Q96F10 (SAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SAT2
Synonyms:	SSAT2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	170 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	putrescine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	diamine N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 170

170

Diamine acetyltransferase 2

PRO_0000074598

Regions

Domain

4 – 168

165

N-acetyltransferase

Region

27 – 28

2

Substrate binding By similarity

Region

94 – 96

3

Acetyl-CoA binding

Region

102 – 107

6

Acetyl-CoA binding

Region

133 – 135

3

Acetyl-CoA binding

Sites

Binding site

92

1

Substrate; via carbonyl oxygen By similarity

Binding site

140

1

Acetyl-CoA

Binding site

152

1

Substrate By similarity

Amino acid modifications

Modified residue

29

1

N6-acetyllysine Ref.4

Natural variations

Natural variant

126

1

R → C.
Corresponds to variant rs13894 [ dbSNP | Ensembl ].

VAR_020465

Secondary structure

1

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170

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

11 – 13

3

Helix

14 – 28

15

Helix

38 – 46

9

Beta strand

47 – 49

3

Beta strand

53 – 59

7

Beta strand

70 – 82

13

Turn

83 – 85

3

Beta strand

86 – 96

11

Helix

98 – 100

3

Beta strand

102 – 104

3

Helix

105 – 119

15

Beta strand

124 – 130

7

Helix

134 – 142

9

Helix

148 – 152

5

Beta strand

154 – 160

7

Helix

162 – 167

6

Sequences

	Sequence		Length	Mass (Da)
	Q96F10 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 68D46F0E28186C68	FASTA	170	19,155
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY.
[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.

IPI

IPI00744810.

RefSeq

NP_597998.1. NM_133491.3.

UniGene

Hs.10846.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BEI	X-ray	1.84	A/B	2-170	[»]
2Q4V	X-ray	1.84	A/B	2-170	[»]

ProteinModelPortal

Q96F10.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96F10. 1 interaction.

MINT

MINT-1476751.

STRING

9606.ENSP00000269298.

PTM databases

PhosphoSite

Q96F10.

Polymorphism databases

DMDM

51339204.

Proteomic databases

PaxDb

Q96F10.

PRIDE

Q96F10.

Protocols and materials databases

DNASU

112483.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000269298; ENSP00000269298; ENSG00000141504.

GeneID

112483.

KEGG

hsa:112483.

UCSC

uc002gic.2. human.

Organism-specific databases

CTD

112483.

GeneCards

GC17M007529.

HGNC

HGNC:23160. SAT2.

HPA

HPA022136.

MIM

611463. gene.

neXtProt

NX_Q96F10.

PharmGKB

PA134979941.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0454.

HOGENOM

HOG000078521.

HOVERGEN

HBG063175.

KO

K00657.

PhylomeDB

Q96F10.

Enzyme and pathway databases

BRENDA

2.3.1.57. 2681.

UniPathway

UPA00188; UER00363.

Gene expression databases

ArrayExpress

Q96F10.

Bgee

Q96F10.

CleanEx

HS_SAT2.

Genevestigator

Q96F10.

GermOnline

ENSG00000141504. Homo sapiens.

Family and domain databases

Gene3D

3.40.630.30. 1 hit.

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]

Pfam

PF00583. Acetyltransf_1. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.

PROSITE

PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00127. Spermine.

EvolutionaryTrace

Q96F10.

GenomeRNAi

112483.

NextBio

78600.

SOURCE

Search...

Entry information

Entry name

SAT2_HUMAN

Accession

Primary (citable) accession number: Q96F10

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.