Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  NAD(P)H-hydrate epimerase  

UniProtKB / Swiss-Prot ID :  NNRE_MOUSE

Gene Name (Synonyms) : 
Apoa1bp, Aibp  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Mitochondrion (By similarity). Secreted. Note=In sperm, secretion gradually increases during capacitation. 

Protein Function :  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. 

Protein Sequence MSGLRTLLGLGLLVAGSRLPRVISQQSVCRARPIWWGTQRRGSETMAGAAVKYLSQEEAQAVDQELFNEY...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
43PhosphoserineQRRGSETMA
28.25Phosphositeplus
Link-
43Phosphoserine; by PKA.QRRGSETMA
28.25UniProtKB
Link-
138N6-acetyllysineIYYPKRPNK
65.45Phosphositeplus
Link
152S-nitrosocysteineLVTQCQKMD
2.83dbSNO
Link
271PhosphoserineLNLPSYPDT
53.08Phosphositeplus
Link
275PhosphothreonineSYPDTECVY
27.12Phosphositeplus
Link
277S-nitrosocysteinePDTECVYRL
3.37dbSNO
Link
279PhosphotyrosineTECVYRLQ
19.77Phosphositeplus
Link
279PhosphotyrosineTECVYRLQ
19.77SysPTM
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Biochemical and structural characterization of apolipoprotein A-Ibinding protein, a novel phosphoprotein with a potential role in spermcapacitation.";
Jha K.N., Shumilin I.A., Digilio L.C., Chertihin O., Zheng H.,Schmitz G., Visconti P.E., Flickinger C.J., Minor W., Herr J.C.;
Endocrinology 149:2108-2120(2008).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF25-282, SUBUNIT, PHOSPHORYLATION AT SER-43, SUBCELLULAR LOCATION, ANDTISSUE SPECIFICITY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures