ID   SAT1_HUMAN              Reviewed;         171 AA.
AC   P21673; Q6ICU9;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   27-MAR-2024, entry version 215.
DE   RecName: Full=Diamine acetyltransferase 1 {ECO:0000305};
DE            EC=2.3.1.57 {ECO:0000269|PubMed:15283699, ECO:0000269|PubMed:16455797, ECO:0000269|PubMed:17516632};
DE   AltName: Full=Polyamine N-acetyltransferase 1 {ECO:0000305};
DE   AltName: Full=Putrescine acetyltransferase {ECO:0000303|PubMed:17516632};
DE   AltName: Full=Spermidine/spermine N(1)-acetyltransferase 1 {ECO:0000303|PubMed:1652956, ECO:0000303|PubMed:8573111};
DE            Short=SSAT {ECO:0000303|PubMed:1652956, ECO:0000303|PubMed:8573111};
DE            Short=SSAT-1;
GN   Name=SAT1 {ECO:0000312|HGNC:HGNC:10540}; Synonyms=SAT;
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].
RX   PubMed=1985966; DOI=10.1016/s0021-9258(17)35245-6;
RA   Casero R.A. Jr., Celano P., Ervin S.J., Applegren N.B., Wiest L.,
RA   Pegg A.E.;
RT   "Isolation and characterization of a cDNA clone that codes for human
RT   spermidine/spermine N1-acetyltransferase.";
RL   J. Biol. Chem. 266:810-814(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=1652956; DOI=10.1016/0006-291x(91)91385-p;
RA   Xiao L., Celano P., Mank A.R., Pegg A.E., Casero R.A. Jr.;
RT   "Characterization of a full-length cDNA which codes for the human
RT   spermidine/spermine N1-acetyltransferase.";
RL   Biochem. Biophys. Res. Commun. 179:407-415(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1417826; DOI=10.1016/0006-291x(92)90471-v;
RA   Xiao L., Celano P., Mank A.R., Griffin C., Wang J.E., Casero R.A. Jr.;
RT   "Structure of the human spermidine/spermine N1-acetyltransferase gene
RT   (exon/intron gene organization and localization to Xp22.1).";
RL   Biochem. Biophys. Res. Commun. 187:1493-1502(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8573111; DOI=10.1042/bj3130691;
RA   Xiao L., Casero R.A. Jr.;
RT   "Differential transcription of the human spermidine/spermine N1-
RT   acetyltransferase (SSAT) gene in human lung carcinoma cells.";
RL   Biochem. J. 313:691-696(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow, and Skin;
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   [10]
RP   PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RX   PubMed=2241897; DOI=10.1042/bj2700615;
RA   Casero R.A. Jr., Celano P., Ervin S.J., Wiest L., Pegg A.E.;
RT   "High specific induction of spermidine/spermine N1-acetyltransferase in a
RT   human large cell lung carcinoma.";
RL   Biochem. J. 270:615-620(1990).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH ACETYL-COENZYME A;
RP   THE SUBSTRATES SPERMINE AND N1,N11-BIS-(ETHYL)-NORSPERMINE, MUTAGENESIS OF
RP   TYR-140, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=16455797; DOI=10.1073/pnas.0511008103;
RA   Bewley M.C., Graziano V., Jiang J., Matz E., Studier F.W., Pegg A.E.,
RA   Coleman C.S., Flanagan J.M.;
RT   "Structures of wild-type and mutant human spermidine/spermine N1-
RT   acetyltransferase, a potential therapeutic drug target.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:2063-2068(2006).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH THE SUBSTRATE AND
RP   ACETYL-COA ANALOG N1-SPERMINE-ACETYL-COENZYME A, BIOPHYSICOCHEMICAL
RP   PROPERTIES, CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=17516632; DOI=10.1021/bi700256z;
RA   Hegde S.S., Chandler J., Vetting M.W., Yu M., Blanchard J.S.;
RT   "Mechanistic and structural analysis of human spermidine/spermine N1-
RT   acetyltransferase.";
RL   Biochemistry 46:7187-7195(2007).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUBUNIT.
RX   PubMed=16544326; DOI=10.1002/prot.20965;
RA   Zhu Y.-Q., Zhu D.-Y., Yin L., Zhang Y., Vonrhein C., Wang D.-C.;
RT   "Crystal structure of human spermidine/spermine N1-acetyltransferase
RT   (hSSAT): the first structure of a new sequence family of transferase
RT   homologous superfamily.";
RL   Proteins 63:1127-1131(2006).
RN   [15]
RP   POSSIBLE INVOLVEMENT IN KERATOSIS FOLLICULARIS SPINULOSA DECALVANS.
RX   PubMed=12215835; DOI=10.1007/s00439-002-0791-6;
RA   Gimelli G., Giglio S., Zuffardi O., Alhonen L., Suppola S., Cusano R.,
RA   Lo Nigro C., Gatti R., Ravazzolo R., Seri M.;
RT   "Gene dosage of the spermidine/spermine N(1)-acetyltransferase (SSAT) gene
RT   with putrescine accumulation in a patient with a Xp21.1p22.12 duplication
RT   and keratosis follicularis spinulosa decalvans (KFSD).";
RL   Hum. Genet. 111:235-241(2002).
CC   -!- FUNCTION: Enzyme which catalyzes the acetylation of polyamines
CC       (PubMed:15283699, PubMed:16455797, PubMed:17516632). Substrate
CC       specificity: norspermidine = spermidine >> spermine > N(1)-
CC       acetylspermine (PubMed:17516632). This highly regulated enzyme allows a
CC       fine attenuation of the intracellular concentration of polyamines
CC       (PubMed:16455797). Also involved in the regulation of polyamine
CC       transport out of cells (PubMed:16455797). Also acts on 1,3-
CC       diaminopropane and 1,5-diaminopentane (PubMed:16455797,
CC       PubMed:17516632). {ECO:0000269|PubMed:15283699,
CC       ECO:0000269|PubMed:16455797, ECO:0000269|PubMed:17516632}.
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:0000269|PubMed:15283699, ECO:0000269|PubMed:16455797,
CC         ECO:0000269|PubMed:17516632};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11117;
CC         Evidence={ECO:0000269|PubMed:15283699, ECO:0000269|PubMed:16455797,
CC         ECO:0000269|PubMed:17516632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(1)-acetylspermidine;
CC         Xref=Rhea:RHEA:28150, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58324; EC=2.3.1.57;
CC         Evidence={ECO:0000269|PubMed:15283699, ECO:0000269|PubMed:17516632};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28151;
CC         Evidence={ECO:0000269|PubMed:15283699, ECO:0000269|PubMed:17516632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + spermine = CoA + H(+) + N(1)-acetylspermine;
CC         Xref=Rhea:RHEA:33099, ChEBI:CHEBI:15378, ChEBI:CHEBI:45725,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58101; EC=2.3.1.57;
CC         Evidence={ECO:0000269|PubMed:15283699, ECO:0000269|PubMed:17516632};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33100;
CC         Evidence={ECO:0000269|PubMed:15283699, ECO:0000269|PubMed:17516632};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.8 uM for acetyl-coenzyme A {ECO:0000269|PubMed:17516632};
CC         KM=5.7 uM for spermine {ECO:0000269|PubMed:17516632};
CC         KM=3.7 uM for spermine {ECO:0000269|PubMed:15283699};
CC         KM=22 uM for spermidine {ECO:0000269|PubMed:17516632};
CC         KM=58 uM for spermidine {ECO:0000269|PubMed:15283699};
CC         Note=kcat is 8.7 sec(-1) with spermidine as substrate
CC         (PubMed:15283699). kcat is 5 sec(-1) with spermine as substrate
CC         (PubMed:15283699). {ECO:0000269|PubMed:15283699};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:17516632};
CC   -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; N-
CC       acetylputrescine from putrescine: step 1/1.
CC       {ECO:0000269|PubMed:16455797, ECO:0000269|PubMed:17516632}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16455797,
CC       ECO:0000269|PubMed:16544326, ECO:0000269|PubMed:17516632}.
CC   -!- INTERACTION:
CC       P21673; Q6UXT9: ABHD15; NbExp=3; IntAct=EBI-711613, EBI-2824666;
CC       P21673; P05067: APP; NbExp=3; IntAct=EBI-711613, EBI-77613;
CC       P21673; Q7RTU4: BHLHA9; NbExp=3; IntAct=EBI-711613, EBI-17508719;
CC       P21673; Q9UFG5: C19orf25; NbExp=3; IntAct=EBI-711613, EBI-741214;
CC       P21673; P55210: CASP7; NbExp=6; IntAct=EBI-711613, EBI-523958;
CC       P21673; Q8NFR7: CCDC148; NbExp=5; IntAct=EBI-711613, EBI-2349862;
CC       P21673; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-711613, EBI-10175300;
CC       P21673; Q00587-2: CDC42EP1; NbExp=3; IntAct=EBI-711613, EBI-11027409;
CC       P21673; P09669: COX6C; NbExp=3; IntAct=EBI-711613, EBI-715040;
CC       P21673; O00148: DDX39A; NbExp=3; IntAct=EBI-711613, EBI-348253;
CC       P21673; Q5VUD6: DIPK1B; NbExp=6; IntAct=EBI-711613, EBI-721274;
CC       P21673; Q9NQL9: DMRT3; NbExp=6; IntAct=EBI-711613, EBI-9679045;
CC       P21673; O15371: EIF3D; NbExp=3; IntAct=EBI-711613, EBI-353818;
CC       P21673; Q8NDB6: FAM156A; NbExp=3; IntAct=EBI-711613, EBI-749727;
CC       P21673; Q86W67: FAM228A; NbExp=3; IntAct=EBI-711613, EBI-12958227;
CC       P21673; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-711613, EBI-12845222;
CC       P21673; P07954: FH; NbExp=3; IntAct=EBI-711613, EBI-1050358;
CC       P21673; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-711613, EBI-7960826;
CC       P21673; P17482: HOXB9; NbExp=6; IntAct=EBI-711613, EBI-745290;
CC       P21673; P22459: KCNA4; NbExp=4; IntAct=EBI-711613, EBI-631235;
CC       P21673; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-711613, EBI-9089060;
CC       P21673; Q9UBR4-2: LHX3; NbExp=5; IntAct=EBI-711613, EBI-12039345;
CC       P21673; Q8TBB1: LNX1; NbExp=8; IntAct=EBI-711613, EBI-739832;
CC       P21673; Q5U5X0: LYRM7; NbExp=3; IntAct=EBI-711613, EBI-13943106;
CC       P21673; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-711613, EBI-16439278;
CC       P21673; P52815: MRPL12; NbExp=3; IntAct=EBI-711613, EBI-358272;
CC       P21673; Q13330: MTA1; NbExp=3; IntAct=EBI-711613, EBI-714236;
CC       P21673; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-711613, EBI-2858213;
CC       P21673; Q9GZT8: NIF3L1; NbExp=5; IntAct=EBI-711613, EBI-740897;
CC       P21673; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-711613, EBI-741158;
CC       P21673; P25786: PSMA1; NbExp=3; IntAct=EBI-711613, EBI-359352;
CC       P21673; Q96I25: RBM17; NbExp=13; IntAct=EBI-711613, EBI-740272;
CC       P21673; Q04864: REL; NbExp=3; IntAct=EBI-711613, EBI-307352;
CC       P21673; Q9BUL9: RPP25; NbExp=8; IntAct=EBI-711613, EBI-366570;
CC       P21673; P21673: SAT1; NbExp=4; IntAct=EBI-711613, EBI-711613;
CC       P21673; Q96F10: SAT2; NbExp=5; IntAct=EBI-711613, EBI-748746;
CC       P21673; O43623: SNAI2; NbExp=3; IntAct=EBI-711613, EBI-9876238;
CC       P21673; Q6ZNM6: SPMIP10; NbExp=3; IntAct=EBI-711613, EBI-18115728;
CC       P21673; Q9BSH4: TACO1; NbExp=4; IntAct=EBI-711613, EBI-747797;
CC       P21673; Q9BQ70: TCF25; NbExp=11; IntAct=EBI-711613, EBI-745182;
CC       P21673; Q15561: TEAD4; NbExp=3; IntAct=EBI-711613, EBI-747736;
CC       P21673; Q08117-2: TLE5; NbExp=3; IntAct=EBI-711613, EBI-11741437;
CC       P21673; P19237: TNNI1; NbExp=3; IntAct=EBI-711613, EBI-746692;
CC       P21673; Q99757: TXN2; NbExp=3; IntAct=EBI-711613, EBI-2932492;
CC       P21673; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-711613, EBI-739895;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:1985966,
CC       ECO:0000305|PubMed:2241897}.
CC   -!- DISEASE: Note=Overexpression of SAT1 and the consequent putrescine
CC       accumulation might play a role in the pathogenesis of keratosis
CC       follicularis spinulosa decalvans. {ECO:0000269|PubMed:12215835}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; M77693; AAA60573.1; -; mRNA.
DR   EMBL; M55580; AAA63260.1; -; mRNA.
DR   EMBL; Z14136; CAA78509.1; -; Genomic_DNA.
DR   EMBL; U40369; AAA98854.1; -; Genomic_DNA.
DR   EMBL; BT006825; AAP35471.1; -; mRNA.
DR   EMBL; CR450294; CAG29290.1; -; mRNA.
DR   EMBL; AK312162; BAG35096.1; -; mRNA.
DR   EMBL; CH471074; EAW99000.1; -; Genomic_DNA.
DR   EMBL; BC002503; AAH02503.1; -; mRNA.
DR   EMBL; BC008424; AAH08424.1; -; mRNA.
DR   CCDS; CCDS14207.1; -.
DR   PIR; JH0783; JH0783.
DR   RefSeq; NP_002961.1; NM_002970.3.
DR   PDB; 2B3U; X-ray; 1.85 A; A/B=1-171.
DR   PDB; 2B3V; X-ray; 1.95 A; A=1-171.
DR   PDB; 2B4B; X-ray; 2.00 A; A/B=1-171.
DR   PDB; 2B4D; X-ray; 2.00 A; A/B=1-171.
DR   PDB; 2B58; X-ray; 1.95 A; A=1-171.
DR   PDB; 2B5G; X-ray; 1.70 A; A/B=1-171.
DR   PDB; 2F5I; X-ray; 2.30 A; A/B=1-171.
DR   PDB; 2FXF; X-ray; 2.00 A; A/B=2-171.
DR   PDB; 2G3T; X-ray; 1.80 A; A/B=1-171.
DR   PDB; 2JEV; X-ray; 2.30 A; A/B=1-171.
DR   PDBsum; 2B3U; -.
DR   PDBsum; 2B3V; -.
DR   PDBsum; 2B4B; -.
DR   PDBsum; 2B4D; -.
DR   PDBsum; 2B58; -.
DR   PDBsum; 2B5G; -.
DR   PDBsum; 2F5I; -.
DR   PDBsum; 2FXF; -.
DR   PDBsum; 2G3T; -.
DR   PDBsum; 2JEV; -.
DR   AlphaFoldDB; P21673; -.
DR   SMR; P21673; -.
DR   BioGRID; 112210; 103.
DR   DIP; DIP-36801N; -.
DR   IntAct; P21673; 93.
DR   MINT; P21673; -.
DR   STRING; 9606.ENSP00000368572; -.
DR   BindingDB; P21673; -.
DR   ChEMBL; CHEMBL4286; -.
DR   DrugBank; DB04633; N-ethyl-N-[3-(propylamino)propyl]propane-1,3-diamine.
DR   DrugBank; DB00127; Spermine.
DR   DrugBank; DB06824; Triethylenetetramine.
DR   DrugCentral; P21673; -.
DR   iPTMnet; P21673; -.
DR   PhosphoSitePlus; P21673; -.
DR   BioMuta; SAT1; -.
DR   DMDM; 114322; -.
DR   EPD; P21673; -.
DR   MassIVE; P21673; -.
DR   PaxDb; 9606-ENSP00000368572; -.
DR   PeptideAtlas; P21673; -.
DR   ProteomicsDB; 53885; -.
DR   Antibodypedia; 24525; 288 antibodies from 22 providers.
DR   DNASU; 6303; -.
DR   Ensembl; ENST00000379270.5; ENSP00000368572.4; ENSG00000130066.17.
DR   GeneID; 6303; -.
DR   KEGG; hsa:6303; -.
DR   MANE-Select; ENST00000379270.5; ENSP00000368572.4; NM_002970.4; NP_002961.1.
DR   UCSC; uc004dau.5; human.
DR   AGR; HGNC:10540; -.
DR   CTD; 6303; -.
DR   DisGeNET; 6303; -.
DR   GeneCards; SAT1; -.
DR   HGNC; HGNC:10540; SAT1.
DR   HPA; ENSG00000130066; Low tissue specificity.
DR   MalaCards; SAT1; -.
DR   MIM; 313020; gene.
DR   neXtProt; NX_P21673; -.
DR   OpenTargets; ENSG00000130066; -.
DR   Orphanet; 2340; Keratosis follicularis spinulosa decalvans.
DR   Orphanet; 93552; Pediatric systemic lupus erythematosus.
DR   PharmGKB; PA162402389; -.
DR   VEuPathDB; HostDB:ENSG00000130066; -.
DR   eggNOG; KOG3216; Eukaryota.
DR   GeneTree; ENSGT00950000183121; -.
DR   HOGENOM; CLU_013985_41_1_1; -.
DR   InParanoid; P21673; -.
DR   OMA; DWNEPSI; -.
DR   OrthoDB; 722999at2759; -.
DR   PhylomeDB; P21673; -.
DR   TreeFam; TF319736; -.
DR   BioCyc; MetaCyc:HS05339-MONOMER; -.
DR   BRENDA; 2.3.1.57; 2681.
DR   PathwayCommons; P21673; -.
DR   Reactome; R-HSA-351200; Interconversion of polyamines.
DR   SignaLink; P21673; -.
DR   SIGNOR; P21673; -.
DR   UniPathway; UPA00188; UER00363.
DR   BioGRID-ORCS; 6303; 21 hits in 788 CRISPR screens.
DR   ChiTaRS; SAT1; human.
DR   EvolutionaryTrace; P21673; -.
DR   GeneWiki; SAT1_(gene); -.
DR   GenomeRNAi; 6303; -.
DR   Pharos; P21673; Tbio.
DR   PRO; PR:P21673; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P21673; Protein.
DR   Bgee; ENSG00000130066; Expressed in nasal cavity epithelium and 205 other cell types or tissues.
DR   ExpressionAtlas; P21673; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0001525; P:angiogenesis; IEP:UniProtKB.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032918; P:spermidine 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:SF36; DIAMINE ACETYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR10545; DIAMINE N-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
DR   Genevisible; P21673; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW   Reference proteome; Transferase.
FT   CHAIN           1..171
FT                   /note="Diamine acetyltransferase 1"
FT                   /id="PRO_0000074591"
FT   DOMAIN          4..171
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:0000305|PubMed:17516632"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:17516632"
FT   BINDING         94..96
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000305|PubMed:17516632"
FT   BINDING         102..107
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000305|PubMed:17516632"
FT   BINDING         126..128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:17516632"
FT   BINDING         133..136
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000305|PubMed:17516632"
FT   BINDING         140..143
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000305|PubMed:17516632"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:17516632"
FT   MUTAGEN         140
FT                   /note="Y->F: Reduces activity by 95%."
FT                   /evidence="ECO:0000269|PubMed:16455797"
FT   CONFLICT        26
FT                   /note="K -> E (in Ref. 3; CAA78509 and 4; AAA98854)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="H -> G (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="W -> P (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..8
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   HELIX           14..25
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:2G3T"
FT   HELIX           31..33
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   HELIX           38..45
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   STRAND          53..58
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   STRAND          71..82
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   STRAND          86..96
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   HELIX           105..120
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   STRAND          123..130
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   HELIX           134..141
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   HELIX           148..152
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   STRAND          154..160
FT                   /evidence="ECO:0007829|PDB:2B5G"
FT   HELIX           161..168
FT                   /evidence="ECO:0007829|PDB:2B5G"
SQ   SEQUENCE   171 AA;  20024 MW;  6A0578B88CD72F09 CRC64;
     MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP FYHCLVAEVP
     KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMRC
     RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMATE E
//