAITAFAA SKHGRAVRCI LERGEDMLIT 840
GGRHPYLGKY KAGFMNDGRI LALDVEHYCN GGCSLDESLW VIEMGLLKLD NAYKFPNLRC 900
RGWACRTNLP SNTALRGFGF PQAGLVTEAC ITEVAIKCGL SPEQVRTINM YKHVDTTHYK 960
QEFSAKALSE CWRECMAKCS YFERKAAIGK FNAENSWKKR GMAVIPLKFP VGIGSVAMGQ 1020
AAALVHIYLD GSALVSHGGI EMGQGVHTKM IQVVSRELRM PMSSVHLRGT STETVPNTNA 1080
SGGSVVADLN GLAVKDACQT LLKRLEPIIS KNPQGTWKDW AQTAFDQSIS LSAVGYFRGY 1140
ESNIDWEKGE GHPFEYFVFG AACSEVEIDC LTGDHKNIRT NIVMDVGHSI NPALDIGQVE 1200
GAFIQGMGLY TIEELSYSPQ GTLYSRGPNQ YKIPAICDIP TEMHISFLPP SEHSNTLYSS 1260
KGLGESGVFL GCSVFFAIHD AVKAARQERG ISGPWKLNSP LTPEKIRMAC EDKFTKMIPR 1320
DEPGSYVPWN IPV 1333 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0004031; F:aldehyde oxidase activity; IDA:MGI.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. 
Interpro
 IPR002888; 2Fe-2S-bd.
 IPR001041; 2Fe-2S_ferredoxin-type.
 IPR006058; 2Fe2S_fd_BS.
 IPR000674; Ald_Oxase/Xan_DH_a/b.
 IPR016208; Ald_Oxase/xanthine_DH.
 IPR014313; Aldehyde_oxidase.
 IPR008274; AldOxase/xan_DH_Mopterin-bd.
 IPR012675; Beta-grasp_dom.
 IPR005107; CO_DH_flav_C.
 IPR016169; CO_DH_flavot_FAD-bd_sub2.
 IPR016166; FAD-bd_2.
 IPR016167; FAD-bd_2_sub1.
 IPR002346; Mopterin_DH_FAD-bd.
 IPR022407; OxRdtase_Mopterin_BS. 
Pfam
 PF01315; Ald_Xan_dh_C
 PF02738; Ald_Xan_dh_C2
 PF03450; CO_deh_flav_C
 PF00941; FAD_binding_5
 PF00111; Fer2
 PF01799; Fer2_2 
SMART
 SM01008; Ald_Xan_dh_C
 SM01092; CO_deh_flav_C 
PROSITE
 PS00197; 2FE2S_FER_1
 PS51085; 2FE2S_FER_2
 PS51387; FAD_PCMH
 PS00559; MOLYBDOPTERIN_EUK 
PRINTS