CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001287
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Short-chain dehydrogenase/reductase 3 
Protein Synonyms/Alias
 DD83.1; Retinal short-chain dehydrogenase/reductase 1; retSDR1 
Gene Name
 DHRS3 
Gene Synonyms/Alias
 UNQ2424/PRO4983 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32VGLVLPAKLRDLSREubiquitination[1]
130NAAVVHGKSLMDSDDubiquitination[2]
142SDDDALLKSQHINTLubiquitination[2, 3, 4]
156LGQFWTTKAFLPRMLubiquitination[1, 3, 4]
242PNLFPPLKPETVARRubiquitination[2, 4]
299YTCMNTFKGRT****ubiquitination[1]
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] 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] 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
Functional Description
 Catalyzes the reduction of all-trans-retinal to all- trans-retinol in the presence of NADPH. 
Sequence Annotation
 ACT_SITE 188 188 Proton acceptor (By similarity).
 BINDING 175 175 Substrate (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Membrane; NADP; Oxidoreductase; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 302 AA 
Protein Sequence
MVWKRLGALV MFPLQMIYLV VKAAVGLVLP AKLRDLSREN VLITGGGRGI GRQLAREFAE 60
RGARKIVLWG RTEKCLKETT EEIRQMGTEC HYFICDVGNR EEVYQTAKAV REKVGDITIL 120
VNNAAVVHGK SLMDSDDDAL LKSQHINTLG QFWTTKAFLP RMLELQNGHI VCLNSVLALS 180
AIPGAIDYCT SKASAFAFME SLTLGLLDCP GVSATTVLPF HTSTEMFQGM RVRFPNLFPP 240
LKPETVARRT VEAVQLNQAL LLLPWTMHAL VILKSILPQA ALEEIHKFSG TYTCMNTFKG 300
RT 302 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0042622; C:photoreceptor outer segment membrane; TAS:Reactome.
 GO:0009055; F:electron carrier activity; TAS:UniProtKB.
 GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:EC.
 GO:0000166; F:nucleotide binding; TAS:ProtInc.
 GO:0007603; P:phototransduction, visible light; TAS:Reactome.
 GO:0042572; P:retinol metabolic process; TAS:UniProtKB.
 GO:0007601; P:visual perception; TAS:ProtInc. 
Interpro
 IPR002198; DH_sc/Rdtase_SDR.
 IPR002347; Glc/ribitol_DH.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF00106; adh_short 
SMART
  
PROSITE
 PS00061; ADH_SHORT 
PRINTS
 PR00081; GDHRDH.
 PR00080; SDRFAMILY.