ID   SAT2_HUMAN              Reviewed;         170 AA.
AC   Q96F10;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Thialysine N-epsilon-acetyltransferase {ECO:0000303|PubMed:15283699};
DE            EC=2.3.1.- {ECO:0000269|PubMed:15283699};
DE   AltName: Full=Diamine acetyltransferase 2 {ECO:0000305};
DE            EC=2.3.1.57 {ECO:0000305|PubMed:12803540};
DE   AltName: Full=Spermidine/spermine N(1)-acetyltransferase 2 {ECO:0000303|PubMed:12803540};
DE            Short=SSAT-2 {ECO:0000303|PubMed:12803540};
GN   Name=SAT2 {ECO:0000312|HGNC:HGNC:23160};
GN   Synonyms=SSAT2 {ECO:0000303|PubMed:12803540};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=15283699; DOI=10.1042/bj20040790;
RA   Coleman C.S., Stanley B.A., Jones A.D., Pegg A.E.;
RT   "Spermidine/spermine-N1-acetyltransferase-2 (SSAT2) acetylates thialysine
RT   and is not involved in polyamine metabolism.";
RL   Biochem. J. 384:139-148(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RC   TISSUE=Lung carcinoma;
RX   PubMed=12803540; DOI=10.1042/bj20030734;
RA   Chen Y., Vujcic S., Liang P., Diegelman P., Kramer D.L., Porter C.W.;
RT   "Genomic identification and biochemical characterization of a second
RT   spermidine/spermine N1-acetyltransferase.";
RL   Biochem. J. 373:661-667(2003).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 2-170 IN COMPLEX WITH ACETYL-COA,
RP   AND SUBUNIT.
RX   PubMed=16596569; DOI=10.1002/prot.20967;
RA   Han B.W., Bingman C.A., Wesenberg G.E., Phillips G.N. Jr.;
RT   "Crystal structure of Homo sapiens thialysine Nepsilon-acetyltransferase
RT   (HsSSAT2) in complex with acetyl coenzyme A.";
RL   Proteins 64:288-293(2006).
CC   -!- FUNCTION: Catalyzes the N-acetylation of the amino acid thialysine (S-
CC       (2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene
CC       group substituted with a sulfur (PubMed:15283699). May also catalyze
CC       acetylation of polyamines, such as norspermidine, spermidine or
CC       spermine (PubMed:12803540). However, ability to acetylate polyamines is
CC       weak, suggesting that it does not act as a diamine acetyltransferase in
CC       vivo (PubMed:15283699). {ECO:0000269|PubMed:12803540,
CC       ECO:0000269|PubMed:15283699}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + S-(2-aminoethyl)-L-cysteine = CoA + H(+) + S-(2-
CC         acetamidoethyl)-L-cysteine; Xref=Rhea:RHEA:64804, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:156132,
CC         ChEBI:CHEBI:156134; Evidence={ECO:0000269|PubMed:15283699};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64805;
CC         Evidence={ECO:0000269|PubMed:15283699};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-
CC         acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116,
CC         Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977,
CC         ChEBI:CHEBI:70988; EC=2.3.1.57;
CC         Evidence={ECO:0000305|PubMed:12803540};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.2 mM for putrescine {ECO:0000269|PubMed:15283699};
CC         KM=13.4 mM for spermidine {ECO:0000269|PubMed:15283699};
CC         KM=4.8 mM for spermine {ECO:0000269|PubMed:15283699};
CC         KM=1.6 mM for 1,3-diaminopropane {ECO:0000269|PubMed:15283699};
CC         KM=6 mM for norspermidine {ECO:0000269|PubMed:15283699};
CC         KM=0.29 mM for thialysine {ECO:0000269|PubMed:15283699};
CC         Note=kcat is 0.0023 sec(-1) with putrescine as substrate
CC         (PubMed:15283699). kcat is 0.0072 sec(-1) with spermidine as
CC         substrate (PubMed:15283699). kcat is 0.0020 sec(-1) with spermine as
CC         substrate (PubMed:15283699). kcat is 0.0137 sec(-1) with
CC         1,3-diaminopropane as substrate (PubMed:15283699). kcat is 5.25
CC         sec(-1) with thialysine as substrate (PubMed:15283699).
CC         {ECO:0000269|PubMed:15283699};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16596569}.
CC   -!- INTERACTION:
CC       Q96F10; P21673: SAT1; NbExp=5; IntAct=EBI-748746, EBI-711613;
CC       Q96F10; Q96F10: SAT2; NbExp=5; IntAct=EBI-748746, EBI-748746;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:12803540}.
CC       Note=Intracellular organelles. {ECO:0000305|PubMed:12803540}.
CC   -!- TISSUE SPECIFICITY: Widely expressed (PubMed:15283699,
CC       PubMed:12803540). Under physiological conditions, SSAT2 is expressed at
CC       lower level that SSAT1 (SSAT). Many tissues express only SSAT1, several
CC       tissues express both SSAT1 and SSAT2, and bone, cervix, ovary and
CC       pineal gland expressed only SSAT2 (PubMed:12803540).
CC       {ECO:0000269|PubMed:12803540, ECO:0000269|PubMed:15283699}.
CC   -!- INDUCTION: Not inducible by polyamine analogs.
CC       {ECO:0000269|PubMed:12803540}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC   -!- CAUTION: Diamine acetyltransferase activity is unclear
CC       (PubMed:15283699, PubMed:12803540). According to a report, mediates
CC       acetylation of polyamines, such as norspermidine, spermidine or
CC       spermine (PubMed:12803540). However, another publication showed that
CC       such activity is weak compared to thialysine acetyltransferase
CC       activity, suggesting that polyamines are not substrates in vivo
CC       (PubMed:15283699). {ECO:0000269|PubMed:12803540,
CC       ECO:0000269|PubMed:15283699}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF348524; AAL83905.1; -; mRNA.
DR   EMBL; BC011751; AAH11751.1; -; mRNA.
DR   CCDS; CCDS11116.1; -.
DR   RefSeq; NP_001307775.1; NM_001320846.1.
DR   RefSeq; NP_001307776.1; NM_001320847.1.
DR   RefSeq; NP_597998.1; NM_133491.4.
DR   PDB; 2BEI; X-ray; 1.84 A; A/B=2-170.
DR   PDB; 2Q4V; X-ray; 1.84 A; A/B=2-170.
DR   PDBsum; 2BEI; -.
DR   PDBsum; 2Q4V; -.
DR   AlphaFoldDB; Q96F10; -.
DR   SMR; Q96F10; -.
DR   BioGRID; 125190; 16.
DR   IntAct; Q96F10; 9.
DR   MINT; Q96F10; -.
DR   STRING; 9606.ENSP00000269298; -.
DR   ChEMBL; CHEMBL3509592; -.
DR   DrugBank; DB00127; Spermine.
DR   iPTMnet; Q96F10; -.
DR   PhosphoSitePlus; Q96F10; -.
DR   BioMuta; SAT2; -.
DR   DMDM; 51339204; -.
DR   EPD; Q96F10; -.
DR   jPOST; Q96F10; -.
DR   MassIVE; Q96F10; -.
DR   MaxQB; Q96F10; -.
DR   PaxDb; 9606-ENSP00000269298; -.
DR   PeptideAtlas; Q96F10; -.
DR   ProteomicsDB; 76483; -.
DR   Pumba; Q96F10; -.
DR   Antibodypedia; 12120; 173 antibodies from 22 providers.
DR   DNASU; 112483; -.
DR   Ensembl; ENST00000269298.10; ENSP00000269298.5; ENSG00000141504.12.
DR   GeneID; 112483; -.
DR   KEGG; hsa:112483; -.
DR   MANE-Select; ENST00000269298.10; ENSP00000269298.5; NM_133491.5; NP_597998.1.
DR   UCSC; uc002gic.3; human.
DR   AGR; HGNC:23160; -.
DR   CTD; 112483; -.
DR   DisGeNET; 112483; -.
DR   GeneCards; SAT2; -.
DR   HGNC; HGNC:23160; SAT2.
DR   HPA; ENSG00000141504; Low tissue specificity.
DR   MIM; 611463; gene.
DR   neXtProt; NX_Q96F10; -.
DR   OpenTargets; ENSG00000141504; -.
DR   PharmGKB; PA134979941; -.
DR   VEuPathDB; HostDB:ENSG00000141504; -.
DR   eggNOG; KOG3216; Eukaryota.
DR   GeneTree; ENSGT00950000183121; -.
DR   HOGENOM; CLU_013985_41_1_1; -.
DR   InParanoid; Q96F10; -.
DR   OMA; GKLLGPC; -.
DR   OrthoDB; 5316510at2759; -.
DR   PhylomeDB; Q96F10; -.
DR   TreeFam; TF319736; -.
DR   BRENDA; 2.3.1.57; 2681.
DR   PathwayCommons; Q96F10; -.
DR   SignaLink; Q96F10; -.
DR   BioGRID-ORCS; 112483; 25 hits in 1147 CRISPR screens.
DR   ChiTaRS; SAT2; human.
DR   EvolutionaryTrace; Q96F10; -.
DR   GeneWiki; SAT2; -.
DR   GenomeRNAi; 112483; -.
DR   Pharos; Q96F10; Tbio.
DR   PRO; PR:Q96F10; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q96F10; Protein.
DR   Bgee; ENSG00000141504; Expressed in kidney epithelium and 181 other cell types or tissues.
DR   ExpressionAtlas; Q96F10; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0004145; F:diamine N-acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046204; P:nor-spermidine metabolic process; IDA:UniProtKB.
DR   GO; GO:0032920; P:putrescine acetylation; IDA:UniProtKB.
DR   GO; GO:0032918; P:spermidine acetylation; IDA:UniProtKB.
DR   GO; GO:0032919; P:spermine acetylation; IDA:UniProtKB.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR10545; DIAMINE N-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10545:SF51; THIALYSINE N-EPSILON-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
DR   Genevisible; Q96F10; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Cytoplasm; Reference proteome;
KW   Transferase.
FT   CHAIN           1..170
FT                   /note="Thialysine N-epsilon-acetyltransferase"
FT                   /id="PRO_0000074598"
FT   DOMAIN          4..168
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   ACT_SITE        140
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A951"
FT   BINDING         27..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21673"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21673"
FT   BINDING         94..96
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:16596569"
FT   BINDING         102..107
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:16596569"
FT   BINDING         133..135
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:16596569"
FT   BINDING         140
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:16596569"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21673"
FT   MOD_RES         29
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         126
FT                   /note="R -> C (in dbSNP:rs13894)"
FT                   /id="VAR_020465"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   HELIX           14..28
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   HELIX           31..33
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   STRAND          70..82
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   STRAND          86..96
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   HELIX           105..119
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   HELIX           134..142
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   HELIX           148..152
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   STRAND          154..160
FT                   /evidence="ECO:0007829|PDB:2BEI"
FT   HELIX           162..167
FT                   /evidence="ECO:0007829|PDB:2BEI"
SQ   SEQUENCE   170 AA;  19155 MW;  68D46F0E28186C68 CRC64;
     MASVRIREAK EGDCGDILRL IRELAEFEKL SDQVKISEEA LRADGFGDNP FYHCLVAEIL
     PAPGKLLGPC VVGYGIYYFI YSTWKGRTIY LEDIYVMPEY RGQGIGSKII KKVAEVALDK
     GCSQFRLAVL DWNQRAMDLY KALGAQDLTE AEGWHFFCFQ GEATRKLAGK
//