CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017295
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NAD(P)H-hydrate epimerase 
Protein Synonyms/Alias
 Apolipoprotein A-I-binding protein; AI-BP; NAD(P)HX epimerase 
Gene Name
 Apoa1bp 
Gene Synonyms/Alias
 Aibp 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
126LVCARHLKLFGYQPTacetylation[1]
138QPTIYYPKRPNKPLFacetylation[2]
138QPTIYYPKRPNKPLFsuccinylation[2]
142YYPKRPNKPLFTGLVacetylation[1, 3]
263FVPPALEKKYQLNLPacetylation[3, 4]
264VPPALEKKYQLNLPSacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 
Functional Description
 Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S- specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. 
Sequence Annotation
 DOMAIN 59 269 YjeF N-terminal.
 REGION 113 117 NAD(P)HX (By similarity).
 REGION 183 189 NAD(P)HX (By similarity).
 METAL 114 114 Potassium (By similarity).
 METAL 179 179 Potassium (By similarity).
 METAL 215 215 Potassium (By similarity).
 BINDING 212 212 NAD(P)HX (By similarity).
 MOD_RES 43 43 Phosphoserine; by PKA.  
Keyword
 3D-structure; Complete proteome; Isomerase; Metal-binding; Mitochondrion; NAD; NADP; Nucleotide-binding; Phosphoprotein; Potassium; Reference proteome; Secreted; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 282 AA 
Protein Sequence
MSGLRTLLGL GLLVAGSRLP RVISQQSVCR ARPIWWGTQR RGSETMAGAA VKYLSQEEAQ 60
AVDQELFNEY QFSVDQLMEL AGLSCATAIA KAYPPTSMSK SPPTVLVICG PGNNGGDGLV 120
CARHLKLFGY QPTIYYPKRP NKPLFTGLVT QCQKMDIPFL GEMPPEPMMV DELYELVVDA 180
IFGFSFKGDV REPFHSILSV LSGLTVPIAS IDIPSGWDVE KGNPSGIQPD LLISLTAPKK 240
SATHFTGRYH YLGGRFVPPA LEKKYQLNLP SYPDTECVYR LQ 282 
Gene Ontology
 GO:0044297; C:cell body; IDA:MGI.
 GO:0005929; C:cilium; IDA:MGI.
 GO:0005615; C:extracellular space; IDA:MGI.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0052856; F:NADHX epimerase activity; IEA:HAMAP.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0042803; F:protein homodimerization activity; IDA:MGI.
 GO:0051289; P:protein homotetramerization; IDA:MGI. 
Interpro
 IPR026600; NnrE/AIBP.
 IPR004443; YjeF_N_dom. 
Pfam
 PF03853; YjeF_N 
SMART
  
PROSITE
 PS51385; YJEF_N 
PRINTS