SAT2_HUMAN
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 03-AUG-2022, entry version 155.
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=6.0 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 1,3-
CC diaminopropane as substrate (PubMed:15283699). kcat is 5.25 sec(-1)
CC 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}.
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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; Q96F10; -.
DR PeptideAtlas; Q96F10; -.
DR PRIDE; Q96F10; -.
DR ProteomicsDB; 76483; -.
DR Antibodypedia; 12120; 155 antibodies from 21 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 CTD; 112483; -.
DR DisGeNET; 112483; -.
DR GeneCards; SAT2; -.
DR HGNC; HGNC:23160; SAT2.
DR HPA; ENSG00000141504; Tissue enhanced (liver).
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; RYSTWKG; -.
DR PhylomeDB; Q96F10; -.
DR TreeFam; TF319736; -.
DR BRENDA; 2.3.1.57; 2681.
DR PathwayCommons; Q96F10; -.
DR SignaLink; Q96F10; -.
DR BioGRID-ORCS; 112483; 24 hits in 1069 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 179 other tissues.
DR ExpressionAtlas; Q96F10; baseline and differential.
DR Genevisible; Q96F10; HS.
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:0019809; F:spermidine binding; IBA:GO_Central.
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 InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032959; SAT2.
DR PANTHER; PTHR10545:SF51; PTHR10545:SF51; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
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
