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Q13423

- NNTM_HUMAN

UniProt

Q13423 - NNTM_HUMAN

Protein

NAD(P) transhydrogenase, mitochondrial

Gene

NNT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    NADPH + NAD+ = NADP+ + NADH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei933 – 9331NADP; via amide nitrogen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi229 – 25931NADBy similarityAdd
    BLAST
    Nucleotide bindingi965 – 9706NADP1 Publication
    Nucleotide bindingi1007 – 10115NADP1 Publication
    Nucleotide bindingi1042 – 10498NADP1 Publication
    Nucleotide bindingi1068 – 10692NADP1 Publication

    GO - Molecular functioni

    1. NAD(P)+ transhydrogenase (AB-specific) activity Source: UniProtKB-EC
    2. NAD(P)+ transhydrogenase (B-specific) activity Source: UniProtKB
    3. NAD(P)+ transhydrogenase activity Source: Reactome
    4. NAD binding Source: UniProtKB
    5. NADP binding Source: UniProtKB

    GO - Biological processi

    1. cellular metabolic process Source: Reactome
    2. hydrogen ion transmembrane transport Source: GOC
    3. oxidation-reduction process Source: UniProtKB
    4. proton transport Source: UniProtKB
    5. reactive oxygen species metabolic process Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. tricarboxylic acid cycle Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03639-MONOMER.
    ReactomeiREACT_1785. Citric acid cycle (TCA cycle).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD(P) transhydrogenase, mitochondrial (EC:1.6.1.2)
    Alternative name(s):
    Nicotinamide nucleotide transhydrogenase
    Pyridine nucleotide transhydrogenase
    Gene namesi
    Name:NNT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:7863. NNT.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane Source: UniProtKB
    3. mitochondrial inner membrane Source: UniProtKB
    4. mitochondrial respiratory chain Source: UniProtKB
    5. mitochondrion Source: LIFEdb

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Glucocorticoid deficiency 4 (GCCD4) [MIM:614736]: A rare, potentially lethal, autosomal recessive disorder characterized by resistance to ACTH action on the adrenal cortex, adrenal insufficiency and an inability of the adrenal cortex to produce cortisol. It usually presents in the neonatal period or in early childhood with episodes of hypoglycemia and other symptoms related to cortisol deficiency, including failure to thrive, recurrent illnesses or infections, convulsions, and shock. In a small number of patients hypoglycemia can be sufficiently severe and persistent that it leads to serious long-term neurological damage or death. The diagnosis is readily confirmed with a low plasma cortisol measurement in the presence of an elevated ACTH level, and normal aldosterone and plasma renin measurements.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti193 – 1931S → N in GCCD4. 1 Publication
    VAR_068781
    Natural varianti357 – 3571T → A in GCCD4. 1 Publication
    VAR_068782
    Natural varianti365 – 3651H → P in GCCD4. 1 Publication
    VAR_068783
    Natural varianti437 – 4371P → L in GCCD4. 1 Publication
    VAR_068784
    Natural varianti533 – 5331A → V in GCCD4. 1 Publication
    VAR_068785
    Natural varianti664 – 6641G → R in GCCD4. 1 Publication
    VAR_068786
    Natural varianti678 – 6781G → R in GCCD4. 1 Publication
    VAR_068787
    Natural varianti862 – 8621G → D in GCCD4. 1 Publication
    VAR_068788
    Natural varianti977 – 9771L → P in GCCD4. 1 Publication
    VAR_068789
    Natural varianti1008 – 10081A → P in GCCD4. 1 Publication
    VAR_068790
    Natural varianti1009 – 10091N → K in GCCD4. 1 Publication
    VAR_068791

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614736. phenotype.
    Orphaneti361. Familial glucocorticoid deficiency.
    PharmGKBiPA31667.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4343MitochondrionBy similarityAdd
    BLAST
    Chaini44 – 10861043NAD(P) transhydrogenase, mitochondrialPRO_0000001055Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701N6-acetyllysine1 Publication
    Modified residuei117 – 1171N6-succinyllysineBy similarity
    Modified residuei224 – 2241N6-succinyllysineBy similarity
    Modified residuei294 – 2941N6-succinyllysineBy similarity
    Modified residuei331 – 3311N6-succinyllysineBy similarity
    Modified residuei397 – 3971N6-acetyllysine1 Publication
    Modified residuei1079 – 10791N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ13423.
    PaxDbiQ13423.
    PeptideAtlasiQ13423.
    PRIDEiQ13423.

    PTM databases

    PhosphoSiteiQ13423.

    Expressioni

    Tissue specificityi

    Widely expressed with expression most readily detectable in adrenal, heart, kidney, thyroid and adipose tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ13423.
    BgeeiQ13423.
    CleanExiHS_NNT.
    GenevestigatoriQ13423.

    Organism-specific databases

    HPAiCAB004975.
    HPA004829.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi117076. 21 interactions.
    IntActiQ13423. 2 interactions.
    MINTiMINT-3027647.
    STRINGi9606.ENSP00000264663.

    Structurei

    Secondary structure

    1
    1086
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi914 – 92310
    Beta strandi925 – 9317
    Helixi933 – 9386
    Helixi941 – 95313
    Beta strandi957 – 9626
    Beta strandi967 – 9693
    Helixi972 – 9798
    Helixi984 – 9863
    Beta strandi987 – 9893
    Helixi990 – 9934
    Helixi994 – 9996
    Beta strandi1001 – 10077
    Helixi1010 – 10123
    Helixi1015 – 10184
    Turni1023 – 10264
    Helixi1032 – 10343
    Beta strandi1035 – 104511
    Helixi1055 – 10584
    Beta strandi1062 – 10676
    Helixi1069 – 108113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DJLX-ray2.00A/B880-1086[»]
    1PT9X-ray2.42A/B880-1086[»]
    1U31X-ray2.20A/B880-1086[»]
    ProteinModelPortaliQ13423.
    SMRiQ13423. Positions 902-1083.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13423.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini44 – 474431Mitochondrial matrixAdd
    BLAST
    Topological domaini579 – 59517Mitochondrial matrixAdd
    BLAST
    Topological domaini723 – 73917CytoplasmicAdd
    BLAST
    Topological domaini880 – 1086207Mitochondrial matrixAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei475 – 49319HelicalSequence AnalysisAdd
    BLAST
    Transmembranei501 – 52121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei527 – 54620HelicalSequence AnalysisAdd
    BLAST
    Transmembranei558 – 57821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei596 – 61621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei622 – 64221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei646 – 66621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei672 – 69120HelicalSequence AnalysisAdd
    BLAST
    Transmembranei702 – 72221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei740 – 76021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei778 – 79720HelicalSequence AnalysisAdd
    BLAST
    Transmembranei801 – 81919HelicalSequence AnalysisAdd
    BLAST
    Transmembranei833 – 85321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei857 – 87923HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    In the N-terminal section; belongs to the AlaDH/PNT family.Curated
    In the C-terminal section; belongs to the PNT beta subunit family.Curated

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1282.
    HOGENOMiHOG000160623.
    HOVERGENiHBG006511.
    InParanoidiQ13423.
    KOiK00323.
    OMAiKPGIPYK.
    OrthoDBiEOG722J7T.
    PhylomeDBiQ13423.
    TreeFamiTF300636.

    Family and domain databases

    Gene3Di3.40.50.1220. 1 hit.
    InterProiIPR008143. Ala_DH/PNT_CS2.
    IPR008142. AlaDH/PNT_CS1.
    IPR007886. AlaDH/PNT_N.
    IPR007698. AlaDH/PNT_NAD(H)-bd.
    IPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR012136. NADH_DH_b.
    IPR026255. NADP_transhyd_a.
    IPR024605. NADP_transhyd_a_C.
    [Graphical view]
    PfamiPF01262. AlaDh_PNT_C. 1 hit.
    PF05222. AlaDh_PNT_N. 1 hit.
    PF12769. DUF3814. 1 hit.
    PF02233. PNTB. 1 hit.
    [Graphical view]
    SMARTiSM01002. AlaDh_PNT_C. 1 hit.
    SM01003. AlaDh_PNT_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 1 hit.
    TIGRFAMsiTIGR00561. pntA. 1 hit.
    PROSITEiPS00836. ALADH_PNT_1. 1 hit.
    PS00837. ALADH_PNT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q13423-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANLLKTVVT GCSCPLLSNL GSCKGLRVKK DFLRTFYTHQ ELWCKAPVKP     50
    GIPYKQLTVG VPKEIFQNEK RVALSPAGVQ NLVKQGFNVV VESGAGEASK 100
    FSDDHYRVAG AQIQGAKEVL ASDLVVKVRA PMVNPTLGVH EADLLKTSGT 150
    LISFIYPAQN PELLNKLSQR KTTVLAMDQV PRVTIAQGYD ALSSMANIAG 200
    YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL ASAGAAKSMG 250
    AIVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE 300
    MKLFAQQCKE VDILISTALI PGKKAPVLFN KEMIESMKEG SVVVDLAAEA 350
    GGNFETTKPG ELYIHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS 400
    PDKDNFYFDV KDDFDFGTMG HVIRGTVVMK DGKVIFPAPT PKNIPQGAPV 450
    KQKTVAELEA EKAATITPFR KTMSTASAYT AGLTGILGLG IAAPNLAFSQ 500
    MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV GGLALMGGHL 550
    YPSTTSQGLA ALAAFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL 600
    PAGTFVGGYL AALYSGYNIE QIMYLGSGLC CVGALAGLST QGTARLGNAL 650
    GMIGVAGGLA ATLGVLKPGP ELLAQMSGAM ALGGTIGLTI AKRIQISDLP 700
    QLVAAFHSLV GLAAVLTCIA EYIIEYPHFA TDAAANLTKI VAYLGTYIGG 750
    VTFSGSLIAY GKLQGLLKSA PLLLPGRHLL NAGLLAASVG GIIPFMVDPS 800
    FTTGITCLGS VSALSAVMGV TLTAAIGGAD MPVVITVLNS YSGWALCAEG 850
    FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG 900
    KPMEISGTHT EINLDNAIDM IREANSIIIT PGYGLCAAKA QYPIADLVKM 950
    LTEQGKKVRF GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINHDFPDT 1000
    DLVLVIGAND TVNSAAQEDP NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA 1050
    AVDNPIFYKP NTAMLLGDAK KTCDALQAKV RESYQK 1086
    Length:1,086
    Mass (Da):113,896
    Last modified:August 16, 2004 - v3
    Checksum:i8A437658CA0EB41B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761A → T in CAA90428. (PubMed:8616157)Curated
    Sequence conflicti212 – 2121G → E in CAD38536. (PubMed:17974005)Curated
    Sequence conflicti246 – 2461A → E in AAC51914. (PubMed:9524818)Curated
    Sequence conflicti262 – 2621A → S in AAC51914. (PubMed:9524818)Curated
    Sequence conflicti706 – 7061F → S in AAC51914. (PubMed:9524818)Curated
    Sequence conflicti731 – 7311T → P in AAC51914. (PubMed:9524818)Curated
    Sequence conflicti810 – 8101S → A in CAA90428. (PubMed:8616157)Curated
    Sequence conflicti824 – 8241A → P in CAA90428. (PubMed:8616157)Curated
    Sequence conflicti871 – 8711I → P in AAC51914. (PubMed:9524818)Curated
    Sequence conflicti929 – 9291I → F in AAC51914. (PubMed:9524818)Curated
    Sequence conflicti1059 – 10591K → R in CAD38536. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti193 – 1931S → N in GCCD4. 1 Publication
    VAR_068781
    Natural varianti357 – 3571T → A in GCCD4. 1 Publication
    VAR_068782
    Natural varianti365 – 3651H → P in GCCD4. 1 Publication
    VAR_068783
    Natural varianti437 – 4371P → L in GCCD4. 1 Publication
    VAR_068784
    Natural varianti533 – 5331A → V in GCCD4. 1 Publication
    VAR_068785
    Natural varianti664 – 6641G → R in GCCD4. 1 Publication
    VAR_068786
    Natural varianti678 – 6781G → R in GCCD4. 1 Publication
    VAR_068787
    Natural varianti862 – 8621G → D in GCCD4. 1 Publication
    VAR_068788
    Natural varianti977 – 9771L → P in GCCD4. 1 Publication
    VAR_068789
    Natural varianti1008 – 10081A → P in GCCD4. 1 Publication
    VAR_068790
    Natural varianti1009 – 10091N → K in GCCD4. 1 Publication
    VAR_068791

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40490 mRNA. Translation: AAC51914.1.
    Z50101 mRNA. Translation: CAA90428.1.
    AL831822 mRNA. Translation: CAD38536.1.
    BC110543 mRNA. Translation: AAI10544.1.
    CCDSiCCDS3949.1.
    PIRiG02257.
    RefSeqiNP_036475.3. NM_012343.3.
    NP_892022.2. NM_182977.2.
    XP_005248331.1. XM_005248274.2.
    UniGeneiHs.482043.

    Genome annotation databases

    EnsembliENST00000264663; ENSP00000264663; ENSG00000112992.
    ENST00000344920; ENSP00000343873; ENSG00000112992.
    GeneIDi23530.
    KEGGihsa:23530.
    UCSCiuc003joe.3. human.

    Polymorphism databases

    DMDMi51338801.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40490 mRNA. Translation: AAC51914.1 .
    Z50101 mRNA. Translation: CAA90428.1 .
    AL831822 mRNA. Translation: CAD38536.1 .
    BC110543 mRNA. Translation: AAI10544.1 .
    CCDSi CCDS3949.1.
    PIRi G02257.
    RefSeqi NP_036475.3. NM_012343.3.
    NP_892022.2. NM_182977.2.
    XP_005248331.1. XM_005248274.2.
    UniGenei Hs.482043.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DJL X-ray 2.00 A/B 880-1086 [» ]
    1PT9 X-ray 2.42 A/B 880-1086 [» ]
    1U31 X-ray 2.20 A/B 880-1086 [» ]
    ProteinModelPortali Q13423.
    SMRi Q13423. Positions 902-1083.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117076. 21 interactions.
    IntActi Q13423. 2 interactions.
    MINTi MINT-3027647.
    STRINGi 9606.ENSP00000264663.

    PTM databases

    PhosphoSitei Q13423.

    Polymorphism databases

    DMDMi 51338801.

    Proteomic databases

    MaxQBi Q13423.
    PaxDbi Q13423.
    PeptideAtlasi Q13423.
    PRIDEi Q13423.

    Protocols and materials databases

    DNASUi 23530.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264663 ; ENSP00000264663 ; ENSG00000112992 .
    ENST00000344920 ; ENSP00000343873 ; ENSG00000112992 .
    GeneIDi 23530.
    KEGGi hsa:23530.
    UCSCi uc003joe.3. human.

    Organism-specific databases

    CTDi 23530.
    GeneCardsi GC05P043638.
    H-InvDB HIX0032203.
    HGNCi HGNC:7863. NNT.
    HPAi CAB004975.
    HPA004829.
    MIMi 607878. gene.
    614736. phenotype.
    neXtProti NX_Q13423.
    Orphaneti 361. Familial glucocorticoid deficiency.
    PharmGKBi PA31667.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1282.
    HOGENOMi HOG000160623.
    HOVERGENi HBG006511.
    InParanoidi Q13423.
    KOi K00323.
    OMAi KPGIPYK.
    OrthoDBi EOG722J7T.
    PhylomeDBi Q13423.
    TreeFami TF300636.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03639-MONOMER.
    Reactomei REACT_1785. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    EvolutionaryTracei Q13423.
    GeneWikii NNT_(gene).
    GenomeRNAii 23530.
    NextBioi 46004.
    PROi Q13423.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13423.
    Bgeei Q13423.
    CleanExi HS_NNT.
    Genevestigatori Q13423.

    Family and domain databases

    Gene3Di 3.40.50.1220. 1 hit.
    InterProi IPR008143. Ala_DH/PNT_CS2.
    IPR008142. AlaDH/PNT_CS1.
    IPR007886. AlaDH/PNT_N.
    IPR007698. AlaDH/PNT_NAD(H)-bd.
    IPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR012136. NADH_DH_b.
    IPR026255. NADP_transhyd_a.
    IPR024605. NADP_transhyd_a_C.
    [Graphical view ]
    Pfami PF01262. AlaDh_PNT_C. 1 hit.
    PF05222. AlaDh_PNT_N. 1 hit.
    PF12769. DUF3814. 1 hit.
    PF02233. PNTB. 1 hit.
    [Graphical view ]
    SMARTi SM01002. AlaDh_PNT_C. 1 hit.
    SM01003. AlaDh_PNT_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52467. SSF52467. 1 hit.
    TIGRFAMsi TIGR00561. pntA. 1 hit.
    PROSITEi PS00836. ALADH_PNT_1. 1 hit.
    PS00837. ALADH_PNT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and deduced amino acid sequence of human nicotinamide nucleotide transhydrogenase."
      Ware J., Zieger B.
      DNA Seq. 7:369-374(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The cDNA sequence of proton-pumping nicotinamide nucleotide transhydrogenase from man and mouse."
      Lagberg E.M., Betsholtz C., Rydstrom J.
      Biochim. Biophys. Acta 1273:203-205(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause familial glucocorticoid deficiency."
      Meimaridou E., Kowalczyk J., Guasti L., Hughes C.R., Wagner F., Frommolt P., Nurnberg P., Mann N.P., Banerjee R., Saka H.N., Chapple J.P., King P.J., Clark A.J., Metherell L.A.
      Nat. Genet. 44:740-742(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, VARIANTS GCCD4 ASN-193; ALA-357; PRO-365; LEU-437; VAL-533; ARG-664; ARG-678; ASP-862; PRO-977; PRO-1008 AND LYS-1009.
    8. "The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria."
      White S.A., Peake S.J., McSweeney S., Leonard G., Cotton N.P.J., Jackson J.B.
      Structure 8:1-12(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 880-1086 IN COMPLEX WITH NADP.

    Entry informationi

    Entry nameiNNTM_HUMAN
    AccessioniPrimary (citable) accession number: Q13423
    Secondary accession number(s): Q16796, Q2TB60, Q8N3V4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3