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P19835

- CEL_HUMAN

UniProt

P19835 - CEL_HUMAN

Protein

Bile salt-activated lipase

Gene

CEL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (07 Jul 2009)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication
    A steryl ester + H2O = a sterol + a fatty acid.1 Publication

    Enzyme regulationi

    Activated by bile salts containing a 7-hydroxyl group.

    Kineticsi

    1. KM=24 µM for lipoyl-4-aminobenzoate1 Publication
    2. KM=15 µM for triacetin1 Publication

    Vmax=45.5 pmol/min/mg enzyme toward lipoyl-4-aminobenzoate1 Publication

    Vmax=323 pmol/min/mg enzyme toward triacetin1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei214 – 2141Acyl-ester intermediate1 PublicationPROSITE-ProRule annotation
    Active sitei340 – 3401Charge relay system1 Publication
    Active sitei455 – 4551Charge relay system1 Publication

    GO - Molecular functioni

    1. acylglycerol lipase activity Source: Reactome
    2. catalytic activity Source: UniProtKB
    3. heparin binding Source: UniProtKB
    4. hydrolase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. sterol esterase activity Source: UniProtKB
    7. triglyceride lipase activity Source: UniProtKB

    GO - Biological processi

    1. cholesterol catabolic process Source: UniProtKB
    2. fatty acid catabolic process Source: UniProtKB
    3. intestinal cholesterol absorption Source: UniProtKB
    4. intestinal lipid catabolic process Source: UniProtKB
    5. lipid digestion Source: Reactome
    6. lipid metabolic process Source: UniProtKB
    7. pancreatic juice secretion Source: UniProtKB
    8. protein esterification Source: UniProtKB
    9. small molecule metabolic process Source: Reactome
    10. triglyceride metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_9518. Digestion of dietary lipid.
    SABIO-RKP19835.

    Protein family/group databases

    MEROPSiS09.985.

    Names & Taxonomyi

    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
    Gene namesi
    Name:CEL
    Synonyms:BAL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:1848. CEL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: RefGenome
    3. extracellular region Source: Reactome
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Maturity-onset diabetes of the young 8 with exocrine dysfunction (MODY8) [MIM:609812]: A 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.1 Publication
    Note: 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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi455 – 4551H → Q: Abolishes lipase activity. Decreases Vmax for esterase activity by 2.5-fold. 1 Publication

    Keywords - Diseasei

    Diabetes mellitus

    Organism-specific databases

    MIMi606391. phenotype.
    609812. phenotype.
    Orphaneti552. MODY syndrome.
    PharmGKBiPA26391.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Chaini21 – 753733Bile salt-activated lipasePRO_0000008631Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi84 ↔ 100
    Glycosylationi207 – 2071N-linked (GlcNAc...) (complex)CAR_000141
    Disulfide bondi266 ↔ 277
    Glycosylationi558 – 5581O-linked (GalNAc...)1 Publication
    Glycosylationi569 – 5691O-linked (GalNAc...)1 Publication
    Glycosylationi579 – 5791O-linked (GalNAc...)1 Publication
    Glycosylationi607 – 6071O-linked (GalNAc...)1 Publication
    Glycosylationi618 – 6181O-linked (GalNAc...)1 Publication
    Glycosylationi629 – 6291O-linked (GalNAc...)1 Publication
    Glycosylationi640 – 6401O-linked (GalNAc...)1 Publication
    Glycosylationi651 – 6511O-linked (GalNAc...)1 Publication
    Glycosylationi662 – 6621O-linked (GalNAc...)1 Publication
    Glycosylationi673 – 6731O-linked (GalNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP19835.
    PaxDbiP19835.
    PRIDEiP19835.

    PTM databases

    PhosphoSiteiP19835.
    UniCarbKBiP19835.

    Expressioni

    Tissue specificityi

    Mammary gland and pancreas. Expressed by eosinophils.1 Publication

    Gene expression databases

    ArrayExpressiP19835.
    BgeeiP19835.
    CleanExiHS_CEL.
    GenevestigatoriP19835.

    Organism-specific databases

    HPAiHPA008023.
    HPA052701.

    Interactioni

    Subunit structurei

    Interacts with CLC.1 Publication

    Protein-protein interaction databases

    BioGridi107485. 1 interaction.
    IntActiP19835. 1 interaction.
    STRINGi9606.ENSP00000361151.

    Structurei

    Secondary structure

    1
    753
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 284
    Beta strandi31 – 344
    Beta strandi36 – 394
    Beta strandi41 – 444
    Beta strandi46 – 549
    Beta strandi72 – 765
    Beta strandi84 – 874
    Beta strandi91 – 988
    Beta strandi102 – 1098
    Beta strandi111 – 1133
    Beta strandi117 – 1248
    Turni128 – 1303
    Beta strandi137 – 1393
    Beta strandi142 – 1454
    Helixi148 – 1547
    Beta strandi157 – 1615
    Helixi166 – 1705
    Beta strandi174 – 1785
    Helixi182 – 19716
    Turni198 – 2025
    Beta strandi203 – 21311
    Helixi215 – 22511
    Helixi227 – 2293
    Turni230 – 2323
    Beta strandi234 – 2407
    Turni246 – 2483
    Helixi253 – 26412
    Helixi271 – 28010
    Helixi283 – 2886
    Helixi302 – 3043
    Beta strandi313 – 3164
    Helixi320 – 3223
    Helixi324 – 3274
    Beta strandi330 – 3378
    Turni338 – 3414
    Helixi342 – 3487
    Helixi350 – 3534
    Beta strandi355 – 3573
    Helixi361 – 37111
    Helixi376 – 38813
    Turni398 – 4014
    Helixi402 – 41211
    Helixi414 – 42512
    Beta strandi433 – 4386
    Turni455 – 4584
    Helixi459 – 4624
    Helixi465 – 4684
    Helixi470 – 4723
    Helixi475 – 49420
    Beta strandi499 – 5024
    Turni513 – 5153
    Beta strandi518 – 5247
    Helixi527 – 5293
    Helixi536 – 5449
    Turni545 – 5484

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F6WX-ray2.30A21-553[»]
    1JMYX-ray2.60A21-538[»]
    ProteinModelPortaliP19835.
    SMRiP19835. Positions 21-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19835.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati559 – 569111Add
    BLAST
    Repeati570 – 580112Add
    BLAST
    Repeati581 – 591113Add
    BLAST
    Repeati592 – 602114Add
    BLAST
    Repeati603 – 613115Add
    BLAST
    Repeati614 – 624116Add
    BLAST
    Repeati625 – 635117Add
    BLAST
    Repeati636 – 646118Add
    BLAST
    Repeati647 – 657119Add
    BLAST
    Repeati658 – 6681110Add
    BLAST
    Repeati669 – 6791111Add
    BLAST
    Repeati680 – 6901112Add
    BLAST
    Repeati691 – 7011113Add
    BLAST
    Repeati702 – 7121114Add
    BLAST
    Repeati713 – 7231115Add
    BLAST
    Repeati724 – 7341116Add
    BLAST
    Repeati735 – 7451117Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 121101Heparin-bindingAdd
    BLAST
    Regioni559 – 74518717 X 11 AA tandem repeats, glycodomain, O-linked (mucin type)Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2272.
    HOGENOMiHOG000091866.
    HOVERGENiHBG008839.
    OrthoDBiEOG7034GN.
    PhylomeDBiP19835.
    TreeFamiTF315470.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    [Graphical view]
    PfamiPF00135. COesterase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
    PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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

    MGRLQLVVLG LTCCWAVASA AKLGAVYTEG GFVEGVNKKL GLLGDSVDIF    50
    KGIPFAAPTK ALENPQPHPG WQGTLKAKNF KKRCLQATIT QDSTYGDEDC 100
    LYLNIWVPQG RKQVSRDLPV MIWIYGGAFL MGSGHGANFL NNYLYDGEEI 150
    ATRGNVIVVT FNYRVGPLGF LSTGDANLPG NYGLRDQHMA IAWVKRNIAA 200
    FGGDPNNITL FGESAGGASV SLQTLSPYNK GLIRRAISQS GVALSPWVIQ 250
    KNPLFWAKKV AEKVGCPVGD AARMAQCLKV TDPRALTLAY KVPLAGLEYP 300
    MLHYVGFVPV IDGDFIPADP INLYANAADI DYIAGTNNMD GHIFASIDMP 350
    AINKGNKKVT EEDFYKLVSE FTITKGLRGA KTTFDVYTES WAQDPSQENK 400
    KKTVVDFETD VLFLVPTEIA LAQHRANAKS AKTYAYLFSH PSRMPVYPKW 450
    VGADHADDIQ YVFGKPFATP TGYRPQDRTV SKAMIAYWTN FAKTGDPNMG 500
    DSAVPTHWEP YTTENSGYLE ITKKMGSSSM KRSLRTNFLR YWTLTYLALP 550
    TVTDQEATPV PPTGDSEATP VPPTGDSETA PVPPTGDSGA PPVPPTGDSG 600
    APPVPPTGDS GAPPVPPTGD SGAPPVPPTG DSGAPPVPPT GDSGAPPVPP 650
    TGDSGAPPVP PTGDSGAPPV PPTGDAGPPP VPPTGDSGAP PVPPTGDSGA 700
    PPVTPTGDSE TAPVPPTGDS GAPPVPPTGD SEAAPVPPTD DSKEAQMPAV 750
    IRF 753
    Length:753
    Mass (Da):79,322
    Last modified:July 7, 2009 - v3
    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

    Sequence cautioni

    The sequence AAA51973.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAA52014.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAC26514.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA38325.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI13412.1 differs from that shown. Reason: Erroneous initiation.
    The sequence EAW88033.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731Missing AA sequence (PubMed:8471055)Curated
    Sequence conflicti235 – 2351R → A in AAB35488. (PubMed:7578248)Curated
    Sequence conflicti284 – 2885RALTL → AAVTV in AAB35488. (PubMed:7578248)Curated
    Sequence conflicti313 – 3131G → E in AAB35488. (PubMed:7578248)Curated
    Sequence conflicti403 – 4031T → I in AAB35488. (PubMed:7578248)Curated
    Sequence conflicti481 – 4811S → F in AAB35488. (PubMed:7578248)Curated
    Sequence conflicti689 – 6891A → P in AAB35488. (PubMed:7578248)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei430 – 49566Missing in isoform Short. CuratedVSP_001463Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAI13412.1. Different initiation.
    CH471090 Genomic DNA. Translation: EAW88033.1. Different initiation.
    PIRiS13586.
    UniGeneiHs.533258.

    Genome annotation databases

    EnsembliENST00000351304; ENSP00000342217; ENSG00000170835. [P19835-2]
    UCSCiuc010naa.2. human. [P19835-1]

    Polymorphism databases

    DMDMi251757481.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAI13412.1 . Different initiation.
    CH471090 Genomic DNA. Translation: EAW88033.1 . Different initiation.
    PIRi S13586.
    UniGenei Hs.533258.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F6W X-ray 2.30 A 21-553 [» ]
    1JMY X-ray 2.60 A 21-538 [» ]
    ProteinModelPortali P19835.
    SMRi P19835. Positions 21-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107485. 1 interaction.
    IntActi P19835. 1 interaction.
    STRINGi 9606.ENSP00000361151.

    Chemistry

    BindingDBi P19835.
    ChEMBLi CHEMBL3219.

    Protein family/group databases

    MEROPSi S09.985.

    PTM databases

    PhosphoSitei P19835.
    UniCarbKBi P19835.

    Polymorphism databases

    DMDMi 251757481.

    Proteomic databases

    MaxQBi P19835.
    PaxDbi P19835.
    PRIDEi P19835.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351304 ; ENSP00000342217 ; ENSG00000170835 . [P19835-2 ]
    UCSCi uc010naa.2. human. [P19835-1 ]

    Organism-specific databases

    GeneCardsi GC09P135937.
    HGNCi HGNC:1848. CEL.
    HPAi HPA008023.
    HPA052701.
    MIMi 114840. gene.
    606391. phenotype.
    609812. phenotype.
    neXtProti NX_P19835.
    Orphaneti 552. MODY syndrome.
    PharmGKBi PA26391.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2272.
    HOGENOMi HOG000091866.
    HOVERGENi HBG008839.
    OrthoDBi EOG7034GN.
    PhylomeDBi P19835.
    TreeFami TF315470.

    Enzyme and pathway databases

    Reactomei REACT_9518. Digestion of dietary lipid.
    SABIO-RK P19835.

    Miscellaneous databases

    EvolutionaryTracei P19835.
    NextBioi 4419.
    PROi P19835.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19835.
    Bgeei P19835.
    CleanExi HS_CEL.
    Genevestigatori P19835.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    [Graphical view ]
    Pfami PF00135. COesterase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
    PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase."
      Nilsson J., Blaeckberg L., Carlsson P., Enerbaeck S., Hernell O., Bjursell G.
      Eur. J. Biochem. 192:543-550(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PARTIAL PROTEIN SEQUENCE.
      Tissue: Mammary gland.
    2. "Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase."
      Hui D.Y., Kissel J.A.
      FEBS Lett. 276:131-134(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Pancreas.
    3. "Structure of human milk bile salt activated lipase."
      Baba T., Downs D., Jackson K.W., Tang J., Wang C.-S.
      Biochemistry 30:500-510(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PROTEIN SEQUENCE OF 21-81; 122-126; 190-194; 275-279; 302-306; 445-449; 485-490; 500-507; 526-528 AND 531-538.
      Tissue: Mammary gland and Milk.
    4. "Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene."
      Lidberg U., Nilsson J., Stroemberg K., Stenman G., Sahlin P., Enerbaeck S., Bjursell G.
      Genomics 13:630-640(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    6. "Structure and organization of the human carboxyl ester lipase locus."
      Madeyski K., Lidberg U., Bjursell G., Nilsson J.
      Mamm. Genome 9:334-338(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase)."
      Hui D.Y., Hayakawa K., Oizumi J.
      Biochem. J. 291:65-69(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 53-76 AND 366-374, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-455.
      Tissue: Milk.
    10. "Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases."
      Christie D.L., Cleverly D.R., O'Connor C.J.O.
      FEBS Lett. 278:190-194(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, ACTIVE SITE.
    11. "Isolation and characterization of human milk bile salt-activated lipase C-tail fragment."
      Wang C.S., Dashti A., Jackson K.W., Yeh J.C., Cummings R.D., Tang J.
      Biochemistry 34:10639-10644(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-558; THR-569; THR-579; THR-607; THR-618; THR-629; THR-640; THR-651; THR-662 AND THR-673.
    12. "Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk."
      Mechref Y., Chen P., Novotny M.V.
      Glycobiology 9:227-234(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF N-LINKED CARBOHYDRATES.
    13. "Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion."
      Ackerman S.J., Liu L., Kwatia M.A., Savage M.P., Leonidas D.D., Swaminathan G.J., Acharya K.R.
      J. Biol. Chem. 277:14859-14868(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLC, TISSUE SPECIFICITY.
    14. "Crystal structure of the catalytic domain of human bile salt activated lipase."
      Terzyan S., Wang C.S., Downs D., Hunter B., Zhang X.C.
      Protein Sci. 9:1783-1790(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-553.
    15. Cited for: INVOLVEMENT IN MODY8.

    Entry informationi

    Entry nameiCEL_HUMAN
    AccessioniPrimary (citable) accession number: P19835
    Secondary accession number(s): Q16398
    , Q5T7U7, Q9UCH1, Q9UP41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 154 of the entry and version 3 of the sequence. [Complete history]
    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.

    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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3