CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015080
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 All-trans-retinol 13,14-reductase 
Protein Synonyms/Alias
 All-trans-13,14-dihydroretinol saturase; RetSat; PPAR-alpha-regulated and starvation-induced gene protein 
Gene Name
 RETSAT 
Gene Synonyms/Alias
 PPSIG; UNQ439/PRO872 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
48PAPLVTDKEARKKVLubiquitination[1]
56EARKKVLKQAFSANQubiquitination[1]
111GCCHTFGKNGLEFDTubiquitination[2]
165LEGPNGRKEYPMYSGubiquitination[1, 3]
174YPMYSGEKAYIQGLKubiquitination[4, 5, 6]
181KAYIQGLKEKFPQEEubiquitination[1]
183YIQGLKEKFPQEEAIacetylation[7]
183YIQGLKEKFPQEEAIubiquitination[1]
193QEEAIIDKYIKLVKVubiquitination[1]
199DKYIKLVKVVSSGAPubiquitination[4, 6]
317AGGAVLTKATVQSVLubiquitination[1]
597RNLYSDLKNLDSRIRubiquitination[1, 3]
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] 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]
 [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]
 [4] 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]
 [5] 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]
 [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] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Retinol saturase carrying out the saturation of the 13- 14 double bond of all-trans-retinol to produce all-trans-13,14- dihydroretinol. Has activity toward all-trans-retinol as substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers as substrates. May play a role in the metabolism of vitamin A (By similarity). 
Sequence Annotation
 NP_BIND 70 98 FAD or NAD or NADP (Potential).  
Keyword
 Alternative splicing; Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; NAD; NADP; Oxidoreductase; Polymorphism; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 610 AA 
Protein Sequence
MWLPLVLLLA VLLLAVLCKV YLGLFSGSSP NPFSEDVKRP PAPLVTDKEA RKKVLKQAFS 60
ANQVPEKLDV VVIGSGFGGL AAAAILAKAG KRVLVLEQHT KAGGCCHTFG KNGLEFDTGI 120
HYIGRMEEGS IGRFILDQIT EGQLDWAPLS SPFDIMVLEG PNGRKEYPMY SGEKAYIQGL 180
KEKFPQEEAI IDKYIKLVKV VSSGAPHAIL LKFLPLPVVQ LLDRCGLLTR FSPFLQASTQ 240
SLAEVLQQLG ASSELQAVLS YIFPTYGVTP NHSAFSMHAL LVNHYMKGGF YPRGGSSEIA 300
FHTIPVIQRA GGAVLTKATV QSVLLDSAGK ACGVSVKKGH ELVNIYCPIV VSNAGLFNTY 360
EHLLPGNARC LPGVKQQLGT VRPGLGMTSV FICLRGTKED LHLPSTNYYV YYDTDMDQAM 420
ERYVSMPREE AAEHIPLLFF AFPSAKDPTW EDRFPGRSTM IMLIPTAYEW FEEWQAELKG 480
KRGSDYETFK NSFVEASMSV VLKLFPQLEG KVESVTAGSP LTNQFYLAAP RGACYGADHD 540
LGRLHPCVMA SLRAQSPIPN LYLTGQDIFT CGLVGALQGA LLCSSAILKR NLYSDLKNLD 600
SRIRAQKKKN 610 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC.
 GO:0005640; C:nuclear outer membrane; ISS:HGNC.
 GO:0051786; F:all-trans-retinol 13,14-reductase activity; ISS:HGNC.
 GO:0042572; P:retinol metabolic process; ISS:HGNC. 
Interpro
  
Pfam
  
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PRINTS