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Entry version 199 (03 Jul 2019)
Sequence version 1 (20 Mar 1987)
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Protein

Phosphatidylcholine-sterol acyltransferase

Gene

LCAT

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

Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs) (PubMed:10329423, PubMed:19065001, PubMed:26195816). The cholesterol ester is then transported back to the liver. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines (PubMed:8820107). Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms (PubMed:10722751).6 Publications

Miscellaneous

Levels of LCAT activity correlates inversely with leptin levels as well as with obesity for a wide range of BMI values.

<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

APOA1 is the most potent activator in plasma. Also activated by APOE, APOC1 and APOA4.1 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

Affinity for LDL is 2.3 to 4-fold lower than for HDL. Relative reactivities are 16% for HDL3, 1.3% for HDL2 and 6.5% for LDL.
  1. KM=0.97 mM for LDL1 Publication
  2. KM=0.4 mM for HDL21 Publication
  3. KM=0.10 mM for HDL31 Publication
  1. Vmax=8.3 mmol/min/mg enzyme with LDL as substrate1 Publication
  2. Vmax=0.58 mmol/min/mg enzyme with HDL2 as substrate1 Publication
  3. Vmax=2.0 mmol/min/mg enzyme with HDL3 as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei173Determinant for substrate specificity1 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 sitei205Nucleophile1 Publication1
Active sitei369Charge relay system1 Publication1
Active sitei401Charge relay system1 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

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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.43 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-8964058 HDL remodeling

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P04180

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P04180

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...
ESTHERi
human-LCAT PC-sterol_acyltransferase

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000660

<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:
Phosphatidylcholine-sterol acyltransferase (EC:2.3.1.437 Publications)
Alternative name(s):
Lecithin-cholesterol acyltransferase
Phospholipid-cholesterol acyltransferase
<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:LCAT
<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 16

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:6522 LCAT

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
606967 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P04180

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Lecithin-cholesterol acyltransferase deficiency (LCATD)15 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of lipoprotein metabolism characterized by inadequate esterification of plasmatic cholesterol. Two clinical forms are recognized: complete LCAT deficiency and fish-eye disease. LCATD is generally referred to the complete form which is associated with absence of both alpha and beta LCAT activities resulting in esterification anomalies involving both HDL (alpha-LCAT activity) and LDL (beta-LCAT activity). It causes a typical triad of diffuse corneal opacities, target cell hemolytic anemia, and proteinuria with renal failure.
Related information in OMIM
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_00425117L → LLLPPAAPFWL in LCATD. 1
Natural variantiVAR_03902029N → I in LCATD. 1 Publication1
Natural variantiVAR_03902237T → M in LCATD. 1 PublicationCorresponds to variant dbSNP:rs971887742Ensembl.1
Natural variantiVAR_00425354G → S in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1461145750Ensembl.1
Natural variantiVAR_00425457G → R in LCATD. 1 Publication1
Natural variantiVAR_004255117A → T in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940886EnsemblClinVar.1
Natural variantiVAR_004257159R → W in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28940887EnsemblClinVar.1
Natural variantiVAR_039028164R → C in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1380009545Ensembl.1
Natural variantiVAR_004258164R → H in LCATD; also in a compound heterozygote carrying R-95 with intermediate phenotype between LCATD and FED; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs769485083Ensembl.1
Natural variantiVAR_004259171R → W in LCATD. 2 Publications1
Natural variantiVAR_004260180Y → N in LCATD. Corresponds to variant dbSNP:rs749740660Ensembl.1
Natural variantiVAR_039030205S → N in LCATD. 1 Publication1
Natural variantiVAR_004262233L → P in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28942087EnsemblClinVar.1
Natural variantiVAR_039031242K → N in LCATD. 1 Publication1
Natural variantiVAR_004263252N → K in LCATD. 1 PublicationCorresponds to variant dbSNP:rs121908049EnsemblClinVar.1
Natural variantiVAR_039032268R → H in LCATD. 1 PublicationCorresponds to variant dbSNP:rs780824776Ensembl.1
Natural variantiVAR_039033298T → A in FED and LCATD. 2 Publications1
Natural variantiVAR_039034298T → I in LCATD. 1 Publication1
Natural variantiVAR_004265317M → I in LCATD; partially defective enzyme. 2 PublicationsCorresponds to variant dbSNP:rs121908048EnsemblClinVar.1
Natural variantiVAR_039035331P → S in LCATD. 1 Publication1
Natural variantiVAR_039036333V → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs776035233Ensembl.1
Natural variantiVAR_004266345T → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940888EnsemblClinVar.1
Natural variantiVAR_039038406F → V in LCATD. 1 Publication1
Fish-eye disease (FED)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of lipoprotein metabolism due to partial lecithin-cholesterol acyltransferase deficiency that affects only alpha-LCAT activity. FED is characterized by low plasma HDL and corneal opacities due to accumulation of cholesterol deposits in the cornea ('fish-eye').
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00425234P → L in FED. 1 PublicationCorresponds to variant dbSNP:rs121908051EnsemblClinVar.1
Natural variantiVAR_03902134P → Q in FED. 1 Publication1
Natural variantiVAR_03902370V → E in FED. 1 PublicationCorresponds to variant dbSNP:rs748427834Ensembl.1
Natural variantiVAR_06686299W → S in FED; loss of activity. 1 Publication1
Natural variantiVAR_039026123R → C in FED. 1 PublicationCorresponds to variant dbSNP:rs140068549Ensembl.1
Natural variantiVAR_004256147T → I in FED. 1 PublicationCorresponds to variant dbSNP:rs121908050EnsemblClinVar.1
Natural variantiVAR_039027159R → Q in FED. 1 PublicationCorresponds to variant dbSNP:rs768017317Ensembl.1
Natural variantiVAR_004264276M → K in FED. 1 PublicationCorresponds to variant dbSNP:rs121908054EnsemblClinVar.1
Natural variantiVAR_039033298T → A in FED and LCATD. 2 Publications1
Natural variantiVAR_066867338L → F in FED; results in reduced protein secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs1330635214Ensembl.1
Natural variantiVAR_066868347R → C in FED; results in reduced activity. 1 PublicationCorresponds to variant dbSNP:rs202017590EnsemblClinVar.1
Natural variantiVAR_004267371T → M in FED. 1 PublicationCorresponds to variant dbSNP:rs121908053EnsemblClinVar.1

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>Mutagenesisi173E → A: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → D: Little change in enzyme specific activity nor in PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → K: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → L: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → Q: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication1

Keywords - Diseasei

Corneal dystrophy, Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
3931

MalaCards human disease database

More...
MalaCardsi
LCAT
MIMi136120 phenotype
245900 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000213398

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
79293 Familial LCAT deficiency
79292 Fish-eye disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA226

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5942

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
LCAT

Domain mapping of disease mutations (DMDM)

More...
DMDMi
125993

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 241 PublicationAdd BLAST24
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001780225 – 440Phosphatidylcholine-sterol acyltransferaseAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi44N-linked (GlcNAc...) (complex) asparagine2 Publications1
<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 bondi74 ↔ 98Combined sources2 Publications
Glycosylationi108N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications1
Glycosylationi296N-linked (GlcNAc...) (complex) asparagineCombined sources3 Publications1
Disulfide bondi337 ↔ 380Combined sources2 Publications
Glycosylationi408N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications1
Glycosylationi431O-linked (GalNAc...) threonine1 Publication1
Glycosylationi433O-linked (GalNAc...) serine1 Publication1

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

O- and N-glycosylated. O-glycosylation on Thr-431 and Ser-433 consists of sialylated galactose beta 1-->3N-acetylgalactosamine structures. N-glycosylated sites contain sialylated triantennary and/or biantennary complex structures.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P04180

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

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PaxDbi
P04180

PeptideAtlas

More...
PeptideAtlasi
P04180

PRoteomics IDEntifications database

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PRIDEi
P04180

ProteomicsDB human proteome resource

More...
ProteomicsDBi
51671

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
495

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P04180

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

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PhosphoSitePlusi
P04180

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P04180

<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

Detected in blood plasma (PubMed:3458198, PubMed:8820107, PubMed:10222237). Detected in cerebral spinal fluid (at protein level) (PubMed:10222237). Detected in liver (PubMed:3797244, PubMed:3458198). Expressed mainly in brain, liver and testes.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000213398 Expressed in 136 organ(s), highest expression level in right lobe of liver

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P04180 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P04180 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA044767

<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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
APOA1P026472EBI-9104464,EBI-701692

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
110123, 6 interactors

Database of interacting proteins

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DIPi
DIP-29620N

Protein interaction database and analysis system

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IntActi
P04180, 1 interactor

STRING: functional protein association networks

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STRINGi
9606.ENSP00000264005

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P04180

<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

1440
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
P04180

Database of comparative protein structure models

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ModBasei
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

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi426 – 439Pro-richAdd BLAST14

<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 AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2369 Eukaryota
ENOG410Y9CF LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160052

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000238654

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P04180

KEGG Orthology (KO)

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KOi
K00650

Identification of Orthologs from Complete Genome Data

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OMAi
FEDGWYM

Database of Orthologous Groups

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OrthoDBi
388324at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P04180

TreeFam database of animal gene trees

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TreeFami
TF313258

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029058 AB_hydrolase
IPR003386 LACT/PDAT_acylTrfase

Pfam protein domain database

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Pfami
View protein in Pfam
PF02450 LCAT, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53474 SSF53474, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00120 LIPASE_SER, 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>Sequence (1+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

P04180-1 [UniParc]FASTAAdd to basket
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MGPPGSPWQW VTLLLGLLLP PAAPFWLLNV LFPPHTTPKA ELSNHTRPVI
60 70 80 90 100
LVPGCLGNQL EAKLDKPDVV NWMCYRKTED FFTIWLDLNM FLPLGVDCWI
110 120 130 140 150
DNTRVVYNRS SGLVSNAPGV QIRVPGFGKT YSVEYLDSSK LAGYLHTLVQ
160 170 180 190 200
NLVNNGYVRD ETVRAAPYDW RLEPGQQEEY YRKLAGLVEE MHAAYGKPVF
210 220 230 240 250
LIGHSLGCLH LLYFLLRQPQ AWKDRFIDGF ISLGAPWGGS IKPMLVLASG
260 270 280 290 300
DNQGIPIMSS IKLKEEQRIT TTSPWMFPSR MAWPEDHVFI STPSFNYTGR
310 320 330 340 350
DFQRFFADLH FEEGWYMWLQ SRDLLAGLPA PGVEVYCLYG VGLPTPRTYI
360 370 380 390 400
YDHGFPYTDP VGVLYEDGDD TVATRSTELC GLWQGRQPQP VHLLPLHGIQ
410 420 430 440
HLNMVFSNLT LEHINAILLG AYRQGPPASP TASPEPPPPE
Length:440
Mass (Da):49,578
Last modified:March 20, 1987 - 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:iB315EF118AA7A378
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 are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
I3L0J6I3L0J6_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
80Annotation 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>
I3L1Q6I3L1Q6_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
107Annotation 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>
J3QSE5J3QSE5_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
255Annotation 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>
J3QKT0J3QKT0_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
138Annotation 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>
I3L3R0I3L3R0_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
93Annotation 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>
I3L215I3L215_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
61Annotation 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 conflicti257I → H in CAB56610 (PubMed:2823898).Curated1
Sequence conflicti257I → H in AAA59499 (PubMed:2823898).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00425117L → LLLPPAAPFWL in LCATD. 1
Natural variantiVAR_03902029N → I in LCATD. 1 Publication1
Natural variantiVAR_00425234P → L in FED. 1 PublicationCorresponds to variant dbSNP:rs121908051EnsemblClinVar.1
Natural variantiVAR_03902134P → Q in FED. 1 Publication1
Natural variantiVAR_03902237T → M in LCATD. 1 PublicationCorresponds to variant dbSNP:rs971887742Ensembl.1
Natural variantiVAR_00425354G → S in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1461145750Ensembl.1
Natural variantiVAR_00425457G → R in LCATD. 1 Publication1
Natural variantiVAR_03902370V → E in FED. 1 PublicationCorresponds to variant dbSNP:rs748427834Ensembl.1
Natural variantiVAR_03902495G → R in a compound heterozygote carrying H-164; intermediate phenotype between LCATD and FED; reduction of activity. 1 Publication1
Natural variantiVAR_06686299W → S in FED; loss of activity. 1 Publication1
Natural variantiVAR_039025115S → P1 PublicationCorresponds to variant dbSNP:rs1412883954Ensembl.1
Natural variantiVAR_004255117A → T in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940886EnsemblClinVar.1
Natural variantiVAR_039026123R → C in FED. 1 PublicationCorresponds to variant dbSNP:rs140068549Ensembl.1
Natural variantiVAR_066863134 – 135EY → DN in a patient with low HDL-cholesterol levels; results in reduced activity. 1 Publication2
Natural variantiVAR_004256147T → I in FED. 1 PublicationCorresponds to variant dbSNP:rs121908050EnsemblClinVar.1
Natural variantiVAR_039027159R → Q in FED. 1 PublicationCorresponds to variant dbSNP:rs768017317Ensembl.1
Natural variantiVAR_004257159R → W in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28940887EnsemblClinVar.1
Natural variantiVAR_039028164R → C in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1380009545Ensembl.1
Natural variantiVAR_004258164R → H in LCATD; also in a compound heterozygote carrying R-95 with intermediate phenotype between LCATD and FED; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs769485083Ensembl.1
Natural variantiVAR_039029165A → T1 PublicationCorresponds to variant dbSNP:rs1369994093Ensembl.1
Natural variantiVAR_004259171R → W in LCATD. 2 Publications1
Natural variantiVAR_004260180Y → N in LCATD. Corresponds to variant dbSNP:rs749740660Ensembl.1
Natural variantiVAR_004261182R → C2 PublicationsCorresponds to variant dbSNP:rs387906300EnsemblClinVar.1
Natural variantiVAR_039030205S → N in LCATD. 1 Publication1
Natural variantiVAR_017030232S → T3 PublicationsCorresponds to variant dbSNP:rs4986970Ensembl.1
Natural variantiVAR_004262233L → P in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28942087EnsemblClinVar.1
Natural variantiVAR_039031242K → N in LCATD. 1 Publication1
Natural variantiVAR_066864246V → F in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive. 1 Publication1
Natural variantiVAR_004263252N → K in LCATD. 1 PublicationCorresponds to variant dbSNP:rs121908049EnsemblClinVar.1
Natural variantiVAR_066865268R → C in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive. 1 PublicationCorresponds to variant dbSNP:rs745320775Ensembl.1
Natural variantiVAR_039032268R → H in LCATD. 1 PublicationCorresponds to variant dbSNP:rs780824776Ensembl.1
Natural variantiVAR_004264276M → K in FED. 1 PublicationCorresponds to variant dbSNP:rs121908054EnsemblClinVar.1
Natural variantiVAR_039033298T → A in FED and LCATD. 2 Publications1
Natural variantiVAR_039034298T → I in LCATD. 1 Publication1
Natural variantiVAR_004265317M → I in LCATD; partially defective enzyme. 2 PublicationsCorresponds to variant dbSNP:rs121908048EnsemblClinVar.1
Natural variantiVAR_066866322R → C in a patient with low HDL-cholesterol levels; reduced protein secretion. 1 PublicationCorresponds to variant dbSNP:rs1407191796Ensembl.1
Natural variantiVAR_039035331P → S in LCATD. 1 Publication1
Natural variantiVAR_039036333V → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs776035233Ensembl.1
Natural variantiVAR_066867338L → F in FED; results in reduced protein secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs1330635214Ensembl.1
Natural variantiVAR_004266345T → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940888EnsemblClinVar.1
Natural variantiVAR_066868347R → C in FED; results in reduced activity. 1 PublicationCorresponds to variant dbSNP:rs202017590EnsemblClinVar.1
Natural variantiVAR_004267371T → M in FED. 1 PublicationCorresponds to variant dbSNP:rs121908053EnsemblClinVar.1
Natural variantiVAR_039037396L → R in a patient with LCATD. 2 Publications1
Natural variantiVAR_039038406F → V in LCATD. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X04981 Genomic DNA Translation: CAA28651.1
M12625 mRNA Translation: AAA59498.1
AY422210 Genomic DNA Translation: AAR03499.1
BT009748 mRNA Translation: AAP88750.1
AC040162 Genomic DNA No translation available.
CH471092 Genomic DNA Translation: EAW83190.1
BC014781 mRNA Translation: AAH14781.1
M26268 mRNA Translation: AAA59499.1
X06537 mRNA Translation: CAB56610.1
M17959 Genomic DNA Translation: AAA59500.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10854.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A00571 XXHUN

NCBI Reference Sequences

More...
RefSeqi
NP_000220.1, NM_000229.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000264005; ENSP00000264005; ENSG00000213398

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3931

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3931

UCSC genome browser

More...
UCSCi
uc002euy.2 human

Keywords - Coding sequence diversityi

Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Lecithin-cholesterol acyltransferase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04981 Genomic DNA Translation: CAA28651.1
M12625 mRNA Translation: AAA59498.1
AY422210 Genomic DNA Translation: AAR03499.1
BT009748 mRNA Translation: AAP88750.1
AC040162 Genomic DNA No translation available.
CH471092 Genomic DNA Translation: EAW83190.1
BC014781 mRNA Translation: AAH14781.1
M26268 mRNA Translation: AAA59499.1
X06537 mRNA Translation: CAB56610.1
M17959 Genomic DNA Translation: AAA59500.1
CCDSiCCDS10854.1
PIRiA00571 XXHUN
RefSeqiNP_000220.1, NM_000229.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4X96X-ray8.69A/B/C/D45-421[»]
4XWGX-ray2.65A25-440[»]
4XX1X-ray3.60A/B/J25-440[»]
5BV7X-ray2.45A25-440[»]
5TXFX-ray3.10A/B/C/D25-440[»]
6MVDX-ray3.10A/B45-421[»]
SMRiP04180
ModBaseiSearch...

Protein-protein interaction databases

BioGridi110123, 6 interactors
DIPiDIP-29620N
IntActiP04180, 1 interactor
STRINGi9606.ENSP00000264005

Chemistry databases

BindingDBiP04180
ChEMBLiCHEMBL5942
SwissLipidsiSLP:000000660

Protein family/group databases

ESTHERihuman-LCAT PC-sterol_acyltransferase

PTM databases

GlyConnecti495
iPTMnetiP04180
PhosphoSitePlusiP04180
UniCarbKBiP04180

Polymorphism and mutation databases

BioMutaiLCAT
DMDMi125993

Proteomic databases

MaxQBiP04180
PaxDbiP04180
PeptideAtlasiP04180
PRIDEiP04180
ProteomicsDBi51671

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P04180

The DNASU plasmid repository

More...
DNASUi
3931
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264005; ENSP00000264005; ENSG00000213398
GeneIDi3931
KEGGihsa:3931
UCSCiuc002euy.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3931
DisGeNETi3931

GeneCards: human genes, protein and diseases

More...
GeneCardsi
LCAT

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0134431
HGNCiHGNC:6522 LCAT
HPAiHPA044767
MalaCardsiLCAT
MIMi136120 phenotype
245900 phenotype
606967 gene
neXtProtiNX_P04180
OpenTargetsiENSG00000213398
Orphaneti79293 Familial LCAT deficiency
79292 Fish-eye disease
PharmGKBiPA226

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2369 Eukaryota
ENOG410Y9CF LUCA
GeneTreeiENSGT00940000160052
HOGENOMiHOG000238654
InParanoidiP04180
KOiK00650
OMAiFEDGWYM
OrthoDBi388324at2759
PhylomeDBiP04180
TreeFamiTF313258

Enzyme and pathway databases

BRENDAi2.3.1.43 2681
ReactomeiR-HSA-8964058 HDL remodeling
SABIO-RKiP04180
SIGNORiP04180

Miscellaneous databases

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

More...
ChiTaRSi
LCAT human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Lecithin%E2%80%94cholesterol_acyltransferase

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

More...
GenomeRNAii
3931

Protein Ontology

More...
PROi
PR:P04180

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000213398 Expressed in 136 organ(s), highest expression level in right lobe of liver
ExpressionAtlasiP04180 baseline and differential
GenevisibleiP04180 HS

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR003386 LACT/PDAT_acylTrfase
PfamiView protein in Pfam
PF02450 LCAT, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiLCAT_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: P04180
Secondary accession number(s): Q53XQ3
<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: March 20, 1987
Last sequence update: March 20, 1987
Last modified: July 3, 2019
This is version 199 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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