P19835 (CEL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bile salt-activated lipase
Short name=BAL
EC=3.1.1.13
EC=3.1.1.3

Alternative name(s):
Bile salt-stimulated lipase
Short name=BSSL
Bucelipase
Carboxyl ester lipase
Cholesterol esterase
Pancreatic lysophospholipase
Sterol esterase

Gene names

Name:	CEL
Synonyms:	BAL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	753 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.9 A steryl ester + H2O = a sterol + a fatty acid. Ref.9
Enzyme regulation	Activated by bile salts containing a 7-hydroxyl group.
Subcellular location	Secreted.
Tissue specificity	Mammary gland and pancreas.
Involvement in disease	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. 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 (Ref.14). Ref.14
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.
Biophysicochemical properties	Kinetic parameters: KM=24 µM for lipoyl-4-aminobenzoate Ref.9 KM=15 µM for triacetin Vmax=45.5 pmol/min/mg enzyme toward lipoyl-4-aminobenzoate Vmax=323 pmol/min/mg enzyme toward triacetin
Sequence caution	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.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Disease	Diabetes mellitus
Domain	Repeat Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ceramide catabolic process Inferred from electronic annotation. Source: Compara cholesterol catabolic process Inferred from direct assay PubMed 12031288. Source: UniProtKB fatty acid catabolic process Non-traceable author statement Ref.5. Source: UniProtKB intestinal cholesterol absorption Non-traceable author statement PubMed 12031288. Source: UniProtKB intestinal lipid catabolic process Non-traceable author statement Ref.5. Source: UniProtKB pancreatic juice secretion Inferred from direct assay PubMed 1854805. Source: UniProtKB protein esterification Non-traceable author statement Ref.5. Source: UniProtKB triglyceride metabolic process Inferred by curator Ref.2. Source: UniProtKB
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome extracellular space Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	acylglycerol lipase activity Traceable author statement. Source: Reactome carboxylesterase activity Inferred from Biological aspect of Ancestor. Source: RefGenome heparin binding Non-traceable author statement Ref.5. Source: UniProtKB retinyl-palmitate esterase activity Inferred from electronic annotation. Source: EC sterol esterase activity Non-traceable author statement PubMed 12031288. Source: UniProtKB triglyceride lipase activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P19835-1)

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.

Isoform Short (identifier: P19835-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.3

Chain

21 – 753

733

Bile salt-activated lipase

PRO_0000008631

Regions

Repeat

559 – 569

11

1

Repeat

570 – 580

11

2

Repeat

581 – 591

11

3

Repeat

592 – 602

11

4

Repeat

603 – 613

11

5

Repeat

614 – 624

11

6

Repeat

625 – 635

11

7

Repeat

636 – 646

11

8

Repeat

647 – 657

11

9

Repeat

658 – 668

11

10

Repeat

669 – 679

11

11

Repeat

680 – 690

11

12

Repeat

691 – 701

11

13

Repeat

702 – 712

11

14

Repeat

713 – 723

11

15

Repeat

724 – 734

11

16

Repeat

735 – 745

11

17

Region

21 – 121

101

Heparin-binding

Region

559 – 745

187

17 X 11 AA tandem repeats, glycodomain, O-linked (mucin type)

Sites

Active site

214

1

Acyl-ester intermediate Ref.10

Active site

340

1

Charge relay system Ref.10

Active site

455

1

Charge relay system Ref.10

Amino acid modifications

Glycosylation

207

1

N-linked (GlcNAc...) (complex)

CAR_000141

Glycosylation

558

1

O-linked (GalNAc...) Ref.11

Glycosylation

569

1

O-linked (GalNAc...) Ref.11

Glycosylation

579

1

O-linked (GalNAc...) Ref.11

Glycosylation

607

1

O-linked (GalNAc...) Ref.11

Glycosylation

618

1

O-linked (GalNAc...) Ref.11

Glycosylation

629

1

O-linked (GalNAc...) Ref.11

Glycosylation

640

1

O-linked (GalNAc...) Ref.11

Glycosylation

651

1

O-linked (GalNAc...) Ref.11

Glycosylation

662

1

O-linked (GalNAc...) Ref.11

Glycosylation

673

1

O-linked (GalNAc...) Ref.11

Disulfide bond

84 ↔ 100

Disulfide bond

266 ↔ 277

Natural variations

Alternative sequence

430 – 495

66

Missing in isoform Short.

VSP_001463

Experimental info

Mutagenesis

455

1

H → Q: Abolishes lipase activity. Decreases Vmax for esterase activity by 2.5-fold. Ref.9

Sequence conflict

73

1

Missing AA sequence Ref.9

Sequence conflict

235

1

R → A in AAB35488. Ref.5

Sequence conflict

284 – 288

5

RALTL → AAVTV in AAB35488. Ref.5

Sequence conflict

313

1

G → E in AAB35488. Ref.5

Sequence conflict

403

1

T → I in AAB35488. Ref.5

Sequence conflict

481

1

S → F in AAB35488. Ref.5

Sequence conflict

689

1

A → P in AAB35488. Ref.5

Secondary structure

1

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753

Helix Strand Turn

Details...

Beta strand

25 – 28

4

Beta strand

31 – 34

4

Beta strand

36 – 39

4

Beta strand

41 – 44

4

Beta strand

46 – 54

9

Beta strand

72 – 76

5

Beta strand

84 – 87

4

Beta strand

91 – 98

8

Beta strand

102 – 109

8

Beta strand

111 – 113

3

Beta strand

117 – 124

8

Turn

128 – 130

3

Beta strand

137 – 139

3

Beta strand

142 – 145

4

Helix

148 – 154

7

Beta strand

157 – 161

5

Helix

166 – 170

5

Beta strand

174 – 178

5

Helix

182 – 197

16

Turn

198 – 202

5

Beta strand

203 – 213

11

Helix

215 – 225

11

Helix

227 – 229

3

Turn

230 – 232

3

Beta strand

234 – 240

7

Turn

246 – 248

3

Helix

253 – 264

12

Helix

271 – 280

10

Helix

283 – 288

6

Helix

302 – 304

3

Beta strand

313 – 316

4

Helix

320 – 322

3

Helix

324 – 327

4

Beta strand

330 – 337

8

Turn

338 – 341

4

Helix

342 – 348

7

Helix

350 – 353

4

Beta strand

355 – 357

3

Helix

361 – 371

11

Helix

376 – 388

13

Turn

398 – 401

4

Helix

402 – 412

11

Helix

414 – 425

12

Beta strand

433 – 438

6

Turn

455 – 458

4

Helix

459 – 462

4

Helix

465 – 468

4

Helix

470 – 472

3

Helix

475 – 494

20

Beta strand

499 – 502

4

Turn

513 – 515

3

Beta strand

518 – 524

7

Helix

527 – 529

3

Helix

536 – 544

9

Turn

545 – 548

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified July 7, 2009. Version 3. Checksum: B3253789D1EABF7F	FASTA	753	79,322
	10 20 30 40 50 60 MGRLQLVVLG LTCCWAVASA AKLGAVYTEG GFVEGVNKKL GLLGDSVDIF KGIPFAAPTK 70 80 90 100 110 120 ALENPQPHPG WQGTLKAKNF KKRCLQATIT QDSTYGDEDC LYLNIWVPQG RKQVSRDLPV 130 140 150 160 170 180 MIWIYGGAFL MGSGHGANFL NNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG 190 200 210 220 230 240 NYGLRDQHMA IAWVKRNIAA FGGDPNNITL FGESAGGASV SLQTLSPYNK GLIRRAISQS 250 260 270 280 290 300 GVALSPWVIQ KNPLFWAKKV AEKVGCPVGD AARMAQCLKV TDPRALTLAY KVPLAGLEYP 310 320 330 340 350 360 MLHYVGFVPV IDGDFIPADP INLYANAADI DYIAGTNNMD GHIFASIDMP AINKGNKKVT 370 380 390 400 410 420 EEDFYKLVSE FTITKGLRGA KTTFDVYTES WAQDPSQENK KKTVVDFETD VLFLVPTEIA 430 440 450 460 470 480 LAQHRANAKS AKTYAYLFSH PSRMPVYPKW VGADHADDIQ YVFGKPFATP TGYRPQDRTV 490 500 510 520 530 540 SKAMIAYWTN FAKTGDPNMG DSAVPTHWEP YTTENSGYLE ITKKMGSSSM KRSLRTNFLR 550 560 570 580 590 600 YWTLTYLALP TVTDQEATPV PPTGDSEATP VPPTGDSETA PVPPTGDSGA PPVPPTGDSG 610 620 630 640 650 660 APPVPPTGDS GAPPVPPTGD SGAPPVPPTG DSGAPPVPPT GDSGAPPVPP TGDSGAPPVP 670 680 690 700 710 720 PTGDSGAPPV PPTGDAGPPP VPPTGDSGAP PVPPTGDSGA PPVTPTGDSE TAPVPPTGDS 730 740 750 GAPPVPPTGD SEAAPVPPTD DSKEAQMPAV IRF
	Isoform Short [UniParc]. Checksum: BD269A05F7FBB9CF	FASTA	687	71,834
	10 20 30 40 50 60 MGRLQLVVLG LTCCWAVASA AKLGAVYTEG GFVEGVNKKL GLLGDSVDIF KGIPFAAPTK 70 80 90 100 110 120 ALENPQPHPG WQGTLKAKNF KKRCLQATIT QDSTYGDEDC LYLNIWVPQG RKQVSRDLPV 130 140 150 160 170 180 MIWIYGGAFL MGSGHGANFL NNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG 190 200 210 220 230 240 NYGLRDQHMA IAWVKRNIAA FGGDPNNITL FGESAGGASV SLQTLSPYNK GLIRRAISQS 250 260 270 280 290 300 GVALSPWVIQ KNPLFWAKKV AEKVGCPVGD AARMAQCLKV TDPRALTLAY KVPLAGLEYP 310 320 330 340 350 360 MLHYVGFVPV IDGDFIPADP INLYANAADI DYIAGTNNMD GHIFASIDMP AINKGNKKVT 370 380 390 400 410 420 EEDFYKLVSE FTITKGLRGA KTTFDVYTES WAQDPSQENK KKTVVDFETD VLFLVPTEIA 430 440 450 460 470 480 LAQHRANAKD PNMGDSAVPT HWEPYTTENS GYLEITKKMG SSSMKRSLRT NFLRYWTLTY 490 500 510 520 530 540 LALPTVTDQE ATPVPPTGDS EATPVPPTGD SETAPVPPTG DSGAPPVPPT GDSGAPPVPP 550 560 570 580 590 600 TGDSGAPPVP PTGDSGAPPV PPTGDSGAPP VPPTGDSGAP PVPPTGDSGA PPVPPTGDSG 610 620 630 640 650 660 APPVPPTGDA GPPPVPPTGD SGAPPVPPTG DSGAPPVTPT GDSETAPVPP TGDSGAPPVP 670 680 PTGDSEAAPV PPTDDSKEAQ MPAVIRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Bile salt-dependent lipase transcripts in human fetal tissues." Roudani S., Miralles F., Margotat A., Escribano M.J., Lombardo D. Biochim. Biophys. Acta 1264:141-150(1995) [PubMed] [Europe PMC] [Abstract] 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"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.
[14]	"Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic exocrine dysfunction." Raeder H., Johansson S., Holm P.I., Haldorsen I.S., Mas E., Sbarra V., Nermoen I., Eide S.A., Grevle L., Bjoerkhaug L., Sagen J.V., Aksnes L., Soevik O., Lombardo D., Molven A., Njoelstad P.R. Nat. Genet. 38:54-62(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MODY8.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00099670.
IPI00218674.

PIR

S13586.

RefSeq

NP_001798.2. NM_001807.4.

UniGene

Hs.533258.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F6W	X-ray	2.30	A	21-553	[»]
1JMY	X-ray	2.60	A	21-538	[»]

ProteinModelPortal

P19835.

ModBase

Search...

Protein-protein interaction databases

IntAct

P19835. 1 interaction.

STRING

9606.ENSP00000361151.

Protein family/group databases

MEROPS

S09.985.

PTM databases

GlycoSuiteDB

P19835.

PhosphoSite

P19835.

Polymorphism databases

DMDM

251757481.

Proteomic databases

PaxDb

P19835.

PRIDE

P19835.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000351304; ENSP00000342217; ENSG00000170835.
ENST00000372080; ENSP00000361151; ENSG00000170835.

GeneID

1056.

KEGG

hsa:1056.

UCSC

uc010naa.1. human.

Organism-specific databases

CTD

1056.

GeneCards

GC09P135937.

HGNC

HGNC:1848. CEL.

HPA

HPA008023.

MIM

114840. gene.
606391. phenotype.
609812. phenotype.

neXtProt

NX_P19835.

Orphanet

552. MODY syndrome.

PharmGKB

PA26391.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2272.

HOGENOM

HOG000091866.

HOVERGEN

HBG008839.

KO

K12298.

OrthoDB

EOG4CC40T.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P19835.

Gene expression databases

ArrayExpress

P19835.

Bgee

P19835.

CleanEx

HS_CEL.

Genevestigator

P19835.

GermOnline

ENSG00000170835. Homo sapiens.

Family and domain databases

InterPro

IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]

Pfam

PF00135. COesterase. 1 hit.
[Graphical view]

PROSITE

PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P19835.

ChEMBL

CHEMBL3219.

EvolutionaryTrace

P19835.

GenomeRNAi

1056.

NextBio

4419.

SOURCE

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Entry information

Entry name

CEL_HUMAN

Accession

Primary (citable) accession number: P19835
Secondary accession number(s): Q16398 , Q5T7U7, Q9UCH1, Q9UP41

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 7, 2009
Last modified:	May 1, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

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.