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Protein

N-terminal acetyltransferase A complex subunit NAT1

Gene

NAT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. NAT1 anchors ARD1 and NAT5 to the ribosome and may present the N termini of nascent polypeptides for acetylation.2 Publications

GO - Biological processi

  • N-terminal protein amino acid acetylation Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:YDL040C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-terminal acetyltransferase A complex subunit NAT1
Short name:
NatA complex subunit NAT1
Alternative name(s):
Amino-terminal, alpha-amino, acetyltransferase 1
Gene namesi
Name:NAT1
Synonyms:AAA1
Ordered Locus Names:YDL040C
ORF Names:D2720
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL040C.
SGDiS000002198. NAT1.

Subcellular locationi

GO - Cellular componenti

  • NatA complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 854853N-terminal acetyltransferase A complex subunit NAT1PRO_0000096739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineSequence analysis
Modified residuei674 – 6741PhosphoserineCombined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP12945.
PeptideAtlasiP12945.

PTM databases

iPTMnetiP12945.

Interactioni

Subunit structurei

Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of ARD1, NAT1 and NAT5. Can self-associate. NAT1 associates with the nascent polypeptide chain and the ribosome.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARD1P0734711EBI-11868,EBI-2796

Protein-protein interaction databases

BioGridi32018. 230 interactions.
DIPiDIP-6329N.
IntActiP12945. 17 interactions.
MINTiMINT-617866.

Structurei

Secondary structure

1
854
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 294Combined sources
Helixi36 – 4914Combined sources
Helixi55 – 6713Combined sources
Helixi70 – 8011Combined sources
Helixi91 – 10313Combined sources
Helixi107 – 11913Combined sources
Helixi126 – 13712Combined sources
Helixi141 – 15414Combined sources
Helixi159 – 17113Combined sources
Helixi175 – 18814Combined sources
Helixi195 – 1973Combined sources
Helixi198 – 21619Combined sources
Helixi220 – 23314Combined sources
Helixi234 – 2363Combined sources
Helixi240 – 25314Combined sources
Helixi257 – 27014Combined sources
Helixi275 – 28511Combined sources
Helixi291 – 30414Combined sources
Helixi309 – 31810Combined sources
Helixi322 – 33817Combined sources
Helixi344 – 37229Combined sources
Turni376 – 3783Combined sources
Helixi380 – 39617Combined sources
Helixi400 – 41314Combined sources
Helixi418 – 43013Combined sources
Helixi434 – 44512Combined sources
Helixi446 – 4483Combined sources
Helixi452 – 46413Combined sources
Helixi468 – 4758Combined sources
Turni478 – 4803Combined sources
Beta strandi482 – 4876Combined sources
Beta strandi488 – 4903Combined sources
Helixi491 – 4933Combined sources
Helixi497 – 52226Combined sources
Helixi536 – 57136Combined sources
Helixi572 – 5743Combined sources
Helixi575 – 5828Combined sources
Helixi585 – 59511Combined sources
Helixi596 – 6005Combined sources
Helixi602 – 62827Combined sources
Turni629 – 6313Combined sources
Helixi648 – 66922Combined sources
Helixi674 – 6763Combined sources
Helixi683 – 6864Combined sources
Helixi691 – 6988Combined sources
Helixi700 – 7067Combined sources
Turni709 – 7113Combined sources
Helixi714 – 72310Combined sources
Helixi727 – 74115Combined sources
Beta strandi743 – 7453Combined sources
Helixi746 – 75813Combined sources
Helixi767 – 77711Combined sources
Helixi778 – 7803Combined sources
Helixi787 – 7915Combined sources
Helixi797 – 8048Combined sources
Helixi810 – 8189Combined sources
Turni819 – 8246Combined sources
Helixi827 – 83711Combined sources
Turni838 – 8403Combined sources
Helixi843 – 85311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HNWX-ray2.80A1-854[»]
4HNYX-ray2.25A/C1-854[»]
ProteinModelPortaliP12945.
SMRiP12945. Positions 15-854.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati20 – 5334TPR 1Add
BLAST
Repeati54 – 8734TPR 2Add
BLAST
Repeati91 – 12434TPR 3Add
BLAST
Repeati126 – 16237TPR 4Add
BLAST
Repeati241 – 27434TPR 5Add
BLAST
Repeati384 – 41734TPR 6Add
BLAST
Repeati452 – 48534TPR 7Add
BLAST
Repeati728 – 76134TPR 8Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili623 – 66745Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 8 TPR repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

GeneTreeiENSGT00390000007676.
HOGENOMiHOG000248749.
InParanoidiP12945.
KOiK00670.
OMAiYDSLPHR.
OrthoDBiEOG7DJSVT.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR021183. NatA_aux_su.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF12569. NARP1. 2 hits.
[Graphical view]
PIRSFiPIRSF000422. N-terminal-AcTrfase-A_aux_su. 1 hit.
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12945-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRKRSTKPK PAAKIALKKE NDQFLEALKL YEGKQYKKSL KLLDAILKKD
60 70 80 90 100
GSHVDSLALK GLDLYSVGEK DDAASYVANA IRKIEGASAS PICCHVLGIY
110 120 130 140 150
MRNTKEYKES IKWFTAALNN GSTNKQIYRD LATLQSQIGD FKNALVSRKK
160 170 180 190 200
YWEAFLGYRA NWTSLAVAQD VNGERQQAIN TLSQFEKLAE GKISDSEKYE
210 220 230 240 250
HSECLMYKND IMYKAASDNQ DKLQNVLKHL NDIEPCVFDK FGLLERKATI
260 270 280 290 300
YMKLGQLKDA SIVYRTLIKR NPDNFKYYKL LEVSLGIQGD NKLKKALYGK
310 320 330 340 350
LEQFYPRCEP PKFIPLTFLQ DKEELSKKLR EYVLPQLERG VPATFSNVKP
360 370 380 390 400
LYQRRKSKVS PLLEKIVLDY LSGLDPTQDP IPFIWTNYYL SQHFLFLKDF
410 420 430 440 450
PKAQEYIDAA LDHTPTLVEF YILKARILKH LGLMDTAAGI LEEGRQLDLQ
460 470 480 490 500
DRFINCKTVK YFLRANNIDK AVEVASLFTK NDDSVNGIKD LHLVEASWFI
510 520 530 540 550
VEQAEAYYRL YLDRKKKLDD LASLKKEVES DKSEQIANDI KENQWLVRKY
560 570 580 590 600
KGLALKRFNA IPKFYKQFED DQLDFHSYCM RKGTPRAYLE MLEWGKALYT
610 620 630 640 650
KPMYVRAMKE ASKLYFQMHD DRLKRKSDSL DENSDEIQNN GQNSSSQKKK
660 670 680 690 700
AKKEAAAMNK RKETEAKSVA AYPSDQDNDV FGEKLIETST PMEDFATEFY
710 720 730 740 750
NNYSMQVRED ERDYILDFEF NYRIGKLALC FASLNKFAKR FGTTSGLFGS
760 770 780 790 800
MAIVLLHATR NDTPFDPILK KVVTKSLEKE YSENFPLNEI SNNSFDWLNF
810 820 830 840 850
YQEKFGKNDI NGLLFLYRYR DDVPIGSSNL KEMIISSLSP LEPHSQNEIL

QYYL
Length:854
Mass (Da):98,905
Last modified:January 23, 2007 - v2
Checksum:iDCFB870D049F91E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23166 mRNA. Translation: AAA88728.1.
X15135 Genomic DNA. Translation: CAA33233.1.
Z71781 Genomic DNA. Translation: CAA96449.1.
Z74088 Genomic DNA. Translation: CAA98599.1.
BK006938 Genomic DNA. Translation: DAA11815.1.
PIRiS05783. XYBYT1.
RefSeqiNP_010244.1. NM_001180099.1.

Genome annotation databases

EnsemblFungiiYDL040C; YDL040C; YDL040C.
GeneIDi851521.
KEGGisce:YDL040C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23166 mRNA. Translation: AAA88728.1.
X15135 Genomic DNA. Translation: CAA33233.1.
Z71781 Genomic DNA. Translation: CAA96449.1.
Z74088 Genomic DNA. Translation: CAA98599.1.
BK006938 Genomic DNA. Translation: DAA11815.1.
PIRiS05783. XYBYT1.
RefSeqiNP_010244.1. NM_001180099.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HNWX-ray2.80A1-854[»]
4HNYX-ray2.25A/C1-854[»]
ProteinModelPortaliP12945.
SMRiP12945. Positions 15-854.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32018. 230 interactions.
DIPiDIP-6329N.
IntActiP12945. 17 interactions.
MINTiMINT-617866.

PTM databases

iPTMnetiP12945.

Proteomic databases

MaxQBiP12945.
PeptideAtlasiP12945.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL040C; YDL040C; YDL040C.
GeneIDi851521.
KEGGisce:YDL040C.

Organism-specific databases

EuPathDBiFungiDB:YDL040C.
SGDiS000002198. NAT1.

Phylogenomic databases

GeneTreeiENSGT00390000007676.
HOGENOMiHOG000248749.
InParanoidiP12945.
KOiK00670.
OMAiYDSLPHR.
OrthoDBiEOG7DJSVT.

Enzyme and pathway databases

BioCyciYEAST:YDL040C-MONOMER.

Miscellaneous databases

PROiP12945.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR021183. NatA_aux_su.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF12569. NARP1. 2 hits.
[Graphical view]
PIRSFiPIRSF000422. N-terminal-AcTrfase-A_aux_su. 1 hit.
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequencing of a cDNA encoding N alpha-acetyltransferase from Saccharomyces cerevisiae."
    Lee F.-J.S., Lin L.-W., Smith J.A.
    J. Biol. Chem. 264:12339-12343(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-101; 130-142; 151-159; 301-307; 313-327; 331-354; 471-479; 587-596; 598-606; 614-622; 668-683 AND 685-705.
  2. "Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast."
    Mullen J.R., Kayne P.S., Moerschell R.P., Tsunasawa S., Gribskov M., Colavito-Shepanski M., Grunstein M., Sherman F., Sternglanz R.
    EMBO J. 8:2067-2075(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity."
    Park E.C., Szostak J.W.
    EMBO J. 11:2087-2093(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARD1.
  6. "The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides."
    Gautschi M., Just S., Mun A., Ross S., Rucknagel P., Dubaquie Y., Ehrenhofer-Murray A., Rospert S.
    Mol. Cell. Biol. 23:7403-7414(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NATA COMPLEX.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNAT1_YEAST
AccessioniPrimary (citable) accession number: P12945
Secondary accession number(s): D6VRV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.