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Protein

N-alpha-acetyltransferase 15, NatA auxiliary subunit

Gene

Naa15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

  • N-acetyltransferase activity Source: MGI
  • poly(A) RNA binding Source: MGI
  • ribosome binding Source: MGI

GO - Biological processi

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
Proteomesi
  • UP000000589 Componenti: 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. Present in the free cytosolic and cytoskeleton-bound polysomes, but not in the membrane-bound polysomes.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001062951 – 865N-alpha-acetyltransferase 15, NatA auxiliary subunitAdd BLAST865

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei262N6-acetyllysineBy similarity1
Modified residuei302PhosphoserineBy similarity1
Modified residuei537PhosphoserineBy similarity1
Modified residuei588PhosphoserineBy similarity1
Modified residuei734N6-acetyllysineBy similarity1
Modified residuei755N6-acetyllysineBy similarity1
Modified residuei854PhosphoserineCombined sources1
Modified residuei855PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ80UM3.
MaxQBiQ80UM3.
PaxDbiQ80UM3.
PeptideAtlasiQ80UM3.
PRIDEiQ80UM3.

PTM databases

iPTMnetiQ80UM3.
PhosphoSitePlusiQ80UM3.

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.

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 interactors.
MINTiMINT-1865089.
STRINGi10090.ENSMUSP00000029303.

Structurei

3D structure databases

ProteinModelPortaliQ80UM3.
SMRiQ80UM3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati46 – 79TPR 1Add BLAST34
Repeati80 – 113TPR 2Add BLAST34
Repeati148 – 184TPR 3Add BLAST37
Repeati224 – 257TPR 4Add BLAST34
Repeati374 – 407TPR 5Add BLAST34
Repeati409 – 441TPR 6Add BLAST33
Repeati485 – 518TPR 7Add BLAST34
Repeati672 – 705TPR 8Add BLAST34
Repeati799 – 834TPR 9Add BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni500 – 865Interaction with HYPKBy similarityAdd BLAST366

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi612 – 629Bipartite nuclear localization signalSequence analysisAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi629 – 632Poly-Asp4

Sequence similaritiesi

Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1156. Eukaryota.
ENOG410XR7D. LUCA.
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_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF12569. NARP1. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
PIRSFiPIRSF000422. N-terminal-AcTrfase-A_aux_su. 1 hit.
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80UM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAVSLPPKE NALFKRILRC YEHKQYRNGL KFCKQILSNP KFAEHGETLA
60 70 80 90 100
MKGLTLNCLG KKEEAYELVR RGLRNDLKSH VCWHVYGLLQ RSDKKYDEAI
110 120 130 140 150
KCYRNALKWD KDNLQILRDL SLLQIQMRDL EGYRETRYQL LQLRPAQRAS
160 170 180 190 200
WIGYAIAYHL LEDYEMAAKI LEEFRKTQQT SPDKVDYEYS ELLLYQNQVL
210 220 230 240 250
REAGLYREAL EHLCTYEKQI CDKLAVEETK GELLLQLCRL EDAADVYRGL
260 270 280 290 300
QERNPGNWAY YKGLEKALKP ANMLERLKIY EEAWTKYPRG LVPRRLPLNF
310 320 330 340 350
LSGEKFKECL DRFLRMNFSK GCPPVFNTLR SLYRDKEKVA IVEELVVGYE
360 370 380 390 400
TSLKSCRLFN PNDDGKEEPP TTLLWVQYYL AQHYDKIGQP SIALEYINTA
410 420 430 440 450
IESTPTLIEL FLVKAKIYKH AGNIKEAARW MDEAQALDTA DRFINSKCAK
460 470 480 490 500
YVLKANLIKE AEEMCSKFTR EGTSAVENLN EMQCMWFQTE CAQAYKAMNK
510 520 530 540 550
FGEALKKCHE IERHFIEITD DQFDFHTYCM RKITLRSYVD LLKLEDVLRQ
560 570 580 590 600
HPFYFKAARI AIEIYLKLHD NPLTDENKEH EADTANMSDK ELKKLRNKQR
610 620 630 640 650
RAQKKAQIEE EKKNAEKEKQ QRNQKKKKDD DDEEIGGPKE ELIPEKLAKV
660 670 680 690 700
ETPLEEAIKF LTPLKNLVKN KIETHLFAFE IYFRKEKFLL MLQSVKRAFA
710 720 730 740 750
IDSGHPWLHE CMIRLFHSVC ESKDLPETVR TVLKQEMNRL FGATNPKNFN
760 770 780 790 800
ETFLKRNSDS LPHRLSAAKM VYYLDSSSQK RAIELATTLD GSLTNRNLQT
810 820 830 840 850
CMEVLEALCD GSLGDCKEAA EAYRASCHKL FPYALAFMPP GYEEDMKITV
860
NGDSSAETEE LANEI
Length:865
Mass (Da):100,961
Last modified:June 1, 2003 - v1
Checksum:i230C5B6EE8697440
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti256G → E (PubMed:12888564).Curated1
Sequence conflicti256G → E (PubMed:10842358).Curated1
Sequence conflicti295R → K (PubMed:12888564).Curated1
Sequence conflicti295R → K (PubMed:10842358).Curated1
Sequence conflicti452V → M (PubMed:12888564).Curated1
Sequence conflicti452V → M (PubMed:10842358).Curated1
Sequence conflicti620Q → P in AAF73953 (PubMed:10842358).Curated1
Sequence conflicti624Q → P in AAF73953 (PubMed:10842358).Curated1
Sequence conflicti704G → S (PubMed:12888564).Curated1
Sequence conflicti704G → S (PubMed:10842358).Curated1
Sequence conflicti814G → R in AAF73953 (PubMed:10842358).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF510858 mRNA. Translation: AAO33713.1.
BC050017 mRNA. Translation: AAH50017.1.
AF237622 mRNA. Translation: AAF73953.2. Sequence problems.
CCDSiCCDS17340.1.
UniGeneiMm.275281.

3D structure databases

ProteinModelPortaliQ80UM3.
SMRiQ80UM3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80UM3. 4 interactors.
MINTiMINT-1865089.
STRINGi10090.ENSMUSP00000029303.

PTM databases

iPTMnetiQ80UM3.
PhosphoSitePlusiQ80UM3.

Proteomic databases

EPDiQ80UM3.
MaxQBiQ80UM3.
PaxDbiQ80UM3.
PeptideAtlasiQ80UM3.
PRIDEiQ80UM3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1922088. Naa15.

Phylogenomic databases

eggNOGiKOG1156. Eukaryota.
ENOG410XR7D. LUCA.
HOGENOMiHOG000191711.
HOVERGENiHBG052576.
InParanoidiQ80UM3.
PhylomeDBiQ80UM3.

Enzyme and pathway databases

BRENDAi2.3.1.88. 3474.

Miscellaneous databases

ChiTaRSiNaa15. mouse.
PROiQ80UM3.
SOURCEiSearch...

Gene expression databases

CleanExiMM_NARG1.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR021183. NatA_aux_su.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF12569. NARP1. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
PIRSFiPIRSF000422. N-terminal-AcTrfase-A_aux_su. 1 hit.
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 124 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

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.