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Entry version 198 (29 Sep 2021)
Sequence version 3 (25 Jul 2003)
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Protein

Sterol O-acyltransferase 1

Gene

SOAT1

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:16154994, PubMed:16647063, PubMed:9020103, PubMed:32433614, PubMed:32433613, PubMed:32944968).

Plays a role in lipoprotein assembly and dietary cholesterol absorption (PubMed:16154994, PubMed:9020103).

Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrate: shows a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions (PubMed:11294643, PubMed:32433614).

7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Cholesterol O-acyltransferase activity is inhibited by nevanimibe.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=31.2 µM for (9Z)-octadecenoyl-CoA1 Publication
  2. KM=20.0 µM for (11Z)-octadecenoyl-CoA1 Publication
  3. KM=16.0 µM for (7Z)-octadecenoyl-CoA1 Publication
  4. KM=50.3 µM for octadecanoyl-CoA1 Publication
  5. KM=20.6 µM for (9Z)-hexadecenoyl-CoA1 Publication
  6. KM=21.1 µM for hexadecanoyl-CoA1 Publication
  1. Vmax=123.1 nmol/min/mg enzyme with (9Z)-octadecenoyl-CoA as substrate1 Publication
  2. Vmax=96.7 nmol/min/mg enzyme with (11Z)-octadecenoyl-CoA as substrate1 Publication
  3. Vmax=66.7 nmol/min/mg enzyme with (7Z)-octadecenoyl-CoA as substrate1 Publication
  4. Vmax=92.8 nmol/min/mg enzyme with octadecanoyl-CoA as substrate1 Publication
  5. Vmax=97.6 nmol/min/mg enzyme with (9Z)-hexadecenoyl-CoA as substrate1 Publication
  6. Vmax=86.8 nmol/min/mg enzyme with hexadecanoyl-CoA as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei137CholesterolCombined sources1 Publication1
Binding sitei415Acyl-CoACombined sources1 Publication1
Binding sitei418Acyl-CoACombined sources1 Publication1
Binding sitei421Acyl-CoACombined sources1 Publication1
Binding sitei425Acyl-CoACombined sources2 Publications1
Binding sitei433Acyl-CoACombined sources1 Publication1
Binding sitei445Acyl-CoACombined sources2 Publications1
Binding sitei456Acyl-CoACombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei460Combined sources4 Publications1

<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

GO - Biological processi

<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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS00706-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.3.1.26, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P35610

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P35610

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P35610

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000702

<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_and_taxonomy_section">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 1Curated (EC:2.3.1.264 Publications)
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase 14 Publications
Short name:
ACAT-11 Publication
Cholesterol acyltransferase 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:SOAT1Imported
Synonyms:ACACT, ACACT1, ACAT1 Publication, ACAT13 Publications, SOAT, STAT
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 1

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:11177, SOAT1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
102642, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P35610

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000057252

<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_location_section">'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 – 138CytoplasmicCuratedAdd BLAST138
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei139 – 160Helical; Name=1Combined sources1 Publication1 PublicationAdd BLAST22
Topological domaini161 – 180LumenalCuratedAdd BLAST20
Transmembranei181 – 206Helical; Name=2Combined sources1 Publication1 PublicationAdd BLAST26
Topological domaini207 – 218CytoplasmicCuratedAdd BLAST12
Transmembranei219 – 244Helical; Name=3Combined sources1 Publication1 PublicationAdd BLAST26
Topological domaini245 – 252LumenalCurated8
Transmembranei253 – 276Helical; Name=4Combined sources1 Publication1 PublicationAdd BLAST24
Topological domaini277 – 319CytoplasmicCuratedAdd BLAST43
Transmembranei320 – 352Helical; Name=5Combined sources1 Publication1 PublicationAdd BLAST33
Topological domaini353 – 369LumenalCuratedAdd BLAST17
Transmembranei370 – 395Helical; Name=6Combined sources1 Publication1 PublicationAdd BLAST26
Topological domaini396 – 443CytoplasmicCuratedAdd BLAST48
Transmembranei444 – 468Helical; Name=7Combined sources1 Publication1 PublicationAdd BLAST25
Topological domaini469 – 474LumenalCurated6
Transmembranei475 – 490Helical; Name=8Combined sources1 Publication1 PublicationAdd BLAST16
Topological domaini491 – 496CytoplasmicCurated6
Transmembranei497 – 528Helical; Name=9Combined sources2 PublicationsAdd BLAST32
Topological domaini529 – 550LumenalCuratedAdd BLAST22

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_and_biotech_section">'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>Mutagenesisi262R → A: Strongly reduced cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi263F → A: Strongly reduced cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi269S → A or T: Nearly normal expression and enzyme activity. 1 Publication1
Mutagenesisi269S → L: No expression nor activity. 1 Publication1
Mutagenesisi306L → N: Strongly reduced cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi367F → A: Abolished homodimerization; when associated with 504-A--A-508. 1 Publication1
Mutagenesisi386H → A: Abolished cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi400D → N: Low expression, loss of enzymatic activity. 1 Publication1
Mutagenesisi407W → A: Almost abolished cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi415N → G: Reduced cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi418R → A: Reduced cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi420W → A: Almost abolished cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi421N → A: Almost abolished cholesterol O-acyltransferase activity. 2 Publications1
Mutagenesisi425H → A: Strongly reduced cholesterol O-acyltransferase activity. 2 Publications1
Mutagenesisi428L → Q: Almost abolished cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi429Y → A: Strongly reduced cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi445K → A: Reduced cholesterol O-acyltransferase activity. 2 Publications1
Mutagenesisi452 – 456VFAVS → QFAVQ in QQ mutant; almost abolished cholesterol O-acyltransferase activity. 1 Publication5
Mutagenesisi452 – 453VF → AA: Almost abolished cholesterol O-acyltransferase activity. 1 Publication2
Mutagenesisi456S → A: Abolished cholesterol O-acyltransferase activity. 2 Publications1
Mutagenesisi460H → A, C or N: Abolished cholesterol O-acyltransferase activity. 4 Publications1
Mutagenesisi504 – 508WTSLF → ATSLA: Abolished homodimerization; when associated with A-367. 1 Publication5
Mutagenesisi507L → A: Strongly reduced cholesterol O-acyltransferase activity. 1 Publication1
Mutagenesisi518Y → F: Loss of enzymatic activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
6646

Open Targets

More...
OpenTargetsi
ENSG00000057252

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA36015

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P35610, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2782

Drug and drug target database

More...
DrugBanki
DB00973, Ezetimibe
DB01094, Hesperetin
DB09539, Omega-3-acid ethyl esters

DrugCentral

More...
DrugCentrali
P35610

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
SOAT1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
33302623

<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_00002076401 – 550Sterol O-acyltransferase 1Add BLAST550

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 residuei1N-acetylmethionineCombined sources1
Modified residuei8PhosphoserineCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi528 ↔ 5461 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P35610

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P35610

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P35610

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P35610

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

More...
PaxDbi
P35610

PeptideAtlas

More...
PeptideAtlasi
P35610

PRoteomics IDEntifications database

More...
PRIDEi
P35610

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
1856
5164
55101 [P35610-1]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P35610, 2 sites, 1 O-linked glycan (2 sites)

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P35610

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

More...
PhosphoSitePlusi
P35610

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P35610

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Highly activated by the presence of cholesterol.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000057252, Expressed in adrenal tissue and 221 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P35610, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P35610, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000057252, Tissue enhanced (adrenal)

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer; composed of two homodimers (PubMed:32433614, PubMed:32433613).

Interacts with UBIAD1 (PubMed:23169578).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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

Hide details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
112529, 231 interactors

Protein interaction database and analysis system

More...
IntActi
P35610, 177 interactors

Molecular INTeraction database

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MINTi
P35610

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000356591

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P35610

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P35610, 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

Secondary structure

1550
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P35610

Database of comparative protein structure models

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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 – 39DisorderedSequence analysisAdd BLAST39

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>Motifi403 – 409FYXDWWN motif1 Publication7

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 biasi1 – 31Basic and acidic residuesSequence analysisAdd BLAST31

<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.1 Publication

<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

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
P35610

Identification of Orthologs from Complete Genome Data

More...
OMAi
PAVWRCY

Database of Orthologous Groups

More...
OrthoDBi
1275897at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P35610

TreeFam database of animal gene trees

More...
TreeFami
TF105767

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_length">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 (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 3 <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 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P35610-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><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
MVGEEKMSLR NRLSKSRENP EEDEDQRNPA KESLETPSNG RIDIKQLIAK
60 70 80 90 100
KIKLTAEAEE LKPFFMKEVG SHFDDFVTNL IEKSASLDNG GCALTTFSVL
110 120 130 140 150
EGEKNNHRAK DLRAPPEQGK IFIARRSLLD ELLEVDHIRT IYHMFIALLI
160 170 180 190 200
LFILSTLVVD YIDEGRLVLE FSLLSYAFGK FPTVVWTWWI MFLSTFSVPY
210 220 230 240 250
FLFQHWATGY SKSSHPLIRS LFHGFLFMIF QIGVLGFGPT YVVLAYTLPP
260 270 280 290 300
ASRFIIIFEQ IRFVMKAHSF VRENVPRVLN SAKEKSSTVP IPTVNQYLYF
310 320 330 340 350
LFAPTLIYRD SYPRNPTVRW GYVAMKFAQV FGCFFYVYYI FERLCAPLFR
360 370 380 390 400
NIKQEPFSAR VLVLCVFNSI LPGVLILFLT FFAFLHCWLN AFAEMLRFGD
410 420 430 440 450
RMFYKDWWNS TSYSNYYRTW NVVVHDWLYY YAYKDFLWFF SKRFKSAAML
460 470 480 490 500
AVFAVSAVVH EYALAVCLSF FYPVLFVLFM FFGMAFNFIV NDSRKKPIWN
510 520 530 540 550
VLMWTSLFLG NGVLLCFYSQ EWYARQHCPL KNPTFLDYVR PRSWTCRYVF
Length:550
Mass (Da):64,735
Last modified:July 25, 2003 - v3
<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:i5F5ACD525D541DEE
GO
Isoform 2 (identifier: P35610-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAE → M

Show »
Length:492
Mass (Da):58,131
Checksum:i285EF79CC80BF5E8
GO
Isoform 3 (identifier: P35610-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.

Show »
Length:485
Mass (Da):57,238
Checksum:i9C0D0F331D69376A
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
B1APM4B1APM4_HUMAN
Sterol O-acyltransferase 1
SOAT1
260Annotation score:

Annotation score:2 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>

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_052031526Q → R1 PublicationCorresponds to variant dbSNP:rs13306731Ensembl.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_0453301 – 65Missing in isoform 3. 1 PublicationAdd BLAST65
Alternative sequenceiVSP_0453311 – 59MVGEE…TAEAE → M in isoform 2. 1 PublicationAdd BLAST59

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
L21934 mRNA Translation: AAC37532.2
AK290659 mRNA Translation: BAF83348.1
AK300551 mRNA Translation: BAG62257.1
AL451075 Genomic DNA No translation available.
AL512326 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91043.1
CH471067 Genomic DNA Translation: EAW91044.1
BC028940 mRNA Translation: AAH28940.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1330.1 [P35610-1]
CCDS58047.1 [P35610-2]
CCDS58048.1 [P35610-3]

Protein sequence database of the Protein Information Resource

More...
PIRi
A59038, A48026

NCBI Reference Sequences

More...
RefSeqi
NP_001239440.1, NM_001252511.1 [P35610-2]
NP_001239441.1, NM_001252512.1 [P35610-3]
NP_003092.4, NM_003101.5 [P35610-1]
XP_011508213.1, XM_011509911.1 [P35610-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000367619; ENSP00000356591; ENSG00000057252 [P35610-1]
ENST00000539888; ENSP00000441356; ENSG00000057252 [P35610-3]
ENST00000540564; ENSP00000445315; ENSG00000057252 [P35610-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6646

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6646

UCSC genome browser

More...
UCSCi
uc001gml.4, human [P35610-1]

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
L21934 mRNA Translation: AAC37532.2
AK290659 mRNA Translation: BAF83348.1
AK300551 mRNA Translation: BAG62257.1
AL451075 Genomic DNA No translation available.
AL512326 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91043.1
CH471067 Genomic DNA Translation: EAW91044.1
BC028940 mRNA Translation: AAH28940.1
CCDSiCCDS1330.1 [P35610-1]
CCDS58047.1 [P35610-2]
CCDS58048.1 [P35610-3]
PIRiA59038, A48026
RefSeqiNP_001239440.1, NM_001252511.1 [P35610-2]
NP_001239441.1, NM_001252512.1 [P35610-3]
NP_003092.4, NM_003101.5 [P35610-1]
XP_011508213.1, XM_011509911.1 [P35610-1]

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
6L47electron microscopy3.50A/B66-550[»]
6L48electron microscopy3.50A/B66-550[»]
6P2Jelectron microscopy3.00A/B1-550[»]
6P2Pelectron microscopy3.10A/B/C/D1-550[»]
6VUMelectron microscopy3.67A/B/C/D1-550[»]
SMRiP35610
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi112529, 231 interactors
IntActiP35610, 177 interactors
MINTiP35610
STRINGi9606.ENSP00000356591

Chemistry databases

BindingDBiP35610
ChEMBLiCHEMBL2782
DrugBankiDB00973, Ezetimibe
DB01094, Hesperetin
DB09539, Omega-3-acid ethyl esters
DrugCentraliP35610
SwissLipidsiSLP:000000702

PTM databases

GlyGeniP35610, 2 sites, 1 O-linked glycan (2 sites)
iPTMnetiP35610
PhosphoSitePlusiP35610
SwissPalmiP35610

Genetic variation databases

BioMutaiSOAT1
DMDMi33302623

Proteomic databases

EPDiP35610
jPOSTiP35610
MassIVEiP35610
MaxQBiP35610
PaxDbiP35610
PeptideAtlasiP35610
PRIDEiP35610
ProteomicsDBi1856
5164
55101 [P35610-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
4027, 182 antibodies

The DNASU plasmid repository

More...
DNASUi
6646

Genome annotation databases

EnsembliENST00000367619; ENSP00000356591; ENSG00000057252 [P35610-1]
ENST00000539888; ENSP00000441356; ENSG00000057252 [P35610-3]
ENST00000540564; ENSP00000445315; ENSG00000057252 [P35610-2]
GeneIDi6646
KEGGihsa:6646
UCSCiuc001gml.4, human [P35610-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6646
DisGeNETi6646

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SOAT1
HGNCiHGNC:11177, SOAT1
HPAiENSG00000057252, Tissue enhanced (adrenal)
MIMi102642, gene
neXtProtiNX_P35610
OpenTargetsiENSG00000057252
PharmGKBiPA36015
VEuPathDBiHostDB:ENSG00000057252

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0380, Eukaryota
GeneTreeiENSGT00950000183081
HOGENOMiCLU_031845_1_0_1
InParanoidiP35610
OMAiPAVWRCY
OrthoDBi1275897at2759
PhylomeDBiP35610
TreeFamiTF105767

Enzyme and pathway databases

BioCyciMetaCyc:HS00706-MONOMER
BRENDAi2.3.1.26, 2681
PathwayCommonsiP35610
ReactomeiR-HSA-8964038, LDL clearance
SABIO-RKiP35610
SIGNORiP35610

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
6646, 8 hits in 1020 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
SOAT1, human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
SOAT1

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

More...
GenomeRNAii
6646
PharosiP35610, Tchem

Protein Ontology

More...
PROi
PR:P35610
RNActiP35610, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000057252, Expressed in adrenal tissue and 221 other tissues
ExpressionAtlasiP35610, baseline and differential
GenevisibleiP35610, 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 nameiSOAT1_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: P35610
Secondary accession number(s): A6NC40
, A8K3P4, A9Z1V7, B4DU95, Q5T0X4, Q8N1E4
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 25, 2003
Last modified: September 29, 2021
This is version 198 of the entry and version 3 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 1
    Human chromosome 1: 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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