Tag | Content |
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CPLM ID | CPLM-024726 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Inosine-5'-monophosphate dehydrogenase 1 |
Protein Synonyms/Alias | IMP dehydrogenase 1; IMPD 1; IMPDH 1 |
Gene Name | Impdh1 |
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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436 | RYFSEGDKVKIAQGV | acetylation | [1] | 511 | HGLHSYEKRLY**** | 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 | Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors (By similarity). |
Sequence Annotation | DOMAIN 114 173 CBS 1. DOMAIN 179 237 CBS 2. NP_BIND 274 276 NAD (By similarity). NP_BIND 324 326 NAD (By similarity). REGION 364 366 IMP binding (By similarity). REGION 387 388 IMP binding (By similarity). REGION 411 415 IMP binding (By similarity). ACT_SITE 331 331 Thioimidate intermediate (By similarity). METAL 326 326 Potassium; via carbonyl oxygen (By METAL 328 328 Potassium; via carbonyl oxygen (By METAL 331 331 Potassium; via carbonyl oxygen (By METAL 500 500 Potassium; via carbonyl oxygen; shared METAL 501 501 Potassium; via carbonyl oxygen; shared METAL 502 502 Potassium; via carbonyl oxygen; shared BINDING 329 329 IMP (By similarity). BINDING 441 441 IMP (By similarity). |
Keyword | CBS domain; Complete proteome; Cytoplasm; GMP biosynthesis; Metal-binding; NAD; Nucleus; Oxidoreductase; Potassium; Purine biosynthesis; Reference proteome; Repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 514 AA |
Protein Sequence | MADYLISGGT GYVPEDGLTA QQLFANADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT 60 LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV 120 LSPSHTVGDV LEAKIQHGFS GIPITATGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT 180 PRIELVVAPA GVTLKEANEI LQRSKKGKLP IVNDQDELVA IIARTDLKKN RDYPLASKDS 240 HKQLLCGAAV GTREDDKYRL DLLTQAGADV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI 300 GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP 360 VIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM 420 EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGAQSLSVLR 480 SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY 514 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |