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Protein

Probable N-acetyltransferase san

Gene

san

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

Functioni

N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (By similarity). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides (By similarity). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins. Autoacetylates (PubMed:14653991). Required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together (PubMed:14653991, PubMed:18801358, PubMed:27996020). Required for the interaction between Scc1/vtd and SMC3, possibly by mediating N-terminal acetylation of Scc1/vtd (PubMed:27996020).By similarity3 Publications

Catalytic activityi

Acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-alanyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-seryl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-valyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-threonyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-lysyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA.By similarity
Acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei31SubstrateBy similarity1
Active sitei73By similarity1
Binding sitei75SubstrateBy similarity1
Active sitei112By similarity1

GO - Molecular functioni

  • N-acetyltransferase activity Source: UniProtKB
  • peptide alpha-N-acetyltransferase activity Source: UniProtKB

GO - Biological processi

  • histone acetylation Source: FlyBase
  • lateral inhibition Source: FlyBase
  • mitotic cell cycle Source: FlyBase
  • mitotic sister chromatid cohesion Source: UniProtKB
  • neuron projection morphogenesis Source: FlyBase
  • N-terminal protein amino acid acetylation Source: UniProtKB

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processCell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Probable N-acetyltransferase san (EC:2.3.1.258By similarity)
Alternative name(s):
N-epsilon-acetyltransferase san (EC:2.3.1.-1 Publication)
Protein atado1 Publication
Protein separation anxiety1 Publication
Gene namesi
Name:san
Synonyms:span
ORF Names:CG12352
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0024188. san.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Flies display disrupt centromeric sister chromatid cohesion very early in division (PubMed:14653991, PubMed:18801358). This failure of sister chromatid cohesion does not require separase and is correlated with a failure of the cohesin component Scc1 to accumulate in centromeric regions (PubMed:14653991). In contrast, no mitotic defects are observed in germ line cells during oogenesis (PubMed:18801358).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi84R → A: Abolishes N-alpha-acetyltransferase activity; impaired sister chromatid cohesion during mitosis.; when associated with F-124. 1 Publication1
Mutagenesisi124Y → F: Abolishes N-alpha-acetyltransferase activity; impaired sister chromatid cohesion during mitosis.; when associated with A-84. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000745781 – 184Probable N-acetyltransferase sanAdd BLAST184

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei47N6-acetyllysine; by autocatalysis1 Publication1

Post-translational modificationi

Autoacetylated.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9NHD5.
PRIDEiQ9NHD5.

PTM databases

iPTMnetiQ9NHD5.

Expressioni

Gene expression databases

BgeeiFBgn0024188.
GenevisibleiQ9NHD5. DM.

Interactioni

Subunit structurei

Component of an acetyltransferase complex, at least composed of san, Ard1 and Nat1.1 Publication

Protein-protein interaction databases

BioGridi69228. 8 interactors.
IntActiQ9NHD5. 1 interactor.
MINTiMINT-938687.
STRINGi7227.FBpp0087227.

Structurei

3D structure databases

ProteinModelPortaliQ9NHD5.
SMRiQ9NHD5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 155N-acetyltransferasePROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni77 – 90Acetyl-CoA bindingBy similarityAdd BLAST14
Regioni117 – 126Coenzyme A bindingBy similarity10
Regioni138 – 141SubstrateBy similarity4

Sequence similaritiesi

Belongs to the acetyltransferase family.Curated

Phylogenomic databases

eggNOGiKOG3138. Eukaryota.
COG0456. LUCA.
GeneTreeiENSGT00390000009110.
InParanoidiQ9NHD5.
KOiK20793.
OMAiIVETKEH.
OrthoDBiEOG091G0PAG.
PhylomeDBiQ9NHD5.

Family and domain databases

InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
PfamiView protein in Pfam
PF00583. Acetyltransf_1. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiView protein in PROSITE
PS51186. GNAT. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9NHD5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRSSIELGD VTPHNIKQLK KLNTVVFPVS YNDKFYVDVL EAGELAKLAY
60 70 80 90 100
YNDIVVGAVC CRIDNTENQR RLYIMTLGCL SPYRRLGIGT VMFEHIMNFA
110 120 130 140 150
EKDGNFDSIF LHVQINNNGA IEFYKKFGFE IVDTKEQYYK RIEPADAHVL
160 170 180
QKTLRRTAPN SNSTATSTTA NSNSRSKARQ FTFV
Length:184
Mass (Da):20,994
Last modified:October 1, 2000 - v1
Checksum:i4C3B707833086974
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF225902 mRNA. Translation: AAF34715.1.
AE013599 Genomic DNA. Translation: AAG22284.1.
AY070826 mRNA. Translation: AAL48448.1.
RefSeqiNP_524779.1. NM_080040.5.
UniGeneiDm.1821.

Genome annotation databases

EnsemblMetazoaiFBtr0088126; FBpp0087227; FBgn0024188.
GeneIDi44724.
KEGGidme:Dmel_CG12352.

Similar proteinsi

Entry informationi

Entry nameiSAN_DROME
AccessioniPrimary (citable) accession number: Q9NHD5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2000
Last modified: October 25, 2017
This is version 112 of the entry and version 1 of the sequence. See 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