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Q13423

- NNTM_HUMAN

UniProt

Q13423 - NNTM_HUMAN

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Protein

NAD(P) transhydrogenase, mitochondrial

Gene

NNT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini44 – 474431Mitochondrial matrixAdd
BLAST
Transmembranei475 – 49319HelicalSequence AnalysisAdd
BLAST
Transmembranei501 – 52121HelicalSequence AnalysisAdd
BLAST
Transmembranei527 – 54620HelicalSequence AnalysisAdd
BLAST
Transmembranei558 – 57821HelicalSequence AnalysisAdd
BLAST
Topological domaini579 – 59517Mitochondrial matrixAdd
BLAST
Transmembranei596 – 61621HelicalSequence AnalysisAdd
BLAST
Transmembranei622 – 64221HelicalSequence AnalysisAdd
BLAST
Transmembranei646 – 66621HelicalSequence AnalysisAdd
BLAST
Transmembranei672 – 69120HelicalSequence AnalysisAdd
BLAST
Transmembranei702 – 72221HelicalSequence AnalysisAdd
BLAST
Topological domaini723 – 73917CytoplasmicAdd
BLAST
Transmembranei740 – 76021HelicalSequence AnalysisAdd
BLAST
Transmembranei778 – 79720HelicalSequence AnalysisAdd
BLAST
Transmembranei801 – 81919HelicalSequence AnalysisAdd
BLAST
Transmembranei833 – 85321HelicalSequence AnalysisAdd
BLAST
Transmembranei857 – 87923HelicalSequence AnalysisAdd
BLAST
Topological domaini880 – 1086207Mitochondrial matrixAdd
BLAST

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
Complete GO annotation...

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

BgeeiQ13423.
CleanExiHS_NNT.
ExpressionAtlasiQ13423. baseline and differential.
GenevestigatoriQ13423.

Organism-specific databases

HPAiCAB004975.
HPA004829.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi117076. 27 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 – 92310Combined sources
Beta strandi925 – 9317Combined sources
Helixi933 – 9386Combined sources
Helixi941 – 95313Combined sources
Beta strandi957 – 9626Combined sources
Beta strandi967 – 9693Combined sources
Helixi972 – 9798Combined sources
Helixi984 – 9863Combined sources
Beta strandi987 – 9893Combined sources
Helixi990 – 9934Combined sources
Helixi994 – 9996Combined sources
Beta strandi1001 – 10077Combined sources
Helixi1010 – 10123Combined sources
Helixi1015 – 10184Combined sources
Turni1023 – 10264Combined sources
Helixi1032 – 10343Combined sources
Beta strandi1035 – 104511Combined sources
Helixi1055 – 10584Combined sources
Beta strandi1062 – 10676Combined sources
Helixi1069 – 108113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00390000004624.
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

        10         20         30         40         50
MANLLKTVVT GCSCPLLSNL GSCKGLRVKK DFLRTFYTHQ ELWCKAPVKP
60 70 80 90 100
GIPYKQLTVG VPKEIFQNEK RVALSPAGVQ NLVKQGFNVV VESGAGEASK
110 120 130 140 150
FSDDHYRVAG AQIQGAKEVL ASDLVVKVRA PMVNPTLGVH EADLLKTSGT
160 170 180 190 200
LISFIYPAQN PELLNKLSQR KTTVLAMDQV PRVTIAQGYD ALSSMANIAG
210 220 230 240 250
YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL ASAGAAKSMG
260 270 280 290 300
AIVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE
310 320 330 340 350
MKLFAQQCKE VDILISTALI PGKKAPVLFN KEMIESMKEG SVVVDLAAEA
360 370 380 390 400
GGNFETTKPG ELYIHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS
410 420 430 440 450
PDKDNFYFDV KDDFDFGTMG HVIRGTVVMK DGKVIFPAPT PKNIPQGAPV
460 470 480 490 500
KQKTVAELEA EKAATITPFR KTMSTASAYT AGLTGILGLG IAAPNLAFSQ
510 520 530 540 550
MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV GGLALMGGHL
560 570 580 590 600
YPSTTSQGLA ALAAFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL
610 620 630 640 650
PAGTFVGGYL AALYSGYNIE QIMYLGSGLC CVGALAGLST QGTARLGNAL
660 670 680 690 700
GMIGVAGGLA ATLGVLKPGP ELLAQMSGAM ALGGTIGLTI AKRIQISDLP
710 720 730 740 750
QLVAAFHSLV GLAAVLTCIA EYIIEYPHFA TDAAANLTKI VAYLGTYIGG
760 770 780 790 800
VTFSGSLIAY GKLQGLLKSA PLLLPGRHLL NAGLLAASVG GIIPFMVDPS
810 820 830 840 850
FTTGITCLGS VSALSAVMGV TLTAAIGGAD MPVVITVLNS YSGWALCAEG
860 870 880 890 900
FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG
910 920 930 940 950
KPMEISGTHT EINLDNAIDM IREANSIIIT PGYGLCAAKA QYPIADLVKM
960 970 980 990 1000
LTEQGKKVRF GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINHDFPDT
1010 1020 1030 1040 1050
DLVLVIGAND TVNSAAQEDP NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA
1060 1070 1080
AVDNPIFYKP NTAMLLGDAK KTCDALQAKV RESYQK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 27 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.
GeneTreei ENSGT00390000004624.
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

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

Gene expression databases

Bgeei Q13423.
CleanExi HS_NNT.
ExpressionAtlasi Q13423. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 149 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