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Protein

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1

Gene

NMNAT1

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

Functioni

Catalyzes the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP (PubMed:17402747). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency (PubMed:17402747). Can use triazofurin monophosphate (TrMP) as substrate (PubMed:17402747). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+ (PubMed:17402747). For the pyrophosphorolytic activity, prefers NAD+ and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively (PubMed:17402747). Involved in the synthesis of ATP in the nucleus, together with PARP1, PARG and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NaADP+ (PubMed:17402747). Protects against axonal degeneration following mechanical or toxic insults (By similarity).By similarity2 Publications

Catalytic activityi

ATP + nicotinamide ribonucleotide = diphosphate + NAD+.1 Publication
ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+.

Cofactori

Zn2+2 Publications, Mg2+2 PublicationsNote: Divalent metal cations. Zn2+ confers higher activity as compared to Mg2+.2 Publications

Enzyme regulationi

Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate (Nap4AD).1 Publication

Kineticsi

  1. KM=34 µM for NMN2 Publications
  2. KM=40 µM for ATP2 Publications
  3. KM=937 µM for PPi2 Publications
  4. KM=59 µM for NAD+2 Publications
  1. Vmax=25 µmol/min/mg enzyme for NAD synthesis2 Publications
  2. Vmax=60.5 µmol/min/µg enzyme for NAD+ cleavage2 Publications
  3. Vmax=8.5 µmol/min/µg enzyme for NADH cleavage2 Publications

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinamide-nucleotide adenylyltransferase, Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMNAT1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (NMNAT3), Nicotinamide-nucleotide adenylyltransferase, Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMNAT2), Nicotinamide-nucleotide adenylyltransferase (NMNAT1)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMNAT1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (NMNAT3), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMNAT2)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei24ATPBy similarity1
Binding sitei58ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 17ATPBy similarity1 Publication3
Nucleotide bindingi156 – 158ATPBy similarity3
Nucleotide bindingi224 – 227ATPBy similarity4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • nicotinamide-nucleotide adenylyltransferase activity Source: UniProtKB
  • nicotinate-nucleotide adenylyltransferase activity Source: UniProtKB

GO - Biological processi

  • 'de novo' NAD biosynthetic process from aspartate Source: GO_Central
  • ATP generation from poly-ADP-D-ribose Source: UniProtKB
  • NAD biosynthetic process Source: UniProtKB
  • NAD metabolic process Source: Reactome
  • response to wounding Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS10701-MONOMER.
ZFISH:HS10701-MONOMER.
BRENDAi2.7.7.1. 2681.
2.7.7.18. 2681.
ReactomeiR-HSA-196807. Nicotinate metabolism.
SABIO-RKQ9HAN9.
UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1Curated (EC:2.7.7.1, EC:2.7.7.18)
Short name:
NMN/NaMN adenylyltransferase 1
Alternative name(s):
Nicotinamide-nucleotide adenylyltransferase 1
Short name:
NMN adenylyltransferase 1
Nicotinate-nucleotide adenylyltransferase 1
Short name:
NaMN adenylyltransferase 1
Gene namesi
Name:NMNAT1
Synonyms:NMNAT
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17877. NMNAT1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Leber congenital amaurosis 9 (LCA9)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.
See also OMIM:608553
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0688569V → M in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 PublicationCorresponds to variant rs387907294dbSNPEnsembl.1
Natural variantiVAR_06885713A → T in LCA9. 3 PublicationsCorresponds to variant rs138613460dbSNPEnsembl.1
Natural variantiVAR_06885820I → N in LCA9. 1 PublicationCorresponds to variant rs761948762dbSNPEnsembl.1
Natural variantiVAR_06885933D → G in LCA9. 1 Publication1
Natural variantiVAR_06886035M → T in LCA9. 1 Publication1
Natural variantiVAR_06886154A → V in LCA9. 1 PublicationCorresponds to variant rs760965874dbSNPEnsembl.1
Natural variantiVAR_06886266R → W in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 PublicationCorresponds to variant rs763325435dbSNPEnsembl.1
Natural variantiVAR_06886367V → F in LCA9. 1 PublicationCorresponds to variant rs756903689dbSNPEnsembl.1
Natural variantiVAR_06886469M → V in LCA9. 2 PublicationsCorresponds to variant rs372066126dbSNPEnsembl.1
Natural variantiVAR_06886572L → H in LCA9. 1 Publication1
Natural variantiVAR_06886698V → G in LCA9. 3 PublicationsCorresponds to variant rs771336246dbSNPEnsembl.1
Natural variantiVAR_068867147A → P in LCA9. 1 Publication1
Natural variantiVAR_068868151V → F in LCA9. 2 PublicationsCorresponds to variant rs387907292dbSNPEnsembl.1
Natural variantiVAR_068869153L → P in LCA9. 1 Publication1
Natural variantiVAR_068870153L → V in LCA9. 1 PublicationCorresponds to variant rs387907293dbSNPEnsembl.1
Natural variantiVAR_068871156G → R in LCA9. 1 Publication1
Natural variantiVAR_068872173D → G in LCA9. 1 Publication1
Natural variantiVAR_068873178V → M in LCA9. 1 PublicationCorresponds to variant rs757724544dbSNPEnsembl.1
Natural variantiVAR_068874181Y → C in LCA9. 1 PublicationCorresponds to variant rs748913297dbSNPEnsembl.1
Natural variantiVAR_068875184I → M in LCA9. 1 Publication1
Natural variantiVAR_068876207R → W in LCA9; results in significantly reduced enzymatic activity. 2 PublicationsCorresponds to variant rs142968179dbSNPEnsembl.1
Natural variantiVAR_068877217I → N in LCA9. 1 Publication1
Natural variantiVAR_068878237R → C in LCA9; does not affect nuclear localization. 2 PublicationsCorresponds to variant rs375110174dbSNPEnsembl.1
Natural variantiVAR_068879237R → L in LCA9. 1 PublicationCorresponds to variant rs368062092dbSNPEnsembl.1
Natural variantiVAR_068880239L → S in LCA9. 1 PublicationCorresponds to variant rs778606847dbSNPEnsembl.1
Natural variantiVAR_068881251H → P in LCA9. 1 Publication1
Natural variantiVAR_068882257E → K in LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm. 3 PublicationsCorresponds to variant rs150726175dbSNPEnsembl.1
Natural variantiVAR_068883273N → D in LCA9; results in significantly reduced enzymatic activity. 2 PublicationsCorresponds to variant rs387907291dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis

Organism-specific databases

DisGeNETi64802.
MalaCardsiNMNAT1.
MIMi608553. phenotype.
OpenTargetsiENSG00000173614.
Orphaneti65. Leber congenital amaurosis.
PharmGKBiPA31660.

Polymorphism and mutation databases

BioMutaiNMNAT1.
DMDMi30580491.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001350121 – 279Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1Add BLAST279

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei117PhosphoserineCombined sources1
Modified residuei119PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9HAN9.
MaxQBiQ9HAN9.
PaxDbiQ9HAN9.
PeptideAtlasiQ9HAN9.
PRIDEiQ9HAN9.

PTM databases

iPTMnetiQ9HAN9.
PhosphoSitePlusiQ9HAN9.

Expressioni

Tissue specificityi

Widely expressed with highest levels in skeletal muscle, heart and kidney. Also expressed in the liver pancreas and placenta. Widely expressed throughout the brain.2 Publications

Gene expression databases

BgeeiENSG00000173614.
CleanExiHS_NMNAT1.
ExpressionAtlasiQ9HAN9. baseline and differential.
GenevisibleiQ9HAN9. HS.

Organism-specific databases

HPAiHPA059447.

Interactioni

Subunit structurei

Homohexamer. Interacts with ADPRT/PARP1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-3917542,EBI-3917542
CCNCP248633EBI-3917542,EBI-395261
KPNA2Q6NVW73EBI-3917542,EBI-9377406
SIRT1Q96EB63EBI-3917542,EBI-1802965

Protein-protein interaction databases

BioGridi122308. 39 interactors.
DIPiDIP-60881N.
IntActiQ9HAN9. 15 interactors.
STRINGi9606.ENSP00000366410.

Structurei

Secondary structure

1279
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 15Combined sources9
Helixi22 – 37Combined sources16
Beta strandi39 – 50Combined sources12
Helixi53 – 55Combined sources3
Helixi63 – 73Combined sources11
Turni74 – 76Combined sources3
Beta strandi78 – 82Combined sources5
Helixi86 – 88Combined sources3
Helixi95 – 106Combined sources12
Beta strandi150 – 156Combined sources7
Helixi157 – 162Combined sources6
Turni166 – 168Combined sources3
Helixi171 – 180Combined sources10
Beta strandi183 – 188Combined sources6
Helixi190 – 198Combined sources9
Helixi201 – 205Combined sources5
Helixi206 – 209Combined sources4
Beta strandi210 – 214Combined sources5
Beta strandi217 – 219Combined sources3
Helixi223 – 231Combined sources9
Helixi242 – 251Combined sources10
Helixi256 – 259Combined sources4
Turni260 – 264Combined sources5
Helixi268 – 274Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GZUX-ray2.90A/B/C2-279[»]
1KKUX-ray2.50A1-279[»]
1KQNX-ray2.20A/B/C/D/E/F1-279[»]
1KQOX-ray2.50A/B/C/D/E/F1-279[»]
1KR2X-ray2.30A/B/C/D/E/F1-279[»]
ProteinModelPortaliQ9HAN9.
SMRiQ9HAN9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HAN9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni55 – 57Substrate binding1 Publication3
Regioni92 – 95Substrate binding2 Publications4
Regioni168 – 169Substrate binding2 Publications2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi123 – 129Nuclear localization signalSequence analysis7

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3199. Eukaryota.
COG1057. LUCA.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ9HAN9.
KOiK06210.
OMAiRVAMCQL.
OrthoDBiEOG091G0JTI.
PhylomeDBiQ9HAN9.
TreeFamiTF315035.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR12039. PTHR12039. 1 hit.
PfamiPF01467. CTP_transf_like. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HAN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENSEKTEVV LLACGSFNPI TNMHLRLFEL AKDYMNGTGR YTVVKGIISP
60 70 80 90 100
VGDAYKKKGL IPAYHRVIMA ELATKNSKWV EVDTWESLQK EWKETLKVLR
110 120 130 140 150
HHQEKLEASD CDHQQNSPTL ERPGRKRKWT ETQDSSQKKS LEPKTKAVPK
160 170 180 190 200
VKLLCGADLL ESFAVPNLWK SEDITQIVAN YGLICVTRAG NDAQKFIYES
210 220 230 240 250
DVLWKHRSNI HVVNEWIAND ISSTKIRRAL RRGQSIRYLV PDLVQEYIEK
260 270
HNLYSSESED RNAGVILAPL QRNTAEAKT
Length:279
Mass (Da):31,932
Last modified:March 1, 2001 - v1
Checksum:i740DE872CD9C22E7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20I → F in AAL76934 (PubMed:11027696).Curated1
Sequence conflicti20I → F in AAL76935 (PubMed:11027696).Curated1
Sequence conflicti217I → F in AAG33629 (PubMed:11891043).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0688569V → M in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 PublicationCorresponds to variant rs387907294dbSNPEnsembl.1
Natural variantiVAR_06885713A → T in LCA9. 3 PublicationsCorresponds to variant rs138613460dbSNPEnsembl.1
Natural variantiVAR_06885820I → N in LCA9. 1 PublicationCorresponds to variant rs761948762dbSNPEnsembl.1
Natural variantiVAR_06885933D → G in LCA9. 1 Publication1
Natural variantiVAR_06886035M → T in LCA9. 1 Publication1
Natural variantiVAR_06886154A → V in LCA9. 1 PublicationCorresponds to variant rs760965874dbSNPEnsembl.1
Natural variantiVAR_06886266R → W in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 PublicationCorresponds to variant rs763325435dbSNPEnsembl.1
Natural variantiVAR_06886367V → F in LCA9. 1 PublicationCorresponds to variant rs756903689dbSNPEnsembl.1
Natural variantiVAR_06886469M → V in LCA9. 2 PublicationsCorresponds to variant rs372066126dbSNPEnsembl.1
Natural variantiVAR_06886572L → H in LCA9. 1 Publication1
Natural variantiVAR_06886698V → G in LCA9. 3 PublicationsCorresponds to variant rs771336246dbSNPEnsembl.1
Natural variantiVAR_068867147A → P in LCA9. 1 Publication1
Natural variantiVAR_068868151V → F in LCA9. 2 PublicationsCorresponds to variant rs387907292dbSNPEnsembl.1
Natural variantiVAR_068869153L → P in LCA9. 1 Publication1
Natural variantiVAR_068870153L → V in LCA9. 1 PublicationCorresponds to variant rs387907293dbSNPEnsembl.1
Natural variantiVAR_068871156G → R in LCA9. 1 Publication1
Natural variantiVAR_068872173D → G in LCA9. 1 Publication1
Natural variantiVAR_068873178V → M in LCA9. 1 PublicationCorresponds to variant rs757724544dbSNPEnsembl.1
Natural variantiVAR_068874181Y → C in LCA9. 1 PublicationCorresponds to variant rs748913297dbSNPEnsembl.1
Natural variantiVAR_068875184I → M in LCA9. 1 Publication1
Natural variantiVAR_068876207R → W in LCA9; results in significantly reduced enzymatic activity. 2 PublicationsCorresponds to variant rs142968179dbSNPEnsembl.1
Natural variantiVAR_068877217I → N in LCA9. 1 Publication1
Natural variantiVAR_068878237R → C in LCA9; does not affect nuclear localization. 2 PublicationsCorresponds to variant rs375110174dbSNPEnsembl.1
Natural variantiVAR_068879237R → L in LCA9. 1 PublicationCorresponds to variant rs368062092dbSNPEnsembl.1
Natural variantiVAR_068880239L → S in LCA9. 1 PublicationCorresponds to variant rs778606847dbSNPEnsembl.1
Natural variantiVAR_068881251H → P in LCA9. 1 Publication1
Natural variantiVAR_068882257E → K in LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm. 3 PublicationsCorresponds to variant rs150726175dbSNPEnsembl.1
Natural variantiVAR_068883273N → D in LCA9; results in significantly reduced enzymatic activity. 2 PublicationsCorresponds to variant rs387907291dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF314163 mRNA. Translation: AAG33632.1.
AF312734 mRNA. Translation: AAG33629.1.
AF459819 mRNA. Translation: AAL76934.1.
AF459823
, AF459820, AF459821, AF459822 Genomic DNA. Translation: AAL76935.1.
AK026065 mRNA. Translation: BAB15345.1.
AK315640 mRNA. Translation: BAG38007.1.
AL603962, AL357140 Genomic DNA. Translation: CAI16813.1.
AL357140, AL603962 Genomic DNA. Translation: CAI16889.1.
CH471130 Genomic DNA. Translation: EAW71635.1.
BC014943 mRNA. Translation: AAH14943.1.
CCDSiCCDS108.1.
RefSeqiNP_001284707.1. NM_001297778.1.
NP_073624.2. NM_022787.3.
XP_016857596.1. XM_017002107.1.
UniGeneiHs.633762.

Genome annotation databases

EnsembliENST00000377205; ENSP00000366410; ENSG00000173614.
ENST00000462686; ENSP00000435134; ENSG00000173614.
GeneIDi64802.
KEGGihsa:64802.
UCSCiuc001aqp.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF314163 mRNA. Translation: AAG33632.1.
AF312734 mRNA. Translation: AAG33629.1.
AF459819 mRNA. Translation: AAL76934.1.
AF459823
, AF459820, AF459821, AF459822 Genomic DNA. Translation: AAL76935.1.
AK026065 mRNA. Translation: BAB15345.1.
AK315640 mRNA. Translation: BAG38007.1.
AL603962, AL357140 Genomic DNA. Translation: CAI16813.1.
AL357140, AL603962 Genomic DNA. Translation: CAI16889.1.
CH471130 Genomic DNA. Translation: EAW71635.1.
BC014943 mRNA. Translation: AAH14943.1.
CCDSiCCDS108.1.
RefSeqiNP_001284707.1. NM_001297778.1.
NP_073624.2. NM_022787.3.
XP_016857596.1. XM_017002107.1.
UniGeneiHs.633762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GZUX-ray2.90A/B/C2-279[»]
1KKUX-ray2.50A1-279[»]
1KQNX-ray2.20A/B/C/D/E/F1-279[»]
1KQOX-ray2.50A/B/C/D/E/F1-279[»]
1KR2X-ray2.30A/B/C/D/E/F1-279[»]
ProteinModelPortaliQ9HAN9.
SMRiQ9HAN9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122308. 39 interactors.
DIPiDIP-60881N.
IntActiQ9HAN9. 15 interactors.
STRINGi9606.ENSP00000366410.

PTM databases

iPTMnetiQ9HAN9.
PhosphoSitePlusiQ9HAN9.

Polymorphism and mutation databases

BioMutaiNMNAT1.
DMDMi30580491.

Proteomic databases

EPDiQ9HAN9.
MaxQBiQ9HAN9.
PaxDbiQ9HAN9.
PeptideAtlasiQ9HAN9.
PRIDEiQ9HAN9.

Protocols and materials databases

DNASUi64802.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377205; ENSP00000366410; ENSG00000173614.
ENST00000462686; ENSP00000435134; ENSG00000173614.
GeneIDi64802.
KEGGihsa:64802.
UCSCiuc001aqp.3. human.

Organism-specific databases

CTDi64802.
DisGeNETi64802.
GeneCardsiNMNAT1.
GeneReviewsiNMNAT1.
HGNCiHGNC:17877. NMNAT1.
HPAiHPA059447.
MalaCardsiNMNAT1.
MIMi608553. phenotype.
608700. gene.
neXtProtiNX_Q9HAN9.
OpenTargetsiENSG00000173614.
Orphaneti65. Leber congenital amaurosis.
PharmGKBiPA31660.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3199. Eukaryota.
COG1057. LUCA.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ9HAN9.
KOiK06210.
OMAiRVAMCQL.
OrthoDBiEOG091G0JTI.
PhylomeDBiQ9HAN9.
TreeFamiTF315035.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.
BioCyciMetaCyc:HS10701-MONOMER.
ZFISH:HS10701-MONOMER.
BRENDAi2.7.7.1. 2681.
2.7.7.18. 2681.
ReactomeiR-HSA-196807. Nicotinate metabolism.
SABIO-RKQ9HAN9.

Miscellaneous databases

ChiTaRSiNMNAT1. human.
EvolutionaryTraceiQ9HAN9.
GeneWikiiNMNAT1.
GenomeRNAii64802.
PROiQ9HAN9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173614.
CleanExiHS_NMNAT1.
ExpressionAtlasiQ9HAN9. baseline and differential.
GenevisibleiQ9HAN9. HS.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR12039. PTHR12039. 1 hit.
PfamiPF01467. CTP_transf_like. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNMNA1_HUMAN
AccessioniPrimary (citable) accession number: Q9HAN9
Secondary accession number(s): B1AN63
, Q8TAE9, Q9H247, Q9H6B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 143 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.