CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000959
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GDP-mannose 4,6 dehydratase 
Protein Synonyms/Alias
 GDP-D-mannose dehydratase; GMD 
Gene Name
 GMDS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21SGDGEMGKPRNVALIubiquitination[1]
70GRIEHLYKNPQAHIEacetylation[2]
70GRIEHLYKNPQAHIEubiquitination[1, 3, 4]
101VKIINEVKPTEIYNLubiquitination[1, 4]
140LRLLDAVKTCGLINSubiquitination[4]
149CGLINSVKFYQASTSubiquitination[4]
161STSELYGKVQEIPQKubiquitination[1, 4, 5]
168KVQEIPQKETTPFYPubiquitination[3, 4]
246SLGNLDAKRDWGHAKubiquitination[4]
301KTIVWEGKNENEVGRubiquitination[1, 4]
322VHVTVDLKYYRPTEVacetylation[5]
340QGDCTKAKQKLNWKPubiquitination[4]
Reference
 [1] 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]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Catalyzes the conversion of GDP-D-mannose to GDP-4- dehydro-6-deoxy-D-mannose. 
Sequence Annotation
 NP_BIND 30 35 NADP.
 NP_BIND 55 58 NADP.
 NP_BIND 86 87 NADP.
 NP_BIND 108 112 NADP.
 ACT_SITE 155 155 By similarity.
 ACT_SITE 157 157 Nucleophile (By similarity).
 ACT_SITE 179 179 Nucleophile (By similarity).
 BINDING 123 123 NADP.
 BINDING 183 183 NADP.
 BINDING 209 209 NADP.
 BINDING 214 214 NADP.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Lyase; NADP; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 372 AA 
Protein Sequence
MAHAPARCPS ARGSGDGEMG KPRNVALITG ITGQDGSYLA EFLLEKGYEV HGIVRRSSSF 60
NTGRIEHLYK NPQAHIEGNM KLHYGDLTDS TCLVKIINEV KPTEIYNLGA QSHVKISFDL 120
AEYTADVDGV GTLRLLDAVK TCGLINSVKF YQASTSELYG KVQEIPQKET TPFYPRSPYG 180
AAKLYAYWIV VNFREAYNLF AVNGILFNHE SPRRGANFVT RKISRSVAKI YLGQLECFSL 240
GNLDAKRDWG HAKDYVEAMW LMLQNDEPED FVIATGEVHS VREFVEKSFL HIGKTIVWEG 300
KNENEVGRCK ETGKVHVTVD LKYYRPTEVD FLQGDCTKAK QKLNWKPRVA FDELVREMVH 360
ADVELMRTNP NA 372 
Gene Ontology
 GO:0005737; C:cytoplasm; IC:UniProtKB.
 GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IDA:UniProtKB.
 GO:0070401; F:NADP+ binding; IDA:UniProtKB.
 GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IDA:UniProtKB.
 GO:0019673; P:GDP-mannose metabolic process; IDA:UniProtKB.
 GO:0007219; P:Notch signaling pathway; ISS:UniProtKB. 
Interpro
 IPR001509; Epimerase_deHydtase.
 IPR006368; GDP_Man_deHydtase.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF01370; Epimerase 
SMART
  
PROSITE
  
PRINTS