Skip Header

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

Q8BNJ3

- NMNA2_MOUSE

UniProt

Q8BNJ3 - NMNA2_MOUSE

(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
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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+ (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Divalent metal cations. Mg(2+) confers the highest activity.By similarity

Enzyme regulationi

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

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: UniProtKB-EC
  3. nicotinate-nucleotide adenylyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_209575. Nicotinate metabolism.
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 1 (EC:2.7.7.18)
Short name:
NaMN adenylyltransferase 1
Gene namesi
Name:Nmnat2
Synonyms:Kiaa0479
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2444155. Nmnat2.

Subcellular locationi

Cytoplasm By similarity. Golgi apparatus By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: MGI
  2. late endosome Source: MGI
  3. synapse Source: MGI
  4. trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Nicotinamide mononucleotide adenylyltransferase 2PRO_0000135015Add
BLAST

Proteomic databases

PRIDEiQ8BNJ3.

PTM databases

PhosphoSiteiQ8BNJ3.

Expressioni

Gene expression databases

BgeeiQ8BNJ3.
CleanExiMM_NMNAT2.
ExpressionAtlasiQ8BNJ3. baseline and differential.
GenevestigatoriQ8BNJ3.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8BNJ3.
SMRiQ8BNJ3. Positions 9-109, 197-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1057.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ8BNJ3.
KOiK06210.
OMAiPMERFTF.
OrthoDBiEOG7PVWPQ.
PhylomeDBiQ8BNJ3.
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]

Sequencei

Sequence statusi: Complete.

Q8BNJ3-1 [UniParc]FASTAAdd to Basket

« 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 HENTQPIYQN SNVPTKPTAA
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):34,505
Last modified:March 1, 2003 - v1
Checksum:iB9B4902D3EE03DC6
GO

Sequence cautioni

The sequence BAC97965.1 differs from that shown. Reason: Frameshift at position 252. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129155 mRNA. Translation: BAC97965.1. Frameshift.
AK083532 mRNA. Translation: BAC38943.1.
CCDSiCCDS15368.1.
RefSeqiNP_780669.1. NM_175460.3.
UniGeneiMm.40548.

Genome annotation databases

EnsembliENSMUST00000043313; ENSMUSP00000041110; ENSMUSG00000042751.
GeneIDi226518.
KEGGimmu:226518.
UCSCiuc007czq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129155 mRNA. Translation: BAC97965.1 . Frameshift.
AK083532 mRNA. Translation: BAC38943.1 .
CCDSi CCDS15368.1.
RefSeqi NP_780669.1. NM_175460.3.
UniGenei Mm.40548.

3D structure databases

ProteinModelPortali Q8BNJ3.
SMRi Q8BNJ3. Positions 9-109, 197-302.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BNJ3.

Proteomic databases

PRIDEi Q8BNJ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000043313 ; ENSMUSP00000041110 ; ENSMUSG00000042751 .
GeneIDi 226518.
KEGGi mmu:226518.
UCSCi uc007czq.1. mouse.

Organism-specific databases

CTDi 23057.
MGIi MGI:2444155. Nmnat2.
Rougei Search...

Phylogenomic databases

eggNOGi COG1057.
GeneTreei ENSGT00530000063189.
HOGENOMi HOG000216047.
HOVERGENi HBG052640.
InParanoidi Q8BNJ3.
KOi K06210.
OMAi PMERFTF.
OrthoDBi EOG7PVWPQ.
PhylomeDBi Q8BNJ3.
TreeFami TF315035.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00600 .
Reactomei REACT_209575. Nicotinate metabolism.

Miscellaneous databases

ChiTaRSi Nmnat2. mouse.
NextBioi 378196.
PROi Q8BNJ3.
SOURCEi Search...

Gene expression databases

Bgeei Q8BNJ3.
CleanExi MM_NMNAT2.
ExpressionAtlasi Q8BNJ3. baseline and differential.
Genevestigatori Q8BNJ3.

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

  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiNMNA2_MOUSE
AccessioniPrimary (citable) accession number: Q8BNJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3