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Q9NHD5 (SAN_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable N-acetyltransferase san

EC=2.3.1.-
Alternative name(s):
Protein separation anxiety
Gene names
Name:san
Synonyms:span
ORF Names:CG12352
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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

Subcellular location

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. Ref.1

Post-translational modification

Autoacetylated Probable.

Disruption phenotype

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. Ref.1

Sequence similarities

Belongs to the acetyltransferase family.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmitotic sister chromatid cohesion

Inferred from mutant phenotype Ref.1. Source: FlyBase

   Cellular componentcohesin core heterodimer

Inferred from direct assay Ref.1. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

protein acetyltransferase complex

Inferred from physical interaction Ref.1. Source: UniProtKB

   Molecular functionN-acetyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Probable N-acetyltransferase san
PRO_0000074578

Regions

Domain6 – 155150N-acetyltransferase

Amino acid modifications

Modified residue471N6-acetyllysine; by autocatalysis Probable

Sequences

Sequence LengthMass (Da)Tools
Q9NHD5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4C3B707833086974

FASTA18420,994
        10         20         30         40         50         60 
MTRSSIELGD VTPHNIKQLK KLNTVVFPVS YNDKFYVDVL EAGELAKLAY YNDIVVGAVC 

        70         80         90        100        110        120 
CRIDNTENQR RLYIMTLGCL SPYRRLGIGT VMFEHIMNFA EKDGNFDSIF LHVQINNNGA 

       130        140        150        160        170        180 
IEFYKKFGFE IVDTKEQYYK RIEPADAHVL QKTLRRTAPN SNSTATSTTA NSNSRSKARQ 


FTFV 

« Hide

References

« Hide 'large scale' references
[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: 14653991] [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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"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. expand/collapse author list , 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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF225902 mRNA. Translation: AAF34715.1.
AE013599 Genomic DNA. Translation: AAG22284.1.
AY070826 mRNA. Translation: AAL48448.1.
RefSeqNP_524779.1. NM_080040.3.
UniGeneDm.1821.

3D structure databases

ProteinModelPortalQ9NHD5.
SMRQ9NHD5. Positions 4-154.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-938687.
STRINGQ9NHD5.

Proteomic databases

PRIDEQ9NHD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088126; FBpp0087227; FBgn0024188.
GeneID44724.
KEGGdme:Dmel_CG12352.
NMPDRfig|7227.3.peg.4647.

Organism-specific databases

CTD44724.
FlyBaseFBgn0024188. san.

Phylogenomic databases

eggNOGinNOG06824.
GeneTreeEMGT00050000005791.
InParanoidQ9NHD5.
OMALAYYNDI.
OrthoDBEOG4WDBV3.
PhylomeDBQ9NHD5.

Gene expression databases

ArrayExpressQ9NHD5.
BgeeQ9NHD5.
GermOnlineCG12352. Drosophila melanogaster.

Family and domain databases

InterProIPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio837572.

Entry information

Entry nameSAN_DROME
AccessionPrimary (citable) accession number: Q9NHD5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families