Skip Header

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

Q96T66

- NMNA3_HUMAN

UniProt

Q96T66 - NMNA3_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 3

Gene

NMNAT3

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. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+. For the pyrophosphorolytic activity, can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+. Protects against axonal degeneration following injury.2 Publications

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Divalent metal cations. Mg(2+) confers the highest activity.1 Publication

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=209 µM for NMN2 Publications
  2. KM=130 µM for NAD+2 Publications
  3. KM=29 µM for ATP2 Publications
  4. KM=390 µM for PPi2 Publications
  5. KM=276 µM for GTP2 Publications
  6. KM=350 µM for ITP2 Publications
  7. KM=111 µM for NaMN2 Publications
  8. KM=130 µM for NMNH2 Publications
  9. KM=2.01 µM for triazofurin monophosphate2 Publications

Vmax=3.6 µmol/min/mg enzyme for NAD synthesis2 Publications

Vmax=12.8 µmol/min/mg enzyme for pyrophosphorolytic NAD+ cleavage2 Publications

Vmax=2.9 µmol/min/mg enzyme for pyrophosphorolytic NADH cleavage2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141Substrate
Binding sitei53 – 531Substrate
Binding sitei137 – 1371Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 2210ATPSequence Analysis
Nucleotide bindingi201 – 2066ATPSequence 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. response to wounding Source: Ensembl
  4. small molecule metabolic process Source: Reactome
  5. vitamin metabolic process Source: Reactome
  6. 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:HS08953-MONOMER.
BRENDAi2.7.7.1. 2681.
ReactomeiREACT_11088. Nicotinate metabolism.
SABIO-RKQ96T66.
UniPathwayiUPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide mononucleotide adenylyltransferase 3
Short name:
NMN adenylyltransferase 3
Alternative name(s):
Nicotinate-nucleotide adenylyltransferase 3 (EC:2.7.7.18)
Short name:
NaMN adenylyltransferase 3
Pyridine nucleotide adenylyltransferase 3 (EC:2.7.7.1)
Short name:
PNAT-3
Gene namesi
Name:NMNAT3
ORF Names:FKSG76
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:20989. NMNAT3.

Subcellular locationi

Mitochondrion 2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134952303.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252Nicotinamide mononucleotide adenylyltransferase 3PRO_0000135016Add
BLAST

Proteomic databases

MaxQBiQ96T66.
PaxDbiQ96T66.
PRIDEiQ96T66.

PTM databases

PhosphoSiteiQ96T66.

Expressioni

Tissue specificityi

Expressed in lung and spleen with lower levels in placenta and kidney.2 Publications

Gene expression databases

BgeeiQ96T66.
CleanExiHS_NMNAT3.
ExpressionAtlasiQ96T66. baseline and differential.
GenevestigatoriQ96T66.

Organism-specific databases

HPAiHPA057402.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi131564. 2 interactions.
STRINGi9606.ENSP00000340523.

Structurei

Secondary structure

1
252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Helixi20 – 3516Combined sources
Beta strandi37 – 4812Combined sources
Beta strandi54 – 563Combined sources
Helixi61 – 7111Combined sources
Helixi72 – 743Combined sources
Beta strandi76 – 805Combined sources
Helixi83 – 864Combined sources
Beta strandi87 – 893Combined sources
Helixi93 – 10412Combined sources
Beta strandi129 – 1357Combined sources
Helixi136 – 1416Combined sources
Turni145 – 1473Combined sources
Helixi150 – 15910Combined sources
Beta strandi162 – 1654Combined sources
Helixi172 – 1787Combined sources
Helixi180 – 1845Combined sources
Helixi186 – 1883Combined sources
Beta strandi189 – 1924Combined sources
Helixi202 – 2109Combined sources
Helixi221 – 2299Combined sources
Turni230 – 2334Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NUPX-ray1.90A/B1-252[»]
1NUQX-ray1.90A/B1-252[»]
1NURX-ray2.15A/B1-252[»]
1NUSX-ray2.20A/B1-252[»]
1NUTX-ray1.90A/B1-252[»]
1NUUX-ray1.90A/B1-252[»]
ProteinModelPortaliQ96T66.
SMRiQ96T66. Positions 3-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96T66.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1057.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ96T66.
KOiK06210.
OMAiHNIYTEE.
PhylomeDBiQ96T66.
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.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96T66-1) [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
MKSRIPVVLL ACGSFNPITN MHLRMFEVAR DHLHQTGMYQ VIQGIISPVN
60 70 80 90 100
DTYGKKDLAA SHHRVAMARL ALQTSDWIRV DPWESEQAQW METVKVLRHH
110 120 130 140 150
HSKLLRSPPQ MEGPDHGKAL FSTPAAVPEL KLLCGADVLK TFQTPNLWKD
160 170 180 190 200
AHIQEIVEKF GLVCVGRVGH DPKGYIAESP ILRMHQHNIH LAKEPVQNEI
210 220 230 240 250
SATYIRRALG QGQSVKYLIP DAVITYIKDH GLYTKGSTWK GKSTQSTEGK

TS
Length:252
Mass (Da):28,322
Last modified:October 17, 2006 - v2
Checksum:i6402CFB2FE789CF4
GO
Isoform 2 (identifier: Q96T66-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.

Note: No experimental confirmation available.

Show »
Length:215
Mass (Da):24,119
Checksum:i0E445A25C77E1800
GO
Isoform 3 (identifier: Q96T66-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-125: Missing.

Note: No experimental confirmation available.

Show »
Length:163
Mass (Da):18,255
Checksum:i0E9550BF1ADADFF2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691G → S in AAK52726. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3737Missing in isoform 2. 1 PublicationVSP_010267Add
BLAST
Alternative sequencei37 – 12589Missing in isoform 3. 1 PublicationVSP_043203Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF345564 mRNA. Translation: AAK52726.1.
AK123208 mRNA. Translation: BAG53878.1.
AC046134 Genomic DNA. No translation available.
AC110716 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79023.1.
CH471052 Genomic DNA. Translation: EAW79024.1.
CH471052 Genomic DNA. Translation: EAW79025.1.
CH471052 Genomic DNA. Translation: EAW79030.1.
CH471052 Genomic DNA. Translation: EAW79031.1.
BC034374 mRNA. Translation: AAH34374.1.
CCDSiCCDS3111.1. [Q96T66-2]
CCDS56282.1. [Q96T66-3]
RefSeqiNP_001186976.1. NM_001200047.1. [Q96T66-3]
NP_835471.1. NM_178177.3. [Q96T66-2]
XP_006713691.1. XM_006713628.1. [Q96T66-1]
XP_006713692.1. XM_006713629.1. [Q96T66-1]
UniGeneiHs.208673.
Hs.745268.

Genome annotation databases

EnsembliENST00000296202; ENSP00000296202; ENSG00000163864. [Q96T66-1]
ENST00000339837; ENSP00000340523; ENSG00000163864. [Q96T66-2]
ENST00000406164; ENSP00000384319; ENSG00000163864. [Q96T66-1]
ENST00000413939; ENSP00000412953; ENSG00000163864. [Q96T66-3]
GeneIDi349565.
KEGGihsa:349565.
UCSCiuc003etj.3. human. [Q96T66-1]
uc010hul.3. human. [Q96T66-3]

Polymorphism databases

DMDMi116242680.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF345564 mRNA. Translation: AAK52726.1 .
AK123208 mRNA. Translation: BAG53878.1 .
AC046134 Genomic DNA. No translation available.
AC110716 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79023.1 .
CH471052 Genomic DNA. Translation: EAW79024.1 .
CH471052 Genomic DNA. Translation: EAW79025.1 .
CH471052 Genomic DNA. Translation: EAW79030.1 .
CH471052 Genomic DNA. Translation: EAW79031.1 .
BC034374 mRNA. Translation: AAH34374.1 .
CCDSi CCDS3111.1. [Q96T66-2 ]
CCDS56282.1. [Q96T66-3 ]
RefSeqi NP_001186976.1. NM_001200047.1. [Q96T66-3 ]
NP_835471.1. NM_178177.3. [Q96T66-2 ]
XP_006713691.1. XM_006713628.1. [Q96T66-1 ]
XP_006713692.1. XM_006713629.1. [Q96T66-1 ]
UniGenei Hs.208673.
Hs.745268.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NUP X-ray 1.90 A/B 1-252 [» ]
1NUQ X-ray 1.90 A/B 1-252 [» ]
1NUR X-ray 2.15 A/B 1-252 [» ]
1NUS X-ray 2.20 A/B 1-252 [» ]
1NUT X-ray 1.90 A/B 1-252 [» ]
1NUU X-ray 1.90 A/B 1-252 [» ]
ProteinModelPortali Q96T66.
SMRi Q96T66. Positions 3-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 131564. 2 interactions.
STRINGi 9606.ENSP00000340523.

PTM databases

PhosphoSitei Q96T66.

Polymorphism databases

DMDMi 116242680.

Proteomic databases

MaxQBi Q96T66.
PaxDbi Q96T66.
PRIDEi Q96T66.

Protocols and materials databases

DNASUi 349565.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296202 ; ENSP00000296202 ; ENSG00000163864 . [Q96T66-1 ]
ENST00000339837 ; ENSP00000340523 ; ENSG00000163864 . [Q96T66-2 ]
ENST00000406164 ; ENSP00000384319 ; ENSG00000163864 . [Q96T66-1 ]
ENST00000413939 ; ENSP00000412953 ; ENSG00000163864 . [Q96T66-3 ]
GeneIDi 349565.
KEGGi hsa:349565.
UCSCi uc003etj.3. human. [Q96T66-1 ]
uc010hul.3. human. [Q96T66-3 ]

Organism-specific databases

CTDi 349565.
GeneCardsi GC03M139279.
HGNCi HGNC:20989. NMNAT3.
HPAi HPA057402.
MIMi 608702. gene.
neXtProti NX_Q96T66.
PharmGKBi PA134952303.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1057.
GeneTreei ENSGT00530000063189.
HOGENOMi HOG000216047.
HOVERGENi HBG052640.
InParanoidi Q96T66.
KOi K06210.
OMAi HNIYTEE.
PhylomeDBi Q96T66.
TreeFami TF315035.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00600 .
BioCyci MetaCyc:HS08953-MONOMER.
BRENDAi 2.7.7.1. 2681.
Reactomei REACT_11088. Nicotinate metabolism.
SABIO-RK Q96T66.

Miscellaneous databases

ChiTaRSi NMNAT3. human.
EvolutionaryTracei Q96T66.
GenomeRNAii 349565.
NextBioi 99518.
PROi Q96T66.
SOURCEi Search...

Gene expression databases

Bgeei Q96T66.
CleanExi HS_NMNAT3.
ExpressionAtlasi Q96T66. baseline and differential.
Genevestigatori Q96T66.

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. "Identification of FKSG76, a novel gene encoding a NMN adenylyltransferase."
    Wang Y.-G., Gong L.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] (ISOFORM 3).
    Tissue: Brain cortex.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Colon and Kidney.
  6. "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.
  7. "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.
  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: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NMN; NAD AND ATP ANALOG, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.

Entry informationi

Entry nameiNMNA3_HUMAN
AccessioniPrimary (citable) accession number: Q96T66
Secondary accession number(s): B3KVR6
, D3DNF2, D3DNF3, Q8N4G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 17, 2006
Last modified: November 26, 2014
This is version 112 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3