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Q96F10

- SAT2_HUMAN

UniProt

Q96F10 - SAT2_HUMAN

Protein

Diamine acetyltransferase 2

Gene

SAT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine > spermidine = spermine >> N1acetylspermine = putrescine.

    Catalytic activityi

    Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921Substrate; via carbonyl oxygenBy similarity
    Binding sitei140 – 1401Acetyl-CoA1 Publication
    Binding sitei152 – 1521SubstrateBy similarity

    GO - Molecular functioni

    1. diamine N-acetyltransferase activity Source: UniProt

    GO - Biological processi

    1. nor-spermidine metabolic process Source: UniProt
    2. putrescine acetylation Source: UniProt
    3. putrescine catabolic process Source: UniProtKB-UniPathway
    4. spermidine acetylation Source: UniProt
    5. spermine acetylation Source: UniProt

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.3.1.57. 2681.
    UniPathwayiUPA00188; UER00363.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diamine acetyltransferase 2 (EC:2.3.1.57)
    Alternative name(s):
    Polyamine N-acetyltransferase 2
    Spermidine/spermine N(1)-acetyltransferase 2
    Thialysine N-epsilon-acetyltransferase
    Gene namesi
    Name:SAT2
    Synonyms:SSAT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:23160. SAT2.

    Subcellular locationi

    Cytoplasm
    Note: Intracellular organelles.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134979941.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 170170Diamine acetyltransferase 2PRO_0000074598Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei29 – 291N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96F10.
    PaxDbiQ96F10.
    PRIDEiQ96F10.

    PTM databases

    PhosphoSiteiQ96F10.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Inductioni

    Not inducible by polyamine analogs.

    Gene expression databases

    ArrayExpressiQ96F10.
    BgeeiQ96F10.
    CleanExiHS_SAT2.
    GenevestigatoriQ96F10.

    Organism-specific databases

    HPAiHPA022136.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi125190. 5 interactions.
    IntActiQ96F10. 1 interaction.
    MINTiMINT-1476751.
    STRINGi9606.ENSP00000269298.

    Structurei

    Secondary structure

    1
    170
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi11 – 133
    Helixi14 – 2815
    Helixi38 – 469
    Beta strandi47 – 493
    Beta strandi53 – 597
    Beta strandi70 – 8213
    Turni83 – 853
    Beta strandi86 – 9611
    Helixi98 – 1003
    Beta strandi102 – 1043
    Helixi105 – 11915
    Beta strandi124 – 1307
    Helixi134 – 1429
    Helixi148 – 1525
    Beta strandi154 – 1607
    Helixi162 – 1676

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BEIX-ray1.84A/B2-170[»]
    2Q4VX-ray1.84A/B2-170[»]
    ProteinModelPortaliQ96F10.
    SMRiQ96F10. Positions 2-170.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96F10.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 168165N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 282Substrate bindingBy similarity
    Regioni94 – 963Acetyl-CoA binding
    Regioni102 – 1076Acetyl-CoA binding
    Regioni133 – 1353Acetyl-CoA binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0454.
    HOGENOMiHOG000078521.
    HOVERGENiHBG063175.
    KOiK00657.
    OMAiDWVGMRV.
    OrthoDBiEOG7M98HM.
    PhylomeDBiQ96F10.
    TreeFamiTF319736.

    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.

    Q96F10-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASVRIREAK EGDCGDILRL IRELAEFEKL SDQVKISEEA LRADGFGDNP    50
    FYHCLVAEIL PAPGKLLGPC VVGYGIYYFI YSTWKGRTIY LEDIYVMPEY 100
    RGQGIGSKII KKVAEVALDK GCSQFRLAVL DWNQRAMDLY KALGAQDLTE 150
    AEGWHFFCFQ GEATRKLAGK 170
    Length:170
    Mass (Da):19,155
    Last modified:December 1, 2001 - v1
    Checksum:i68D46F0E28186C68
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti126 – 1261R → C.
    Corresponds to variant rs13894 [ dbSNP | Ensembl ].
    VAR_020465

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF348524 mRNA. Translation: AAL83905.1.
    BC011751 mRNA. Translation: AAH11751.1.
    CCDSiCCDS11116.1.
    RefSeqiNP_597998.1. NM_133491.3.
    UniGeneiHs.10846.

    Genome annotation databases

    EnsembliENST00000269298; ENSP00000269298; ENSG00000141504.
    GeneIDi112483.
    KEGGihsa:112483.
    UCSCiuc002gic.2. human.

    Polymorphism databases

    DMDMi51339204.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF348524 mRNA. Translation: AAL83905.1 .
    BC011751 mRNA. Translation: AAH11751.1 .
    CCDSi CCDS11116.1.
    RefSeqi NP_597998.1. NM_133491.3.
    UniGenei Hs.10846.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BEI X-ray 1.84 A/B 2-170 [» ]
    2Q4V X-ray 1.84 A/B 2-170 [» ]
    ProteinModelPortali Q96F10.
    SMRi Q96F10. Positions 2-170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125190. 5 interactions.
    IntActi Q96F10. 1 interaction.
    MINTi MINT-1476751.
    STRINGi 9606.ENSP00000269298.

    Chemistry

    DrugBanki DB00127. Spermine.

    PTM databases

    PhosphoSitei Q96F10.

    Polymorphism databases

    DMDMi 51339204.

    Proteomic databases

    MaxQBi Q96F10.
    PaxDbi Q96F10.
    PRIDEi Q96F10.

    Protocols and materials databases

    DNASUi 112483.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269298 ; ENSP00000269298 ; ENSG00000141504 .
    GeneIDi 112483.
    KEGGi hsa:112483.
    UCSCi uc002gic.2. human.

    Organism-specific databases

    CTDi 112483.
    GeneCardsi GC17M007529.
    HGNCi HGNC:23160. SAT2.
    HPAi HPA022136.
    MIMi 611463. gene.
    neXtProti NX_Q96F10.
    PharmGKBi PA134979941.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0454.
    HOGENOMi HOG000078521.
    HOVERGENi HBG063175.
    KOi K00657.
    OMAi DWVGMRV.
    OrthoDBi EOG7M98HM.
    PhylomeDBi Q96F10.
    TreeFami TF319736.

    Enzyme and pathway databases

    UniPathwayi UPA00188 ; UER00363 .
    BRENDAi 2.3.1.57. 2681.

    Miscellaneous databases

    EvolutionaryTracei Q96F10.
    GeneWikii SAT2.
    GenomeRNAii 112483.
    NextBioi 78600.
    PROi Q96F10.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96F10.
    Bgeei Q96F10.
    CleanExi HS_SAT2.
    Genevestigatori Q96F10.

    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. Coleman C.C.S., Pegg A.E., Chau V.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    3. "Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase."
      Chen Y., Vujcic S., Liang P., Diegelman P., Kramer D.L., Porter C.W.
      Biochem. J. 373:661-667(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Tissue: Lung carcinoma.
    4. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "Crystal structure of Homo sapiens thialysine Nepsilon-acetyltransferase (HsSSAT2) in complex with acetyl coenzyme A."
      Han B.W., Bingman C.A., Wesenberg G.E., Phillips G.N. Jr.
      Proteins 64:288-293(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 2-170 IN COMPLEX WITH ACETYL-COA, SUBUNIT.

    Entry informationi

    Entry nameiSAT2_HUMAN
    AccessioniPrimary (citable) accession number: Q96F10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Under physiological conditions, SSAT2 is expressed at lower level that SSAT1 (SSAT). Many tissues express only SSAT1, several tissues express both SSAT1 and SSAT2, and bone, cervix, ovary and pineal gland expressed only SSAT2.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3