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Protein

N-acetylaspartate synthetase

Gene

NAT8L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the regulation of lipogenesis by producing N-acetylaspartate acid (NAA), a brain-specific metabolite. NAA occurs in high concentration in brain and its hydrolysis plays a significant part in the maintenance of intact white matter. Promotes dopamine uptake by regulating TNF-alpha expression. Attenuates methamphetamine-induced inhibition of dopamine uptake.1 Publication

Catalytic activityi

Acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate.

Enzyme regulationi

Aminooxyacetic acid (AOAA) blocks its activity in both cytoplasm and mitochondria.1 Publication

GO - Molecular functioni

  • aspartate N-acetyltransferase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.17. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylaspartate synthetase (EC:2.3.1.17)
Short name:
NAA synthetase
Alternative name(s):
Camello-like protein 3
N-acetyltransferase 8-like protein
Gene namesi
Name:NAT8L
Synonyms:CML3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:26742. NAT8L.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei121 – 14121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial membrane Source: UniProtKB
  • mitochondrion Source: HPA
  • rough endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

N-acetylaspartate deficiency (NACED)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA metabolic disorder resulting in truncal ataxia, marked developmental delay, seizures, and secondary microcephaly.
See also OMIM:614063

Organism-specific databases

MalaCardsiNAT8L.
MIMi614063. phenotype.
PharmGKBiPA162396985.

Polymorphism and mutation databases

BioMutaiNAT8L.
DMDMi259016335.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302N-acetylaspartate synthetasePRO_0000305229Add
BLAST

Proteomic databases

EPDiQ8N9F0.
MaxQBiQ8N9F0.
PaxDbiQ8N9F0.
PeptideAtlasiQ8N9F0.
PRIDEiQ8N9F0.

Expressioni

Tissue specificityi

Expressed in brain.1 Publication

Inductioni

By methamphetamine in brain, via dopamine receptor activation (at protein level).1 Publication

Gene expression databases

BgeeiQ8N9F0.
CleanExiHS_NAT8L.
ExpressionAtlasiQ8N9F0. baseline and differential.
GenevisibleiQ8N9F0. HS.

Organism-specific databases

HPAiHPA040677.

Interactioni

Protein-protein interaction databases

BioGridi130978. 4 interactions.
STRINGi9606.ENSP00000413064.

Structurei

3D structure databases

ProteinModelPortaliQ8N9F0.
SMRiQ8N9F0. Positions 143-289.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini143 – 283141N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi40 – 7334Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the camello family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KDG3. Eukaryota.
ENOG410YY26. LUCA.
GeneTreeiENSGT00390000009559.
HOGENOMiHOG000202639.
HOVERGENiHBG108173.
InParanoidiQ8N9F0.
KOiK18309.
OMAiPDMVCET.
OrthoDBiEOG73Z2W2.
PhylomeDBiQ8N9F0.
TreeFamiTF324687.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N9F0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHCGPPDMVC ETKIVAAEDH EALPGAKKDA LLAAAGAMWP PLPAAPGPAA
60 70 80 90 100
APPAPPPAPV AQPHGGAGGA GPPGGRGVCI REFRAAEQEA ARRIFYDGIM
110 120 130 140 150
ERIPNTAFRG LRQHPRAQLL YALLAALCFA VSRSLLLTCL VPAALLGLRY
160 170 180 190 200
YYSRKVIRAY LECALHTDMA DIEQYYMKPP GSCFWVAVLD GNVVGIVAAR
210 220 230 240 250
AHEEDNTVEL LRMSVDSRFR GKGIAKALGR KVLEFAVVHN YSAVVLGTTA
260 270 280 290 300
VKVAAHKLYE SLGFRHMGAS DHYVLPGMTL SLAERLFFQV RYHRYRLQLR

EE
Length:302
Mass (Da):32,837
Last modified:September 22, 2009 - v3
Checksum:i2080E54930F3292B
GO

Sequence cautioni

The sequence AAH93906.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH93908.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAI03749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC04426.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAM15218.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132868 Genomic DNA. Translation: CAM15218.1. Sequence problems.
CN256164 mRNA. No translation available.
BC093906 mRNA. Translation: AAH93906.1. Different initiation.
BC093908 mRNA. Translation: AAH93908.1. Different initiation.
BC103748 mRNA. Translation: AAI03749.1. Different initiation.
AK094797 mRNA. Translation: BAC04426.1. Different initiation.
CCDSiCCDS3359.2.
RefSeqiNP_848652.2. NM_178557.3.
UniGeneiHs.318529.

Genome annotation databases

EnsembliENST00000423729; ENSP00000413064; ENSG00000185818.
GeneIDi339983.
KEGGihsa:339983.
UCSCiuc003geq.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132868 Genomic DNA. Translation: CAM15218.1. Sequence problems.
CN256164 mRNA. No translation available.
BC093906 mRNA. Translation: AAH93906.1. Different initiation.
BC093908 mRNA. Translation: AAH93908.1. Different initiation.
BC103748 mRNA. Translation: AAI03749.1. Different initiation.
AK094797 mRNA. Translation: BAC04426.1. Different initiation.
CCDSiCCDS3359.2.
RefSeqiNP_848652.2. NM_178557.3.
UniGeneiHs.318529.

3D structure databases

ProteinModelPortaliQ8N9F0.
SMRiQ8N9F0. Positions 143-289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130978. 4 interactions.
STRINGi9606.ENSP00000413064.

Polymorphism and mutation databases

BioMutaiNAT8L.
DMDMi259016335.

Proteomic databases

EPDiQ8N9F0.
MaxQBiQ8N9F0.
PaxDbiQ8N9F0.
PeptideAtlasiQ8N9F0.
PRIDEiQ8N9F0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000423729; ENSP00000413064; ENSG00000185818.
GeneIDi339983.
KEGGihsa:339983.
UCSCiuc003geq.3. human.

Organism-specific databases

CTDi339983.
GeneCardsiNAT8L.
H-InvDBHIX0024613.
HGNCiHGNC:26742. NAT8L.
HPAiHPA040677.
MalaCardsiNAT8L.
MIMi610647. gene.
614063. phenotype.
neXtProtiNX_Q8N9F0.
PharmGKBiPA162396985.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KDG3. Eukaryota.
ENOG410YY26. LUCA.
GeneTreeiENSGT00390000009559.
HOGENOMiHOG000202639.
HOVERGENiHBG108173.
InParanoidiQ8N9F0.
KOiK18309.
OMAiPDMVCET.
OrthoDBiEOG73Z2W2.
PhylomeDBiQ8N9F0.
TreeFamiTF324687.

Enzyme and pathway databases

BRENDAi2.3.1.17. 2681.

Miscellaneous databases

ChiTaRSiNAT8L. human.
GenomeRNAii339983.
PROiQ8N9F0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N9F0.
CleanExiHS_NAT8L.
ExpressionAtlasiQ8N9F0. baseline and differential.
GenevisibleiQ8N9F0. HS.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation."
    Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y., Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J., Stanton L.W.
    Nat. Biotechnol. 22:707-716(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-291.
  3. "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] OF 112-302.
    Tissue: Brain and PNS.
  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] OF 117-302.
    Tissue: Brain.
  5. "Overexpression of camello, a member of a novel protein family, reduces blastomere adhesion and inhibits gastrulation in Xenopus laevis."
    Popsueva A.E., Luchinskaya N.N., Ludwig A.V., Zinovjeva O.Y., Poteryaev D.A., Feigelman M.M., Ponomarev M.B., Berekelya L., Belyavsky A.V.
    Dev. Biol. 234:483-496(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "Evidence for mitochondrial and cytoplasmic N-acetylaspartate synthesis in SH-SY5Y neuroblastoma cells."
    Arun P., Moffett J.R., Namboodiri A.M.
    Neurochem. Int. 55:219-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. Cited for: TISSUE SPECIFICITY, INVOLVEMENT IN NACED.
  8. "Methamphetamine-induced neuronal protein NAT8L is the NAA biosynthetic enzyme: implications for specialized acetyl coenzyme A metabolism in the CNS."
    Ariyannur P.S., Moffett J.R., Manickam P., Pattabiraman N., Arun P., Nitta A., Nabeshima T., Madhavarao C.N., Namboodiri A.M.
    Brain Res. 1335:1-13(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INDUCTION BY METHAMPHETAMINE, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiNAT8L_HUMAN
AccessioniPrimary (citable) accession number: Q8N9F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 22, 2009
Last modified: July 6, 2016
This is version 109 of the entry and version 3 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 4
    Human chromosome 4: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.