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Q80UM3

- NAA15_MOUSE

UniProt

Q80UM3 - NAA15_MOUSE

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Protein
N-alpha-acetyltransferase 15, NatA auxiliary subunit
Gene
Naa15, Narg1, Nat1, Tbdn-1, Tubedown
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. N-acetyltransferase activity Source: MGI
  2. protein binding Source: MGI
Complete GO annotation...

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Differentiation, Transcription, Transcription regulation

Enzyme and pathway databases

BRENDAi2.3.1.88. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
N-alpha-acetyltransferase 15, NatA auxiliary subunit
Alternative name(s):
N-terminal acetyltransferase 1
NMDA receptor-regulated protein 1
Protein tubedown-1
Gene namesi
Name:Naa15
Synonyms:Narg1, Nat1, Tbdn-1, Tubedown
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1922088. Naa15.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: UniProtKB-SubCell
  3. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 865865N-alpha-acetyltransferase 15, NatA auxiliary subunit
PRO_0000106295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 2621N6-acetyllysine By similarity
Modified residuei399 – 3991Phosphothreonine By similarity
Modified residuei403 – 4031Phosphoserine By similarity
Modified residuei588 – 5881Phosphoserine By similarity
Modified residuei734 – 7341N6-acetyllysine By similarity
Modified residuei755 – 7551N6-acetyllysine By similarity
Modified residuei854 – 8541Phosphoserine1 Publication
Modified residuei855 – 8551Phosphoserine1 Publication

Post-translational modificationi

Acetylated.1 Publication
Cleaved by caspases during apoptosis By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ80UM3.
PaxDbiQ80UM3.
PRIDEiQ80UM3.

PTM databases

PhosphoSiteiQ80UM3.

Expressioni

Tissue specificityi

Endothelial cells, osteoblasts and myeloid cells of the hematopoietic tissue. Present in adult ovary, bone marrow, brain, heart, kidney, testis and osteoblasts.3 Publications

Developmental stagei

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.1 Publication

Inductioni

Regulated by NMDA receptor.1 Publication

Gene expression databases

CleanExiMM_NARG1.
GenevestigatoriQ80UM3.

Interactioni

Subunit structurei

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 NAA10.2 Publications

Protein-protein interaction databases

IntActiQ80UM3. 4 interactions.
MINTiMINT-1865089.

Structurei

3D structure databases

ProteinModelPortaliQ80UM3.
SMRiQ80UM3. Positions 1-778.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati46 – 7934TPR 1
Add
BLAST
Repeati80 – 11334TPR 2
Add
BLAST
Repeati148 – 18437TPR 3
Add
BLAST
Repeati224 – 25734TPR 4
Add
BLAST
Repeati374 – 40734TPR 5
Add
BLAST
Repeati409 – 44133TPR 6
Add
BLAST
Repeati485 – 51834TPR 7
Add
BLAST
Repeati672 – 70534TPR 8
Add
BLAST
Repeati799 – 83436TPR 9
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni500 – 865366Interaction with HYPK By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi612 – 62918Bipartite nuclear localization signal Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi629 – 6324Poly-Asp

Sequence similaritiesi

Contains 9 TPR repeats.

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
HOGENOMiHOG000191711.
HOVERGENiHBG052576.
InParanoidiQ80UM3.
PhylomeDBiQ80UM3.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR021183. NatA_aux_su.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF12569. NARP1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000422. N-terminal-AcTrfase-A_aux_su. 1 hit.
SMARTiSM00028. TPR. 4 hits.
[Graphical view]
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80UM3-1 [UniParc]FASTAAdd to Basket

« Hide

MPAVSLPPKE NALFKRILRC YEHKQYRNGL KFCKQILSNP KFAEHGETLA    50
MKGLTLNCLG KKEEAYELVR RGLRNDLKSH VCWHVYGLLQ RSDKKYDEAI 100
KCYRNALKWD KDNLQILRDL SLLQIQMRDL EGYRETRYQL LQLRPAQRAS 150
WIGYAIAYHL LEDYEMAAKI LEEFRKTQQT SPDKVDYEYS ELLLYQNQVL 200
REAGLYREAL EHLCTYEKQI CDKLAVEETK GELLLQLCRL EDAADVYRGL 250
QERNPGNWAY YKGLEKALKP ANMLERLKIY EEAWTKYPRG LVPRRLPLNF 300
LSGEKFKECL DRFLRMNFSK GCPPVFNTLR SLYRDKEKVA IVEELVVGYE 350
TSLKSCRLFN PNDDGKEEPP TTLLWVQYYL AQHYDKIGQP SIALEYINTA 400
IESTPTLIEL FLVKAKIYKH AGNIKEAARW MDEAQALDTA DRFINSKCAK 450
YVLKANLIKE AEEMCSKFTR EGTSAVENLN EMQCMWFQTE CAQAYKAMNK 500
FGEALKKCHE IERHFIEITD DQFDFHTYCM RKITLRSYVD LLKLEDVLRQ 550
HPFYFKAARI AIEIYLKLHD NPLTDENKEH EADTANMSDK ELKKLRNKQR 600
RAQKKAQIEE EKKNAEKEKQ QRNQKKKKDD DDEEIGGPKE ELIPEKLAKV 650
ETPLEEAIKF LTPLKNLVKN KIETHLFAFE IYFRKEKFLL MLQSVKRAFA 700
IDSGHPWLHE CMIRLFHSVC ESKDLPETVR TVLKQEMNRL FGATNPKNFN 750
ETFLKRNSDS LPHRLSAAKM VYYLDSSSQK RAIELATTLD GSLTNRNLQT 800
CMEVLEALCD GSLGDCKEAA EAYRASCHKL FPYALAFMPP GYEEDMKITV 850
NGDSSAETEE LANEI 865
Length:865
Mass (Da):100,961
Last modified:June 1, 2003 - v1
Checksum:i230C5B6EE8697440
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561G → E1 Publication
Sequence conflicti256 – 2561G → E1 Publication
Sequence conflicti295 – 2951R → K1 Publication
Sequence conflicti295 – 2951R → K1 Publication
Sequence conflicti452 – 4521V → M1 Publication
Sequence conflicti452 – 4521V → M1 Publication
Sequence conflicti620 – 6201Q → P in AAF73953. 1 Publication
Sequence conflicti624 – 6241Q → P in AAF73953. 1 Publication
Sequence conflicti704 – 7041G → S1 Publication
Sequence conflicti704 – 7041G → S1 Publication
Sequence conflicti814 – 8141G → R in AAF73953. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF510858 mRNA. Translation: AAO33713.1.
BC050017 mRNA. Translation: AAH50017.1.
AF237622 mRNA. Translation: AAF73953.2. Sequence problems.
CCDSiCCDS17340.1.
UniGeneiMm.275281.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF510858 mRNA. Translation: AAO33713.1 .
BC050017 mRNA. Translation: AAH50017.1 .
AF237622 mRNA. Translation: AAF73953.2 . Sequence problems.
CCDSi CCDS17340.1.
UniGenei Mm.275281.

3D structure databases

ProteinModelPortali Q80UM3.
SMRi Q80UM3. Positions 1-778.
ModBasei Search...

Protein-protein interaction databases

IntActi Q80UM3. 4 interactions.
MINTi MINT-1865089.

PTM databases

PhosphoSitei Q80UM3.

Proteomic databases

MaxQBi Q80UM3.
PaxDbi Q80UM3.
PRIDEi Q80UM3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:1922088. Naa15.

Phylogenomic databases

eggNOGi COG0457.
HOGENOMi HOG000191711.
HOVERGENi HBG052576.
InParanoidi Q80UM3.
PhylomeDBi Q80UM3.

Enzyme and pathway databases

BRENDAi 2.3.1.88. 3474.

Miscellaneous databases

PROi Q80UM3.
SOURCEi Search...

Gene expression databases

CleanExi MM_NARG1.
Genevestigatori Q80UM3.

Family and domain databases

Gene3Di 1.25.40.10. 3 hits.
InterProi IPR021183. NatA_aux_su.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view ]
Pfami PF12569. NARP1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000422. N-terminal-AcTrfase-A_aux_su. 1 hit.
SMARTi SM00028. TPR. 4 hits.
[Graphical view ]
PROSITEi PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854 AND SER-855, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNAA15_MOUSE
AccessioniPrimary (citable) accession number: Q80UM3
Secondary accession number(s): Q811Z9, Q9JID5
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi