CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-033039
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Inosine-5'-monophosphate dehydrogenase 
Protein Synonyms/Alias
 IMP dehydrogenase; IMPD; IMPDH 
Gene Name
 IMPDH1 
Gene Synonyms/Alias
 IMPDH 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
194APAGVTLKEANEILQubiquitination[1, 2]
205EILQRSKKGKLPIVNubiquitination[1, 3]
207LQRSKKGKLPIVNDCubiquitination[1, 2, 4]
241LASKDSQKQLLCGAAubiquitination[1, 2, 4, 5]
310VVTAAQAKNLIDAGVubiquitination[3, 6]
409SDGVRLKKYRGMGSLubiquitination[6]
421GSLDAMEKSSSSQKRubiquitination[1]
435RYFSEGDKVKIAQGVacetylation[2]
435RYFSEGDKVKIAQGVubiquitination[1]
437FSEGDKVKIAQGVSGubiquitination[1]
449VSGSIQDKGSIQKFVubiquitination[1, 6]
454QDKGSIQKFVPYLIAubiquitination[1]
Reference
 [1] 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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] 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] 
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 113 172 CBS 1 (By similarity).
 DOMAIN 178 236 CBS 2 (By similarity).
 NP_BIND 273 275 NAD (By similarity).
 NP_BIND 323 325 NAD (By similarity).
 REGION 363 365 IMP binding (By similarity).
 REGION 386 387 IMP binding (By similarity).
 REGION 410 414 IMP binding (By similarity).
 ACT_SITE 330 330 Thioimidate intermediate (By similarity).
 METAL 325 325 Potassium; via carbonyl oxygen (By
 METAL 327 327 Potassium; via carbonyl oxygen (By
 METAL 330 330 Potassium; via carbonyl oxygen (By
 METAL 495 495 Potassium; via carbonyl oxygen; shared
 BINDING 328 328 IMP (By similarity).
 BINDING 440 440 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
 513 AA 
Protein Sequence
MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT 60
LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKFE QGFITDPVVL 120
SPSHTVGDVL EAKMRHGFSG IPITETGTMG SKLVGIVTSR DIDFLAEKDH TTLLSEVMTP 180
RIELVVAPAG VTLKEANEIL QRSKKGKLPI VNDCDELVAI IARTDLKKNR DYPLASKDSQ 240
KQLLCGAAVG TREDDKYRLD LLTQAGVDVI VLDSSQGNSV YQIAMVHYIK QKYPHLQVIG 300
GNVVTAAQAK NLIDAGVDGL RVGMGCGSIC ITQEVMACGR PQGTAVYKVA EYARRFGVPI 360
IADGGIQTVG HVVKALALGA STVMMGSLLA ATTEAPGEYF FSDGVRLKKY RGMGSLDAME 420
KSSSSQKRYF SEGDKVKIAQ GVSGSIQDKG SIQKFVPYLI AGIQHGCQDI GARSLSVLRS 480
MMYSGELKFE KRTMSAQIEG GVHGLHSYEK RLY 513 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003938; F:IMP dehydrogenase activity; IEA:HAMAP.
 GO:0046872; F:metal ion binding; IEA:HAMAP.
 GO:0000166; F:nucleotide binding; IEA:HAMAP.
 GO:0006177; P:GMP biosynthetic process; IEA:HAMAP. 
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