Q95SX8 (NAA60_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-alpha-acetyltransferase 60
Short name=dNaa60
EC=2.3.1.48
EC=2.3.1.88

Alternative name(s):
NatF catalytic subunit

Gene names

ORF Names:

CG18177

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	276 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Displays alpha (N-terminal) acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. Isoform A has histone acetyltransferase toward free histones, while isoform B has no histone acetyltransferase activity. Ref.4 Ref.5
Catalytic activity	Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA. Ref.4 Ref.5 Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.4
Sequence similarities	Belongs to the acetyltransferase family. NAA60 subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	Chromosome partition
Coding sequence diversity	Alternative splicing
Molecular function	Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-terminal peptidyl-methionine acetylation Inferred from direct assay Ref.5. Source: UniProtKB chromosome segregation Inferred from mutant phenotype Ref.5. Source: UniProtKB histone acetylation Inferred from electronic annotation. Source: GOC mitotic anaphase Inferred from mutant phenotype Ref.5. Source: FlyBase
Cellular_component	cytoplasm Inferred by curator Ref.5. Source: FlyBase
Molecular_function	H4 histone acetyltransferase activity Inferred from direct assay Ref.4. Source: UniProtKB histone acetyltransferase activity Inferred from electronic annotation. Source: EC peptide alpha-N-acetyltransferase activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform A Ref.1 (identifier: Q95SX8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform B Ref.1 (identifier: Q95SX8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     102-122: Missing.

Note: No experimental confirmation available.

Isoform C Ref.1 (identifier: Q95SX8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     102-122: Missing.
     234-276: DHIKHYASMVRHTSSLCAWLAGRVQQVVRWFYHKLLTRFNFIE → YPFSKYLYALGCIAFLSMISLYFWLPS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 276	276	N-alpha-acetyltransferase 60		PRO_0000413363
Regions
	Domain	34 – 239	206	N-acetyltransferase
Natural variations
	Alternative sequence	102 – 122	21	Missing in isoform B and isoform C. Ref.1		VSP_041889
	Alternative sequence	234 – 276	43	DHIKH…FNFIE → YPFSKYLYALGCIAFLSMIS LYFWLPS in isoform C. Ref.1		VSP_041890

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 45958EEBB2C3FFD3	FASTA	276	31,869
	10 20 30 40 50 60 MAQFTLYNKH SAPPSSESTR VDCEHVPLCS INDVQLRFLV PDDLTEVRQL CQEWFPIDYP 70 80 90 100 110 120 LSWYEDITSS TRFFALAAVY NLAIIGLIVA EIKPYRNVNK EVIANMSDSD ELYTRLSGFP 130 140 150 160 170 180 MQDKGILPDS MGRSADVGYI LSLGVHRSHR RNGIGSLLLD ALMNHLTTAE RHSVKAIFLH 190 200 210 220 230 240 TLTTNQPAIF FYEKRRFTLH SFLPYYYNIR GKGKDGFTYV NYINGGHPPW TLLDHIKHYA 250 260 270 SMVRHTSSLC AWLAGRVQQV VRWFYHKLLT RFNFIE
	Isoform B [UniParc]. Checksum: 7B426F05C7A96DEE	FASTA	255	29,512
	10 20 30 40 50 60 MAQFTLYNKH SAPPSSESTR VDCEHVPLCS INDVQLRFLV PDDLTEVRQL CQEWFPIDYP 70 80 90 100 110 120 LSWYEDITSS TRFFALAAVY NLAIIGLIVA EIKPYRNVNK EDKGILPDSM GRSADVGYIL 130 140 150 160 170 180 SLGVHRSHRR NGIGSLLLDA LMNHLTTAER HSVKAIFLHT LTTNQPAIFF YEKRRFTLHS 190 200 210 220 230 240 FLPYYYNIRG KGKDGFTYVN YINGGHPPWT LLDHIKHYAS MVRHTSSLCA WLAGRVQQVV 250 RWFYHKLLTR FNFIE
	Isoform C [UniParc]. Checksum: 24E10C5B25881F1C	FASTA	239	27,461
	10 20 30 40 50 60 MAQFTLYNKH SAPPSSESTR VDCEHVPLCS INDVQLRFLV PDDLTEVRQL CQEWFPIDYP 70 80 90 100 110 120 LSWYEDITSS TRFFALAAVY NLAIIGLIVA EIKPYRNVNK EDKGILPDSM GRSADVGYIL 130 140 150 160 170 180 SLGVHRSHRR NGIGSLLLDA LMNHLTTAER HSVKAIFLHT LTTNQPAIFF YEKRRFTLHS 190 200 210 220 230 FLPYYYNIRG KGKDGFTYVN YINGGHPPWT LLYPFSKYLY ALGCIAFLSM ISLYFWLPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B). Strain: Berkeley. Tissue: Embryo.
[4]	"HAT4, a Golgi apparatus-anchored B-type histone acetyltransferase, acetylates free histone H4 and facilitates chromatin assembly." Yang X., Yu W., Shi L., Sun L., Liang J., Yi X., Li Q., Zhang Y., Yang F., Han X., Zhang D., Yang J., Yao Z., Shang Y. Mol. Cell 44:39-50(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION (ISOFORM A), CATALYTIC ACTIVITY.
[5]	"NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation." Van Damme P., Hole K., Pimenta-Marques A., Helsens K., Vandekerckhove J., Martinho R.G., Gevaert K., Arnesen T. PLoS Genet. 7:E1002169-E1002169(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014296 Genomic DNA. Translation: AAF50213.2. AE014296 Genomic DNA. Translation: AAS65049.1. AE014296 Genomic DNA. Translation: ACL83284.1. AY060437 mRNA. Translation: AAL25476.1. BT001491 mRNA. Translation: AAN71246.1.
RefSeq	NP_001137929.1. NM_001144457.3. NP_648353.3. NM_140096.5. NP_996032.1. NM_206310.3.
UniGene	Dm.917.
3D structure databases
ProteinModelPortal	Q95SX8.
ModBase	Search...
Proteomic databases
PRIDE	Q95SX8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0089411; FBpp0089006; FBgn0036039.
GeneID	39142.
KEGG	dme:Dmel_CG18177.
UCSC	CG18177-RA. d. melanogaster.
Organism-specific databases
CTD	79903.
FlyBase	FBgn0036039. CG18177.
Phylogenomic databases
eggNOG	NOG276305.
GeneTree	ENSGT00390000008314.
InParanoid	Q9VT42.
OMA	PWTILYP.
OrthoDB	EOG4VQ857.
PhylomeDB	Q95SX8.
Gene expression databases
Bgee	Q95SX8.
Family and domain databases
Gene3D	3.40.630.30. 2 hits.
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
GenomeRNAi	39142.
NextBio	812130.

Entry information

Entry name

NAA60_DROME

Accession

Primary (citable) accession number: Q95SX8
Secondary accession number(s): B7Z0F9, Q8IH11, Q9VT42

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project