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UniProtKB - O75908 (SOAT2_HUMAN)

Entry version 169 (25 May 2022)
Sequence version 1 (01 Nov 1998)
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Protein

Sterol O-acyltransferase 2

Gene

SOAT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol (PubMed:16647063, PubMed:11294643).

Plays a role in lipoprotein assembly and dietary cholesterol absorption (PubMed:11294643).

Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates (PubMed:11294643).

May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa (PubMed:11294643).

2 Publications

Has lower enzymatic activity compared to isoform 1.

1 Publication

Has lower enzymatic activity compared to isoform 1.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei119CholesterolBy similarity1
Binding sitei389Acyl-CoABy similarity1
Binding sitei392Acyl-CoABy similarity1
Binding sitei395Acyl-CoABy similarity1
Binding sitei399Acyl-CoABy similarity1
Binding sitei407Acyl-CoABy similarity1
Binding sitei430Acyl-CoABy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei4341 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.26, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		O75908

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-8964038, LDL clearance

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		O75908

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		O75908

Protein family/group databases

Transport Classification Database

More...TCDBi		2.A.50.4.11, the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001262 [O75908-1]

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sterol O-acyltransferase 2Curated (EC:2.3.1.261 Publication1 Publication)
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase 2
Short name:
ACAT-2
Cholesterol acyltransferase 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SOAT2Imported
Synonyms:ACACT2, ACAT2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:11178, SOAT2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601311, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O75908

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000167780

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 120CytoplasmicCuratedAdd BLAST120
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei121 – 142Helical; Name=1By similarityAdd BLAST22
Topological domaini143 – 162LumenalCuratedAdd BLAST20
Transmembranei163 – 188Helical; Name=2By similarityAdd BLAST26
Topological domaini189 – 196CytoplasmicCurated8
Transmembranei197 – 220Helical; Name=3By similarityAdd BLAST24
Topological domaini221 – 228LumenalCurated8
Transmembranei229 – 252Helical; Name=4By similarityAdd BLAST24
Topological domaini253 – 293CytoplasmicCuratedAdd BLAST41
Transmembranei294 – 326Helical; Name=5By similarityAdd BLAST33
Topological domaini327 – 343LumenalCuratedAdd BLAST17
Transmembranei344 – 369Helical; Name=6By similarityAdd BLAST26
Topological domaini370 – 417CytoplasmicCuratedAdd BLAST48
Transmembranei418 – 442Helical; Name=7By similarityAdd BLAST25
Topological domaini443 – 448LumenalCurated6
Transmembranei449 – 464Helical; Name=8By similarityAdd BLAST16
Topological domaini465 – 470CytoplasmicCurated6
Transmembranei471 – 502Helical; Name=9By similarityAdd BLAST32
Topological domaini503 – 522LumenalCuratedAdd BLAST20

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi49K → R in K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-80, R-100, R-102, R-108, R-242 and R-299. 1 Publication1
Mutagenesisi80K → R in K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-100, R-102, R-108, R-242 and R-299. 1 Publication1
Mutagenesisi100K → R in K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-102, R-108, R-242 and R-299. 1 Publication1
Mutagenesisi102K → R in K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-108, R-242 and R-299. 1 Publication1
Mutagenesisi108K → R in K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-102, R-242 and R-299. 1 Publication1
Mutagenesisi242K → R in K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-102, R-108 and R-299. 1 Publication1
Mutagenesisi254T → A: Does not affect ubiquitination and sterol-regulated stabilization; when associated with R-279. 1 Publication1
Mutagenesisi267 – 270SFSS → AFAA: Does not affect ubiquitination and sterol-regulated stabilization. 1 Publication4
Mutagenesisi277C → A: Abolished ubiquitination and sterol-regulated stabilization. 1 Publication1
Mutagenesisi279T → A: Does not affect ubiquitination and sterol-regulated stabilization; when associated with R-54. 1 Publication1
Mutagenesisi299K → R in K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-102, R-108 and R-242. 1 Publication1
Mutagenesisi360H → A: Abolished cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi399H → A: Abolished cholesterol O-acyltransferase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		8435

Open Targets

More...OpenTargetsi		ENSG00000167780

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA36016

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		O75908, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4465

Drug and drug target database

More...DrugBanki		DB01094, Hesperetin

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		SOAT2

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002076451 – 522Sterol O-acyltransferase 2Add BLAST522

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei277Cysteine sulfenic acid (-SOH); alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki277Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Polyubiquitinated by AMFR/gp78 at Cys-277, leading to its degradation when the lipid levels are low (PubMed:28604676). Association with AMFR/gp78 is mediated via interaction with INSIG1 (PubMed:28604676). High concentration of cholesterol and fatty acid results in Cys-277 oxidation, preventing ubiquitination at the same site, resulting in protein stabilization (PubMed:28604676).1 Publication
Oxidized at Cys-277: high concentration of cholesterol and fatty acid induce reactive oxygen species, which oxidizes Cys-277, preventing ubiquitination at the same site, and resulting in protein stabilization.1 Publication

Keywords - PTMi

Oxidation, Thioester bond, Ubl conjugation

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		O75908

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		O75908

PeptideAtlas

More...PeptideAtlasi		O75908

PRoteomics IDEntifications database

More...PRIDEi		O75908

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		27608
50258 [O75908-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O75908

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		O75908

SwissPalm database of S-palmitoylation events

More...SwissPalmi		O75908

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expression seems confined in hepatocytes and enterocytes.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000167780, Expressed in liver and 87 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O75908, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O75908, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000167780, Tissue enriched (intestine)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

May form homo- or heterodimers (By similarity).

Interacts with INSIG1; the interaction is direct and promotes association with AMFR/gp78 (PubMed:28604676).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		114015, 5 interactors

Protein interaction database and analysis system

More...IntActi		O75908, 3 interactors

Molecular INTeraction database

More...MINTi		O75908

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000301466

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O75908

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O75908, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		O75908

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		O75908

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 36DisorderedSequence analysisAdd BLAST36
Regioni74 – 96DisorderedSequence analysisAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi377 – 383FYXDWWN motifBy similarity7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi13 – 28Basic and acidic residuesSequence analysisAdd BLAST16

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Each protomer consists of 9 transmembrane segments, which enclose a cytosolic tunnel and a transmembrane tunnel that converge at the predicted catalytic site: acyl-CoA enters the active site through the cytosolic tunnel, whereas cholesterol enters from the side through the transmembrane tunnel.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0380, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183081

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_031845_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O75908

Identification of Orthologs from Complete Genome Data

More...OMAi		MHDRHTG

Database of Orthologous Groups

More...OrthoDBi		1275897at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O75908

TreeFam database of animal gene trees

More...TreeFami		TF315226

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004299, MBOAT_fam
IPR014371, Oat_ACAT_DAG_ARE
IPR030687, Sterol_acyltranf_meta

The PANTHER Classification System

More...PANTHERi		PTHR10408, PTHR10408, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03062, MBOAT, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000439, Oat_ACAT_DAG_ARE, 1 hit
PIRSF500230, Sterol_acyltranf_ACAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 4 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: O75908-1) [UniParc]FASTAAdd to basket
Also known as: ACAD2a

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEPGGARLRL QRTEGLGGER ERQPCGDGNT ETHRAPDLVQ WTRHMEAVKA 
        60         70         80         90        100
QLLEQAQGQL RELLDRAMRE AIQSYPSQDK PLPPPPPGSL SRTQEPSLGK 
       110        120        130        140        150
QKVFIIRKSL LDELMEVQHF RTIYHMFIAG LCVFIISTLA IDFIDEGRLL 
       160        170        180        190        200
LEFDLLIFSF GQLPLALVTW VPMFLSTLLA PYQALRLWAR GTWTQATGLG 
       210        220        230        240        250
CALLAAHAVV LCALPVHVAV EHQLPPASRC VLVFEQVRFL MKSYSFLREA 
       260        270        280        290        300
VPGTLRARRG EGIQAPSFSS YLYFLFCPTL IYRETYPRTP YVRWNYVAKN 
       310        320        330        340        350
FAQALGCVLY ACFILGRLCV PVFANMSREP FSTRALVLSI LHATLPGIFM 
       360        370        380        390        400
LLLIFFAFLH CWLNAFAEML RFGDRMFYRD WWNSTSFSNY YRTWNVVVHD 
       410        420        430        440        450
WLYSYVYQDG LRLLGARARG VAMLGVFLVS AVAHEYIFCF VLGFFYPVML 
       460        470        480        490        500
ILFLVIGGML NFMMHDQRTG PAWNVLMWTM LFLGQGIQVS LYCQEWYARR 
       510        520 
HCPLPQATFW GLVTPRSWSC HT
Length:522
Mass (Da):59,896
Last modified:November 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEEAC2DB569FFE729
GO
Isoform 2 (identifier: O75908-2) [UniParc]FASTAAdd to basket
Also known as: ACAD2b

The sequence of this isoform differs from the canonical sequence as follows:
     93-112: Missing.

Show »
Length:502
Mass (Da):57,614
Checksum:i4E8DA0CFFF4E2688
GO
Isoform 3 (identifier: O75908-3) [UniParc]FASTAAdd to basket
Also known as: ACAD2c

The sequence of this isoform differs from the canonical sequence as follows:
     93-148: Missing.
     236-261: Missing.

Show »
Length:440
Mass (Da):50,351
Checksum:iC891C005392C572C
GO
Isoform 4 (identifier: O75908-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     289-310: TPYVRWNYVAKNFAQALGCVLY → PWDVCSMPASSWAASVFLSLPT
     311-522: Missing.

Show »
Length:310
Mass (Da):34,882
Checksum:iA5C0D66A8ECCA6EC
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8VPE9F8VPE9_HUMAN
Sterol O-acyltransferase 2
SOAT2
170Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti22R → P in AAK48829 (PubMed:11401500).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02037314E → G1 PublicationCorresponds to variant dbSNP:rs9658625Ensembl.1
Natural variantiVAR_020374254T → I2 PublicationsCorresponds to variant dbSNP:rs2272296Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_05715893 – 148Missing in isoform 3. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_05715993 – 112Missing in isoform 2. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_057160236 – 261Missing in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_057161289 – 310TPYVR…GCVLY → PWDVCSMPASSWAASVFLSL PT in isoform 4. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_057162311 – 522Missing in isoform 4. 1 PublicationAdd BLAST212

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF059203 mRNA Translation: AAC63998.1
AF099031 mRNA Translation: AAC78335.2
AF331516 AF331515 Genomic DNA Translation: AAK18275.1
AF332858, AF332857 Genomic DNA Translation: AAK48829.1
AC073573 Genomic DNA No translation available.
BC096090 mRNA Translation: AAH96090.1
BC096091 mRNA Translation: AAH96091.1
BC096092 mRNA Translation: AAH96092.1
BC099626 mRNA Translation: AAH99626.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS8847.1 [O75908-1]

NCBI Reference Sequences

More...RefSeqi		NP_003569.1, NM_003578.3 [O75908-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000301466.8; ENSP00000301466.3; ENSG00000167780.12
ENST00000542365.1; ENSP00000442234.1; ENSG00000167780.12 [O75908-4]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		8435

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:8435

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000301466.8; ENSP00000301466.3; NM_003578.4; NP_003569.1

UCSC genome browser

More...UCSCi		uc001sbv.4, human [O75908-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059203 mRNA Translation: AAC63998.1
AF099031 mRNA Translation: AAC78335.2
AF331516 AF331515 Genomic DNA Translation: AAK18275.1
AF332858, AF332857 Genomic DNA Translation: AAK48829.1
AC073573 Genomic DNA No translation available.
BC096090 mRNA Translation: AAH96090.1
BC096091 mRNA Translation: AAH96091.1
BC096092 mRNA Translation: AAH96092.1
BC099626 mRNA Translation: AAH99626.1
CCDSiCCDS8847.1 [O75908-1]
RefSeqiNP_003569.1, NM_003578.3 [O75908-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
7N6Qelectron microscopy3.87A/B/C/D2-522[»]
7N6Relectron microscopy3.93A/B/C/D2-522[»]
AlphaFoldDBiO75908
SMRiO75908
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114015, 5 interactors
IntActiO75908, 3 interactors
MINTiO75908
STRINGi9606.ENSP00000301466

Chemistry databases

BindingDBiO75908
ChEMBLiCHEMBL4465
DrugBankiDB01094, Hesperetin
SwissLipidsiSLP:000001262 [O75908-1]

Protein family/group databases

TCDBi2.A.50.4.11, the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family

PTM databases

iPTMnetiO75908
PhosphoSitePlusiO75908
SwissPalmiO75908

Genetic variation databases

BioMutaiSOAT2

Proteomic databases

MassIVEiO75908
PaxDbiO75908
PeptideAtlasiO75908
PRIDEiO75908
ProteomicsDBi27608
50258 [O75908-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		43294, 142 antibodies from 21 providers

The DNASU plasmid repository

More...DNASUi		8435

Genome annotation databases

EnsembliENST00000301466.8; ENSP00000301466.3; ENSG00000167780.12
ENST00000542365.1; ENSP00000442234.1; ENSG00000167780.12 [O75908-4]
GeneIDi8435
KEGGihsa:8435
MANE-SelectiENST00000301466.8; ENSP00000301466.3; NM_003578.4; NP_003569.1
UCSCiuc001sbv.4, human [O75908-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8435
DisGeNETi8435

GeneCards: human genes, protein and diseases

More...GeneCardsi		SOAT2
HGNCiHGNC:11178, SOAT2
HPAiENSG00000167780, Tissue enriched (intestine)
MIMi601311, gene
neXtProtiNX_O75908
OpenTargetsiENSG00000167780
PharmGKBiPA36016
VEuPathDBiHostDB:ENSG00000167780

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0380, Eukaryota
GeneTreeiENSGT00950000183081
HOGENOMiCLU_031845_1_0_1
InParanoidiO75908
OMAiMHDRHTG
OrthoDBi1275897at2759
PhylomeDBiO75908
TreeFamiTF315226

Enzyme and pathway databases

BRENDAi2.3.1.26, 2681
PathwayCommonsiO75908
ReactomeiR-HSA-8964038, LDL clearance
SABIO-RKiO75908
SignaLinkiO75908

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		8435, 18 hits in 1068 CRISPR screens

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		SOAT2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		8435
PharosiO75908, Tchem

Protein Ontology

More...PROi		PR:O75908
RNActiO75908, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000167780, Expressed in liver and 87 other tissues
ExpressionAtlasiO75908, baseline and differential
GenevisibleiO75908, HS

Family and domain databases

InterProiView protein in InterPro
IPR004299, MBOAT_fam
IPR014371, Oat_ACAT_DAG_ARE
IPR030687, Sterol_acyltranf_meta
PANTHERiPTHR10408, PTHR10408, 1 hit
PfamiView protein in Pfam
PF03062, MBOAT, 1 hit
PIRSFiPIRSF000439, Oat_ACAT_DAG_ARE, 1 hit
PIRSF500230, Sterol_acyltranf_ACAT, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSOAT2_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O75908
Secondary accession number(s): F5H7W4
, I6L9H9, Q4VB99, Q4VBA1, Q96TD4, Q9UNR2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1998
Last modified: May 25, 2022
This is version 169 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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