Skip Header

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

Q9BZQ4

- NMNA2_HUMAN

UniProt

Q9BZQ4 - NMNA2_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 2

Gene

NMNAT2

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 but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+. For the pyrophosphorolytic activity prefers NAD+, NADH and NAAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+.2 Publications

Catalytic activityi

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

Cofactori

Mg2+3 PublicationsNote: Divalent metal cations. Mg(2+) confers the highest activity.3 Publications

Enzyme regulationi

Inhibited by P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate (Np3AD) and P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate (Np4AD).1 Publication

Kineticsi

KM is >100 µM for triazofurin monophosphate.

  1. KM=32 µM for NMN2 Publications
  2. KM=70 µM for NAD+2 Publications
  3. KM=204 µM for ATP2 Publications
  4. KM=1119 µM for PPi2 Publications
  5. KM=14.5 µM for NaMN2 Publications
  6. KM=304 µM for NMNH2 Publications

Vmax=1.1 µmol/min/mg enzyme for NAD synthesis2 Publications

Vmax=3 µmol/min/mg enzyme for pyrophosphorolytic NAD+ cleavage2 Publications

Vmax=7 µmol/min/mg enzyme for pyrophosphorolytic NADH cleavage2 Publications

pH dependencei

Optimum pH is 6.0-9.0.3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei16 – 161SubstrateBy similarity
Binding sitei55 – 551SubstrateBy similarity
Binding sitei202 – 2021SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 2410ATPSequence Analysis
Nucleotide bindingi269 – 2746ATPSequence Analysis

GO - Molecular functioni

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

Enzyme and pathway databases

BioCyciMetaCyc:HS08173-MONOMER.
BRENDAi2.7.7.1. 2681.
ReactomeiREACT_11088. Nicotinate metabolism.
SABIO-RKQ9BZQ4.
UniPathwayiUPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide mononucleotide adenylyltransferase 2 (EC:2.7.7.1)
Short name:
NMN adenylyltransferase 2
Alternative name(s):
Nicotinate-nucleotide adenylyltransferase 2 (EC:2.7.7.18)
Short name:
NaMN adenylyltransferase 2
Gene namesi
Name:NMNAT2
Synonyms:C1orf15, KIAA0479
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16789. NMNAT2.

Subcellular locationi

Cytoplasm 1 Publication. Golgi apparatus 1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. Golgi membrane Source: Reactome
  3. late endosome Source: Ensembl
  4. synapse Source: Ensembl
  5. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241H → A: Reduces activity by 95%. 1 Publication
Mutagenesisi92 – 921W → G: Reduces activity by 95%. 1 Publication

Organism-specific databases

PharmGKBiPA25604.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Nicotinamide mononucleotide adenylyltransferase 2PRO_0000135014Add
BLAST

Proteomic databases

PaxDbiQ9BZQ4.
PRIDEiQ9BZQ4.

PTM databases

PhosphoSiteiQ9BZQ4.

Expressioni

Tissue specificityi

Highly expressed in brain, in particular in cerebrum, cerebellum, occipital lobe, frontal lobe, temporal lobe and putamen. Also found in the heart, skeletal muscle, pancreas and islets of Langerhans.3 Publications

Gene expression databases

BgeeiQ9BZQ4.
CleanExiHS_NMNAT2.
GenevestigatoriQ9BZQ4.

Organism-specific databases

HPAiHPA015240.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi116693. 1 interaction.
DIPiDIP-60169N.
STRINGi9606.ENSP00000287713.

Structurei

3D structure databases

ProteinModelPortaliQ9BZQ4.
SMRiQ9BZQ4. Positions 9-109, 197-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1057.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ9BZQ4.
KOiK06210.
OMAiPMERFTF.
OrthoDBiEOG7PVWPQ.
PhylomeDBiQ9BZQ4.
TreeFamiTF315035.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BZQ4-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP
60 70 80 90 100
VHDSYGKQGL VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE
110 120 130 140 150
HHRDLMKRVT GCILSNVNTP SMTPVIGQPQ NETPQPIYQN SNVATKPTAA
160 170 180 190 200
KILGKVGESL SRICCVRPPV ERFTFVDENA NLGTVMRYEE IELRILLLCG
210 220 230 240 250
SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI MNHSSILRKY
260 270 280 290 300
KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ

LYINASG
Length:307
Mass (Da):34,439
Last modified:June 1, 2001 - v1
Checksum:i702F1C74B38ECECB
GO
Isoform 2 (identifier: Q9BZQ4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: MTETTKTHVILLACGSFNPITKGHIQMF → MEIQELEEIQACQGLWEVFVTLS

Note: No experimental confirmation available.

Show »
Length:302
Mass (Da):34,015
Checksum:i782C9FB1D5B0E153
GO

Sequence cautioni

The sequence BAA32324.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828MTETT…HIQMF → MEIQELEEIQACQGLWEVFV TLS in isoform 2. 1 PublicationVSP_015571Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288395 mRNA. Translation: AAG60615.1.
AB007948 mRNA. Translation: BAA32324.1. Different initiation.
AL354953, AL356981 Genomic DNA. Translation: CAH70979.1.
AL354953, AL356981, AL449223 Genomic DNA. Translation: CAH70982.1.
AL356981, AL354953 Genomic DNA. Translation: CAI15467.1.
AL356981, AL354953, AL449223 Genomic DNA. Translation: CAI15468.1.
AL449223, AL354953, AL356981 Genomic DNA. Translation: CAI16624.1.
BC020998 mRNA. Translation: AAH20998.1.
CCDSiCCDS1353.1. [Q9BZQ4-1]
CCDS1354.1. [Q9BZQ4-2]
RefSeqiNP_055854.1. NM_015039.3. [Q9BZQ4-1]
NP_733820.1. NM_170706.3. [Q9BZQ4-2]
UniGeneiHs.497123.

Genome annotation databases

EnsembliENST00000287713; ENSP00000287713; ENSG00000157064. [Q9BZQ4-1]
ENST00000294868; ENSP00000294868; ENSG00000157064. [Q9BZQ4-2]
GeneIDi23057.
KEGGihsa:23057.
UCSCiuc001gqb.2. human. [Q9BZQ4-2]
uc001gqc.2. human. [Q9BZQ4-1]

Polymorphism databases

DMDMi30580486.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288395 mRNA. Translation: AAG60615.1 .
AB007948 mRNA. Translation: BAA32324.1 . Different initiation.
AL354953 , AL356981 Genomic DNA. Translation: CAH70979.1 .
AL354953 , AL356981 , AL449223 Genomic DNA. Translation: CAH70982.1 .
AL356981 , AL354953 Genomic DNA. Translation: CAI15467.1 .
AL356981 , AL354953 , AL449223 Genomic DNA. Translation: CAI15468.1 .
AL449223 , AL354953 , AL356981 Genomic DNA. Translation: CAI16624.1 .
BC020998 mRNA. Translation: AAH20998.1 .
CCDSi CCDS1353.1. [Q9BZQ4-1 ]
CCDS1354.1. [Q9BZQ4-2 ]
RefSeqi NP_055854.1. NM_015039.3. [Q9BZQ4-1 ]
NP_733820.1. NM_170706.3. [Q9BZQ4-2 ]
UniGenei Hs.497123.

3D structure databases

ProteinModelPortali Q9BZQ4.
SMRi Q9BZQ4. Positions 9-109, 197-302.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116693. 1 interaction.
DIPi DIP-60169N.
STRINGi 9606.ENSP00000287713.

PTM databases

PhosphoSitei Q9BZQ4.

Polymorphism databases

DMDMi 30580486.

Proteomic databases

PaxDbi Q9BZQ4.
PRIDEi Q9BZQ4.

Protocols and materials databases

DNASUi 23057.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000287713 ; ENSP00000287713 ; ENSG00000157064 . [Q9BZQ4-1 ]
ENST00000294868 ; ENSP00000294868 ; ENSG00000157064 . [Q9BZQ4-2 ]
GeneIDi 23057.
KEGGi hsa:23057.
UCSCi uc001gqb.2. human. [Q9BZQ4-2 ]
uc001gqc.2. human. [Q9BZQ4-1 ]

Organism-specific databases

CTDi 23057.
GeneCardsi GC01M183217.
HGNCi HGNC:16789. NMNAT2.
HPAi HPA015240.
MIMi 608701. gene.
neXtProti NX_Q9BZQ4.
PharmGKBi PA25604.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1057.
GeneTreei ENSGT00530000063189.
HOGENOMi HOG000216047.
HOVERGENi HBG052640.
InParanoidi Q9BZQ4.
KOi K06210.
OMAi PMERFTF.
OrthoDBi EOG7PVWPQ.
PhylomeDBi Q9BZQ4.
TreeFami TF315035.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00600 .
BioCyci MetaCyc:HS08173-MONOMER.
BRENDAi 2.7.7.1. 2681.
Reactomei REACT_11088. Nicotinate metabolism.
SABIO-RK Q9BZQ4.

Miscellaneous databases

ChiTaRSi NMNAT2. human.
GeneWikii NMNAT2.
GenomeRNAii 23057.
NextBioi 44115.
PROi Q9BZQ4.
SOURCEi Search...

Gene expression databases

Bgeei Q9BZQ4.
CleanExi HS_NMNAT2.
Genevestigatori Q9BZQ4.

Family and domain databases

Gene3Di 3.40.50.620. 2 hits.
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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus."
    Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M., Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H., Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M., Carpten J.D.
    Genomics 73:211-222(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
    Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
    DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "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].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lung carcinoma.
  5. "Identification of a novel human nicotinamide mononucleotide adenylyltransferase."
    Raffaelli N., Sorci L., Amici A., Emanuelli M., Mazzola F., Magni G.
    Biochem. Biophys. Res. Commun. 297:835-840(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, COFACTOR, TISSUE SPECIFICITY, PH DEPENDENCE.
  6. "Characterization of human brain nicotinamide 5'-mononucleotide adenylyltransferase-2 and expression in human pancreas."
    Yalowitz J.A., Xiao S., Biju M.P., Antony A.C., Cummings O.W., Deeg M.A., Jayaram H.N.
    Biochem. J. 377:317-326(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-24 AND TRP-92, COFACTOR, TISSUE SPECIFICITY.
  7. "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: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "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.

Entry informationi

Entry nameiNMNA2_HUMAN
AccessioniPrimary (citable) accession number: Q9BZQ4
Secondary accession number(s): O75067
, Q5T1Q3, Q8WU99, Q96QW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 111 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3