Q9HAN9 (NMNA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Protein existence	Evidence 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.13
Subcellular location	Nucleus Ref.1 Ref.8 Ref.9 Ref.11.
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.11 Ref.15 Ref.16 Ref.17
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

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Nucleus
Disease	Disease mutation Leber congenital amaurosis
Ligand	ATP-binding Magnesium NAD Nucleotide-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred by curator Ref.9. Source: UniProtKB response to wounding Inferred from electronic annotation. Source: Compara water-soluble vitamin metabolic process Traceable author statement. Source: Reactome
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nicotinamide-nucleotide adenylyltransferase activity Inferred from direct assay Ref.2. Source: UniProtKB nicotinate-nucleotide adenylyltransferase activity Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SIRT1	Q96EB6	3	EBI-3917542,EBI-1802965

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 279

279

Nicotinamide mononucleotide adenylyltransferase 1

PRO_0000135012

Regions

Nucleotide binding

15 – 24

10

ATP Potential

Nucleotide binding

222 – 227

6

ATP Potential

Motif

123 – 129

7

Nuclear localization signal Potential

Sites

Binding site

16

1

Substrate By similarity

Binding site

55

1

Substrate By similarity

Binding site

158

1

Substrate By similarity

Natural variations

Natural variant

9

1

V → M in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. Ref.17

VAR_068856

Natural variant

13

1

A → T in LCA9. Ref.11 Ref.16 Ref.17
Corresponds to variant rs138613460 [ dbSNP | Ensembl ].

VAR_068857

Natural variant

20

1

I → N in LCA9. Ref.17

VAR_068858

Natural variant

33

1

D → G in LCA9. Ref.17

VAR_068859

Natural variant

35

1

M → T in LCA9. Ref.15

VAR_068860

Natural variant

54

1

A → V in LCA9. Ref.17

VAR_068861

Natural variant

66

1

R → W in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. Ref.17

VAR_068862

Natural variant

67

1

V → F in LCA9. Ref.11

VAR_068863

Natural variant

69

1

M → V in LCA9. Ref.16 Ref.17

VAR_068864

Natural variant

72

1

L → H in LCA9. Ref.17

VAR_068865

Natural variant

98

1

V → G in LCA9. Ref.11 Ref.15 Ref.17

VAR_068866

Natural variant

147

1

A → P in LCA9. Ref.16

VAR_068867

Natural variant

151

1

V → F in LCA9. Ref.11 Ref.15

VAR_068868

Natural variant

153

1

L → P in LCA9. Ref.16

VAR_068869

Natural variant

153

1

L → V in LCA9. Ref.15

VAR_068870

Natural variant

156

1

G → R in LCA9. Ref.17

VAR_068871

Natural variant

173

1

D → G in LCA9. Ref.16

VAR_068872

Natural variant

178

1

V → M in LCA9. Ref.16

VAR_068873

Natural variant

181

1

Y → C in LCA9. Ref.16

VAR_068874

Natural variant

184

1

I → M in LCA9. Ref.17

VAR_068875

Natural variant

207

1

R → W in LCA9; results in significantly reduced enzymatic activity. Ref.11 Ref.16
Corresponds to variant rs142968179 [ dbSNP | Ensembl ].

VAR_068876

Natural variant

217

1

I → N in LCA9. Ref.16

VAR_068877

Natural variant

237

1

R → C in LCA9; does not affect nuclear localization. Ref.16 Ref.17

VAR_068878

Natural variant

237

1

R → L in LCA9. Ref.11

VAR_068879

Natural variant

239

1

L → S in LCA9. Ref.16

VAR_068880

Natural variant

251

1

H → P in LCA9. Ref.16

VAR_068881

Natural variant

257

1

E → K in LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm. Ref.11 Ref.15 Ref.17
Corresponds to variant rs150726175 [ dbSNP | Ensembl ].

VAR_068882

Natural variant

273

1

N → D in LCA9; results in significantly reduced enzymatic activity. Ref.11 Ref.15

VAR_068883

Experimental info

Sequence conflict

20

1

I → F in AAL76934. Ref.2

Sequence conflict

20

1

I → F in AAL76935. Ref.2

Sequence conflict

217

1

I → F in AAG33629. Ref.3

Secondary structure

1

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279

Helix Strand Turn

Details...

Beta strand

7 – 15

9

Helix

22 – 37

16

Beta strand

39 – 50

12

Helix

53 – 55

3

Helix

63 – 73

11

Turn

74 – 76

3

Beta strand

78 – 82

5

Helix

86 – 88

3

Helix

95 – 106

12

Beta strand

150 – 156

7

Helix

157 – 162

6

Turn

166 – 168

3

Helix

171 – 180

10

Beta strand

183 – 188

6

Helix

190 – 198

9

Helix

201 – 205

5

Helix

206 – 209

4

Beta strand

210 – 214

5

Beta strand

217 – 219

3

Helix

223 – 231

9

Helix

242 – 251

10

Helix

256 – 259

4

Turn

260 – 264

5

Helix

268 – 274

7

Sequences

	Sequence		Length	Mass (Da)
	Q9HAN9 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 740DE872CD9C22E7	FASTA	279	31,932
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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. , 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.
[12]	"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.
[13]	"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).
[14]	"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).
[15]	"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. , 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.
[16]	"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. , 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.
[17]	"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. , 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 , 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.

IPI

IPI00009726.

RefSeq

NP_073624.2. NM_022787.3.

UniGene

Hs.633762.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GZU	X-ray	2.90	A/B/C	2-279	[»]
1KKU	X-ray	2.50	A	1-279	[»]
1KQN	X-ray	2.20	A/B/C/D/E/F	1-279	[»]
1KQO	X-ray	2.50	A/B/C/D/E/F	1-279	[»]
1KR2	X-ray	2.30	A/B/C/D/E/F	1-279	[»]

ProteinModelPortal

Q9HAN9.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9HAN9. 6 interactions.

STRING

9606.ENSP00000366410.

PTM databases

PhosphoSite

Q9HAN9.

Polymorphism databases

DMDM

30580491.

Proteomic databases

PaxDb

Q9HAN9.

PeptideAtlas

Q9HAN9.

PRIDE

Q9HAN9.

Protocols and materials databases

DNASU

64802.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000377205; ENSP00000366410; ENSG00000173614.
ENST00000462686; ENSP00000435134; ENSG00000173614.

GeneID

64802.

KEGG

hsa:64802.

UCSC

uc001aqp.3. human.

Organism-specific databases

CTD

64802.

GeneCards

GC01P010003.

HGNC

HGNC:17877. NMNAT1.

MIM

608553. phenotype.
608700. gene.

neXtProt

NX_Q9HAN9.

PharmGKB

PA31660.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1057.

HOGENOM

HOG000216047.

HOVERGEN

HBG052640.

InParanoid

Q9HAN9.

KO

K06210.

OMA

LISAHHR.

OrthoDB

EOG48SGV2.

PhylomeDB

Q9HAN9.

Enzyme and pathway databases

BRENDA

2.7.7.1. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

Q9HAN9.

UniPathway

UPA00253; UER00600.

Gene expression databases

ArrayExpress

Q9HAN9.

Bgee

Q9HAN9.

CleanEx

HS_NMNAT1.

Genevestigator

Q9HAN9.

GermOnline

ENSG00000173614. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

InterPro

IPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

PANTHER

PTHR12039. PTHR12039. 1 hit.

Pfam

PF01467. CTP_transf_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00482. TIGR00482. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

NMNAT1. human.

EvolutionaryTrace

Q9HAN9.

GenomeRNAi

64802.

NextBio

66892.

SOURCE

Search...

Entry information

Entry name

NMNA1_HUMAN

Accession

Primary (citable) accession number: Q9HAN9
Secondary accession number(s): B1AN63 , Q8TAE9, Q9H247, Q9H6B6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.