SAT1_HUMAN
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 03-AUG-2022, entry version 206.
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; 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; Q6ZNM6: TEX43; NbExp=3; IntAct=EBI-711613, EBI-18115728;
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 DrugCentral; P21673; -.
DR iPTMnet; P21673; -.
DR PhosphoSitePlus; P21673; -.
DR BioMuta; SAT1; -.
DR DMDM; 114322; -.
DR EPD; P21673; -.
DR MassIVE; P21673; -.
DR PaxDb; P21673; -.
DR PeptideAtlas; P21673; -.
DR PRIDE; P21673; -.
DR ProteomicsDB; 53885; -.
DR Antibodypedia; 24525; 259 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 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 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; AVERQCG; -.
DR OrthoDB; 1228251at2759; -.
DR PhylomeDB; P21673; -.
DR TreeFam; TF319736; -.
DR BioCyc; MetaCyc:HS05339-MON; -.
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; 15 hits in 712 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 203 other tissues.
DR ExpressionAtlas; P21673; baseline and differential.
DR Genevisible; P21673; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032957; SAT1.
DR PANTHER; PTHR10545:SF36; PTHR10545:SF36; 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; 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
