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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

Probable acetyltransferase 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.1 Publication

GO - Molecular functioni

  1. N-acetyltransferase activity Source: UniProtKB
  2. peptide alpha-N-acetyltransferase activity Source: GO_Central

GO - Biological processi

  1. lateral inhibition Source: FlyBase
  2. mitotic nuclear division Source: FlyBase
  3. mitotic sister chromatid cohesion Source: FlyBase
  4. neuron projection morphogenesis Source: FlyBase
  5. N-terminal protein amino acid acetylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Probable N-acetyltransferase san (EC:2.3.1.-)
Alternative name(s):
Protein separation anxiety
Gene namesi
Name:san
Synonyms:span
ORF Names:CG12352
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0024188. san.

Subcellular locationi

Cytoplasm 1 Publication
Note: During interphase, it localizes to the cytoplasm. During the entry into mitosis, it becomes distributed throughout the entire cell in a punctate pattern. From metaphase through telophase, it is distributed uniformly throughout the cell.

GO - Cellular componenti

  1. cohesin core heterodimer Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. protein acetyltransferase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Flies display disrupt centromeric sister chromatid cohesion very early in division. 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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 184184Probable N-acetyltransferase sanPRO_0000074578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471N6-acetyllysine; by autocatalysis1 Publication

Post-translational modificationi

Autoacetylated.Curated

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9NHD5.
PRIDEiQ9NHD5.

Expressioni

Gene expression databases

BgeeiQ9NHD5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi69228. 5 interactions.
IntActiQ9NHD5. 1 interaction.
MINTiMINT-938687.
STRINGi7227.FBpp0087227.

Structurei

3D structure databases

ProteinModelPortaliQ9NHD5.
SMRiQ9NHD5. Positions 4-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 155150N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the acetyltransferase family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0456.
GeneTreeiENSGT00390000009110.
InParanoidiQ9NHD5.
OMAiSAIDFYQ.
OrthoDBiEOG7MWGZK.
PhylomeDBiQ9NHD5.

Family and domain databases

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

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9NHD5.
SMRiQ9NHD5. Positions 4-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi69228. 5 interactions.
IntActiQ9NHD5. 1 interaction.
MINTiMINT-938687.
STRINGi7227.FBpp0087227.

Proteomic databases

PaxDbiQ9NHD5.
PRIDEiQ9NHD5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi44724.
FlyBaseiFBgn0024188. san.

Phylogenomic databases

eggNOGiCOG0456.
GeneTreeiENSGT00390000009110.
InParanoidiQ9NHD5.
OMAiSAIDFYQ.
OrthoDBiEOG7MWGZK.
PhylomeDBiQ9NHD5.

Miscellaneous databases

GenomeRNAii44724.
NextBioi837572.
PROiQ9NHD5.

Gene expression databases

BgeeiQ9NHD5.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Two putative acetyltransferases, san and deco, are required for establishing sister chromatid cohesion in Drosophila."
    Williams B.C., Garrett-Engele C.M., Li Z., Williams E.V., Rosenman E.D., Goldberg M.L.
    Curr. Biol. 13:2025-2036(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH ARD1 AND NAT1, ACETYLATION AT LYS-47, DISRUPTION PHENOTYPE.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Testis.

Entry informationi

Entry nameiSAN_DROME
AccessioniPrimary (citable) accession number: Q9NHD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2000
Last modified: February 4, 2015
This is version 90 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

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 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.