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P41227

- NAA10_HUMAN

UniProt

P41227 - NAA10_HUMAN

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Protein

N-alpha-acetyltransferase 10

Gene

NAA10

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

Functioni

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.4 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. N-acetyltransferase activity Source: ProtInc
  2. peptide alpha-N-acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA packaging Source: ProtInc
  2. internal protein amino acid acetylation Source: ProtInc
  3. N-terminal protein amino acid acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:NAA10
Synonyms:ARD1, ARD1A, TE2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:18704. NAA10.

Subcellular locationi

Cytoplasm. Nucleus
Note: According to PubMed:12464182 it is cytoplasmic. According to PubMed:15496142, it is nuclear and cytoplasmic. Also present in the free cytosolic and cytoskeleton-bound polysomes.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. intracellular Source: LIFEdb
  3. membrane Source: UniProtKB
  4. NatA complex Source: UniProt
  5. nucleolus Source: HPA
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371S → 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%. 1 Publication
VAR_066652
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091S → A: Abolishes phosphorylation by IKKB and reduces cell growth. 1 Publication

Keywords - Diseasei

Disease mutation, Microphthalmia

Organism-specific databases

MIMi300855. phenotype.
309800. phenotype.
Orphaneti568. Microphthalmia, Lenz type.
276432. Premature aging appearance-developmental delay-cardiac arrhythmia syndrome.
PharmGKBiPA38648.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235N-alpha-acetyltransferase 10PRO_0000074532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei182 – 1821Phosphoserine3 Publications
Modified residuei186 – 1861Phosphoserine1 Publication
Modified residuei205 – 2051Phosphoserine3 Publications
Modified residuei209 – 2091Phosphoserine; by IKKB1 Publication
Modified residuei213 – 2131Phosphoserine1 Publication
Modified residuei216 – 2161Phosphoserine1 Publication

Post-translational modificationi

Cleaved by caspases during apoptosis.
Phosphorylation by IKBKB/IKKB at Ser-209 promotes its proteasome-mediated degradation.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41227.
PaxDbiP41227.
PRIDEiP41227.

PTM databases

PhosphoSiteiP41227.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiP41227.
CleanExiHS_ARD1A.
ExpressionAtlasiP41227. baseline and differential.
GenevestigatoriP41227.

Organism-specific databases

HPAiCAB006269.
HPA030711.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi113881. 26 interactions.
IntActiP41227. 15 interactions.
MINTiMINT-1499850.
STRINGi9606.ENSP00000417763.

Structurei

3D structure databases

ProteinModelPortaliP41227.
SMRiP41227. Positions 1-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 152152N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5858Interaction with NAA15Add
BLAST

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0456.
GeneTreeiENSGT00550000074803.
HOGENOMiHOG000078523.
HOVERGENiHBG050561.
InParanoidiP41227.
KOiK00670.
PhylomeDBiP41227.
TreeFamiTF300078.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P41227-1) [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
MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG
60 70 80 90 100
KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE
110 120 130 140 150
NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD
160 170 180 190 200
LTQMADELRR HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL
210 220 230
AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS
Length:235
Mass (Da):26,459
Last modified:February 1, 1995 - v1
Checksum:i6393A907F5C2DDC4
GO
Isoform 2 (identifier: P41227-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:220
Mass (Da):24,784
Checksum:iFF22A79BB1ACA0BC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371S → 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%. 1 Publication
VAR_066652

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei114 – 12815Missing in isoform 2. CuratedVSP_046205Add
BLAST
Alternative sequencei129 – 1291Q → R in isoform 2. CuratedVSP_046206

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14737.1. [P41227-1]
CCDS59179.1. [P41227-2]
PIRiI38333.
RefSeqiNP_001243048.1. NM_001256119.1. [P41227-2]
NP_003482.1. NM_003491.3. [P41227-1]
UniGeneiHs.433291.

Genome annotation databases

EnsembliENST00000370009; ENSP00000359026; ENSG00000102030. [P41227-2]
ENST00000464845; ENSP00000417763; ENSG00000102030. [P41227-1]
GeneIDi8260.
KEGGihsa:8260.
UCSCiuc004fjm.2. human. [P41227-1]
uc004fjn.2. human.

Polymorphism databases

DMDMi728880.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS14737.1. [P41227-1 ]
CCDS59179.1. [P41227-2 ]
PIRi I38333.
RefSeqi NP_001243048.1. NM_001256119.1. [P41227-2 ]
NP_003482.1. NM_003491.3. [P41227-1 ]
UniGenei Hs.433291.

3D structure databases

ProteinModelPortali P41227.
SMRi P41227. Positions 1-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113881. 26 interactions.
IntActi P41227. 15 interactions.
MINTi MINT-1499850.
STRINGi 9606.ENSP00000417763.

PTM databases

PhosphoSitei P41227.

Polymorphism databases

DMDMi 728880.

Proteomic databases

MaxQBi P41227.
PaxDbi P41227.
PRIDEi P41227.

Protocols and materials databases

DNASUi 8260.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370009 ; ENSP00000359026 ; ENSG00000102030 . [P41227-2 ]
ENST00000464845 ; ENSP00000417763 ; ENSG00000102030 . [P41227-1 ]
GeneIDi 8260.
KEGGi hsa:8260.
UCSCi uc004fjm.2. human. [P41227-1 ]
uc004fjn.2. human.

Organism-specific databases

CTDi 8260.
GeneCardsi GC0XM153194.
HGNCi HGNC:18704. NAA10.
HPAi CAB006269.
HPA030711.
MIMi 300013. gene.
300855. phenotype.
309800. phenotype.
neXtProti NX_P41227.
Orphaneti 568. Microphthalmia, Lenz type.
276432. Premature aging appearance-developmental delay-cardiac arrhythmia syndrome.
PharmGKBi PA38648.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0456.
GeneTreei ENSGT00550000074803.
HOGENOMi HOG000078523.
HOVERGENi HBG050561.
InParanoidi P41227.
KOi K00670.
PhylomeDBi P41227.
TreeFami TF300078.

Miscellaneous databases

ChiTaRSi NAA10. human.
GeneWikii ARD1A.
GenomeRNAii 8260.
NextBioi 31019.
PROi P41227.
SOURCEi Search...

Gene expression databases

Bgeei P41227.
CleanExi HS_ARD1A.
ExpressionAtlasi P41227. baseline and differential.
Genevestigatori P41227.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view ]
Pfami PF00583. Acetyltransf_1. 1 hit.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
PROSITEi PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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. Cited for: VARIANT NATD PRO-37, CHARACTERIZATION OF VARIANT NATD PRO-37.

Entry informationi

Entry nameiNAA10_HUMAN
AccessioniPrimary (citable) accession number: P41227
Secondary accession number(s): A6NM98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 145 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 X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3