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Q9NHD5

- SAN_DROME

UniProt

Q9NHD5 - SAN_DROME

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Protein

Probable N-acetyltransferase san

Gene
san, span, CG12352
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

GO - Biological processi

  1. lateral inhibition Source: FlyBase
  2. metabolic process Source: GOC
  3. mitotic nuclear division Source: FlyBase
  4. mitotic sister chromatid cohesion Source: FlyBase
  5. neuron projection morphogenesis Source: FlyBase
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
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.1 Publication

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 autocatalysis Inferred

Post-translational modificationi

Autoacetylated Inferred.1 Publication

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.
MINTiMINT-938687.
STRINGi7227.FBpp0087227.

Structurei

3D structure databases

ProteinModelPortaliQ9NHD5.
SMRiQ9NHD5. Positions 4-154.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 155150N-acetyltransferaseAdd
BLAST

Sequence similaritiesi

Belongs to the acetyltransferase family.

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

MTRSSIELGD VTPHNIKQLK KLNTVVFPVS YNDKFYVDVL EAGELAKLAY    50
YNDIVVGAVC CRIDNTENQR RLYIMTLGCL SPYRRLGIGT VMFEHIMNFA 100
EKDGNFDSIF LHVQINNNGA IEFYKKFGFE IVDTKEQYYK RIEPADAHVL 150
QKTLRRTAPN SNSTATSTTA NSNSRSKARQ FTFV 184
Length:184
Mass (Da):20,994
Last modified:October 1, 2000 - v1
Checksum:i4C3B707833086974
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF225902 mRNA. Translation: AAF34715.1.
AE013599 Genomic DNA. Translation: AAG22284.1.
AY070826 mRNA. Translation: AAL48448.1.
RefSeqiNP_524779.1. NM_080040.4.
UniGeneiDm.1821.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF225902 mRNA. Translation: AAF34715.1 .
AE013599 Genomic DNA. Translation: AAG22284.1 .
AY070826 mRNA. Translation: AAL48448.1 .
RefSeqi NP_524779.1. NM_080040.4.
UniGenei Dm.1821.

3D structure databases

ProteinModelPortali Q9NHD5.
SMRi Q9NHD5. Positions 4-154.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 69228. 5 interactions.
MINTi MINT-938687.
STRINGi 7227.FBpp0087227.

Proteomic databases

PaxDbi Q9NHD5.
PRIDEi Q9NHD5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0088126 ; FBpp0087227 ; FBgn0024188 .
GeneIDi 44724.
KEGGi dme:Dmel_CG12352.

Organism-specific databases

CTDi 44724.
FlyBasei FBgn0024188. san.

Phylogenomic databases

eggNOGi COG0456.
GeneTreei ENSGT00390000009110.
InParanoidi Q9NHD5.
OMAi SAIDFYQ.
OrthoDBi EOG7MWGZK.
PhylomeDBi Q9NHD5.

Miscellaneous databases

GenomeRNAii 44724.
NextBioi 837572.
PROi Q9NHD5.

Gene expression databases

Bgeei Q9NHD5.

Family and domain databases

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

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: September 3, 2014
This is version 86 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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