UniProtKB - P19835 (CEL_HUMAN)
Bile salt-activated lipase
CEL
Functioni
Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFAs) (PubMed:8471055, PubMed:27509211, PubMed:10220579, PubMed:27650499).
Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs (By similarity).
Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins (PubMed:8471055, PubMed:27509211, PubMed:10220579, PubMed:27650499).
By similarity4 PublicationsCatalytic activityi
- EC:3.1.1.31 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- EC:3.1.1.131 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- EC:3.1.1.61 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- 9-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 9-hydroxy-octadecanoate + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + sn-glycerol 3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- 12-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 12-hydroxyoctadecanoate + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 13-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 13-hydroxy-octadecanoate + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 9-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 9-hydroxy-octadecanoate + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- 13-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 13-hydroxy-octadecanoate + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- 5-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 5-hydroxy-octadecanoate + H+By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
Activity regulationi
Kineticsi
- KM=24 µM for lipoyl-4-aminobenzoate1 Publication
- 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 214 | Acyl-ester intermediatePROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 340 | Charge relay system1 Publication | 1 | |
Active sitei | 455 | Charge relay system1 Publication | 1 |
GO - Molecular functioni
- acetylesterase activity Source: UniProtKB-EC
- 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
GO - Biological processi
- ceramide catabolic process Source: Ensembl
- chemical synaptic transmission Source: GO_Central
- cholesterol catabolic process Source: UniProtKB
- fatty acid catabolic process Source: UniProtKB
- intestinal cholesterol absorption Source: UniProtKB
- intestinal lipid catabolic process Source: UniProtKB
- lipid metabolic process Source: UniProtKB
- modulation of chemical synaptic transmission Source: GO_Central
- neuron cell-cell adhesion Source: GO_Central
- pancreatic juice secretion Source: UniProtKB
- postsynaptic membrane assembly Source: GO_Central
- presynaptic membrane assembly Source: GO_Central
- protein esterification Source: UniProtKB
- synaptic vesicle endocytosis Source: GO_Central
Keywordsi
Molecular function | Hydrolase, Serine esterase |
Biological process | Lipid degradation, Lipid metabolism |
Enzyme and pathway databases
BRENDAi | 3.1.1.13, 2681 |
PathwayCommonsi | P19835 |
Reactomei | R-HSA-192456, Digestion of dietary lipid |
SABIO-RKi | P19835 |
SignaLinki | P19835 |
Protein family/group databases
ESTHERi | human-CEL, Cholesterol_esterase |
MEROPSi | S09.985 |
Chemistry databases
SwissLipidsi | SLP:000000874 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:CEL Synonyms:BAL |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:1848, CEL |
MIMi | 114840, gene |
neXtProti | NX_P19835 |
VEuPathDBi | HostDB:ENSG00000170835 |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
- extracellular region Source: Reactome
- extracellular space Source: UniProtKB
Plasma Membrane
- integral component of plasma membrane Source: GO_Central
- integral component of postsynaptic specialization membrane Source: GO_Central
Other locations
- cell surface Source: GO_Central
- cytoplasm Source: UniProtKB
- presynapse Source: GOC
- synapse Source: GO_Central
Keywords - Cellular componenti
SecretedPathology & Biotechi
Involvement in diseasei
Maturity-onset diabetes of the young 8 with exocrine dysfunction (MODY8)1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 455 | H → Q: Abolishes lipase activity. Decreases Vmax for esterase activity by 2.5-fold. 1 Publication | 1 |
Keywords - Diseasei
Diabetes mellitusOrganism-specific databases
GeneReviewsi | CEL |
MalaCardsi | CEL |
MIMi | 609812, phenotype |
OpenTargetsi | ENSG00000170835 |
Orphaneti | 552, MODY |
PharmGKBi | PA26391 |
Miscellaneous databases
Pharosi | P19835, Tchem |
Chemistry databases
ChEMBLi | CHEMBL3219 |
DrugBanki | DB04348, Taurocholic acid |
Genetic variation databases
BioMutai | CEL |
DMDMi | 251757481 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 20 | 1 PublicationAdd BLAST | 20 | |
ChainiPRO_0000008631 | 21 – 753 | Bile salt-activated lipaseAdd BLAST | 733 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 84 ↔ 100 | |||
GlycosylationiCAR_000141 | 207 | N-linked (GlcNAc...) (complex) asparagine | 1 | |
Disulfide bondi | 266 ↔ 277 | |||
Glycosylationi | 558 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 569 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 579 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 607 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 618 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 629 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 640 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 651 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 662 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 673 | O-linked (GalNAc...) threonine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
jPOSTi | P19835 |
MassIVEi | P19835 |
MaxQBi | P19835 |
PaxDbi | P19835 |
PeptideAtlasi | P19835 |
PRIDEi | P19835 |
ProteomicsDBi | 53692 [P19835-1] 53693 [P19835-2] |
PTM databases
GlyConnecti | 74, 15 N-Linked glycans (1 site), 9 O-Linked glycans |
GlyGeni | P19835, 12 sites, 25 N-linked glycans (2 sites), 17 O-linked glycans (1 site) |
iPTMneti | P19835 |
PhosphoSitePlusi | P19835 |
Expressioni
Tissue specificityi
Gene expression databases
ExpressionAtlasi | P19835, baseline and differential |
Organism-specific databases
HPAi | ENSG00000170835, Tissue enriched (pancreas) |
Interactioni
Subunit structurei
Interacts with CLC.
1 PublicationGO - Molecular functioni
- neurexin family protein binding Source: GO_Central
Protein-protein interaction databases
IntActi | P19835, 1 interactor |
STRINGi | 9606.ENSP00000361151 |
Chemistry databases
BindingDBi | P19835 |
Miscellaneous databases
RNActi | P19835, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P19835 |
SMRi | P19835 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P19835 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 559 – 569 | 1Add BLAST | 11 | |
Repeati | 570 – 580 | 2Add BLAST | 11 | |
Repeati | 581 – 591 | 3Add BLAST | 11 | |
Repeati | 592 – 602 | 4Add BLAST | 11 | |
Repeati | 603 – 613 | 5Add BLAST | 11 | |
Repeati | 614 – 624 | 6Add BLAST | 11 | |
Repeati | 625 – 635 | 7Add BLAST | 11 | |
Repeati | 636 – 646 | 8Add BLAST | 11 | |
Repeati | 647 – 657 | 9Add BLAST | 11 | |
Repeati | 658 – 668 | 10Add BLAST | 11 | |
Repeati | 669 – 679 | 11Add BLAST | 11 | |
Repeati | 680 – 690 | 12Add BLAST | 11 | |
Repeati | 691 – 701 | 13Add BLAST | 11 | |
Repeati | 702 – 712 | 14Add BLAST | 11 | |
Repeati | 713 – 723 | 15Add BLAST | 11 | |
Repeati | 724 – 734 | 16Add BLAST | 11 | |
Repeati | 735 – 745 | 17Add BLAST | 11 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 21 – 121 | Heparin-bindingAdd BLAST | 101 | |
Regioni | 555 – 753 | DisorderedSequence analysisAdd BLAST | 199 | |
Regioni | 559 – 745 | 17 X 11 AA tandem repeats, glycodomain, O-linked (mucin type)Add BLAST | 187 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 585 – 700 | Pro residuesSequence analysisAdd BLAST | 116 | |
Compositional biasi | 717 – 733 | Pro residuesSequence analysisAdd BLAST | 17 |
Sequence similaritiesi
Keywords - Domaini
Repeat, SignalPhylogenomic databases
eggNOGi | KOG1516, Eukaryota |
GeneTreei | ENSGT00940000156231 |
InParanoidi | P19835 |
PhylomeDBi | P19835 |
TreeFami | TF315470 |
Family and domain databases
Gene3Di | 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR033560, BAL IPR002018, CarbesteraseB IPR019826, Carboxylesterase_B_AS IPR019819, Carboxylesterase_B_CS IPR032059, Mucin-like |
PANTHERi | PTHR43903:SF1, PTHR43903:SF1, 1 hit |
Pfami | View protein in Pfam PF00135, COesterase, 1 hit PF16058, Mucin-like, 3 hits |
SUPFAMi | SSF53474, SSF53474, 1 hit |
PROSITEi | View protein in PROSITE PS00122, CARBOXYLESTERASE_B_1, 1 hit PS00941, CARBOXYLESTERASE_B_2, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
The sequence of this isoform differs from the canonical sequence as follows:
430-495: Missing.
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 73 | Missing AA sequence (PubMed:8471055).Curated | 1 | |
Sequence conflicti | 235 | R → A in AAB35488 (PubMed:7578248).Curated | 1 | |
Sequence conflicti | 284 – 288 | RALTL → AAVTV in AAB35488 (PubMed:7578248).Curated | 5 | |
Sequence conflicti | 313 | G → E in AAB35488 (PubMed:7578248).Curated | 1 | |
Sequence conflicti | 403 | T → I in AAB35488 (PubMed:7578248).Curated | 1 | |
Sequence conflicti | 481 | S → F in AAB35488 (PubMed:7578248).Curated | 1 | |
Sequence conflicti | 689 | A → P in AAB35488 (PubMed:7578248).Curated | 1 |
Polymorphismi
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_001463 | 430 – 495 | Missing in isoform Short. CuratedAdd BLAST | 66 |
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. |
CCDSi | CCDS43896.1 [P19835-1] |
PIRi | S13586 |
Genome annotation databases
Ensembli | ENST00000372080.8; ENSP00000361151.6; ENSG00000170835.17 |
MANE-Selecti | ENST00000372080.8; ENSP00000361151.6; NM_001807.6; NP_001798.3 |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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. |
CCDSi | CCDS43896.1 [P19835-1] |
PIRi | S13586 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1F6W | X-ray | 2.30 | A | 21-553 | [»] | |
1JMY | X-ray | 2.60 | A | 21-538 | [»] | |
6H0T | X-ray | 1.90 | A | 22-553 | [»] | |
6H0V | X-ray | 2.20 | A | 22-553 | [»] | |
6H18 | X-ray | 1.85 | A | 22-553 | [»] | |
6H19 | X-ray | 1.89 | A | 22-553 | [»] | |
6H1A | X-ray | 1.75 | A | 22-553 | [»] | |
AlphaFoldDBi | P19835 | |||||
SMRi | P19835 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P19835, 1 interactor |
STRINGi | 9606.ENSP00000361151 |
Chemistry databases
BindingDBi | P19835 |
ChEMBLi | CHEMBL3219 |
DrugBanki | DB04348, Taurocholic acid |
SwissLipidsi | SLP:000000874 |
Protein family/group databases
ESTHERi | human-CEL, Cholesterol_esterase |
MEROPSi | S09.985 |
PTM databases
GlyConnecti | 74, 15 N-Linked glycans (1 site), 9 O-Linked glycans |
GlyGeni | P19835, 12 sites, 25 N-linked glycans (2 sites), 17 O-linked glycans (1 site) |
iPTMneti | P19835 |
PhosphoSitePlusi | P19835 |
Genetic variation databases
BioMutai | CEL |
DMDMi | 251757481 |
Proteomic databases
jPOSTi | P19835 |
MassIVEi | P19835 |
MaxQBi | P19835 |
PaxDbi | P19835 |
PeptideAtlasi | P19835 |
PRIDEi | P19835 |
ProteomicsDBi | 53692 [P19835-1] 53693 [P19835-2] |
Protocols and materials databases
Antibodypediai | 1990, 233 antibodies from 27 providers |
Genome annotation databases
Ensembli | ENST00000372080.8; ENSP00000361151.6; ENSG00000170835.17 |
MANE-Selecti | ENST00000372080.8; ENSP00000361151.6; NM_001807.6; NP_001798.3 |
Organism-specific databases
GeneCardsi | CEL |
GeneReviewsi | CEL |
HGNCi | HGNC:1848, CEL |
HPAi | ENSG00000170835, Tissue enriched (pancreas) |
MalaCardsi | CEL |
MIMi | 114840, gene 609812, phenotype |
neXtProti | NX_P19835 |
OpenTargetsi | ENSG00000170835 |
Orphaneti | 552, MODY |
PharmGKBi | PA26391 |
VEuPathDBi | HostDB:ENSG00000170835 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1516, Eukaryota |
GeneTreei | ENSGT00940000156231 |
InParanoidi | P19835 |
PhylomeDBi | P19835 |
TreeFami | TF315470 |
Enzyme and pathway databases
BRENDAi | 3.1.1.13, 2681 |
PathwayCommonsi | P19835 |
Reactomei | R-HSA-192456, Digestion of dietary lipid |
SABIO-RKi | P19835 |
SignaLinki | P19835 |
Miscellaneous databases
ChiTaRSi | CEL, human |
EvolutionaryTracei | P19835 |
Pharosi | P19835, Tchem |
PROi | PR:P19835 |
RNActi | P19835, protein |
SOURCEi | Search... |
Gene expression databases
ExpressionAtlasi | P19835, baseline and differential |
Family and domain databases
Gene3Di | 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR033560, BAL IPR002018, CarbesteraseB IPR019826, Carboxylesterase_B_AS IPR019819, Carboxylesterase_B_CS IPR032059, Mucin-like |
PANTHERi | PTHR43903:SF1, PTHR43903:SF1, 1 hit |
Pfami | View protein in Pfam PF00135, COesterase, 1 hit PF16058, Mucin-like, 3 hits |
SUPFAMi | SSF53474, SSF53474, 1 hit |
PROSITEi | View protein in PROSITE PS00122, CARBOXYLESTERASE_B_1, 1 hit PS00941, CARBOXYLESTERASE_B_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CEL_HUMAN | |
Accessioni | P19835Primary (citable) accession number: P19835 Secondary accession number(s): Q16398 Q9UP41 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1991 |
Last sequence update: | July 7, 2009 | |
Last modified: | May 25, 2022 | |
This is version 205 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families