SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9HAN9

- NMNA1_HUMAN

UniProt

Q9HAN9 - NMNA1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Nicotinamide mononucleotide adenylyltransferase 1
Gene
NMNAT1, NMNAT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Divalent metal cations. Zinc confers higher activity as compared to magnesium.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 ATP
  3. KM=937 µM for PPi
  4. 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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei16 – 161Substrate By similarity
Binding sitei55 – 551Substrate By similarity
Binding sitei158 – 1581Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 2410ATP Reviewed prediction
Nucleotide bindingi222 – 2276ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nicotinamide-nucleotide adenylyltransferase activity Source: UniProtKB
  3. nicotinate-nucleotide adenylyltransferase activity Source: UniProtKB
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB
  2. NAD metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
  4. vitamin metabolic process Source: Reactome
  5. water-soluble vitamin metabolic process Source: Reactome
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.
BRENDAi2.7.7.1. 2681.
ReactomeiREACT_11088. Nicotinate metabolism.
SABIO-RKQ9HAN9.
UniPathwayiUPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide mononucleotide adenylyltransferase 1 (EC:2.7.7.1)
Short name:
NMN adenylyltransferase 1
Alternative name(s):
Nicotinate-nucleotide adenylyltransferase 1 (EC:2.7.7.18)
Short name:
NaMN adenylyltransferase 1
Gene namesi
Name:NMNAT1
Synonyms:NMNAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:17877. NMNAT1.

Subcellular locationi

Nucleus 4 Publications

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91V → M in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 Publication
VAR_068856
Natural varianti13 – 131A → T in LCA9. 3 Publications
Corresponds to variant rs138613460 [ dbSNP | Ensembl ].
VAR_068857
Natural varianti20 – 201I → N in LCA9. 1 Publication
VAR_068858
Natural varianti33 – 331D → G in LCA9. 1 Publication
VAR_068859
Natural varianti35 – 351M → T in LCA9. 1 Publication
VAR_068860
Natural varianti54 – 541A → V in LCA9. 1 Publication
VAR_068861
Natural varianti66 – 661R → W in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 Publication
VAR_068862
Natural varianti67 – 671V → F in LCA9. 1 Publication
VAR_068863
Natural varianti69 – 691M → V in LCA9. 2 Publications
VAR_068864
Natural varianti72 – 721L → H in LCA9. 1 Publication
VAR_068865
Natural varianti98 – 981V → G in LCA9. 3 Publications
VAR_068866
Natural varianti147 – 1471A → P in LCA9. 1 Publication
VAR_068867
Natural varianti151 – 1511V → F in LCA9. 2 Publications
VAR_068868
Natural varianti153 – 1531L → P in LCA9. 1 Publication
VAR_068869
Natural varianti153 – 1531L → V in LCA9. 1 Publication
VAR_068870
Natural varianti156 – 1561G → R in LCA9. 1 Publication
VAR_068871
Natural varianti173 – 1731D → G in LCA9. 1 Publication
VAR_068872
Natural varianti178 – 1781V → M in LCA9. 1 Publication
VAR_068873
Natural varianti181 – 1811Y → C in LCA9. 1 Publication
VAR_068874
Natural varianti184 – 1841I → M in LCA9. 1 Publication
VAR_068875
Natural varianti207 – 2071R → W in LCA9; results in significantly reduced enzymatic activity. 2 Publications
Corresponds to variant rs142968179 [ dbSNP | Ensembl ].
VAR_068876
Natural varianti217 – 2171I → N in LCA9. 1 Publication
VAR_068877
Natural varianti237 – 2371R → C in LCA9; does not affect nuclear localization. 2 Publications
VAR_068878
Natural varianti237 – 2371R → L in LCA9. 1 Publication
VAR_068879
Natural varianti239 – 2391L → S in LCA9. 1 Publication
VAR_068880
Natural varianti251 – 2511H → P in LCA9. 1 Publication
VAR_068881
Natural varianti257 – 2571E → K in LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm. 3 Publications
Corresponds to variant rs150726175 [ dbSNP | Ensembl ].
VAR_068882
Natural varianti273 – 2731N → D in LCA9; results in significantly reduced enzymatic activity. 2 Publications
VAR_068883

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis

Organism-specific databases

MIMi608553. phenotype.
Orphaneti65. Leber congenital amaurosis.
PharmGKBiPA31660.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279Nicotinamide mononucleotide adenylyltransferase 1
PRO_0000135012Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HAN9.
PaxDbiQ9HAN9.
PeptideAtlasiQ9HAN9.
PRIDEiQ9HAN9.

PTM databases

PhosphoSiteiQ9HAN9.

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

ArrayExpressiQ9HAN9.
BgeeiQ9HAN9.
CleanExiHS_NMNAT1.
GenevestigatoriQ9HAN9.

Organism-specific databases

HPAiHPA059447.

Interactioni

Subunit structurei

Homohexamer. Interacts with ADPRT/PARP1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SIRT1Q96EB63EBI-3917542,EBI-1802965

Protein-protein interaction databases

BioGridi122308. 8 interactions.
IntActiQ9HAN9. 6 interactions.
STRINGi9606.ENSP00000366410.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159
Helixi22 – 3716
Beta strandi39 – 5012
Helixi53 – 553
Helixi63 – 7311
Turni74 – 763
Beta strandi78 – 825
Helixi86 – 883
Helixi95 – 10612
Beta strandi150 – 1567
Helixi157 – 1626
Turni166 – 1683
Helixi171 – 18010
Beta strandi183 – 1886
Helixi190 – 1989
Helixi201 – 2055
Helixi206 – 2094
Beta strandi210 – 2145
Beta strandi217 – 2193
Helixi223 – 2319
Helixi242 – 25110
Helixi256 – 2594
Turni260 – 2645
Helixi268 – 2747

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 6-275.

Miscellaneous databases

EvolutionaryTraceiQ9HAN9.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi123 – 1297Nuclear localization signal Reviewed prediction

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1057.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ9HAN9.
KOiK06210.
OMAiHRVAMCQ.
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_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HAN9-1 [UniParc]FASTAAdd to Basket

« Hide

MENSEKTEVV LLACGSFNPI TNMHLRLFEL AKDYMNGTGR YTVVKGIISP    50
VGDAYKKKGL IPAYHRVIMA ELATKNSKWV EVDTWESLQK EWKETLKVLR 100
HHQEKLEASD CDHQQNSPTL ERPGRKRKWT ETQDSSQKKS LEPKTKAVPK 150
VKLLCGADLL ESFAVPNLWK SEDITQIVAN YGLICVTRAG NDAQKFIYES 200
DVLWKHRSNI HVVNEWIAND ISSTKIRRAL RRGQSIRYLV PDLVQEYIEK 250
HNLYSSESED RNAGVILAPL QRNTAEAKT 279
Length:279
Mass (Da):31,932
Last modified:March 1, 2001 - v1
Checksum:i740DE872CD9C22E7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91V → M in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 Publication
VAR_068856
Natural varianti13 – 131A → T in LCA9. 3 Publications
Corresponds to variant rs138613460 [ dbSNP | Ensembl ].
VAR_068857
Natural varianti20 – 201I → N in LCA9. 1 Publication
VAR_068858
Natural varianti33 – 331D → G in LCA9. 1 Publication
VAR_068859
Natural varianti35 – 351M → T in LCA9. 1 Publication
VAR_068860
Natural varianti54 – 541A → V in LCA9. 1 Publication
VAR_068861
Natural varianti66 – 661R → W in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 Publication
VAR_068862
Natural varianti67 – 671V → F in LCA9. 1 Publication
VAR_068863
Natural varianti69 – 691M → V in LCA9. 2 Publications
VAR_068864
Natural varianti72 – 721L → H in LCA9. 1 Publication
VAR_068865
Natural varianti98 – 981V → G in LCA9. 3 Publications
VAR_068866
Natural varianti147 – 1471A → P in LCA9. 1 Publication
VAR_068867
Natural varianti151 – 1511V → F in LCA9. 2 Publications
VAR_068868
Natural varianti153 – 1531L → P in LCA9. 1 Publication
VAR_068869
Natural varianti153 – 1531L → V in LCA9. 1 Publication
VAR_068870
Natural varianti156 – 1561G → R in LCA9. 1 Publication
VAR_068871
Natural varianti173 – 1731D → G in LCA9. 1 Publication
VAR_068872
Natural varianti178 – 1781V → M in LCA9. 1 Publication
VAR_068873
Natural varianti181 – 1811Y → C in LCA9. 1 Publication
VAR_068874
Natural varianti184 – 1841I → M in LCA9. 1 Publication
VAR_068875
Natural varianti207 – 2071R → W in LCA9; results in significantly reduced enzymatic activity. 2 Publications
Corresponds to variant rs142968179 [ dbSNP | Ensembl ].
VAR_068876
Natural varianti217 – 2171I → N in LCA9. 1 Publication
VAR_068877
Natural varianti237 – 2371R → C in LCA9; does not affect nuclear localization. 2 Publications
VAR_068878
Natural varianti237 – 2371R → L in LCA9. 1 Publication
VAR_068879
Natural varianti239 – 2391L → S in LCA9. 1 Publication
VAR_068880
Natural varianti251 – 2511H → P in LCA9. 1 Publication
VAR_068881
Natural varianti257 – 2571E → K in LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm. 3 Publications
Corresponds to variant rs150726175 [ dbSNP | Ensembl ].
VAR_068882
Natural varianti273 – 2731N → D in LCA9; results in significantly reduced enzymatic activity. 2 Publications
VAR_068883

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201I → F in AAL76934. 1 Publication
Sequence conflicti20 – 201I → F in AAL76935. 1 Publication
Sequence conflicti217 – 2171I → F in AAG33629. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_073624.2. NM_022787.3.
XP_006710887.1. XM_006710824.1.
UniGeneiHs.633762.

Genome annotation databases

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

Polymorphism databases

DMDMi30580491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS108.1.
RefSeqi NP_073624.2. NM_022787.3.
XP_006710887.1. XM_006710824.1.
UniGenei Hs.633762.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q9HAN9.
SMRi Q9HAN9. Positions 6-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122308. 8 interactions.
IntActi Q9HAN9. 6 interactions.
STRINGi 9606.ENSP00000366410.

PTM databases

PhosphoSitei Q9HAN9.

Polymorphism databases

DMDMi 30580491.

Proteomic databases

MaxQBi Q9HAN9.
PaxDbi Q9HAN9.
PeptideAtlasi Q9HAN9.
PRIDEi Q9HAN9.

Protocols and materials databases

DNASUi 64802.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377205 ; ENSP00000366410 ; ENSG00000173614 .
ENST00000462686 ; ENSP00000435134 ; ENSG00000173614 .
GeneIDi 64802.
KEGGi hsa:64802.
UCSCi uc001aqp.3. human.

Organism-specific databases

CTDi 64802.
GeneCardsi GC01P010003.
GeneReviewsi NMNAT1.
HGNCi HGNC:17877. NMNAT1.
HPAi HPA059447.
MIMi 608553. phenotype.
608700. gene.
neXtProti NX_Q9HAN9.
Orphaneti 65. Leber congenital amaurosis.
PharmGKBi PA31660.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1057.
HOGENOMi HOG000216047.
HOVERGENi HBG052640.
InParanoidi Q9HAN9.
KOi K06210.
OMAi HRVAMCQ.
PhylomeDBi Q9HAN9.
TreeFami TF315035.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00600 .
BioCyci MetaCyc:HS10701-MONOMER.
BRENDAi 2.7.7.1. 2681.
Reactomei REACT_11088. Nicotinate metabolism.
SABIO-RK Q9HAN9.

Miscellaneous databases

ChiTaRSi NMNAT1. human.
EvolutionaryTracei Q9HAN9.
GeneWikii NMNAT1.
GenomeRNAii 64802.
NextBioi 66892.
PROi Q9HAN9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9HAN9.
Bgeei Q9HAN9.
CleanExi HS_NMNAT1.
Genevestigatori Q9HAN9.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
InterProi IPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
PANTHERi PTHR12039. PTHR12039. 1 hit.
Pfami PF01467. CTP_transf_2. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00482. TIGR00482. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: VARIANTS LCA9 THR-35; GLY-98; PHE-151; VAL-153; LYS-257 AND ASP-273.
  17. 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. 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.

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: September 3, 2014
This is version 119 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

External Data

Dasty 3

Similar proteinsi