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P41227 (NAA10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-alpha-acetyltransferase 10

EC=2.3.1.-
EC=2.3.1.88
Alternative name(s):
N-terminal acetyltransferase complex ARD1 subunit homolog A
NatA catalytic subunit Naa10
Gene names
Name:NAA10
Synonyms:ARD1, ARD1A, TE2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation. Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration. Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development. Ref.2 Ref.6 Ref.14 Ref.16

Catalytic activity

Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.

Subunit structure

Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 and NAA15 or NAA16. Interacts with HIF1A (via its ODD domain); the interaction increases HIF1A protein stability during normoxia, an down-regulates it when induced by hypoxia. Interacts with NAA50 and with the ribosome. Binds to MYLK. Associates with HYPK when in complex with NAA15. Interacts (via its C-terminal domain) with TSC2, leading to its acetylation. Ref.2 Ref.6 Ref.8 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

Cytoplasm. Nucleus. Note: According to Ref.6 it is cytoplasmic. According to Ref.2, it is nuclear and cytoplasmic. Also present in the free cytosolic and cytoskeleton-bound polysomes. Ref.2 Ref.6

Tissue specificity

Ubiquitous. Ref.6

Post-translational modification

Cleaved by caspases during apoptosis.

Phosphorylation by IKBKB/IKKB at Ser-209 promotes its proteasome-mediated degradation.

Involvement in disease

N-terminal acetyltransferase deficiency (NATD) [MIM:300855]: An enzymatic deficiency resulting in postnatal growth failure with severe delays and dysmorphic features. It is clinically characterized by wrinkled forehead, prominent eyes, widely opened anterior and posterior fontanels, downsloping palpebral fissures, thickened lids, large ears, flared nares, hypoplastic alae, short columella, protruding upper lip, and microretrognathia. There are also delayed closing of fontanels and broad great toes. Skin is characterized by redundancy or laxity with minimal subcutaneous fat, cutaneous capillary malformations, and very fine hair and eyebrows. Death results from cardiogenic shock following arrhythmia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Microphthalmia, syndromic, 1 (MCOPS1) [MIM:309800]: A rare syndrome defined by the canonical features of unilateral or bilateral microphthalmia or anophthalmia and defects in the skeletal and genitourinary systems. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. Anomalies of the digits, teeth, and ears are hallmarks of MCOPS1. Intellectual disability ranges from mild to severe, with self-mutilating behaviors and seizures in severely affected MCOPS1 individuals.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Sequence similarities

Belongs to the acetyltransferase family. ARD1 subfamily.

Contains 1 N-acetyltransferase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARHGEF6Q150523EBI-747693,EBI-1642523
ARHGEF7Q141553EBI-747693,EBI-717515
Arhgef7O550433EBI-747693,EBI-3649585From a different organism.
NAA50Q9GZZ12EBI-747693,EBI-1052523

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P41227-1)

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.
Isoform 2 (identifier: P41227-2)

The sequence of this isoform differs from the canonical sequence as follows:
     114-128: Missing.
     129-129: Q → R

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 235235N-alpha-acetyltransferase 10
PRO_0000074532

Regions

Domain1 – 152152N-acetyltransferase
Region1 – 5858Interaction with NAA15

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10
Modified residue1821Phosphoserine Ref.7 Ref.17 Ref.19
Modified residue1861Phosphoserine Ref.9
Modified residue2051Phosphoserine Ref.9 Ref.17 Ref.19
Modified residue2091Phosphoserine; by IKKB Ref.13
Modified residue2131Phosphoserine Ref.17
Modified residue2161Phosphoserine Ref.17

Natural variations

Alternative sequence114 – 12815Missing in isoform 2.
VSP_046205
Alternative sequence1291Q → R in isoform 2.
VSP_046206
Natural variant371S → P in NATD; in vitro assays of protein function demonstrates 60 to 80% reduction in NAT activity of the mutant protein toward the in vivo substrate RPP30 protein; the activity toward the substrate HMGA1 protein is reduced by only 20%. Ref.21
VAR_066652

Experimental info

Mutagenesis2091S → A: Abolishes phosphorylation by IKKB and reduces cell growth. Ref.13

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 6393A907F5C2DDC4

FASTA23526,459
        10         20         30         40         50         60 
MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM 

        70         80         90        100        110        120 
EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH 

       130        140        150        160        170        180 
LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV 

       190        200        210        220        230 
ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS 

« Hide

Isoform 2 [UniParc].

Checksum: FF22A79BB1ACA0BC
Show »

FASTA22024,784

References

« Hide 'large scale' references
[1]"Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae."
Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C., Torri G., Toniolo D.
Hum. Mol. Genet. 3:1061-1068(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification and characterization of the human ARD1-NATH protein acetyltransferase complex."
Arnesen T., Anderson D., Baldersheim C., Lanotte M., Varhaug J.E., Lillehaug J.R.
Biochem. J. 386:433-443(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NAA15 AND RIBOSOMAL PROTEINS.
Tissue: Thyroid carcinoma.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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 1).
Tissue: Lung.
[6]"Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation."
Jeong J.-W., Bae M.-K., Ahn M.-Y., Kim S.-H., Sohn T.-K., Bae M.-H., Yoo M.-A., Song E.-J., Lee K.-J., Kim K.-W.
Cell 111:709-720(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIF1A, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex."
Arnesen T., Anderson D., Torsvik J., Halseth H.B., Varhaug J.E., Lillehaug J.R.
Gene 371:291-295(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAA50.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"A novel human NatA Nalpha-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)."
Arnesen T., Gromyko D., Kagabo D., Betts M.J., Starheim K.K., Varhaug J.E., Anderson D., Lillehaug J.R.
BMC Biochem. 10:15-15(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAA16.
[12]"A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates."
Polevoda B., Arnesen T., Sherman F.
BMC Proc. 3:S2-S2(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[13]"Phosphorylation of ARD1 by IKKbeta contributes to its destabilization and degradation."
Kuo H.P., Lee D.F., Xia W., Lai C.C., Li L.Y., Hung M.C.
Biochem. Biophys. Res. Commun. 389:156-161(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-209 BY IKBKB, MUTAGENESIS OF SER-209, INTERACTION WITH IKBKB.
[14]"Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase."
Shin D.H., Chun Y.-S., Lee K.-H., Shin H.-W., Park J.-W.
PLoS ONE 4:E7451-E7451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYLK.
[15]"The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation."
Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H., Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.
Mol. Cell. Biol. 30:1898-1909(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[16]"ARD1 stabilization of TSC2 suppresses tumorigenesis through the mTOR signaling pathway."
Kuo H.P., Lee D.F., Chen C.T., Liu M., Chou C.K., Lee H.J., Du Y., Xie X., Wei Y., Xia W., Weihua Z., Yang J.Y., Yen C.J., Huang T.H., Tan M., Xing G., Zhao Y., Lin C.H. expand/collapse author list , Tsai S.F., Fidler I.J., Hung M.C.
Sci. Signal. 3:RA9-RA9(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TSC2, FUNCTION IN ACETYLATION OF TSC2.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-205; SER-213 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"A splice donor mutation in NAA10 results in the dysregulation of the retinoic acid signalling pathway and causes Lenz microphthalmia syndrome."
Esmailpour T., Riazifar H., Liu L., Donkervoort S., Huang V.H., Madaan S., Shoucri B.M., Busch A., Wu J., Towbin A., Chadwick R.B., Sequeira A., Vawter M.P., Sun G., Johnston J.J., Biesecker L.G., Kawaguchi R., Sun H., Kimonis V., Huang T.
J. Med. Genet. 51:185-196(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MCOPS1.
[21]"Using VAAST to identify an X-linked disorder resulting in lethality in male infants due to N-terminal acetyltransferase deficiency."
Rope A.F., Wang K., Evjenth R., Xing J., Johnston J.J., Swensen J.J., Johnson W.E., Moore B., Huff C.D., Bird L.M., Carey J.C., Opitz J.M., Stevens C.A., Jiang T., Schank C., Fain H.D., Robison R., Dalley B. expand/collapse author list , Chin S., South S.T., Pysher T.J., Jorde L.B., Hakonarson H., Lillehaug J.R., Biesecker L.G., Yandell M., Arnesen T., Lyon G.J.
Am. J. Hum. Genet. 89:28-43(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NATD PRO-37, CHARACTERIZATION OF VARIANT NATD PRO-37.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77588 mRNA. Translation: CAA54691.1.
U52112 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72774.1.
BC000308 mRNA. Translation: AAH00308.1.
BC019312 mRNA. Translation: AAH19312.1.
CCDSCCDS14737.1. [P41227-1]
CCDS59179.1. [P41227-2]
PIRI38333.
RefSeqNP_001243048.1. NM_001256119.1. [P41227-2]
NP_003482.1. NM_003491.3. [P41227-1]
UniGeneHs.433291.

3D structure databases

ProteinModelPortalP41227.
SMRP41227. Positions 1-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113881. 20 interactions.
IntActP41227. 16 interactions.
MINTMINT-1499850.
STRING9606.ENSP00000417763.

PTM databases

PhosphoSiteP41227.

Polymorphism databases

DMDM728880.

Proteomic databases

MaxQBP41227.
PaxDbP41227.
PRIDEP41227.

Protocols and materials databases

DNASU8260.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370009; ENSP00000359026; ENSG00000102030. [P41227-2]
ENST00000464845; ENSP00000417763; ENSG00000102030. [P41227-1]
ENST00000596061; ENSP00000469041; ENSG00000268281. [P41227-2]
ENST00000596770; ENSP00000469576; ENSG00000268281. [P41227-1]
GeneID8260.
KEGGhsa:8260.
UCSCuc004fjm.2. human. [P41227-1]
uc004fjn.2. human.

Organism-specific databases

CTD8260.
GeneCardsGC0XM153194.
HGNCHGNC:18704. NAA10.
HPACAB006269.
HPA030711.
MIM300013. gene.
300855. phenotype.
309800. phenotype.
neXtProtNX_P41227.
Orphanet568. Microphthalmia, Lenz type.
276432. Premature ageing appearance-developmental delay-cardiac arrhythmia syndrome.
PharmGKBPA38648.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0456.
HOGENOMHOG000078523.
HOVERGENHBG050561.
InParanoidP41227.
KOK00670.
PhylomeDBP41227.
TreeFamTF300078.

Gene expression databases

ArrayExpressP41227.
BgeeP41227.
CleanExHS_ARD1A.
GenevestigatorP41227.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNAA10. human.
GeneWikiARD1A.
GenomeRNAi8260.
NextBio31019.
PROP41227.
SOURCESearch...

Entry information

Entry nameNAA10_HUMAN
AccessionPrimary (citable) accession number: P41227
Secondary accession number(s): A6NM98
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM