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Q9NHD5

- SAN_DROME

UniProt

Q9NHD5 - SAN_DROME

Protein

Probable N-acetyltransferase san

Gene

san

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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

    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

    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.
    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

    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

    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: October 1, 2014
    This is version 87 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