Q04751 (NAT4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-specific N-acetyltransferase NAT4
EC=2.3.1.-

Gene names

Name:	NAT4
Ordered Locus Names:	YMR069W
ORF Names:	YM9916.08

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Responsible for the acetylation of the N-terminal residues of histones H4 and H2A. Ref.4
Subcellular location	Nucleus. Cytoplasm Ref.5.
Sequence similarities	Belongs to the acetyltransferase family. GNAT subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: SGD nucleus Inferred from direct assay Ref.5. Source: SGD
Molecular_function	histone acetyltransferase activity Inferred from mutant phenotype Ref.4. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 285	285	Histone-specific N-acetyltransferase NAT4		PRO_0000074636
Regions
	Domain	88 – 274	187	N-acetyltransferase
Amino acid modifications
	Modified residue	256	1	Phosphoserine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q04751 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 20127B782E1F5F1A	FASTA	285	32,334
	10 20 30 40 50 60 MRSSVYSENT YNCIRTSKEH LTERRRVAMA PMFQHFLNLC VEKFPESIEH KDTDGNGNFT 70 80 90 100 110 120 TAILEREIIY IPEDDTDSID SVDSLKCINY KLHKSRGDQV LDACVQLIDK HLGAKYRRAS 130 140 150 160 170 180 RIMYGNRKPW KANKLAEMKS AGLVYVCYWD NGVLGAFTSF MLTEETGLVE GDALHEVSVP 190 200 210 220 230 240 VIYLYEVHVA SAHRGHGIGR RLLEHALCDG VARHTRRMCD NFFGVALTVF SDNTRARRLY 250 260 270 280 EALGFYRAPG SPAPASPTIR HTRHGGGRVV VPCDPLYYVY CLHMP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A." Song O.-K., Wang X., Waterborg J.H., Sternglanz R. J. Biol. Chem. 278:38109-38112(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"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-256, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z48952 Genomic DNA. Translation: CAA88794.1. AY557984 Genomic DNA. Translation: AAS56310.1. BK006946 Genomic DNA. Translation: DAA09967.1.
PIR	S52829.
RefSeq	NP_013785.1. NM_001182567.1.
3D structure databases
ProteinModelPortal	Q04751.
SMR	Q04751. Positions 138-252.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2745N.
IntAct	Q04751. 2 interactions.
MINT	MINT-575427.
STRING	4932.YMR069W.
Proteomic databases
PaxDb	Q04751.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR069W; YMR069W; YMR069W.
GeneID	855091.
KEGG	sce:YMR069W.
Organism-specific databases
CYGD	YMR069w.
SGD	S000004673. NAT4.
Phylogenomic databases
eggNOG	COG0454.
OrthoDB	EOG4NCQP6.
Enzyme and pathway databases
BRENDA	2.3.1.48. 984.
Gene expression databases
Genevestigator	Q04751.
GermOnline	YMR069W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GNAT_dom. [Graphical view]
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	978396.

Entry information

Entry name

NAT4_YEAST

Accession

Primary (citable) accession number: Q04751
Secondary accession number(s): D6VZP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program