Q9NHD5 (SAN_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable N-acetyltransferase san
EC=2.3.1.-

Alternative name(s):
Protein separation anxiety

Gene names

Name:	san
Synonyms:	span
ORF Names:	CG12352

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cell cycle
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mitotic sister chromatid cohesion Inferred from mutant phenotype Ref.1. Source: FlyBase
Cellular component	cohesin 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 function	N-acetyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 184	184	Probable N-acetyltransferase san		PRO_0000074578
Regions
	Domain	6 – 155	150	N-acetyltransferase
Amino acid modifications
	Modified residue	47	1	N6-acetyllysine; by autocatalysis Probable

Sequences

	Sequence		Length	Mass (Da)
	Q9NHD5 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 4C3B707833086974	FASTA	184	20,994
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
RefSeq	NP_524779.1. NM_080040.3.
UniGene	Dm.1821.
3D structure databases
ProteinModelPortal	Q9NHD5.
SMR	Q9NHD5. Positions 4-154.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-938687.
STRING	Q9NHD5.
Proteomic databases
PRIDE	Q9NHD5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0088126; FBpp0087227; FBgn0024188.
GeneID	44724.
KEGG	dme:Dmel_CG12352.
NMPDR	fig|7227.3.peg.4647.
Organism-specific databases
CTD	44724.
FlyBase	FBgn0024188. san.
Phylogenomic databases
eggNOG	inNOG06824.
GeneTree	EMGT00050000005791.
InParanoid	Q9NHD5.
OMA	LAYYNDI.
OrthoDB	EOG4WDBV3.
PhylomeDB	Q9NHD5.
Gene expression databases
ArrayExpress	Q9NHD5.
Bgee	Q9NHD5.
GermOnline	CG12352. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000182. AcTrfase_GCN5-related_dom. IPR016181. Acyl_CoA_acyltransferase. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	837572.

Entry information

Entry name

SAN_DROME

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project