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Q9HAN9 (NMNA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicotinamide mononucleotide adenylyltransferase 1

Short name=NMN adenylyltransferase 1
EC=2.7.7.1
Alternative name(s):
Nicotinate-nucleotide adenylyltransferase 1
Short name=NaMN adenylyltransferase 1
EC=2.7.7.18
Gene names
Name:NMNAT1
Synonyms:NMNAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+. 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. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+. Protects against axonal degeneration following mechanical or toxic insults. Ref.10

Catalytic activity

ATP + nicotinamide ribonucleotide = diphosphate + NAD+. Ref.2

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

Cofactor

Divalent metal cations. Zinc confers higher activity as compared to magnesium. Ref.2 Ref.10

Enzyme regulation

Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate (Nap4AD). Ref.10

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.

Subunit structure

Homohexamer. Interacts with ADPRT/PARP1. Ref.1 Ref.14

Subcellular location

Nucleus Ref.1 Ref.8 Ref.9 Ref.12.

Tissue specificity

Widely expressed with highest levels in skeletal muscle, heart and kidney. Also expressed in the liver pancreas and placenta. Widely expressed throughout the brain. Ref.2 Ref.3

Involvement in disease

Leber congenital amaurosis 9 (LCA9) [MIM:608553]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the eukaryotic NMN adenylyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=34 µM for NMN Ref.9 Ref.10

KM=40 µM for ATP

KM=937 µM for PPi

KM=59 µM for NAD+

Vmax=25 µmol/min/mg enzyme for NAD synthesis

Vmax=60.5 µmol/min/µg enzyme for NAD+ cleavage

Vmax=8.5 µmol/min/µg enzyme for NADH cleavage

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SIRT1Q96EB63EBI-3917542,EBI-1802965

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 279279Nicotinamide mononucleotide adenylyltransferase 1
PRO_0000135012

Regions

Nucleotide binding15 – 2410ATP Potential
Nucleotide binding222 – 2276ATP Potential
Motif123 – 1297Nuclear localization signal Potential

Sites

Binding site161Substrate By similarity
Binding site551Substrate By similarity
Binding site1581Substrate By similarity

Natural variations

Natural variant91V → M in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. Ref.18
VAR_068856
Natural variant131A → T in LCA9. Ref.12 Ref.17 Ref.18
Corresponds to variant rs138613460 [ dbSNP | Ensembl ].
VAR_068857
Natural variant201I → N in LCA9. Ref.18
VAR_068858
Natural variant331D → G in LCA9. Ref.18
VAR_068859
Natural variant351M → T in LCA9. Ref.16
VAR_068860
Natural variant541A → V in LCA9. Ref.18
VAR_068861
Natural variant661R → W in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. Ref.18
VAR_068862
Natural variant671V → F in LCA9. Ref.12
VAR_068863
Natural variant691M → V in LCA9. Ref.17 Ref.18
VAR_068864
Natural variant721L → H in LCA9. Ref.18
VAR_068865
Natural variant981V → G in LCA9. Ref.12 Ref.16 Ref.18
VAR_068866
Natural variant1471A → P in LCA9. Ref.17
VAR_068867
Natural variant1511V → F in LCA9. Ref.12 Ref.16
VAR_068868
Natural variant1531L → P in LCA9. Ref.17
VAR_068869
Natural variant1531L → V in LCA9. Ref.16
VAR_068870
Natural variant1561G → R in LCA9. Ref.18
VAR_068871
Natural variant1731D → G in LCA9. Ref.17
VAR_068872
Natural variant1781V → M in LCA9. Ref.17
VAR_068873
Natural variant1811Y → C in LCA9. Ref.17
VAR_068874
Natural variant1841I → M in LCA9. Ref.18
VAR_068875
Natural variant2071R → W in LCA9; results in significantly reduced enzymatic activity. Ref.12 Ref.17
Corresponds to variant rs142968179 [ dbSNP | Ensembl ].
VAR_068876
Natural variant2171I → N in LCA9. Ref.17
VAR_068877
Natural variant2371R → C in LCA9; does not affect nuclear localization. Ref.17 Ref.18
VAR_068878
Natural variant2371R → L in LCA9. Ref.12
VAR_068879
Natural variant2391L → S in LCA9. Ref.17
VAR_068880
Natural variant2511H → P in LCA9. Ref.17
VAR_068881
Natural variant2571E → K in LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm. Ref.12 Ref.16 Ref.18
Corresponds to variant rs150726175 [ dbSNP | Ensembl ].
VAR_068882
Natural variant2731N → D in LCA9; results in significantly reduced enzymatic activity. Ref.12 Ref.16
VAR_068883

Experimental info

Sequence conflict201I → F in AAL76934. Ref.2
Sequence conflict201I → F in AAL76935. Ref.2
Sequence conflict2171I → F in AAG33629. Ref.3

Secondary structure

............................................ 279
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HAN9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 740DE872CD9C22E7

FASTA27931,932
        10         20         30         40         50         60 
MENSEKTEVV LLACGSFNPI TNMHLRLFEL AKDYMNGTGR YTVVKGIISP VGDAYKKKGL 

        70         80         90        100        110        120 
IPAYHRVIMA ELATKNSKWV EVDTWESLQK EWKETLKVLR HHQEKLEASD CDHQQNSPTL 

       130        140        150        160        170        180 
ERPGRKRKWT ETQDSSQKKS LEPKTKAVPK VKLLCGADLL ESFAVPNLWK SEDITQIVAN 

       190        200        210        220        230        240 
YGLICVTRAG NDAQKFIYES DVLWKHRSNI HVVNEWIAND ISSTKIRRAL RRGQSIRYLV 

       250        260        270 
PDLVQEYIEK HNLYSSESED RNAGVILAPL QRNTAEAKT 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis."
Schweiger M., Hennig K., Lerner F., Niere M., Hirsch-Kauffmann M., Specht T., Weise C., Oei S.L., Ziegler M.
FEBS Lett. 492:95-100(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 208-225 AND 262-272, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH ADPRT.
[2]"Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase."
Emanuelli M., Carnevali F., Saccucci F., Pierella F., Amici A., Raffaelli N., Magni G.
J. Biol. Chem. 276:406-412(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 238-250 AND 262-272, COFACTOR, TISSUE SPECIFICITY.
Tissue: Placenta.
[3]"Human homologue of a gene mutated in the slow Wallerian degeneration (C57BL/Wld(s)) mouse."
Fernando F.S., Conforti L., Tosi S., Smith A.D., Coleman M.P.
Gene 284:23-29(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Synovium.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Eye.
[8]"Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis."
Zhang X., Kurnasov O.V., Karthikeyan S., Grishin N.V., Osterman A.L., Zhang H.
J. Biol. Chem. 278:13503-13511(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms."
Berger F., Lau C., Dahlmann M., Ziegler M.
J. Biol. Chem. 280:36334-36341(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[10]"Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis."
Sorci L., Cimadamore F., Scotti S., Petrelli R., Cappellacci L., Franchetti P., Orsomando G., Magni G.
Biochemistry 46:4912-4922(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Mutations in NMNAT1 cause Leber congenital amaurosis and identify a new disease pathway for retinal degeneration."
Koenekoop R.K., Wang H., Majewski J., Wang X., Lopez I., Ren H., Chen Y., Li Y., Fishman G.A., Genead M., Schwartzentruber J., Solanki N., Traboulsi E.I., Cheng J., Logan C.V., McKibbin M., Hayward B.E., Parry D.A. expand/collapse author list , Johnson C.A., Nageeb M., Poulter J.A., Mohamed M.D., Jafri H., Rashid Y., Taylor G.R., Keser V., Mardon G., Xu H., Inglehearn C.F., Fu Q., Toomes C., Chen R.
Nat. Genet. 44:1035-1039(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, VARIANTS LCA9 THR-13; PHE-67; GLY-98; PHE-151; TRP-207; LEU-237; LYS-257 AND ASP-273, CHARACTERIZATION OF VARIANTS LCA9 TRP-207; LYS-257 AND ASP-273.
[13]"Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN."
Werner E., Ziegler M., Lerner F., Schweiger M., Heinemann U.
FEBS Lett. 516:239-244(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 5-278.
[14]"Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis."
Garavaglia S., D'Angelo I., Emanuelli M., Carnevali F., Pierella F., Magni G., Rizzi M.
J. Biol. Chem. 277:8524-8530(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[15]"Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin."
Zhou T., Kurnasov O., Tomchick D.R., Binns D.D., Grishin N.V., Marquez V.E., Osterman A.L., Zhang H.
J. Biol. Chem. 277:13148-13154(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[16]"Exome sequencing identifies NMNAT1 mutations as a cause of Leber congenital amaurosis."
Chiang P.W., Wang J., Chen Y., Fu Q., Zhong J., Chen Y., Yi X., Wu R., Gan H., Shi Y., Chen Y., Barnett C., Wheaton D., Day M., Sutherland J., Heon E., Weleber R.G., Gabriel L.A. expand/collapse author list , Cong P., Chuang K., Ye S., Sallum J.M., Qi M.
Nat. Genet. 44:972-974(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA9 THR-35; GLY-98; PHE-151; VAL-153; LYS-257 AND ASP-273.
[17]"Mutations in NMNAT1 cause Leber congenital amaurosis with early-onset severe macular and optic atrophy."
Perrault I., Hanein S., Zanlonghi X., Serre V., Nicouleau M., Defoort-Delhemmes S., Delphin N., Fares-Taie L., Gerber S., Xerri O., Edelson C., Goldenberg A., Duncombe A., Le Meur G., Hamel C., Silva E., Nitschke P., Calvas P. expand/collapse author list , Munnich A., Roche O., Dollfus H., Kaplan J., Rozet J.M.
Nat. Genet. 44:975-977(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA9 THR-13; VAL-69; PRO-147; PRO-153; GLY-173; MET-178; CYS-181; TRP-207; ASN-217; CYS-237; SER-239 AND PRO-251.
[18]"NMNAT1 mutations cause Leber congenital amaurosis."
Falk M.J., Zhang Q., Nakamaru-Ogiso E., Kannabiran C., Fonseca-Kelly Z., Chakarova C., Audo I., Mackay D.S., Zeitz C., Borman A.D., Staniszewska M., Shukla R., Palavalli L., Mohand-Said S., Waseem N.H., Jalali S., Perin J.C., Place E. expand/collapse author list , Ostrovsky J., Xiao R., Bhattacharya S.S., Consugar M., Webster A.R., Sahel J.A., Moore A.T., Berson E.L., Liu Q., Gai X., Pierce E.A.
Nat. Genet. 44:1040-1045(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA9 MET-9; THR-13; ASN-20; GLY-33; VAL-54; TRP-66; VAL-69; HIS-72; GLY-98; ARG-156; MET-184; CYS-237 AND LYS-257, CHARACTERIZATION OF VARIANTS LCA9 MET-9; TRP-66 AND CYS-237.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF314163 mRNA. Translation: AAG33632.1.
AF312734 mRNA. Translation: AAG33629.1.
AF459819 mRNA. Translation: AAL76934.1.
AF459823 expand/collapse EMBL AC list , 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.
RefSeqNP_073624.2. NM_022787.3.
UniGeneHs.633762.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9HAN9.
SMRQ9HAN9. Positions 6-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122308. 9 interactions.
IntActQ9HAN9. 6 interactions.
STRING9606.ENSP00000366410.

PTM databases

PhosphoSiteQ9HAN9.

Polymorphism databases

DMDM30580491.

Proteomic databases

PaxDbQ9HAN9.
PeptideAtlasQ9HAN9.
PRIDEQ9HAN9.

Protocols and materials databases

DNASU64802.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377205; ENSP00000366410; ENSG00000173614.
ENST00000462686; ENSP00000435134; ENSG00000173614.
GeneID64802.
KEGGhsa:64802.
UCSCuc001aqp.3. human.

Organism-specific databases

CTD64802.
GeneCardsGC01P010003.
HGNCHGNC:17877. NMNAT1.
HPAHPA059447.
MIM608553. phenotype.
608700. gene.
neXtProtNX_Q9HAN9.
Orphanet65. Leber congenital amaurosis.
PharmGKBPA31660.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1057.
HOGENOMHOG000216047.
HOVERGENHBG052640.
InParanoidQ9HAN9.
KOK06210.
OMAVDPWEAF.
PhylomeDBQ9HAN9.
TreeFamTF315035.

Enzyme and pathway databases

BRENDA2.7.7.1. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ9HAN9.
UniPathwayUPA00253; UER00600.

Gene expression databases

ArrayExpressQ9HAN9.
BgeeQ9HAN9.
CleanExHS_NMNAT1.
GenevestigatorQ9HAN9.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR12039. PTHR12039. 1 hit.
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00482. TIGR00482. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNMNAT1. human.
EvolutionaryTraceQ9HAN9.
GeneWikiNMNAT1.
GenomeRNAi64802.
NextBio66892.
PROQ9HAN9.
SOURCESearch...

Entry information

Entry nameNMNA1_HUMAN
AccessionPrimary (citable) accession number: Q9HAN9
Secondary accession number(s): B1AN63 expand/collapse secondary AC list , Q8TAE9, Q9H247, Q9H6B6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM