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Q96F10 (SAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SAT2
Synonyms:SSAT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length170 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Amine and polyamine degradation; putrescine degradation; N-acetylputrescine from putrescine: step 1/1.

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasm. Note: Intracellular organelles.

Tissue specificity

Widely expressed.

Induction

Not inducible by polyamine analogs.

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.

Sequence similarities

Belongs to the acetyltransferase family.

Contains 1 N-acetyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 170170Diamine acetyltransferase 2
PRO_0000074598

Regions

Domain4 – 168165N-acetyltransferase
Region27 – 282Substrate binding By similarity
Region94 – 963Acetyl-CoA binding
Region102 – 1076Acetyl-CoA binding
Region133 – 1353Acetyl-CoA binding

Sites

Binding site921Substrate; via carbonyl oxygen By similarity
Binding site1401Acetyl-CoA
Binding site1521Substrate By similarity

Amino acid modifications

Modified residue291N6-acetyllysine Ref.4

Natural variations

Natural variant1261R → C.
Corresponds to variant rs13894 [ dbSNP | Ensembl ].
VAR_020465

Secondary structure

.............................. 170
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96F10 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 68D46F0E28186C68

FASTA17019,155
        10         20         30         40         50         60 
MASVRIREAK EGDCGDILRL IRELAEFEKL SDQVKISEEA LRADGFGDNP FYHCLVAEIL 

        70         80         90        100        110        120 
PAPGKLLGPC VVGYGIYYFI YSTWKGRTIY LEDIYVMPEY RGQGIGSKII KKVAEVALDK 

       130        140        150        160        170 
GCSQFRLAVL DWNQRAMDLY KALGAQDLTE AEGWHFFCFQ GEATRKLAGK 

« Hide

References

« Hide 'large scale' references
[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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF348524 mRNA. Translation: AAL83905.1.
BC011751 mRNA. Translation: AAH11751.1.
RefSeqNP_597998.1. NM_133491.3.
UniGeneHs.10846.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BEIX-ray1.84A/B2-170[»]
2Q4VX-ray1.84A/B2-170[»]
ProteinModelPortalQ96F10.
SMRQ96F10. Positions 2-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125190. 5 interactions.
IntActQ96F10. 1 interaction.
MINTMINT-1476751.
STRING9606.ENSP00000269298.

Chemistry

DrugBankDB00127. Spermine.

PTM databases

PhosphoSiteQ96F10.

Polymorphism databases

DMDM51339204.

Proteomic databases

PaxDbQ96F10.
PRIDEQ96F10.

Protocols and materials databases

DNASU112483.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269298; ENSP00000269298; ENSG00000141504.
GeneID112483.
KEGGhsa:112483.
UCSCuc002gic.2. human.

Organism-specific databases

CTD112483.
GeneCardsGC17M007529.
HGNCHGNC:23160. SAT2.
HPAHPA022136.
MIM611463. gene.
neXtProtNX_Q96F10.
PharmGKBPA134979941.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0454.
HOGENOMHOG000078521.
HOVERGENHBG063175.
KOK00657.
OMAKERNCGR.
OrthoDBEOG7M98HM.
PhylomeDBQ96F10.
TreeFamTF319736.

Enzyme and pathway databases

BRENDA2.3.1.57. 2681.
UniPathwayUPA00188; UER00363.

Gene expression databases

ArrayExpressQ96F10.
BgeeQ96F10.
CleanExHS_SAT2.
GenevestigatorQ96F10.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ96F10.
GeneWikiSAT2.
GenomeRNAi112483.
NextBio78600.
PROQ96F10.
SOURCESearch...

Entry information

Entry nameSAT2_HUMAN
AccessionPrimary (citable) accession number: Q96F10
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 1, 2001
Last modified: March 19, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM