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UniProtKB - P19835 (CEL_HUMAN)

Protein

Bile salt-activated lipase

Gene

CEL

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 fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.

<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 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

Activated by bile salts containing a 7-hydroxyl group.

<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=24 µM for lipoyl-4-aminobenzoate1 Publication
  2. KM=15 µM for triacetin1 Publication
  1. Vmax=45.5 pmol/min/mg enzyme toward lipoyl-4-aminobenzoate1 Publication
  2. Vmax=323 pmol/min/mg enzyme toward triacetin1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei214Acyl-ester intermediatePROSITE-ProRule annotation1 Publication1
Active sitei340Charge relay system1 Publication1
Active sitei455Charge 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

  • acylglycerol lipase activity Source: Reactome
  • catalytic activity Source: UniProtKB
  • heparin binding Source: UniProtKB
  • hydrolase activity Source: UniProtKB
  • neurexin family protein binding Source: GO_Central
  • signaling receptor activity Source: GO_Central
  • sterol esterase activity Source: GO_Central
  • triglyceride lipase activity Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Molecular functionHydrolase, Serine esterase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-192456 Digestion of dietary lipid

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P19835

Protein family/group databases

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

More...ESTHERi		human-CEL Cholesterol_esterase

MEROPS protease database

More...MEROPSi		S09.985

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000874

<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:
Bile salt-activated lipase (EC:3.1.1.13, EC:3.1.1.3)
Short name:
BAL
Alternative name(s):
Bile salt-stimulated lipase
Short name:
BSSL
Bucelipase
Carboxyl ester lipase
Cholesterol esterase
Pancreatic lysophospholipase
Sterol esterase
<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:CEL
Synonyms:BAL
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_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: Unplaced

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:1848 CEL

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		114840 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P19835

<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; 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

Maturity-onset diabetes of the young 8 with exocrine dysfunction (MODY8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. The disease can be caused by frameshift deletions in the variable number of tandem repeats (VNTR)-containing exon 11 of the CEL gene (PubMed:16369531).1 Publication
Disease descriptionA form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.
See also OMIM:609812

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>Mutagenesisi455H → Q: Abolishes lipase activity. Decreases Vmax for esterase activity by 2.5-fold. 1 Publication1

Keywords - Diseasei

Diabetes mellitus

Organism-specific databases

DisGeNET

More...DisGeNETi		1056

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		CEL

MalaCards human disease database

More...MalaCardsi		CEL
MIMi606391 phenotype
609812 phenotype

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

More...Orphaneti		552 MODY

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26391

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3219

Drug and drug target database

More...DrugBanki		DB04348 Taurocholic Acid

Polymorphism and mutation databases

Domain mapping of disease mutations (DMDM)

More...DMDMi		251757481

<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 – 201 PublicationAdd BLAST20
<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_000000863121 – 753Bile salt-activated lipaseAdd BLAST733

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi84 ↔ 100
<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>GlycosylationiCAR_000141207N-linked (GlcNAc...) (complex) asparagine1
Disulfide bondi266 ↔ 277
Glycosylationi558O-linked (GalNAc...) threonine1 Publication1
Glycosylationi569O-linked (GalNAc...) threonine1 Publication1
Glycosylationi579O-linked (GalNAc...) threonine1 Publication1
Glycosylationi607O-linked (GalNAc...) threonine1 Publication1
Glycosylationi618O-linked (GalNAc...) threonine1 Publication1
Glycosylationi629O-linked (GalNAc...) threonine1 Publication1
Glycosylationi640O-linked (GalNAc...) threonine1 Publication1
Glycosylationi651O-linked (GalNAc...) threonine1 Publication1
Glycosylationi662O-linked (GalNAc...) threonine1 Publication1
Glycosylationi673O-linked (GalNAc...) threonine1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

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

More...PaxDbi		P19835

PeptideAtlas

More...PeptideAtlasi		P19835

PRoteomics IDEntifications database

More...PRIDEi		P19835

ProteomicsDB human proteome resource

More...ProteomicsDBi		53692
53693 [P19835-2]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		74

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P19835

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

More...PhosphoSitePlusi		P19835

UniCarbKB; an annotated and curated database of glycan structures

More...UniCarbKBi		P19835

<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

Mammary gland and pancreas. Expressed by eosinophils.1 Publication

Gene expression databases

CleanEx database of gene expression profiles

More...CleanExi		HS_CEL

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA008023
HPA052701

<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

Interacts with CLC.1 Publication

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P19835, 1 interactor

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000361151

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P19835

<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

1753
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P19835

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

More...SMRi		P19835

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P19835

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati559 – 5691Add BLAST11
Repeati570 – 5802Add BLAST11
Repeati581 – 5913Add BLAST11
Repeati592 – 6024Add BLAST11
Repeati603 – 6135Add BLAST11
Repeati614 – 6246Add BLAST11
Repeati625 – 6357Add BLAST11
Repeati636 – 6468Add BLAST11
Repeati647 – 6579Add BLAST11
Repeati658 – 66810Add BLAST11
Repeati669 – 67911Add BLAST11
Repeati680 – 69012Add BLAST11
Repeati691 – 70113Add BLAST11
Repeati702 – 71214Add BLAST11
Repeati713 – 72315Add BLAST11
Repeati724 – 73416Add BLAST11
Repeati735 – 74517Add BLAST11

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>Regioni21 – 121Heparin-bindingAdd BLAST101
Regioni559 – 74517 X 11 AA tandem repeats, glycodomain, O-linked (mucin type)Add BLAST187

<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 type-B carboxylesterase/lipase family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1516 Eukaryota
COG2272 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000091866

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG008839

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P19835

Database for complete collections of gene phylogenies

More...PhylomeDBi		P19835

TreeFam database of animal gene trees

More...TreeFami		TF315470

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029058 AB_hydrolase
IPR033560 BAL
IPR002018 CarbesteraseB
IPR019826 Carboxylesterase_B_AS
IPR019819 Carboxylesterase_B_CS
IPR032059 Mucin-like

The PANTHER Classification System

More...PANTHERi		PTHR43903:SF1 PTHR43903:SF1, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00135 COesterase, 1 hit
PF16058 Mucin-like, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53474 SSF53474, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00122 CARBOXYLESTERASE_B_1, 1 hit
PS00941 CARBOXYLESTERASE_B_2, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)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 describes 2 <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 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform Long (identifier: P19835-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MGRLQLVVLG LTCCWAVASA AKLGAVYTEG GFVEGVNKKL GLLGDSVDIF 
        60         70         80         90        100
KGIPFAAPTK ALENPQPHPG WQGTLKAKNF KKRCLQATIT QDSTYGDEDC 
       110        120        130        140        150
LYLNIWVPQG RKQVSRDLPV MIWIYGGAFL MGSGHGANFL NNYLYDGEEI 
       160        170        180        190        200
ATRGNVIVVT FNYRVGPLGF LSTGDANLPG NYGLRDQHMA IAWVKRNIAA 
       210        220        230        240        250
FGGDPNNITL FGESAGGASV SLQTLSPYNK GLIRRAISQS GVALSPWVIQ 
       260        270        280        290        300
KNPLFWAKKV AEKVGCPVGD AARMAQCLKV TDPRALTLAY KVPLAGLEYP 
       310        320        330        340        350
MLHYVGFVPV IDGDFIPADP INLYANAADI DYIAGTNNMD GHIFASIDMP 
       360        370        380        390        400
AINKGNKKVT EEDFYKLVSE FTITKGLRGA KTTFDVYTES WAQDPSQENK 
       410        420        430        440        450
KKTVVDFETD VLFLVPTEIA LAQHRANAKS AKTYAYLFSH PSRMPVYPKW 
       460        470        480        490        500
VGADHADDIQ YVFGKPFATP TGYRPQDRTV SKAMIAYWTN FAKTGDPNMG 
       510        520        530        540        550
DSAVPTHWEP YTTENSGYLE ITKKMGSSSM KRSLRTNFLR YWTLTYLALP 
       560        570        580        590        600
TVTDQEATPV PPTGDSEATP VPPTGDSETA PVPPTGDSGA PPVPPTGDSG 
       610        620        630        640        650
APPVPPTGDS GAPPVPPTGD SGAPPVPPTG DSGAPPVPPT GDSGAPPVPP 
       660        670        680        690        700
TGDSGAPPVP PTGDSGAPPV PPTGDAGPPP VPPTGDSGAP PVPPTGDSGA 
       710        720        730        740        750
PPVTPTGDSE TAPVPPTGDS GAPPVPPTGD SEAAPVPPTD DSKEAQMPAV 

IRF
Length:753
Mass (Da):79,322
Last modified:July 7, 2009 - 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:iB3253789D1EABF7F
GO
Isoform Short (identifier: P19835-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     430-495: Missing.

Show »
Length:687
Mass (Da):71,834
Checksum:iBD269A05F7FBB9CF
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
X6R868X6R868_HUMAN
Bile salt-activated lipase
CEL
756Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA51973 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAA52014 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAC26514 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA38325 differs from that shown. Reason: Erroneous initiation.Curated
The sequence EAW88033 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti73Missing AA sequence (PubMed:8471055).Curated1
Sequence conflicti235R → A in AAB35488 (PubMed:7578248).Curated1
Sequence conflicti284 – 288RALTL → AAVTV in AAB35488 (PubMed:7578248).Curated5
Sequence conflicti313G → E in AAB35488 (PubMed:7578248).Curated1
Sequence conflicti403T → I in AAB35488 (PubMed:7578248).Curated1
Sequence conflicti481S → F in AAB35488 (PubMed:7578248).Curated1
Sequence conflicti689A → P in AAB35488 (PubMed:7578248).Curated1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_001463430 – 495Missing in isoform Short. CuratedAdd BLAST66

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
X54457 mRNA Translation: CAA38325.1 Different initiation.
M85201 mRNA Translation: AAA52014.1 Different initiation.
M54994 mRNA Translation: AAA63211.1
M94579 Genomic DNA Translation: AAA51973.1 Different initiation.
S79774 mRNA Translation: AAB35488.2
AF072711 Genomic DNA Translation: AAC26514.1 Different initiation.
AL162417 Genomic DNA No translation available.
CH471090 Genomic DNA Translation: EAW88033.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...PIRi		S13586

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.533258

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000351304; ENSP00000342217; ENSG00000170835

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
X54457 mRNA Translation: CAA38325.1 Different initiation.
M85201 mRNA Translation: AAA52014.1 Different initiation.
M54994 mRNA Translation: AAA63211.1
M94579 Genomic DNA Translation: AAA51973.1 Different initiation.
S79774 mRNA Translation: AAB35488.2
AF072711 Genomic DNA Translation: AAC26514.1 Different initiation.
AL162417 Genomic DNA No translation available.
CH471090 Genomic DNA Translation: EAW88033.1 Different initiation.
PIRiS13586
UniGeneiHs.533258

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
1F6WX-ray2.30A21-553[»]
1JMYX-ray2.60A21-538[»]
ProteinModelPortaliP19835
SMRiP19835
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP19835, 1 interactor
STRINGi9606.ENSP00000361151

Chemistry databases

BindingDBiP19835
ChEMBLiCHEMBL3219
DrugBankiDB04348 Taurocholic Acid
SwissLipidsiSLP:000000874

Protein family/group databases

ESTHERihuman-CEL Cholesterol_esterase
MEROPSiS09.985

PTM databases

GlyConnecti74
iPTMnetiP19835
PhosphoSitePlusiP19835
UniCarbKBiP19835

Polymorphism and mutation databases

DMDMi251757481

Proteomic databases

PaxDbiP19835
PeptideAtlasiP19835
PRIDEiP19835
ProteomicsDBi53692
53693 [P19835-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000351304; ENSP00000342217; ENSG00000170835

Organism-specific databases

DisGeNETi1056

GeneCards: human genes, protein and diseases

More...GeneCardsi		CEL
GeneReviewsiCEL
HGNCiHGNC:1848 CEL
HPAiHPA008023
HPA052701
MalaCardsiCEL
MIMi114840 gene
606391 phenotype
609812 phenotype
neXtProtiNX_P19835
Orphaneti552 MODY
PharmGKBiPA26391

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1516 Eukaryota
COG2272 LUCA
HOGENOMiHOG000091866
HOVERGENiHBG008839
InParanoidiP19835
PhylomeDBiP19835
TreeFamiTF315470

Enzyme and pathway databases

ReactomeiR-HSA-192456 Digestion of dietary lipid
SABIO-RKiP19835

Miscellaneous databases

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

More...ChiTaRSi		CEL human
EvolutionaryTraceiP19835

Protein Ontology

More...PROi		PR:P19835

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

CleanExiHS_CEL

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR033560 BAL
IPR002018 CarbesteraseB
IPR019826 Carboxylesterase_B_AS
IPR019819 Carboxylesterase_B_CS
IPR032059 Mucin-like
PANTHERiPTHR43903:SF1 PTHR43903:SF1, 1 hit
PfamiView protein in Pfam
PF00135 COesterase, 1 hit
PF16058 Mucin-like, 2 hits
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00122 CARBOXYLESTERASE_B_1, 1 hit
PS00941 CARBOXYLESTERASE_B_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiCEL_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: P19835
Secondary accession number(s): Q16398
, Q5T7U7, Q9UCH1, Q9UP41
<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: February 1, 1991
Last sequence update: July 7, 2009
Last modified: December 5, 2018
This is version 186 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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