Tag | Content |
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CPLM ID | CPLM-039025 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aldehyde oxidase |
Protein Synonyms/Alias | |
Gene Name | Aox1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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233 | ELVEAKFKYPGAPIV | acetylation | [1] | 486 | AGSAPGGKVEFKRTL | acetylation | [1] | 936 | QIDNTHYKQEFSAKT | acetylation | [1] | 966 | ERKTAVGKFNAENSW | acetylation | [1] |
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Reference | [1] 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] |
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 | 1309 AA |
Protein Sequence | MLLPYLRKNL RLTGTKYGCG GGGCGACTVM ISRYNPSTKS IRHHPVNACL TPICSLYGTA 60 VTTVEGIGNT RTRLHPVQER IAKCHGTQCG FCTPGMVMSM YALLRNHPEP SLDQLTDALG 120 GNLCRCTGYR PIIDACKTFC RASGCCESKE NGVCCLDQGI NGSAEFQEGD ETSPELFSEK 180 EFQPLDPTQE LIFPPELMRI AEKQPPKTRV FYSNRMTWIS PVTLEELVEA KFKYPGAPIV 240 MGYTSVGPEV KFKGVFHPII ISPDRIEELS IINQTGDGLT LGAGLSLDQV KDILTDVVQK 300 LPEETTQTYR ALLKHLRTLA GSQIRNMASL GGHIVSRHLD SDLNPLLAVG NCTLNLLSKD 360 GKRQIPLSEQ FLRKCPDSDL KPQEVLVSVN IPFPLSWEFV SAFRQAQRQQ NALAIVNSGM 420 RVLFREGGGV IKELSILYGG VGPTTIGAKN SCQKLIGRPW NEEMLDTACR LVLDEVTLAG 480 SAPGGKVEFK RTLIISFLFK FYLEVLQGLK REDPGHYPSL TNNYESALED LHSKHHWRTL 540 THQNVDSMQL PQDPIGRPIM HLSGIKHATG EAIYCDDMPA VDRELFLTFV TSSRAHAKIV 600 SIDLSEALSL PGVVDIITAD HLQDTTTFGT ETLLATDKVH CVGQLVCAVI ADSETRAKQA 660 AKHVKVVYRD LEPLILTIEE AIQHKSFFES ERKLECGNVD EAFKIADQIL EGEIHIGGQE 720 HFYMETQSML VVPKGEDGEI DIYVSTQFPK HIQDIVAATL KLSVNKVMCH VRRVGGAFGG 780 KVGKTSIMAA ITAFAASKHG RAVRCTLERG EDMLITGGRH PYLGKYKVGF MRDGRIVALD 840 VEHYCNGGSS LDESLWVIEM GLLKMDNAYK FPNLRCRGWA CRTNLPSNTA LRGFGFPQAG 900 LVTEACVTEV AIRCGLSPEQ VRTINMYKQI DNTHYKQEFS AKTLFECWRE CMAKCSYSER 960 KTAVGKFNAE NSWKKRGMAV IPLKFPVGVG SVAMGQAAAL VHIYLDGSAL VSHGGIEMGQ 1020 GVHTKMIQVV SRELKMPMSS VHLRGTSTET VPNTNASGGS VVADLNGLAV KDACQTLLKR 1080 LEPIISKNPQ GTWKDWAQTA FDQSVSLSAV GYFRGYESNI NWEKGEGHPF EYFVYGAACS 1140 EVEIDCLTGD HKNIRTDIVM DVGHSINPAL DIGQVEGAFI QGMGLYTIEE LSYSPQGILY 1200 SRGPNQYKIP AICDIPTEMH ISFLPPSEHS NTLYSSKGLG ESGVFLGCSV FFAIHDAVRA 1260 ARQERGISGP WKLTSPLTPE KIRMACEDKF TKMIPRDEPG SYVPWNIPV 1309 |
Gene Ontology | GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. 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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |