CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004903
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; IMPDH-I 
Gene Name
 IMPDH1 
Gene Synonyms/Alias
 IMPD1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
134VGDVLEAKMRHGFSGubiquitination[1, 2]
169DIDFLAEKDHTTLLSubiquitination[3]
195APAGVTLKEANEILQubiquitination[3]
205NEILQRSKKGKLPIVubiquitination[3]
206EILQRSKKGKLPIVNubiquitination[3]
208LQRSKKGKLPIVNDCubiquitination[3]
238RDYPLASKDSQKQLLubiquitination[2]
242LASKDSQKQLLCGAAubiquitination[1, 3]
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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
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. 
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.
 REGION 387 388 IMP binding.
 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.
 BINDING 441 441 IMP (By similarity).  
Keyword
 3D-structure; Alternative splicing; CBS domain; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; DNA-binding; GMP biosynthesis; Leber congenital amaurosis; Metal-binding; NAD; Nucleus; Oxidoreductase; Potassium; Purine biosynthesis; Reference proteome; Repeat; Retinitis pigmentosa; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 514 AA 
Protein Sequence
MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT 60
LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV 120
LSPSHTVGDV LEAKMRHGFS GIPITETGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT 180
PRIELVVAPA GVTLKEANEI LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS 240
QKQLLCGAAV GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI 300
GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP 360
IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM 420
EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGARSLSVLR 480
SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY 514 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0003938; F:IMP dehydrogenase activity; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:HAMAP.
 GO:0000166; F:nucleotide binding; IEA:HAMAP.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006177; P:GMP biosynthetic process; IEA:HAMAP.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR000644; Cysta_beta_synth_core.
 IPR005990; IMP_DH.
 IPR015875; IMP_DH/GMP_Rdtase_CS.
 IPR001093; IMP_DH_GMPRt. 
Pfam
 PF00571; CBS
 PF00478; IMPDH 
SMART
 SM00116; CBS 
PROSITE
 PS51371; CBS
 PS00487; IMP_DH_GMP_RED 
PRINTS