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Q80UM3 (NAA15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-alpha-acetyltransferase 15, NatA auxiliary subunit
Alternative name(s):
N-terminal acetyltransferase 1
NMDA receptor-regulated protein 1
Protein tubedown-1
Gene names
Name:Naa15
Synonyms:Narg1, Nat1, Tbdn-1, Tubedown
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length865 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Auxillary 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. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. Ref.1 Ref.2 Ref.4 Ref.6

Subunit structure

Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 or probably NAA11 and NAA15. Interacts with XRCC6, NAA50 and XRCC5. Associates with HYPK when in a complex with NAA10. Ref.1 Ref.2

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Cytoplasmperinuclear region By similarity. Note: Mainly cytoplasmic, nuclear in some cases By similarity. Present in the free cytosolic and cytoskeleton-bound polysomes, but not in the membrane-bound polysomes By similarity. Ref.1 Ref.2

Tissue specificity

Endothelial cells, osteoblasts and myeloid cells of the hematopoietic tissue. Present in adult ovary, bone marrow, brain, heart, kidney, testis and osteoblasts. Ref.1 Ref.2 Ref.5

Developmental stage

Highly expressed in endothelial cells during embryonic vasculogenesis, and then down-regulated and restricted to specific endothelial cells. In the brain, expression is highest in regions that contain dividing and proliferating cells. As brain development progresses, expression restricts to the hippocampus and cerebellar cortex. Ref.5

Induction

Regulated by NMDA receptor. Ref.5

Post-translational modification

Acetylated. Ref.4

Cleaved by caspases during apoptosis By similarity.

Sequence similarities

Contains 9 TPR repeats.

Sequence caution

The sequence AAF73953.2 differs from that shown. Reason: Frameshift at several positions.

The sequence AAF73953.2 differs from that shown. Reason: Contaminating sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 865865N-alpha-acetyltransferase 15, NatA auxiliary subunit
PRO_0000106295

Regions

Repeat46 – 7934TPR 1
Repeat80 – 11334TPR 2
Repeat148 – 18437TPR 3
Repeat224 – 25734TPR 4
Repeat374 – 40734TPR 5
Repeat409 – 44133TPR 6
Repeat485 – 51834TPR 7
Repeat672 – 70534TPR 8
Repeat799 – 83436TPR 9
Region500 – 865366Interaction with HYPK By similarity
Motif612 – 62918Bipartite nuclear localization signal Potential
Compositional bias629 – 6324Poly-Asp

Amino acid modifications

Modified residue2621N6-acetyllysine By similarity
Modified residue3991Phosphothreonine By similarity
Modified residue4031Phosphoserine By similarity
Modified residue5881Phosphoserine By similarity
Modified residue7341N6-acetyllysine By similarity
Modified residue7551N6-acetyllysine By similarity
Modified residue8541Phosphoserine Ref.7
Modified residue8551Phosphoserine Ref.7

Experimental info

Sequence conflict2561G → E Ref.2
Sequence conflict2561G → E Ref.4
Sequence conflict2951R → K Ref.2
Sequence conflict2951R → K Ref.4
Sequence conflict4521V → M Ref.2
Sequence conflict4521V → M Ref.4
Sequence conflict6201Q → P in AAF73953. Ref.4
Sequence conflict6241Q → P in AAF73953. Ref.4
Sequence conflict7041G → S Ref.2
Sequence conflict7041G → S Ref.4
Sequence conflict8141G → R in AAF73953. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q80UM3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 230C5B6EE8697440

FASTA865100,961
        10         20         30         40         50         60 
MPAVSLPPKE NALFKRILRC YEHKQYRNGL KFCKQILSNP KFAEHGETLA MKGLTLNCLG 

        70         80         90        100        110        120 
KKEEAYELVR RGLRNDLKSH VCWHVYGLLQ RSDKKYDEAI KCYRNALKWD KDNLQILRDL 

       130        140        150        160        170        180 
SLLQIQMRDL EGYRETRYQL LQLRPAQRAS WIGYAIAYHL LEDYEMAAKI LEEFRKTQQT 

       190        200        210        220        230        240 
SPDKVDYEYS ELLLYQNQVL REAGLYREAL EHLCTYEKQI CDKLAVEETK GELLLQLCRL 

       250        260        270        280        290        300 
EDAADVYRGL QERNPGNWAY YKGLEKALKP ANMLERLKIY EEAWTKYPRG LVPRRLPLNF 

       310        320        330        340        350        360 
LSGEKFKECL DRFLRMNFSK GCPPVFNTLR SLYRDKEKVA IVEELVVGYE TSLKSCRLFN 

       370        380        390        400        410        420 
PNDDGKEEPP TTLLWVQYYL AQHYDKIGQP SIALEYINTA IESTPTLIEL FLVKAKIYKH 

       430        440        450        460        470        480 
AGNIKEAARW MDEAQALDTA DRFINSKCAK YVLKANLIKE AEEMCSKFTR EGTSAVENLN 

       490        500        510        520        530        540 
EMQCMWFQTE CAQAYKAMNK FGEALKKCHE IERHFIEITD DQFDFHTYCM RKITLRSYVD 

       550        560        570        580        590        600 
LLKLEDVLRQ HPFYFKAARI AIEIYLKLHD NPLTDENKEH EADTANMSDK ELKKLRNKQR 

       610        620        630        640        650        660 
RAQKKAQIEE EKKNAEKEKQ QRNQKKKKDD DDEEIGGPKE ELIPEKLAKV ETPLEEAIKF 

       670        680        690        700        710        720 
LTPLKNLVKN KIETHLFAFE IYFRKEKFLL MLQSVKRAFA IDSGHPWLHE CMIRLFHSVC 

       730        740        750        760        770        780 
ESKDLPETVR TVLKQEMNRL FGATNPKNFN ETFLKRNSDS LPHRLSAAKM VYYLDSSSQK 

       790        800        810        820        830        840 
RAIELATTLD GSLTNRNLQT CMEVLEALCD GSLGDCKEAA EAYRASCHKL FPYALAFMPP 

       850        860 
GYEEDMKITV NGDSSAETEE LANEI 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of osteocalcin gene expression by a novel Ku antigen transcription factor complex."
Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S., Ornitz D.M., Towler D.A.
J. Biol. Chem. 277:37280-37291(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH XRCC6 AND XRCC5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
Tissue: Heart.
[2]"An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development."
Sugiura N., Adams S.M., Corriveau R.A.
J. Biol. Chem. 278:40113-40120(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NAA10.
Tissue: Testis.
[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].
Strain: ICR.
Tissue: Trophoblast stem cell.
[4]"Tubedown-1, a novel acetyltransferase associated with blood vessel development."
Gendron R.L., Adams L.C., Paradis H.
Dev. Dyn. 218:300-315(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 158-865, CHARACTERIZATION, ACETYLATION, FUNCTION.
Strain: ICR.
Tissue: Embryo.
[5]"N-methyl-D-aspartate receptors regulate a group of transiently expressed genes in the developing brain."
Sugiura N., Patel R.G., Corriveau R.A.
J. Biol. Chem. 276:14257-14263(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, INDUCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[6]"Conditional knockdown of tubedown-1 in endothelial cells leads to neovascular retinopathy."
Wall D.S., Gendron R.L., Good W.V., Miskiewicz E., Woodland M., Leblanc K., Paradis H.
Invest. Ophthalmol. Vis. Sci. 45:3704-3712(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854 AND SER-855, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF510858 mRNA. Translation: AAO33713.1.
BC050017 mRNA. Translation: AAH50017.1.
AF237622 mRNA. Translation: AAF73953.2. Sequence problems.
CCDSCCDS17340.1.
UniGeneMm.275281.

3D structure databases

ProteinModelPortalQ80UM3.
SMRQ80UM3. Positions 1-778.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ80UM3. 4 interactions.
MINTMINT-1865089.

PTM databases

PhosphoSiteQ80UM3.

Proteomic databases

MaxQBQ80UM3.
PaxDbQ80UM3.
PRIDEQ80UM3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1922088. Naa15.

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000191711.
HOVERGENHBG052576.
InParanoidQ80UM3.
PhylomeDBQ80UM3.

Enzyme and pathway databases

BRENDA2.3.1.88. 3474.

Gene expression databases

CleanExMM_NARG1.
GenevestigatorQ80UM3.

Family and domain databases

Gene3D1.25.40.10. 3 hits.
InterProIPR021183. NatA_aux_su.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF12569. NARP1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PIRSFPIRSF000422. N-terminal-AcTrfase-A_aux_su. 1 hit.
SMARTSM00028. TPR. 4 hits.
[Graphical view]
PROSITEPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

PROQ80UM3.
SOURCESearch...

Entry information

Entry nameNAA15_MOUSE
AccessionPrimary (citable) accession number: Q80UM3
Secondary accession number(s): Q811Z9, Q9JID5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot