Tag | Content |
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CPLM ID | CPLM-004836 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | NADH-cytochrome b5 reductase 3 |
Protein Synonyms/Alias | B5R; Cytochrome b5 reductase; Diaphorase-1; NADH-cytochrome b5 reductase 3 membrane-bound form; NADH-cytochrome b5 reductase 3 soluble form |
Gene Name | Cyb5r3 |
Gene Synonyms/Alias | Dia1 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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25 | FVYSLFMKLFQRSSP | acetylation | [1] | 42 | TLENPDIKYPLRLID | acetylation | [1] | 50 | YPLRLIDKEIISHDT | acetylation | [1] | 115 | LVVKVYFKDTHPKFP | acetylation | [1] | 120 | YFKDTHPKFPAGGKM | acetylation | [1] | 156 | LVYQGKGKFAIRADK | 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 | Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. |
Sequence Annotation | DOMAIN 40 152 FAD-binding FR-type. NP_BIND 132 147 FAD. NP_BIND 171 206 FAD. MOD_RES 42 42 N6-acetyllysine (By similarity). MOD_RES 43 43 Phosphotyrosine (By similarity). MOD_RES 120 120 N6-acetyllysine (By similarity). MOD_RES 130 130 Phosphotyrosine (By similarity). LIPID 2 2 N-myristoyl glycine. |
Keyword | 3D-structure; Acetylation; Alternative initiation; Alternative promoter usage; Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; Myristate; NAD; Oxidoreductase; Phosphoprotein; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 301 AA |
Protein Sequence | MGAQLSTLSR VVLSPVWFVY SLFMKLFQRS SPAITLENPD IKYPLRLIDK EIISHDTRRF 60 RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD DDKGFVDLVV KVYFKDTHPK 120 FPAGGKMSQY LENMNIGDTI EFRGPNGLLV YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG 180 GTGITPMLQV IRAVLKDPND HTVCYLLFAN QSEKDILLRP ELEELRNEHS SRFKLWYTVD 240 KAPDAWDYSQ GFVNEEMIRD HLPPPGEETL ILMCGPPPMI QFACLPNLER VGHPKERCFT 300 F 301 |
Gene Ontology | GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC. GO:0005811; C:lipid particle; IEA:Compara. GO:0005743; C:mitochondrial inner membrane; IEA:Compara. GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. GO:0043531; F:ADP binding; IDA:RGD. GO:0016208; F:AMP binding; IDA:RGD. GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; TAS:RGD. GO:0071949; F:FAD binding; IEA:Compara. GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD. GO:0051287; F:NAD binding; IDA:RGD. GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. |
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