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Protein

Diamine acetyltransferase 2

Gene

SAT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine > spermidine = spermine >> N1acetylspermine = putrescine.

Catalytic activityi

Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921Substrate; via carbonyl oxygenBy similarity
Binding sitei140 – 1401Acetyl-CoA1 Publication
Binding sitei152 – 1521SubstrateBy similarity

GO - Molecular functioni

  1. diamine N-acetyltransferase activity Source: UniProtKB

GO - Biological processi

  1. nor-spermidine metabolic process Source: UniProtKB
  2. putrescine acetylation Source: UniProtKB
  3. putrescine catabolic process Source: UniProtKB-UniPathway
  4. spermidine acetylation Source: UniProtKB
  5. spermine acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.57. 2681.
UniPathwayiUPA00188; UER00363.

Names & Taxonomyi

Protein namesi
Recommended name:
Diamine acetyltransferase 2 (EC:2.3.1.57)
Alternative name(s):
Polyamine N-acetyltransferase 2
Spermidine/spermine N(1)-acetyltransferase 2
Thialysine N-epsilon-acetyltransferase
Gene namesi
Name:SAT2
Synonyms:SSAT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:23160. SAT2.

Subcellular locationi

Cytoplasm
Note: Intracellular organelles.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134979941.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Diamine acetyltransferase 2PRO_0000074598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ96F10.
PaxDbiQ96F10.
PRIDEiQ96F10.

PTM databases

PhosphoSiteiQ96F10.

Expressioni

Tissue specificityi

Widely expressed.

Inductioni

Not inducible by polyamine analogs.

Gene expression databases

BgeeiQ96F10.
CleanExiHS_SAT2.
ExpressionAtlasiQ96F10. baseline and differential.
GenevestigatoriQ96F10.

Organism-specific databases

HPAiHPA022136.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi125190. 6 interactions.
IntActiQ96F10. 1 interaction.
MINTiMINT-1476751.
STRINGi9606.ENSP00000269298.

Structurei

Secondary structure

1
170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi11 – 133Combined sources
Helixi14 – 2815Combined sources
Helixi38 – 469Combined sources
Beta strandi47 – 493Combined sources
Beta strandi53 – 597Combined sources
Beta strandi70 – 8213Combined sources
Turni83 – 853Combined sources
Beta strandi86 – 9611Combined sources
Helixi98 – 1003Combined sources
Beta strandi102 – 1043Combined sources
Helixi105 – 11915Combined sources
Beta strandi124 – 1307Combined sources
Helixi134 – 1429Combined sources
Helixi148 – 1525Combined sources
Beta strandi154 – 1607Combined sources
Helixi162 – 1676Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BEIX-ray1.84A/B2-170[»]
2Q4VX-ray1.84A/B2-170[»]
ProteinModelPortaliQ96F10.
SMRiQ96F10. Positions 2-170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96F10.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 168165N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 282Substrate bindingBy similarity
Regioni94 – 963Acetyl-CoA binding
Regioni102 – 1076Acetyl-CoA binding
Regioni133 – 1353Acetyl-CoA binding

Sequence similaritiesi

Belongs to the acetyltransferase family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0454.
GeneTreeiENSGT00440000039972.
HOGENOMiHOG000078521.
HOVERGENiHBG063175.
InParanoidiQ96F10.
KOiK00657.
OMAiSIKFYEQ.
OrthoDBiEOG7M98HM.
PhylomeDBiQ96F10.
TreeFamiTF319736.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96F10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVRIREAK EGDCGDILRL IRELAEFEKL SDQVKISEEA LRADGFGDNP
60 70 80 90 100
FYHCLVAEIL PAPGKLLGPC VVGYGIYYFI YSTWKGRTIY LEDIYVMPEY
110 120 130 140 150
RGQGIGSKII KKVAEVALDK GCSQFRLAVL DWNQRAMDLY KALGAQDLTE
160 170
AEGWHFFCFQ GEATRKLAGK
Length:170
Mass (Da):19,155
Last modified:December 1, 2001 - v1
Checksum:i68D46F0E28186C68
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti126 – 1261R → C.
Corresponds to variant rs13894 [ dbSNP | Ensembl ].
VAR_020465

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF348524 mRNA. Translation: AAL83905.1.
BC011751 mRNA. Translation: AAH11751.1.
CCDSiCCDS11116.1.
RefSeqiNP_597998.1. NM_133491.3.
UniGeneiHs.10846.

Genome annotation databases

EnsembliENST00000269298; ENSP00000269298; ENSG00000141504.
GeneIDi112483.
KEGGihsa:112483.
UCSCiuc002gic.2. human.

Polymorphism databases

DMDMi51339204.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF348524 mRNA. Translation: AAL83905.1.
BC011751 mRNA. Translation: AAH11751.1.
CCDSiCCDS11116.1.
RefSeqiNP_597998.1. NM_133491.3.
UniGeneiHs.10846.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BEIX-ray1.84A/B2-170[»]
2Q4VX-ray1.84A/B2-170[»]
ProteinModelPortaliQ96F10.
SMRiQ96F10. Positions 2-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125190. 6 interactions.
IntActiQ96F10. 1 interaction.
MINTiMINT-1476751.
STRINGi9606.ENSP00000269298.

Chemistry

DrugBankiDB00127. Spermine.

PTM databases

PhosphoSiteiQ96F10.

Polymorphism databases

DMDMi51339204.

Proteomic databases

MaxQBiQ96F10.
PaxDbiQ96F10.
PRIDEiQ96F10.

Protocols and materials databases

DNASUi112483.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269298; ENSP00000269298; ENSG00000141504.
GeneIDi112483.
KEGGihsa:112483.
UCSCiuc002gic.2. human.

Organism-specific databases

CTDi112483.
GeneCardsiGC17M007529.
HGNCiHGNC:23160. SAT2.
HPAiHPA022136.
MIMi611463. gene.
neXtProtiNX_Q96F10.
PharmGKBiPA134979941.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0454.
GeneTreeiENSGT00440000039972.
HOGENOMiHOG000078521.
HOVERGENiHBG063175.
InParanoidiQ96F10.
KOiK00657.
OMAiSIKFYEQ.
OrthoDBiEOG7M98HM.
PhylomeDBiQ96F10.
TreeFamiTF319736.

Enzyme and pathway databases

UniPathwayiUPA00188; UER00363.
BRENDAi2.3.1.57. 2681.

Miscellaneous databases

EvolutionaryTraceiQ96F10.
GeneWikiiSAT2.
GenomeRNAii112483.
NextBioi78600.
PROiQ96F10.
SOURCEiSearch...

Gene expression databases

BgeeiQ96F10.
CleanExiHS_SAT2.
ExpressionAtlasiQ96F10. baseline and differential.
GenevestigatoriQ96F10.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Coleman C.C.S., Pegg A.E., Chau V.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. "Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase."
    Chen Y., Vujcic S., Liang P., Diegelman P., Kramer D.L., Porter C.W.
    Biochem. J. 373:661-667(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Lung carcinoma.
  4. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Crystal structure of Homo sapiens thialysine Nepsilon-acetyltransferase (HsSSAT2) in complex with acetyl coenzyme A."
    Han B.W., Bingman C.A., Wesenberg G.E., Phillips G.N. Jr.
    Proteins 64:288-293(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 2-170 IN COMPLEX WITH ACETYL-COA, SUBUNIT.

Entry informationi

Entry nameiSAT2_HUMAN
AccessioniPrimary (citable) accession number: Q96F10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 1, 2001
Last modified: March 4, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Under physiological conditions, SSAT2 is expressed at lower level that SSAT1 (SSAT). Many tissues express only SSAT1, several tissues express both SSAT1 and SSAT2, and bone, cervix, ovary and pineal gland expressed only SSAT2.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.