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Diamine acetyltransferase 1 (EC 2.3.1.57) (Polyamine N-acetyltransferase 1) (Putrescine acetyltransferase) (Spermidine/spermine N(1)-acetyltransferase 1) (SSAT) (SSAT-1)

 SAT1_HUMAN              Reviewed;         171 AA.
P21673; Q6ICU9;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
18-JUL-2018, entry version 181.
RecName: Full=Diamine acetyltransferase 1;
EC=2.3.1.57 {ECO:0000269|PubMed:16455797, ECO:0000269|PubMed:17516632};
AltName: Full=Polyamine N-acetyltransferase 1;
AltName: Full=Putrescine acetyltransferase;
AltName: Full=Spermidine/spermine N(1)-acetyltransferase 1;
Short=SSAT;
Short=SSAT-1;
Name=SAT1; Synonyms=SAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1985966;
Casero R.A. Jr., Celano P., Ervin S.J., Applegren N.B., Wiest L.,
Pegg A.E.;
"Isolation and characterization of a cDNA clone that codes for human
spermidine/spermine N1-acetyltransferase.";
J. Biol. Chem. 266:810-814(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=1652956; DOI=10.1016/0006-291X(91)91385-P;
Xiao L., Celano P., Mank A.R., Pegg A.E., Casero R.A. Jr.;
"Characterization of a full-length cDNA which codes for the human
spermidine/spermine N1-acetyltransferase.";
Biochem. Biophys. Res. Commun. 179:407-415(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1417826; DOI=10.1016/0006-291X(92)90471-V;
Xiao L., Celano P., Mank A.R., Griffin C., Wang J.E., Casero R.A. Jr.;
"Structure of the human spermidine/spermine N1-acetyltransferase gene
(exon/intron gene organization and localization to Xp22.1).";
Biochem. Biophys. Res. Commun. 187:1493-1502(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8573111; DOI=10.1042/bj3130691;
Xiao L., Casero R.A. Jr.;
"Differential transcription of the human spermidine/spermine N1-
acetyltransferase (SSAT) gene in human lung carcinoma cells.";
Biochem. J. 313:691-696(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PARTIAL PROTEIN SEQUENCE.
PubMed=2241897; DOI=10.1042/bj2700615;
Casero R.A. Jr., Celano P., Ervin S.J., Wiest L., Pegg A.E.;
"High specific induction of spermidine/spermine N1-acetyltransferase
in a human large cell lung carcinoma.";
Biochem. J. 270:615-620(1990).
[11]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH
ACETYL-COENZYME A; THE SUBSTRATES SPERMINE AND
N1,N11-BIS-(ETHYL)-NORSPERMINE, MUTAGENESIS OF TYR-140, CATALYTIC
ACTIVITY, AND SUBUNIT.
PubMed=16455797; DOI=10.1073/pnas.0511008103;
Bewley M.C., Graziano V., Jiang J., Matz E., Studier F.W., Pegg A.E.,
Coleman C.S., Flanagan J.M.;
"Structures of wild-type and mutant human spermidine/spermine N1-
acetyltransferase, a potential therapeutic drug target.";
Proc. Natl. Acad. Sci. U.S.A. 103:2063-2068(2006).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH THE SUBSTRATE
AND ACETYL-COA ANALOG N1-SPERMINE-ACETYL-COENZYME A,
BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=17516632; DOI=10.1021/bi700256z;
Hegde S.S., Chandler J., Vetting M.W., Yu M., Blanchard J.S.;
"Mechanistic and structural analysis of human spermidine/spermine N1-
acetyltransferase.";
Biochemistry 46:7187-7195(2007).
[13]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUBUNIT.
PubMed=16544326; DOI=10.1002/prot.20965;
Zhu Y.-Q., Zhu D.-Y., Yin L., Zhang Y., Vonrhein C., Wang D.-C.;
"Crystal structure of human spermidine/spermine N1-acetyltransferase
(hSSAT): the first structure of a new sequence family of transferase
homologous superfamily.";
Proteins 63:1127-1131(2006).
[14]
INVOLVEMENT IN KFSDX.
PubMed=9341865; DOI=10.1007/s004390050546;
Oosterwijk J.C., Richard G., van der Wielen M.J.R., van de Vosse E.,
Harth W., Sandkuijl L.A., Bakker E., van Ommen G.-J.B.;
"Molecular genetic analysis of two families with keratosis
follicularis spinulosa decalvans: refinement of gene localization and
evidence for genetic heterogeneity.";
Hum. Genet. 100:520-524(1997).
[15]
INVOLVEMENT IN KFSDX.
PubMed=12215835; DOI=10.1007/s00439-002-0791-6;
Gimelli G., Giglio S., Zuffardi O., Alhonen L., Suppola S., Cusano R.,
Lo Nigro C., Gatti R., Ravazzolo R., Seri M.;
"Gene dosage of the spermidine/spermine N(1)-acetyltransferase (SSAT)
gene with putrescine accumulation in a patient with a Xp21.1p22.12
duplication and keratosis follicularis spinulosa decalvans (KFSD).";
Hum. Genet. 111:235-241(2002).
-!- FUNCTION: Enzyme which catalyzes the acetylation of polyamines.
Substrate specificity: norspermidine = spermidine >> spermine >
N(1)-acetylspermine > putrescine. This highly regulated enzyme
allows a fine attenuation of the intracellular concentration of
polyamines. Also involved in the regulation of polyamine transport
out of cells. Acts on 1,3-diaminopropane, 1,5-diaminopentane,
putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine),
spermine, N(1)-acetylspermidine and N(8)-acetylspermidine.
{ECO:0000269|PubMed:16455797, ECO:0000269|PubMed:17516632}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an alkane-alpha,omega-diamine =
CoA + an N-acetyldiamine. {ECO:0000269|PubMed:16455797,
ECO:0000269|PubMed:17516632}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.8 uM for acetyl-coenzyme A {ECO:0000269|PubMed:17516632};
KM=5.7 uM for spermine {ECO:0000269|PubMed:17516632};
KM=22 uM for spermidine {ECO:0000269|PubMed:17516632};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:17516632};
-!- PATHWAY: Amine and polyamine degradation; putrescine degradation;
N-acetylputrescine from putrescine: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16455797,
ECO:0000269|PubMed:16544326, ECO:0000269|PubMed:17516632}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-711613, EBI-711613;
Q9UFG5:C19orf25; NbExp=3; IntAct=EBI-711613, EBI-741214;
P55210:CASP7; NbExp=5; IntAct=EBI-711613, EBI-523958;
Q8NFR7:CCDC148; NbExp=5; IntAct=EBI-711613, EBI-2349862;
Q8TD31-3:CCHCR1; NbExp=7; IntAct=EBI-711613, EBI-10175300;
O00148:DDX39A; NbExp=3; IntAct=EBI-711613, EBI-348253;
Q9NQL9:DMRT3; NbExp=5; IntAct=EBI-711613, EBI-9679045;
O15371:EIF3D; NbExp=3; IntAct=EBI-711613, EBI-353818;
Q8NDB6:FAM156A; NbExp=3; IntAct=EBI-711613, EBI-749727;
Q5VUD6:FAM69B; NbExp=5; IntAct=EBI-711613, EBI-721274;
P17482:HOXB9; NbExp=6; IntAct=EBI-711613, EBI-745290;
P22459:KCNA4; NbExp=3; IntAct=EBI-711613, EBI-631235;
Q8TBB1:LNX1; NbExp=8; IntAct=EBI-711613, EBI-739832;
Q13330:MTA1; NbExp=3; IntAct=EBI-711613, EBI-714236;
Q9GZT8:NIF3L1; NbExp=4; IntAct=EBI-711613, EBI-740897;
Q96I25:RBM17; NbExp=9; IntAct=EBI-711613, EBI-740272;
Q04864:REL; NbExp=3; IntAct=EBI-711613, EBI-307352;
Q9BUL9:RPP25; NbExp=4; IntAct=EBI-711613, EBI-366570;
Q96F10:SAT2; NbExp=3; IntAct=EBI-711613, EBI-748746;
O43623:SNAI2; NbExp=3; IntAct=EBI-711613, EBI-9876238;
Q9BSH4:TACO1; NbExp=3; IntAct=EBI-711613, EBI-747797;
Q9BQ70:TCF25; NbExp=9; IntAct=EBI-711613, EBI-745182;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DISEASE: Keratosis follicularis spinulosa decalvans X-linked
(KFSDX) [MIM:308800]: A rare disorder affecting the skin and the
eye. Affected men show thickening of the skin of the neck, ears,
and extremities, especially the palms and soles, loss of eyebrows,
eyelashes and beard, thickening of the eyelids with blepharitis
and ectropion, and corneal degeneration.
{ECO:0000269|PubMed:12215835, ECO:0000269|PubMed:9341865}.
Note=The disease may be caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the acetyltransferase family.
{ECO:0000305}.
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EMBL; M77693; AAA60573.1; -; mRNA.
EMBL; M55580; AAA63260.1; -; mRNA.
EMBL; Z14136; CAA78509.1; -; Genomic_DNA.
EMBL; U40369; AAA98854.1; -; Genomic_DNA.
EMBL; BT006825; AAP35471.1; -; mRNA.
EMBL; CR450294; CAG29290.1; -; mRNA.
EMBL; AK312162; BAG35096.1; -; mRNA.
EMBL; CH471074; EAW99000.1; -; Genomic_DNA.
EMBL; BC002503; AAH02503.1; -; mRNA.
EMBL; BC008424; AAH08424.1; -; mRNA.
CCDS; CCDS14207.1; -.
PIR; JH0783; JH0783.
RefSeq; NP_002961.1; NM_002970.3.
UniGene; Hs.28491; -.
PDB; 2B3U; X-ray; 1.85 A; A/B=1-171.
PDB; 2B3V; X-ray; 1.95 A; A=1-171.
PDB; 2B4B; X-ray; 2.00 A; A/B=1-171.
PDB; 2B4D; X-ray; 2.00 A; A/B=1-171.
PDB; 2B58; X-ray; 1.95 A; A=1-171.
PDB; 2B5G; X-ray; 1.70 A; A/B=1-171.
PDB; 2F5I; X-ray; 2.30 A; A/B=1-171.
PDB; 2FXF; X-ray; 2.00 A; A/B=2-171.
PDB; 2G3T; X-ray; 1.80 A; A/B=1-171.
PDB; 2JEV; X-ray; 2.30 A; A/B=1-171.
PDBsum; 2B3U; -.
PDBsum; 2B3V; -.
PDBsum; 2B4B; -.
PDBsum; 2B4D; -.
PDBsum; 2B58; -.
PDBsum; 2B5G; -.
PDBsum; 2F5I; -.
PDBsum; 2FXF; -.
PDBsum; 2G3T; -.
PDBsum; 2JEV; -.
ProteinModelPortal; P21673; -.
SMR; P21673; -.
BioGrid; 112210; 73.
DIP; DIP-36801N; -.
IntAct; P21673; 88.
MINT; P21673; -.
STRING; 9606.ENSP00000368572; -.
BindingDB; P21673; -.
ChEMBL; CHEMBL4286; -.
DrugBank; DB00127; Spermine.
iPTMnet; P21673; -.
PhosphoSitePlus; P21673; -.
BioMuta; SAT1; -.
DMDM; 114322; -.
EPD; P21673; -.
PaxDb; P21673; -.
PeptideAtlas; P21673; -.
PRIDE; P21673; -.
ProteomicsDB; 53885; -.
DNASU; 6303; -.
Ensembl; ENST00000379270; ENSP00000368572; ENSG00000130066.
GeneID; 6303; -.
KEGG; hsa:6303; -.
UCSC; uc004dau.5; human.
CTD; 6303; -.
DisGeNET; 6303; -.
EuPathDB; HostDB:ENSG00000130066.16; -.
GeneCards; SAT1; -.
H-InvDB; HIX0176797; -.
HGNC; HGNC:10540; SAT1.
HPA; CAB047343; -.
HPA; CAB069914; -.
HPA; HPA055312; -.
MalaCards; SAT1; -.
MIM; 308800; phenotype.
MIM; 313020; gene.
neXtProt; NX_P21673; -.
OpenTargets; ENSG00000130066; -.
Orphanet; 2340; Keratosis follicularis spinulosa decalvans.
PharmGKB; PA162402389; -.
eggNOG; KOG3216; Eukaryota.
eggNOG; COG0454; LUCA.
GeneTree; ENSGT00440000039972; -.
HOGENOM; HOG000078521; -.
HOVERGEN; HBG063175; -.
InParanoid; P21673; -.
KO; K00657; -.
OMA; VKCRCSS; -.
OrthoDB; EOG091G0UNU; -.
PhylomeDB; P21673; -.
TreeFam; TF319736; -.
BioCyc; MetaCyc:HS05339-MONOMER; -.
BRENDA; 2.3.1.57; 2681.
Reactome; R-HSA-351200; Interconversion of polyamines.
SIGNOR; P21673; -.
UniPathway; UPA00188; UER00363.
ChiTaRS; SAT1; human.
EvolutionaryTrace; P21673; -.
GeneWiki; SAT1_(gene); -.
GenomeRNAi; 6303; -.
PRO; PR:P21673; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000130066; -.
CleanEx; HS_SAT1; -.
ExpressionAtlas; P21673; baseline and differential.
Genevisible; P21673; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0004145; F:diamine N-acetyltransferase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019809; F:spermidine binding; IBA:GO_Central.
GO; GO:0001525; P:angiogenesis; IEP:UniProtKB.
GO; GO:0006596; P:polyamine biosynthetic process; TAS:Reactome.
GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0032918; P:spermidine acetylation; IBA:GO_Central.
GO; GO:0046208; P:spermine catabolic process; IBA:GO_Central.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000182; GNAT_dom.
InterPro; IPR032957; SAT1.
PANTHER; PTHR10545:SF36; PTHR10545:SF36; 1.
Pfam; PF00583; Acetyltransf_1; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Complete proteome; Cytoplasm;
Direct protein sequencing; Reference proteome; Transferase.
CHAIN 1 171 Diamine acetyltransferase 1.
/FTId=PRO_0000074591.
DOMAIN 4 171 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
REGION 27 28 Substrate binding.
{ECO:0000305|PubMed:17516632}.
REGION 94 96 Acetyl-CoA binding.
{ECO:0000305|PubMed:17516632}.
REGION 102 107 Acetyl-CoA binding.
{ECO:0000305|PubMed:17516632}.
REGION 126 128 Substrate binding.
{ECO:0000305|PubMed:17516632}.
REGION 133 136 Acetyl-CoA binding.
{ECO:0000305|PubMed:17516632}.
REGION 140 143 Acetyl-CoA binding.
{ECO:0000305|PubMed:17516632}.
BINDING 92 92 Substrate; via carbonyl oxygen.
{ECO:0000305|PubMed:17516632}.
BINDING 152 152 Substrate. {ECO:0000305|PubMed:17516632}.
MUTAGEN 140 140 Y->F: Reduces activity by 95%.
{ECO:0000269|PubMed:16455797}.
CONFLICT 26 26 K -> E (in Ref. 3; CAA78509 and 4;
AAA98854). {ECO:0000305}.
CONFLICT 69 69 H -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 84 84 W -> P (in Ref. 10; AA sequence).
{ECO:0000305}.
STRAND 5 8 {ECO:0000244|PDB:2B5G}.
HELIX 11 13 {ECO:0000244|PDB:2B5G}.
HELIX 14 25 {ECO:0000244|PDB:2B5G}.
STRAND 28 30 {ECO:0000244|PDB:2G3T}.
HELIX 31 33 {ECO:0000244|PDB:2B5G}.
HELIX 38 45 {ECO:0000244|PDB:2B5G}.
STRAND 46 49 {ECO:0000244|PDB:2B5G}.
STRAND 53 58 {ECO:0000244|PDB:2B5G}.
HELIX 61 63 {ECO:0000244|PDB:2B5G}.
STRAND 71 82 {ECO:0000244|PDB:2B5G}.
TURN 83 85 {ECO:0000244|PDB:2B5G}.
STRAND 86 96 {ECO:0000244|PDB:2B5G}.
HELIX 98 100 {ECO:0000244|PDB:2B5G}.
STRAND 102 104 {ECO:0000244|PDB:2B5G}.
HELIX 105 120 {ECO:0000244|PDB:2B5G}.
STRAND 123 130 {ECO:0000244|PDB:2B5G}.
HELIX 134 141 {ECO:0000244|PDB:2B5G}.
TURN 142 144 {ECO:0000244|PDB:2B5G}.
HELIX 148 152 {ECO:0000244|PDB:2B5G}.
STRAND 154 160 {ECO:0000244|PDB:2B5G}.
HELIX 161 168 {ECO:0000244|PDB:2B5G}.
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


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EIAAB37324 Chicken,Diamine acetyltransferase 1,Gallus gallus,Polyamine N-acetyltransferase 1,Putrescine acetyltransferase,SAT,SAT1,Spermidine_spermine N(1)-acetyltransferase 1,SSAT,SSAT,SSAT-1
EIAAB37329 Diamine acetyltransferase 2,Homo sapiens,Human,Polyamine N-acetyltransferase 2,SAT2,Spermidine_spermine N(1)-acetyltransferase 2,SSAT2,Thialysine N-epsilon-acetyltransferase
EIAAB37327 Diamine acetyltransferase 2,Mouse,Mus musculus,Polyamine N-acetyltransferase 2,Sat2,Spermidine_spermine N(1)-acetyltransferase 2,Ssat2
EIAAB37328 Bos taurus,Bovine,Diamine acetyltransferase 2,Polyamine N-acetyltransferase 2,SAT2,Spermidine_spermine N(1)-acetyltransferase 2,SSAT2
EIAAB37330 Diamine acetyltransferase 2,Pig,Polyamine N-acetyltransferase 2,SAT2,Spermidine_spermine N(1)-acetyltransferase 2,SSAT2,Sus scrofa
EIAAB26223 hNAT5,Homo sapiens,hSAN,Human,MAK3,NAA50,N-acetyltransferase 13,N-acetyltransferase 5,N-acetyltransferase san homolog,N-alpha-acetyltransferase 50,NAT13,NAT5,NatE catalytic subunit
26-320 NAT12 belongs to the acetyltransferase family, MAK3 subfamily. It contains 1 N-acetyltransferase domain. It is a probable N-acetyltransferase. 0.05 mg
30-419 NAT12 belongs to the acetyltransferase family, MAK3 subfamily. It contains 1 N-acetyltransferase domain. It is a probable N-acetyltransferase. 0.05 mg
EIAAB26212 Mak3,Mouse,Mus musculus,Naa30,N-acetyltransferase 12,N-acetyltransferase MAK3 homolog,N-alpha-acetyltransferase 30,Nat12,NatC catalytic subunit
EIAAB26213 C14orf35,Homo sapiens,Human,MAK3,NAA30,N-acetyltransferase 12,N-acetyltransferase MAK3 homolog,N-alpha-acetyltransferase 30,NAT12,NatC catalytic subunit
enz-587 Recombinant Human Spermidine per Spermine N1-Acetyltransferase 2 20
REN-433 Recombinant Human Spermidine Spermine N1-Acetyltransferase 1 5
REN-587 Recombinant Human Spermidine Spermine N1-Acetyltransferase 2 5
enz-433 Recombinant Human Spermidine per Spermine N1-Acetyltransferase 1 1mg
enz-587 Recombinant Human Spermidine per Spermine N1-Acetyltransferase 2 5
enz-433 Recombinant Human Spermidine per Spermine N1-Acetyltransferase 1 5
enz-433 Recombinant Human Spermidine per Spermine N1-Acetyltransferase 1 20
enz-587 Recombinant Human Spermidine per Spermine N1-Acetyltransferase 2 1mg
228-11409-1 Recombinant Human Spermidine _ Spermine N1-Acetyltransferase 1 5
228-11409-2 Recombinant Human Spermidine _ Spermine N1-Acetyltransferase 1 20
228-11409-3 Recombinant Human Spermidine _ Spermine N1-Acetyltransferase 1 1 mg


 

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