LCAT

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.

Catalytic activityⁱ

a 1,2-diacyl-sn-glycero-3-phosphocholine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
a sterol
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
a 1-acyl-sn-glycero-3-phosphocholine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
a sterol ester
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10037
8 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "Cloning and expression of human lecithin-cholesterol acyltransferase cDNA."
  McLean J., Fielding C., Drayna D., Dieplinger H., Baer B., Kohr W., Henzel W., Lawn R.
  Proc. Natl. Acad. Sci. U.S.A. 83:2335-2339(1986) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-39; 172-182; 269-280 AND 387-406, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Ref.12
  "Comparative studies on the substrate specificity of lecithin:cholesterol acyltransferase towards the molecular species of phosphatidylcholine in the plasma of 14 vertebrates."
  Subbaiah P.V., Liu M.
  J. Lipid Res. 37:113-122(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Ref.13
  "Secretion of lecithin:cholesterol acyltransferase by brain neuroglial cell lines."
  Collet X., Francone O., Besnard F., Fielding C.J.
  Biochem. Biophys. Res. Commun. 258:73-76(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
- Ref.14
  "Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins."
  Kosek A.B., Durbin D., Jonas A.
  Biochem. Biophys. Res. Commun. 258:548-551(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Ref.16
  "Negative charge at amino acid 149 is the molecular determinant for substrate specificity of lecithin: cholesterol acyltransferase for phosphatidylcholine containing 20-carbon sn-2 fatty acyl chains."
  Zhao Y., Wang J., Gebre A.K., Chisholm J.W., Parks J.S.
  Biochemistry 42:13941-13949(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBSTRATE SPECIFICITY, MUTAGENESIS OF GLU-173, FUNCTION, CATALYTIC ACTIVITY.
- Ref.19
  "LCAT synthesized by primary astrocytes esterifies cholesterol on glia-derived lipoproteins."
  Hirsch-Reinshagen V., Donkin J., Stukas S., Chan J., Wilkinson A., Fan J., Parks J.S., Kuivenhoven J.A., Lutjohann D., Pritchard H., Wellington C.L.
  J. Lipid Res. 50:885-893(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: ACTIVITY REGULATION, SUBCELLULAR LOCATION, FUNCTION.
- Ref.20
  "The high resolution crystal structure of human LCAT."
  Piper D.E., Romanow W.G., Gunawardane R.N., Fordstrom P., Masterman S., Pan O., Thibault S.T., Zhang R., Meininger D., Schwarz M., Wang Z., King C., Zhou M., Walker N.P.
  J. Lipid Res. 56:1711-1719(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-440, DISULFIDE BONDS, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-108; ASN-296 AND ASN-408.
- Ref.21
  "Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase."
  Glukhova A., Hinkovska-Galcheva V., Kelly R., Abe A., Shayman J.A., Tesmer J.J.
  Nat. Commun. 6:6250-6250(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (8.69 ANGSTROMS) OF 45-421, CATALYTIC ACTIVITY, DISULFIDE BONDS, GLYCOSYLATION AT ASN-108; ASN-296 AND ASN-408.
EC:
2.3.1.43
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10037
8 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "Cloning and expression of human lecithin-cholesterol acyltransferase cDNA."
  McLean J., Fielding C., Drayna D., Dieplinger H., Baer B., Kohr W., Henzel W., Lawn R.
  Proc. Natl. Acad. Sci. U.S.A. 83:2335-2339(1986) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-39; 172-182; 269-280 AND 387-406, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Ref.12
  "Comparative studies on the substrate specificity of lecithin:cholesterol acyltransferase towards the molecular species of phosphatidylcholine in the plasma of 14 vertebrates."
  Subbaiah P.V., Liu M.
  J. Lipid Res. 37:113-122(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Ref.13
  "Secretion of lecithin:cholesterol acyltransferase by brain neuroglial cell lines."
  Collet X., Francone O., Besnard F., Fielding C.J.
  Biochem. Biophys. Res. Commun. 258:73-76(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
- Ref.14
  "Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins."
  Kosek A.B., Durbin D., Jonas A.
  Biochem. Biophys. Res. Commun. 258:548-551(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Ref.16
  "Negative charge at amino acid 149 is the molecular determinant for substrate specificity of lecithin: cholesterol acyltransferase for phosphatidylcholine containing 20-carbon sn-2 fatty acyl chains."
  Zhao Y., Wang J., Gebre A.K., Chisholm J.W., Parks J.S.
  Biochemistry 42:13941-13949(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBSTRATE SPECIFICITY, MUTAGENESIS OF GLU-173, FUNCTION, CATALYTIC ACTIVITY.
- Ref.19
  "LCAT synthesized by primary astrocytes esterifies cholesterol on glia-derived lipoproteins."
  Hirsch-Reinshagen V., Donkin J., Stukas S., Chan J., Wilkinson A., Fan J., Parks J.S., Kuivenhoven J.A., Lutjohann D., Pritchard H., Wellington C.L.
  J. Lipid Res. 50:885-893(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: ACTIVITY REGULATION, SUBCELLULAR LOCATION, FUNCTION.
- Ref.20
  "The high resolution crystal structure of human LCAT."
  Piper D.E., Romanow W.G., Gunawardane R.N., Fordstrom P., Masterman S., Pan O., Thibault S.T., Zhang R., Meininger D., Schwarz M., Wang Z., King C., Zhou M., Walker N.P.
  J. Lipid Res. 56:1711-1719(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-440, DISULFIDE BONDS, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-108; ASN-296 AND ASN-408.
- Ref.21
  "Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase."
  Glukhova A., Hinkovska-Galcheva V., Kelly R., Abe A., Shayman J.A., Tesmer J.J.
  Nat. Commun. 6:6250-6250(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (8.69 ANGSTROMS) OF 45-421, CATALYTIC ACTIVITY, DISULFIDE BONDS, GLYCOSYLATION AT ASN-108; ASN-296 AND ASN-408.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
a 1,2-diacyl-sn-glycero-3-phosphocholine
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+
a sterol
zoom
=
a 1-acyl-sn-glycero-3-phosphocholine
zoom
+
a sterol ester
zoom

Activity regulationⁱ

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

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.

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	173	Determinant for substrate specificity1 Publication	1
Active siteⁱ	205	Nucleophile1 Publication	1
Active siteⁱ	369	Charge relay system1 Publication	1
Active siteⁱ	401	Charge relay system1 Publication	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase
Biological process	Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDAⁱ	2.3.1.43 2681
Reactomeⁱ	R-HSA-8964058 HDL remodeling
SABIO-RKⁱ	P04180
SIGNORⁱ	P04180

Protein family/group databases

ESTHERⁱ	human-LCAT PC-sterol_acyltransferase

ESTHERⁱ

human-LCAT PC-sterol_acyltransferase

Chemistry databases

SwissLipidsⁱ	SLP:000000660

SwissLipidsⁱ

SLP:000000660

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Phosphatidylcholine-sterol acyltransferase (EC:2.3.1.437 Publications) Alternative name(s): Lecithin-cholesterol acyltransferase Phospholipid-cholesterol acyltransferase
Gene namesⁱ	Name:LCAT
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 16

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6522 LCAT
MIMⁱ	606967 gene
neXtProtⁱ	NX_P04180

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

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 key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_004251	17	L → LLLPPAAPFWL in LCATD.	1
Natural variantⁱVAR_039020	29	N → I in LCATD. 1 Publication	1
Natural variantⁱVAR_039022	37	T → M in LCATD. 1 PublicationCorresponds to variant dbSNP:rs971887742Ensembl.	1
Natural variantⁱVAR_004253	54	G → S in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1461145750Ensembl.	1
Natural variantⁱVAR_004254	57	G → R in LCATD. 1 Publication	1
Natural variantⁱVAR_004255	117	A → T in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940886EnsemblClinVar.	1
Natural variantⁱVAR_004257	159	R → W in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28940887EnsemblClinVar.	1
Natural variantⁱVAR_039028	164	R → C in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1380009545Ensembl.	1
Natural variantⁱVAR_004258	164	R → 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_004259	171	R → W in LCATD. 2 Publications	1
Natural variantⁱVAR_004260	180	Y → N in LCATD. Corresponds to variant dbSNP:rs749740660Ensembl.	1
Natural variantⁱVAR_039030	205	S → N in LCATD. 1 Publication	1
Natural variantⁱVAR_004262	233	L → P in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28942087EnsemblClinVar.	1
Natural variantⁱVAR_039031	242	K → N in LCATD. 1 Publication	1
Natural variantⁱVAR_004263	252	N → K in LCATD. 1 PublicationCorresponds to variant dbSNP:rs121908049EnsemblClinVar.	1
Natural variantⁱVAR_039032	268	R → H in LCATD. 1 PublicationCorresponds to variant dbSNP:rs780824776Ensembl.	1
Natural variantⁱVAR_039033	298	T → A in FED and LCATD. 2 Publications	1
Natural variantⁱVAR_039034	298	T → I in LCATD. 1 Publication	1
Natural variantⁱVAR_004265	317	M → I in LCATD; partially defective enzyme. 2 PublicationsCorresponds to variant dbSNP:rs121908048EnsemblClinVar.	1
Natural variantⁱVAR_039035	331	P → S in LCATD. 1 Publication	1
Natural variantⁱVAR_039036	333	V → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs776035233EnsemblClinVar.	1
Natural variantⁱVAR_004266	345	T → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940888EnsemblClinVar.	1
Natural variantⁱVAR_039038	406	F → V in LCATD. 1 Publication	1

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 key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_004252	34	P → L in FED. 1 PublicationCorresponds to variant dbSNP:rs121908051EnsemblClinVar.	1
Natural variantⁱVAR_039021	34	P → Q in FED. 1 Publication	1
Natural variantⁱVAR_039023	70	V → E in FED. 1 PublicationCorresponds to variant dbSNP:rs748427834Ensembl.	1
Natural variantⁱVAR_066862	99	W → S in FED; loss of activity. 1 Publication	1
Natural variantⁱVAR_039026	123	R → C in FED. 1 PublicationCorresponds to variant dbSNP:rs140068549EnsemblClinVar.	1
Natural variantⁱVAR_004256	147	T → I in FED. 1 PublicationCorresponds to variant dbSNP:rs121908050EnsemblClinVar.	1
Natural variantⁱVAR_039027	159	R → Q in FED. 1 PublicationCorresponds to variant dbSNP:rs768017317Ensembl.	1
Natural variantⁱVAR_004264	276	M → K in FED. 1 PublicationCorresponds to variant dbSNP:rs121908054EnsemblClinVar.	1
Natural variantⁱVAR_039033	298	T → A in FED and LCATD. 2 Publications	1
Natural variantⁱVAR_066867	338	L → F in FED; results in reduced protein secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs1330635214Ensembl.	1
Natural variantⁱVAR_066868	347	R → C in FED; results in reduced activity. 1 PublicationCorresponds to variant dbSNP:rs202017590EnsemblClinVar.	1
Natural variantⁱVAR_004267	371	T → M in FED. 1 PublicationCorresponds to variant dbSNP:rs121908053EnsemblClinVar.	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	173	E → A: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication	1
Mutagenesisⁱ	173	E → D: Little change in enzyme specific activity nor in PAPC/POPC activity ratio. 1 Publication	1
Mutagenesisⁱ	173	E → K: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication	1
Mutagenesisⁱ	173	E → L: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication	1
Mutagenesisⁱ	173	E → Q: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication	1

Keywords - Diseaseⁱ

Corneal dystrophy, Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3931
MalaCards human disease database More...MalaCardsⁱ	LCAT
MIMⁱ	136120 phenotype 245900 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000213398
Orphanetⁱ	79293 Familial LCAT deficiency 79292 Fish-eye disease
PharmGKBⁱ	PA226

Miscellaneous databases

Pharosⁱ	P04180

Pharosⁱ

P04180

Chemistry databases

ChEMBLⁱ	CHEMBL5942

ChEMBLⁱ

CHEMBL5942

Polymorphism and mutation databases

BioMutaⁱ	LCAT
DMDMⁱ	125993

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 24	1 PublicationAdd BLAST		24
ChainⁱPRO_0000017802	25 – 440	Phosphatidylcholine-sterol acyltransferaseAdd BLAST		416

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	44	N-linked (GlcNAc...) (complex) asparagine2 Publications	1
Disulfide bondⁱ	74 ↔ 98	Combined sources2 Publications
Glycosylationⁱ	108	N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications	1
Glycosylationⁱ	296	N-linked (GlcNAc...) (complex) asparagineCombined sources3 Publications	1
Disulfide bondⁱ	337 ↔ 380	Combined sources2 Publications
Glycosylationⁱ	408	N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications	1
Glycosylationⁱ	431	O-linked (GalNAc...) threonine1 Publication	1
Glycosylationⁱ	433	O-linked (GalNAc...) serine1 Publication	1

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

MassIVEⁱ	P04180
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P04180
PaxDbⁱ	P04180
PeptideAtlas More...PeptideAtlasⁱ	P04180
PRIDEⁱ	P04180
ProteomicsDBⁱ	51671

PTM databases

GlyConnectⁱ	495
iPTMnetⁱ	P04180
PhosphoSitePlusⁱ	P04180
UniCarbKBⁱ	P04180

Expressionⁱ

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

Bgeeⁱ	ENSG00000213398 Expressed in 136 organ(s), highest expression level in right lobe of liver
ExpressionAtlasⁱ	P04180 baseline and differential
Genevisibleⁱ	P04180 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA044767

HPAⁱ

HPA044767

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
APOA1	P02647	2	EBI-9104464,EBI-701692

With

Entry

#Exp.

IntAct

Notes

APOA1

P02647

2

EBI-9104464,EBI-701692

GO - Molecular functionⁱ

apolipoprotein A-I binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- "Interaction of rat lecithin-cholesterol acyltransferase with rat apolipoprotein A-I and with lecithin-cholesterol vesicles."
  Furukawa Y., Urano T., Hida Y., Itoh H., Takahashi C., Kimura S.
  J. Biochem. 111:413-418(1992) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	110123, 6 interactors
Database of interacting proteins More...DIPⁱ	DIP-29620N
IntActⁱ	P04180, 1 interactor
STRINGⁱ	9606.ENSP00000264005

Chemistry databases

BindingDBⁱ

P04180

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	49 – 52	Combined sources	4
Beta strandⁱ	60 – 63	Combined sources	4
Beta strandⁱ	82 – 86	Combined sources	5
Helixⁱ	88 – 91	Combined sources	4
Helixⁱ	95 – 103	Combined sources	9
Beta strandⁱ	105 – 107	Combined sources	3
Turnⁱ	109 – 111	Combined sources	3
Beta strandⁱ	114 – 117	Combined sources	4
Beta strandⁱ	121 – 123	Combined sources	3
Turnⁱ	125 – 128	Combined sources	4
Helixⁱ	131 – 134	Combined sources	4
Beta strandⁱ	135 – 137	Combined sources	3
Beta strandⁱ	142 – 145	Combined sources	4
Helixⁱ	146 – 153	Combined sources	8
Turnⁱ	154 – 156	Combined sources	3
Turnⁱ	160 – 162	Combined sources	3
Beta strandⁱ	163 – 165	Combined sources	3
Helixⁱ	174 – 176	Combined sources	3
Helixⁱ	178 – 195	Combined sources	18
Beta strandⁱ	199 – 204	Combined sources	6
Helixⁱ	206 – 217	Combined sources	12
Helixⁱ	220 – 226	Combined sources	7
Beta strandⁱ	227 – 234	Combined sources	8
Helixⁱ	242 – 248	Combined sources	7
Turnⁱ	250 – 252	Combined sources	3
Turnⁱ	255 – 257	Combined sources	3
Beta strandⁱ	258 – 260	Combined sources	3
Beta strandⁱ	270 – 272	Combined sources	3
Helixⁱ	274 – 276	Combined sources	3
Turnⁱ	280 – 282	Combined sources	3
Beta strandⁱ	288 – 291	Combined sources	4
Beta strandⁱ	296 – 298	Combined sources	3
Helixⁱ	299 – 301	Combined sources	3
Helixⁱ	302 – 308	Combined sources	7
Helixⁱ	312 – 321	Combined sources	10
Turnⁱ	322 – 327	Combined sources	6
Beta strandⁱ	335 – 350	Combined sources	16
Turnⁱ	353 – 357	Combined sources	5
Beta strandⁱ	361 – 373	Combined sources	13
Helixⁱ	374 – 377	Combined sources	4
Helixⁱ	378 – 383	Combined sources	6
Beta strandⁱ	386 – 389	Combined sources	4
Beta strandⁱ	391 – 397	Combined sources	7
Helixⁱ	401 – 403	Combined sources	3
Turnⁱ	404 – 406	Combined sources	3
Helixⁱ	408 – 419	Combined sources	12
Turnⁱ	420 – 422	Combined sources	3

Show more details

3D structure databases

SMRⁱ	P04180
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	426 – 439	Pro-richAdd BLAST		14

Sequence similaritiesⁱ

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	KOG2369 Eukaryota ENOG410Y9CF LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000160052
HOGENOMⁱ	HOG000238654
InParanoidⁱ	P04180
KEGG Orthology (KO) More...KOⁱ	K00650
OMAⁱ	LPTPHTY
Database of Orthologous Groups More...OrthoDBⁱ	388324at2759
PhylomeDBⁱ	P04180
TreeFamⁱ	TF313258

Family and domain databases

Gene3Dⁱ	3.40.50.1820, 1 hit
InterProⁱ	View protein in InterPro IPR029058 AB_hydrolase IPR003386 LACT/PDAT_acylTrfase
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02450 LCAT, 1 hit
SUPFAMⁱ	SSF53474 SSF53474, 1 hit
PROSITEⁱ	View protein in PROSITE PS00120 LIPASE_SER, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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 all Align All

P04180-1 [UniParc]FASTA Add 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

Checksum:ⁱB315EF118AA7A378

GO

Computationally mapped potential isoform sequencesⁱ

There are 6 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

I3L0J6	I3L0J6_HUMAN	Phosphatidylcholine-sterol acyltran... Phosphatidylcholine-sterol acyltransferase	LCAT	80	Annotation score:
I3L1Q6	I3L1Q6_HUMAN	Phosphatidylcholine-sterol acyltran... Phosphatidylcholine-sterol acyltransferase	LCAT	107	Annotation score:
J3QSE5	J3QSE5_HUMAN	Phosphatidylcholine-sterol acyltran... Phosphatidylcholine-sterol acyltransferase	LCAT	255	Annotation score:
J3QKT0	J3QKT0_HUMAN	Phosphatidylcholine-sterol acyltran... Phosphatidylcholine-sterol acyltransferase	LCAT	138	Annotation score:
I3L3R0	I3L3R0_HUMAN	Phosphatidylcholine-sterol acyltran... Phosphatidylcholine-sterol acyltransferase	LCAT	93	Annotation score:
I3L215	I3L215_HUMAN	Phosphatidylcholine-sterol acyltran... Phosphatidylcholine-sterol acyltransferase	LCAT	61	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	257	I → H in CAB56610 (PubMed:2823898).Curated		1
Sequence conflictⁱ	257	I → H in AAA59499 (PubMed:2823898).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_004251	17	L → LLLPPAAPFWL in LCATD.	1
Natural variantⁱVAR_039020	29	N → I in LCATD. 1 Publication	1
Natural variantⁱVAR_004252	34	P → L in FED. 1 PublicationCorresponds to variant dbSNP:rs121908051EnsemblClinVar.	1
Natural variantⁱVAR_039021	34	P → Q in FED. 1 Publication	1
Natural variantⁱVAR_039022	37	T → M in LCATD. 1 PublicationCorresponds to variant dbSNP:rs971887742Ensembl.	1
Natural variantⁱVAR_004253	54	G → S in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1461145750Ensembl.	1
Natural variantⁱVAR_004254	57	G → R in LCATD. 1 Publication	1
Natural variantⁱVAR_039023	70	V → E in FED. 1 PublicationCorresponds to variant dbSNP:rs748427834Ensembl.	1
Natural variantⁱVAR_039024	95	G → R in a compound heterozygote carrying H-164; intermediate phenotype between LCATD and FED; reduction of activity. 1 Publication	1
Natural variantⁱVAR_066862	99	W → S in FED; loss of activity. 1 Publication	1
Natural variantⁱVAR_039025	115	S → P1 PublicationCorresponds to variant dbSNP:rs1412883954Ensembl.	1
Natural variantⁱVAR_004255	117	A → T in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940886EnsemblClinVar.	1
Natural variantⁱVAR_039026	123	R → C in FED. 1 PublicationCorresponds to variant dbSNP:rs140068549EnsemblClinVar.	1
Natural variantⁱVAR_066863	134 – 135	EY → DN in a patient with low HDL-cholesterol levels; results in reduced activity. 1 Publication	2
Natural variantⁱVAR_004256	147	T → I in FED. 1 PublicationCorresponds to variant dbSNP:rs121908050EnsemblClinVar.	1
Natural variantⁱVAR_039027	159	R → Q in FED. 1 PublicationCorresponds to variant dbSNP:rs768017317Ensembl.	1
Natural variantⁱVAR_004257	159	R → W in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28940887EnsemblClinVar.	1
Natural variantⁱVAR_039028	164	R → C in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1380009545Ensembl.	1
Natural variantⁱVAR_004258	164	R → 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_039029	165	A → T1 PublicationCorresponds to variant dbSNP:rs1369994093Ensembl.	1
Natural variantⁱVAR_004259	171	R → W in LCATD. 2 Publications	1
Natural variantⁱVAR_004260	180	Y → N in LCATD. Corresponds to variant dbSNP:rs749740660Ensembl.	1
Natural variantⁱVAR_004261	182	R → C2 PublicationsCorresponds to variant dbSNP:rs387906300EnsemblClinVar.	1
Natural variantⁱVAR_039030	205	S → N in LCATD. 1 Publication	1
Natural variantⁱVAR_017030	232	S → T3 PublicationsCorresponds to variant dbSNP:rs4986970Ensembl.	1
Natural variantⁱVAR_004262	233	L → P in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28942087EnsemblClinVar.	1
Natural variantⁱVAR_039031	242	K → N in LCATD. 1 Publication	1
Natural variantⁱVAR_066864	246	V → F in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive. 1 Publication	1
Natural variantⁱVAR_004263	252	N → K in LCATD. 1 PublicationCorresponds to variant dbSNP:rs121908049EnsemblClinVar.	1
Natural variantⁱVAR_066865	268	R → 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_039032	268	R → H in LCATD. 1 PublicationCorresponds to variant dbSNP:rs780824776Ensembl.	1
Natural variantⁱVAR_004264	276	M → K in FED. 1 PublicationCorresponds to variant dbSNP:rs121908054EnsemblClinVar.	1
Natural variantⁱVAR_039033	298	T → A in FED and LCATD. 2 Publications	1
Natural variantⁱVAR_039034	298	T → I in LCATD. 1 Publication	1
Natural variantⁱVAR_004265	317	M → I in LCATD; partially defective enzyme. 2 PublicationsCorresponds to variant dbSNP:rs121908048EnsemblClinVar.	1
Natural variantⁱVAR_066866	322	R → C in a patient with low HDL-cholesterol levels; reduced protein secretion. 1 PublicationCorresponds to variant dbSNP:rs1407191796Ensembl.	1
Natural variantⁱVAR_039035	331	P → S in LCATD. 1 Publication	1
Natural variantⁱVAR_039036	333	V → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs776035233EnsemblClinVar.	1
Natural variantⁱVAR_066867	338	L → F in FED; results in reduced protein secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs1330635214Ensembl.	1
Natural variantⁱVAR_004266	345	T → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940888EnsemblClinVar.	1
Natural variantⁱVAR_066868	347	R → C in FED; results in reduced activity. 1 PublicationCorresponds to variant dbSNP:rs202017590EnsemblClinVar.	1
Natural variantⁱVAR_004267	371	T → M in FED. 1 PublicationCorresponds to variant dbSNP:rs121908053EnsemblClinVar.	1
Natural variantⁱVAR_039037	396	L → R in a patient with LCATD. 2 Publications	1
Natural variantⁱVAR_039038	406	F → V in LCATD. 1 Publication	1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10854.1
PIRⁱ	A00571 XXHUN
NCBI Reference Sequences More...RefSeqⁱ	NP_000220.1, NM_000229.1

Genome annotation databases

Ensemblⁱ	ENST00000264005; ENSP00000264005; ENSG00000213398
GeneIDⁱ	3931
KEGGⁱ	hsa:3931
UCSC genome browser More...UCSCⁱ	uc002euy.2 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P04180	Testicular secretory protein Li 24		HUMAN		440	UniRef100_P04180
LCAT isoform 1		PANTR		440
Uncharacterized protein		PANPA		440
Phosphatidylcholine-sterol acyltransferase (Fragment)		HUMAN		255
LCAT isoform 3 (Fragment)		PANTR		255

Protein	Similar proteins		Species	Score	Length	Source
P04180	Phosphatidylcholine-sterol acyltransferase		PAPAN		440	UniRef90_P04180
Testicular secretory protein Li 24		HUMAN		440
LCAT isoform 1		PANTR		440
Uncharacterized protein		PANPA		440
Uncharacterized protein		CALJA		442
+43

Protein	Similar proteins		Species	Score	Length	Source
P04180	Phosphatidylcholine-sterol acyltransferase		PAPAN		440	UniRef50_P04180
Phosphatidylcholine-sterol acyltransferase (Fragment)		CHICK		413
Phosphatidylcholine-sterol acyltransferase		RABIT		440
Phosphatidylcholine-sterol acyltransferase		RAT		440
Phosphatidylcholine-sterol acyltransferase		MOUSE		438
+423

Cross-referencesⁱ

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
CCDSⁱ	CCDS10854.1
PIRⁱ	A00571 XXHUN
RefSeqⁱ	NP_000220.1, NM_000229.1

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4X96	X-ray	8.69	A/B/C/D	45-421	[»]
	4XWG	X-ray	2.65	A	25-440	[»]
	4XX1	X-ray	3.60	A/B/J	25-440	[»]
	5BV7	X-ray	2.45	A	25-440	[»]
	5TXF	X-ray	3.10	A/B/C/D	25-440	[»]
	6MVD	X-ray	3.10	A/B	45-421	[»]
SMRⁱ	P04180
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110123, 6 interactors
DIPⁱ	DIP-29620N
IntActⁱ	P04180, 1 interactor
STRINGⁱ	9606.ENSP00000264005

Chemistry databases

BindingDBⁱ	P04180
ChEMBLⁱ	CHEMBL5942
SwissLipidsⁱ	SLP:000000660

Protein family/group databases

ESTHERⁱ	human-LCAT PC-sterol_acyltransferase

ESTHERⁱ

human-LCAT PC-sterol_acyltransferase

PTM databases

GlyConnectⁱ	495
iPTMnetⁱ	P04180
PhosphoSitePlusⁱ	P04180
UniCarbKBⁱ	P04180

Polymorphism and mutation databases

BioMutaⁱ	LCAT
DMDMⁱ	125993

Proteomic databases

MassIVEⁱ	P04180
MaxQBⁱ	P04180
PaxDbⁱ	P04180
PeptideAtlasⁱ	P04180
PRIDEⁱ	P04180
ProteomicsDBⁱ	51671

Protocols and materials databases

ABCDⁱ	P04180
The DNASU plasmid repository More...DNASUⁱ	3931

Genome annotation databases

Ensemblⁱ	ENST00000264005; ENSP00000264005; ENSG00000213398
GeneIDⁱ	3931
KEGGⁱ	hsa:3931
UCSCⁱ	uc002euy.2 human

Organism-specific databases

CTDⁱ	3931
DisGeNETⁱ	3931
GeneCardsⁱ	LCAT
HGNCⁱ	HGNC:6522 LCAT
HPAⁱ	HPA044767
MalaCardsⁱ	LCAT
MIMⁱ	136120 phenotype 245900 phenotype 606967 gene
neXtProtⁱ	NX_P04180
OpenTargetsⁱ	ENSG00000213398
Orphanetⁱ	79293 Familial LCAT deficiency 79292 Fish-eye disease
PharmGKBⁱ	PA226
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2369 Eukaryota ENOG410Y9CF LUCA
GeneTreeⁱ	ENSGT00940000160052
HOGENOMⁱ	HOG000238654
InParanoidⁱ	P04180
KOⁱ	K00650
OMAⁱ	LPTPHTY
OrthoDBⁱ	388324at2759
PhylomeDBⁱ	P04180
TreeFamⁱ	TF313258

Enzyme and pathway databases

BRENDAⁱ	2.3.1.43 2681
Reactomeⁱ	R-HSA-8964058 HDL remodeling
SABIO-RKⁱ	P04180
SIGNORⁱ	P04180

Miscellaneous databases

ChiTaRSⁱ	LCAT human
GeneWikiⁱ	Lecithin%E2%80%94cholesterol_acyltransferase
GenomeRNAiⁱ	3931
Pharosⁱ	P04180
Protein Ontology More...PROⁱ	PR:P04180
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000213398 Expressed in 136 organ(s), highest expression level in right lobe of liver
ExpressionAtlasⁱ	P04180 baseline and differential
Genevisibleⁱ	P04180 HS

Family and domain databases

Gene3Dⁱ	3.40.50.1820, 1 hit
InterProⁱ	View protein in InterPro IPR029058 AB_hydrolase IPR003386 LACT/PDAT_acylTrfase
Pfamⁱ	View protein in Pfam PF02450 LCAT, 1 hit
SUPFAMⁱ	SSF53474 SSF53474, 1 hit
PROSITEⁱ	View protein in PROSITE PS00120 LIPASE_SER, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LCAT_HUMAN
Accessionⁱ	P04180Primary (citable) accession number: P04180 Secondary accession number(s): Q53XQ3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
	Last sequence update:	March 20, 1987
	Last modified:	October 16, 2019
	This is version 202 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

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UniProtKB - P04180 (LCAT_HUMAN)

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Phosphatidylcholine-sterol acyltransferase

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<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

Miscellaneous

<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 ‘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

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GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

Chemistry databases

<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

Organism-specific databases

<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

Extracellular region or secreted

Keywords - Cellular componenti

<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

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Keywords - Diseasei

Organism-specific databases

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Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

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Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

<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

<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

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ