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P19835

- CEL_HUMAN

UniProt

P19835 - CEL_HUMAN

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Protein

Bile salt-activated lipase

Gene

CEL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. sterol esterase activity Source: UniProtKB
  6. 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
Complete GO annotation...

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: UniProtKB
Complete GO annotation...

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

BgeeiP19835.
CleanExiHS_CEL.
ExpressionAtlasiP19835. baseline and differential.
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 – 284Combined sources
Beta strandi31 – 344Combined sources
Beta strandi36 – 394Combined sources
Beta strandi41 – 444Combined sources
Beta strandi46 – 549Combined sources
Beta strandi72 – 765Combined sources
Beta strandi84 – 874Combined sources
Beta strandi91 – 988Combined sources
Beta strandi102 – 1098Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi117 – 1248Combined sources
Turni128 – 1303Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi142 – 1454Combined sources
Helixi148 – 1547Combined sources
Beta strandi157 – 1615Combined sources
Helixi166 – 1705Combined sources
Beta strandi174 – 1785Combined sources
Helixi182 – 19716Combined sources
Turni198 – 2025Combined sources
Beta strandi203 – 21311Combined sources
Helixi215 – 22511Combined sources
Helixi227 – 2293Combined sources
Turni230 – 2323Combined sources
Beta strandi234 – 2407Combined sources
Turni246 – 2483Combined sources
Helixi253 – 26412Combined sources
Helixi271 – 28010Combined sources
Helixi283 – 2886Combined sources
Helixi302 – 3043Combined sources
Beta strandi313 – 3164Combined sources
Helixi320 – 3223Combined sources
Helixi324 – 3274Combined sources
Beta strandi330 – 3378Combined sources
Turni338 – 3414Combined sources
Helixi342 – 3487Combined sources
Helixi350 – 3534Combined sources
Beta strandi355 – 3573Combined sources
Helixi361 – 37111Combined sources
Helixi376 – 38813Combined sources
Turni398 – 4014Combined sources
Helixi402 – 41211Combined sources
Helixi414 – 42512Combined sources
Beta strandi433 – 4386Combined sources
Turni455 – 4584Combined sources
Helixi459 – 4624Combined sources
Helixi465 – 4684Combined sources
Helixi470 – 4723Combined sources
Helixi475 – 49420Combined sources
Beta strandi499 – 5024Combined sources
Turni513 – 5153Combined sources
Beta strandi518 – 5247Combined sources
Helixi527 – 5293Combined sources
Helixi536 – 5449Combined sources
Turni545 – 5484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP19835.
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

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

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:
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. Translation: CAI13412.1. Different initiation.
CH471090 Genomic DNA. Translation: EAW88033.1. Different initiation.
PIRiS13586.
UniGeneiHs.533258.

Genome annotation databases

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

Polymorphism databases

DMDMi251757481.

Keywords - Coding sequence diversityi

Alternative splicing

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. 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:
PDBei
RCSB PDBi
PDBji
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 .
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.
GeneTreei ENSGT00760000118946.
HOGENOMi HOG000091866.
HOVERGENi HBG008839.
InParanoidi P19835.
OrthoDBi EOG7034GN.
PhylomeDBi P19835.
TreeFami TF315470.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi CEL. human.
EvolutionaryTracei P19835.
NextBioi 4419.
PROi P19835.
SOURCEi Search...

Gene expression databases

Bgeei P19835.
CleanExi HS_CEL.
ExpressionAtlasi P19835. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 156 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