CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014388
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
267AAALEQFKSLGAEPLubiquitination[1]
279EPLEVDLKESGEGQGubiquitination[1]
323STALIPGKKAPVLFSacetylation[2]
331KAPVLFSKEMIESMKacetylation[3, 4]
331KAPVLFSKEMIESMKsuccinylation[4]
394LYSNNITKLLKAISPacetylation[2, 3, 5]
394LYSNNITKLLKAISPubiquitination[1]
397NNITKLLKAISPDKDacetylation[2]
403LKAISPDKDNFHFEVacetylation[2]
433TVVMKDGKVIFPAPTacetylation[5]
451IPEEAPVKPKTVAELacetylation[2]
768GKLQGILKSAPLLLPubiquitination[1]
1071MLLGDAKKTCDALQAacetylation[2, 4]
1071MLLGDAKKTCDALQAsuccinylation[4]
1079TCDALQAKVRESYQKacetylation[2, 4]
1079TCDALQAKVRESYQKsuccinylation[4]
1079TCDALQAKVRESYQKubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] 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]
 [4] 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]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
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 (By similarity). 
Sequence Annotation
 NP_BIND 229 259 NAD (By similarity).
 NP_BIND 965 970 NADP (By similarity).
 NP_BIND 1007 1011 NADP (By similarity).
 NP_BIND 1042 1049 NADP (By similarity).
 NP_BIND 1068 1069 NADP (By similarity).
 MOD_RES 70 70 N6-acetyllysine (By similarity).
 MOD_RES 397 397 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; 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
MAHLLKTVVA GCSCPFLSNL GSSKVLPGKR DFVRTLRTHQ ALWCKSPVKP GIPYKQLTVG 60
VPKEIFQNEK RVALSPAGVQ ALVKQGFNVV VESGAGEASK FPDDLYRAAG AQIQGMKEVL 120
ASDLVVKVRA PMVNPTLGAH EADFLKPSGT LISFIYPAQN PDLLNKLSER KTTVLAMDQV 180
PRVTIAQGYD ALSSMANISG YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL 240
ASAGAAKSMG AVVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE 300
MKLFAQQCKE VDILISTALI PGKKAPVLFS KEMIESMKEG SVVVDLAAEA GGNFETTKPG 360
ELYVHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS PDKDNFHFEV KDDFDFGTMS 420
HVIRGTVVMK DGKVIFPAPT PKNIPEEAPV KPKTVAELEA EKAGTVSMYT KTLTTASVYS 480
AGLTGMLGLG IVAPNVAFSQ MVTTFGLAGI IGYHTVWGVT PALHSPLMSV TNAISGLTAV 540
GGLALMGGHF YPSTTSQSLA ALATFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL 600
PGGTFVGGYL AALYGGYNIE EIMYLGSGLC CVGALGGLST QGTARLGNAL GMIGVAGGLA 660
ATLGGLKPDP QLLAQMSGAM AMGGTIGLTI AKRIQISDLP QLVAAFHSLV GLAAVLTCMA 720
EYIVEYPHFA MDATSNFTKI VAYLGTYIGG VTFSGSLVAY GKLQGILKSA PLLLPGRHAL 780
NAGLLAASVG GIIPFMADPS FTTGITCLGS VSGLSTLMGV TLTAAIGGAD MPVVITVLNS 840
YSGWALCAEG FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG 900
KPMEISGTHT EINLDNAVEM IREANSIVIT PGYGLCAAKA QYPIADLVKM LTEQGKKVRF 960
GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINSDFPDT DLVLVIGAND TVNSAAQEDP 1020
NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA AVDNPIFYKP NTAMLLGDAK KTCDALQAKV 1080
RESYQK 1086 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:EC.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0015992; P:proton transport; IEA:InterPro.
 GO:0072593; P:reactive oxygen species metabolic process; ISS: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