CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012178
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GDP-L-fucose synthase 
Protein Synonyms/Alias
 GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase; Protein FX; Red cell NADP(H)-binding protein; Short-chain dehydrogenase/reductase family 4E member 1 
Gene Name
 TSTA3 
Gene Synonyms/Alias
 SDR4E1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21GGSGLVGKAIQKVVAubiquitination[1, 2, 3, 4, 5, 6]
44DWVFVSSKDADLTDTubiquitination[2, 5]
89YNLDFWRKNVHMNDNubiquitination[3, 4]
147NFGYSYAKRMIDVQNacetylation[7]
Reference
 [1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] 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]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Catalyzes the two-step NADP-dependent conversion of GDP- 4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. 
Sequence Annotation
 NP_BIND 14 20 NADP.
 NP_BIND 170 173 NADP.
 ACT_SITE 143 143 Proton donor/acceptor (By similarity).
 BINDING 147 147 NADP.
 BINDING 186 186 NADP.
 BINDING 194 194 Substrate.
 BINDING 208 208 Substrate.
 BINDING 215 215 Substrate.
 BINDING 277 277 Substrate.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Isomerase; Multifunctional enzyme; NADP; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 321 AA 
Protein Sequence
MGEPQGSMRI LVTGGSGLVG KAIQKVVADG AGLPGEDWVF VSSKDADLTD TAQTRALFEK 60
VQPTHVIHLA AMVGGLFRNI KYNLDFWRKN VHMNDNVLHS AFEVGARKVV SCLSTCIFPD 120
KTTYPIDETM IHNGPPHNSN FGYSYAKRMI DVQNRAYFQQ YGCTFTAVIP TNVFGPHDNF 180
NIEDGHVLPG LIHKVHLAKS SGSALTVWGT GNPRRQFIYS LDLAQLFIWV LREYNEVEPI 240
ILSVGEEDEV SIKEAAEAVV EAMDFHGEVT FDTTKSDGQF KKTASNSKLR TYLPDFRFTP 300
FKQAVKETCA WFTDNYEQAR K 321 
Gene Ontology
 GO:0005737; C:cytoplasm; IC:UniProtKB.
 GO:0050662; F:coenzyme binding; IEA:InterPro.
 GO:0009055; F:electron carrier activity; TAS:UniProtKB.
 GO:0042356; F:GDP-4-dehydro-D-rhamnose reductase activity; TAS:UniProtKB.
 GO:0050577; F:GDP-L-fucose synthase activity; IDA:UniProtKB.
 GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
 GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IDA:UniProtKB.
 GO:0019835; P:cytolysis; IEA:Compara.
 GO:0019673; P:GDP-mannose metabolic process; IDA:UniProtKB.
 GO:0007159; P:leukocyte cell-cell adhesion; NAS:UniProtKB. 
Interpro
 IPR001509; Epimerase_deHydtase.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF01370; Epimerase 
SMART
  
PROSITE
  
PRINTS