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Q95SX8

- NAA60_DROME

UniProt

Q95SX8 - NAA60_DROME

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Protein

N-alpha-acetyltransferase 60

Gene
Naa60, CG18177
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 shows histone acetyltransferase activity toward free histones while isoform B does not.2 Publications

Catalytic activityi

Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA.2 Publications
Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

GO - Molecular functioni

  1. H4 histone acetyltransferase activity Source: UniProtKB
  2. histone acetyltransferase activity Source: UniProtKB-EC
  3. peptide alpha-N-acetyltransferase activity Source: UniProtKB

GO - Biological processi

  1. chromosome segregation Source: UniProtKB
  2. histone H4 acetylation Source: UniProtKB
  3. N-terminal peptidyl-methionine acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Chromosome partition

Names & Taxonomyi

Protein namesi
Recommended name:
N-alpha-acetyltransferase 60 (EC:2.3.1.48, EC:2.3.1.88)
Short name:
dNaa60
Alternative name(s):
NatF catalytic subunit
Gene namesi
Name:Naa60
ORF Names:CG18177
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036039. Naa60.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 276276N-alpha-acetyltransferase 60PRO_0000413363Add
BLAST

Proteomic databases

PRIDEiQ95SX8.

Expressioni

Gene expression databases

BgeeiQ95SX8.

Structurei

3D structure databases

ProteinModelPortaliQ95SX8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 239206N-acetyltransferaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG276305.
GeneTreeiENSGT00390000008314.
InParanoidiQ9VT42.
OMAiKEVIANM.
OrthoDBiEOG7M0NT7.
PhylomeDBiQ95SX8.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform A1 Publication (identifier: Q95SX8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAQFTLYNKH SAPPSSESTR VDCEHVPLCS INDVQLRFLV PDDLTEVRQL    50
CQEWFPIDYP LSWYEDITSS TRFFALAAVY NLAIIGLIVA EIKPYRNVNK 100
EVIANMSDSD ELYTRLSGFP MQDKGILPDS MGRSADVGYI LSLGVHRSHR 150
RNGIGSLLLD ALMNHLTTAE RHSVKAIFLH TLTTNQPAIF FYEKRRFTLH 200
SFLPYYYNIR GKGKDGFTYV NYINGGHPPW TLLDHIKHYA SMVRHTSSLC 250
AWLAGRVQQV VRWFYHKLLT RFNFIE 276

Note: No experimental confirmation available.

Length:276
Mass (Da):31,869
Last modified:December 1, 2001 - v1
Checksum:i45958EEBB2C3FFD3
GO
Isoform B1 Publication (identifier: Q95SX8-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:255
Mass (Da):29,512
Checksum:i7B426F05C7A96DEE
GO
Isoform C1 Publication (identifier: Q95SX8-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:239
Mass (Da):27,461
Checksum:i24E10C5B25881F1C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei102 – 12221Missing in isoform B and isoform C. 1 PublicationVSP_041889Add
BLAST
Alternative sequencei234 – 27643DHIKH…FNFIE → YPFSKYLYALGCIAFLSMIS LYFWLPS in isoform C. 1 PublicationVSP_041890Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_001137929.1. NM_001144457.3. [Q95SX8-3]
NP_648353.3. NM_140096.5. [Q95SX8-2]
NP_996032.1. NM_206310.3. [Q95SX8-1]
UniGeneiDm.917.

Genome annotation databases

EnsemblMetazoaiFBtr0089411; FBpp0089006; FBgn0036039. [Q95SX8-1]
GeneIDi39142.
KEGGidme:Dmel_CG18177.
UCSCiCG18177-RA. d. melanogaster. [Q95SX8-1]
CG18177-RB. d. melanogaster.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_001137929.1. NM_001144457.3. [Q95SX8-3 ]
NP_648353.3. NM_140096.5. [Q95SX8-2 ]
NP_996032.1. NM_206310.3. [Q95SX8-1 ]
UniGenei Dm.917.

3D structure databases

ProteinModelPortali Q95SX8.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q95SX8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0089411 ; FBpp0089006 ; FBgn0036039 . [Q95SX8-1 ]
GeneIDi 39142.
KEGGi dme:Dmel_CG18177.
UCSCi CG18177-RA. d. melanogaster. [Q95SX8-1 ]
CG18177-RB. d. melanogaster.

Organism-specific databases

CTDi 79903.
FlyBasei FBgn0036039. Naa60.

Phylogenomic databases

eggNOGi NOG276305.
GeneTreei ENSGT00390000008314.
InParanoidi Q9VT42.
OMAi KEVIANM.
OrthoDBi EOG7M0NT7.
PhylomeDBi Q95SX8.

Miscellaneous databases

GenomeRNAii 39142.
NextBioi 812130.
PROi Q95SX8.

Gene expression databases

Bgeei Q95SX8.

Family and domain databases

Gene3Di 3.40.630.30. 2 hits.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view ]
Pfami PF00583. Acetyltransf_1. 1 hit.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 2 hits.
PROSITEi PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiNAA60_DROME
AccessioniPrimary (citable) accession number: Q95SX8
Secondary accession number(s): B7Z0F9, Q8IH11, Q9VT42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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