CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012089
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NAD(P) transhydrogenase, mitochondrial 
Protein Synonyms/Alias
 Nicotinamide nucleotide transhydrogenase; Pyridine nucleotide transhydrogenase 
Gene Name
 NNT 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55VKPGIPYKQLTVGVPubiquitination[1, 2, 3]
70KEIFQNEKRVALSPAacetylation[4]
100SGAGEASKFSDDHYRacetylation[4]
267AAALEQFKSLGAEPLubiquitination[5]
279EPLEVDLKESGEGQGubiquitination[5]
331KAPVLFNKEMIESMKacetylation[4]
394LYSNNITKLLKAISPacetylation[4, 6]
397NNITKLLKAISPDKDacetylation[4]
442IFPAPTPKNIPQGAPubiquitination[5]
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] 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]
 [3] 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]
 [4] 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]
 [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] 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
 The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland. 
Sequence Annotation
 NP_BIND 229 259 NAD (By similarity).
 NP_BIND 965 970 NADP.
 NP_BIND 1007 1011 NADP.
 NP_BIND 1042 1049 NADP.
 NP_BIND 1068 1069 NADP.
 BINDING 933 933 NADP; via amide nitrogen.
 MOD_RES 70 70 N6-acetyllysine.
 MOD_RES 397 397 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Disease mutation; Membrane; Mitochondrion; Mitochondrion inner membrane; NAD; NADP; Oxidoreductase; Reference proteome; Transit peptide; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1086 AA 
Protein Sequence
MANLLKTVVT GCSCPLLSNL GSCKGLRVKK DFLRTFYTHQ ELWCKAPVKP GIPYKQLTVG 60
VPKEIFQNEK RVALSPAGVQ NLVKQGFNVV VESGAGEASK FSDDHYRVAG AQIQGAKEVL 120
ASDLVVKVRA PMVNPTLGVH EADLLKTSGT LISFIYPAQN PELLNKLSQR KTTVLAMDQV 180
PRVTIAQGYD ALSSMANIAG YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL 240
ASAGAAKSMG AIVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE 300
MKLFAQQCKE VDILISTALI PGKKAPVLFN KEMIESMKEG SVVVDLAAEA GGNFETTKPG 360
ELYIHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS PDKDNFYFDV KDDFDFGTMG 420
HVIRGTVVMK DGKVIFPAPT PKNIPQGAPV KQKTVAELEA EKAATITPFR KTMSTASAYT 480
AGLTGILGLG IAAPNLAFSQ MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV 540
GGLALMGGHL YPSTTSQGLA ALAAFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL 600
PAGTFVGGYL AALYSGYNIE QIMYLGSGLC CVGALAGLST QGTARLGNAL GMIGVAGGLA 660
ATLGVLKPGP ELLAQMSGAM ALGGTIGLTI AKRIQISDLP QLVAAFHSLV GLAAVLTCIA 720
EYIIEYPHFA TDAAANLTKI VAYLGTYIGG VTFSGSLIAY GKLQGLLKSA PLLLPGRHLL 780
NAGLLAASVG GIIPFMVDPS FTTGITCLGS VSALSAVMGV TLTAAIGGAD MPVVITVLNS 840
YSGWALCAEG FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG 900
KPMEISGTHT EINLDNAIDM IREANSIIIT PGYGLCAAKA QYPIADLVKM LTEQGKKVRF 960
GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINHDFPDT DLVLVIGAND TVNSAAQEDP 1020
NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA AVDNPIFYKP NTAMLLGDAK KTCDALQAKV 1080
RESYQK 1086 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005746; C:mitochondrial respiratory chain; TAS:UniProtKB.
 GO:0051287; F:NAD binding; TAS:UniProtKB.
 GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:EC.
 GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; TAS:UniProtKB.
 GO:0050661; F:NADP binding; IDA:UniProtKB.
 GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006099; P:tricarboxylic acid cycle; TAS:UniProtKB. 
Interpro
 IPR008142; Ala_DH/PNT_CS1.
 IPR008143; Ala_DH/PNT_CS2.
 IPR007886; AlaDH/PNT_N.
 IPR007698; AlaDH/PNT_NAD(H)-bd.
 IPR012136; NADH_DH_b.
 IPR026255; NADP_transhyd_a.
 IPR024605; NADP_transhyd_a_C. 
Pfam
 PF01262; AlaDh_PNT_C
 PF05222; AlaDh_PNT_N
 PF12769; DUF3814
 PF02233; PNTB 
SMART
 SM01002; AlaDh_PNT_C
 SM01003; AlaDh_PNT_N 
PROSITE
 PS00836; ALADH_PNT_1
 PS00837; ALADH_PNT_2 
PRINTS