UniProtKB - Q96IY4 (CBPB2_HUMAN)
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- BLAST>sp|Q96IY4|CBPB2_HUMAN Carboxypeptidase B2 OS=Homo sapiens OX=9606 GN=CPB2 PE=1 SV=2 MKLCSLAVLVPIVLFCEQHVFAFQSGQVLAALPRTSRQVQVLQNLTTTYEIVLWQPVTAD LIVKKKQVHFFVNASDVDNVKAHLNVSGIPCSVLLADVEDLIQQQISNDTVSPRASASYY EQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQAAKNAIWIDCGI HAREWISPAFCLWFIGHITQFYGIIGQYTNLLRLVDFYVMPVVNVDGYDYSWKKNRMWRK NRSFYANNHCIGTDLNRNFASKHWCEEGASSSSCSETYCGLYPESEPEVKAVASFLRRNI NQIKAYISMHSYSQHIVFPYSYTRSKSKDHEELSLVASEAVRAIEKISKNTRYTHGHGSE TLYLAPGGGDDWIYDLGIKYSFTIELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVI RNV
- Align
Carboxypeptidase B2
CPB2
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>Select a section on the left to see content.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans."
Mao S.S., Cooper C.M., Wood T., Shafer J.A., Gardell S.J.
J. Biol. Chem. 274:35046-35052(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
<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. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans."
Mao S.S., Cooper C.M., Wood T., Shafer J.A., Gardell S.J.
J. Biol. Chem. 274:35046-35052(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation."
Marx P.F., Brondijk T.H., Plug T., Romijn R.A., Hemrika W., Meijers J.C., Huizinga E.G.
Blood 112:2803-2809(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-423 ALONE AND IN COMPLEX WITH ZINC IONS AND INHIBITOR, GLYCOSYLATION AT ASN-44; ASN-73; ASN-85 AND ASN-108, ZINC-BINDING SITES, COFACTOR, ENZYME REGULATION, DISULFIDE BONDS. - Ref.14"Insights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitor."
Sanglas L., Arolas J.L., Valnickova Z., Aviles F.X., Enghild J.J., Gomis-Ruth F.X.
J. Thromb. Haemost. 8:1056-1065(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 115-423 IN COMPLEX WITH ZINC AND INHIBITOR, DISULFIDE BONDS, COFACTOR.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation."
Marx P.F., Brondijk T.H., Plug T., Romijn R.A., Hemrika W., Meijers J.C., Huizinga E.G.
Blood 112:2803-2809(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-423 ALONE AND IN COMPLEX WITH ZINC IONS AND INHIBITOR, GLYCOSYLATION AT ASN-44; ASN-73; ASN-85 AND ASN-108, ZINC-BINDING SITES, COFACTOR, ENZYME REGULATION, DISULFIDE BONDS. - Ref.14"Insights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitor."
Sanglas L., Arolas J.L., Valnickova Z., Aviles F.X., Enghild J.J., Gomis-Ruth F.X.
J. Thromb. Haemost. 8:1056-1065(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 115-423 IN COMPLEX WITH ZINC AND INHIBITOR, DISULFIDE BONDS, COFACTOR.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation."
Marx P.F., Brondijk T.H., Plug T., Romijn R.A., Hemrika W., Meijers J.C., Huizinga E.G.
Blood 112:2803-2809(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-423 ALONE AND IN COMPLEX WITH ZINC IONS AND INHIBITOR, GLYCOSYLATION AT ASN-44; ASN-73; ASN-85 AND ASN-108, ZINC-BINDING SITES, COFACTOR, ENZYME REGULATION, DISULFIDE BONDS.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 181 | Zinc; catalytic2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 184 | Zinc; catalytic2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 239 | SubstrateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 310 | Zinc; catalytic2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 363 | SubstrateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 sitei | 385 | Proton donor/acceptorBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<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
- metallocarboxypeptidase activity Source: GO_Central
- zinc ion binding Source: InterPro
<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 - Biological processi
- blood coagulation Source: UniProtKB-KW
- cellular response to glucose stimulus Source: Ensembl
- fibrinolysis Source: UniProtKB-KW
- liver regeneration Source: Ensembl
- negative regulation of fibrinolysis Source: Ensembl
- negative regulation of hepatocyte proliferation Source: Ensembl
- negative regulation of plasminogen activation Source: Ensembl
- positive regulation of extracellular matrix constituent secretion Source: Ensembl
- proteolysis Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- regulation of complement activation Source: Reactome
- response to drug Source: Ensembl
- response to heat Source: Ensembl
<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 function | Carboxypeptidase, Hydrolase, Metalloprotease, Protease |
| Biological process | Blood coagulation, Fibrinolysis, Hemostasis |
| Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.17.20 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins R-HSA-977606 Regulation of Complement cascade |
Protein family/group databases
MEROPS protease database More...MEROPSi | M14.009 |
<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: Carboxypeptidase B2 (EC:3.4.17.201 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Alternative name(s): Carboxypeptidase U Short name: CPU Plasma carboxypeptidase B Short name: pCPB Thrombin-activable fibrinolysis inhibitor Short name: TAFI |
| <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:CPB2 |
| <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>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000080618.13 |
Human Gene Nomenclature Database More...HGNCi | HGNC:2300 CPB2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 603101 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q96IY4 |
<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
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular region Source: Reactome
- extracellular space Source: GO_Central
Other locations
- cell Source: GOC
<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>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
Organism-specific databases
DisGeNET More...DisGeNETi | 1361 |
Open Targets More...OpenTargetsi | ENSG00000080618 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26822 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3419 |
Drug and drug target database More...DrugBanki | DB05712 AZD-9684 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1594 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 317373332 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 peptidei | 1 – 22 | Sequence analysisAdd BLAST | 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000004377 | 23 – 114 | Activation peptideAdd BLAST | 92 | |
| <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_0000004378 | 115 – 423 | Carboxypeptidase B2Add BLAST | 309 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Glycosylationi | 44 | N-linked (GlcNAc...) asparagine3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 73 | N-linked (GlcNAc...) asparagine3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 85 | N-linked (GlcNAc...) asparagine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 108 | N-linked (GlcNAc...) (complex) asparagine5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bondi | 178 ↔ 191 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <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>Glycosylationi | 241 | N-linked (GlcNAc...) asparagine; partial1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bondi | 250 ↔ 274 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <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 bondi | 265 ↔ 279 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44; ASN-73 AND ASN-108. - Ref.10"Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation."
Valnickova Z., Christensen T., Skottrup P., Thogersen I.B., Hojrup P., Enghild J.J.
Biochemistry 45:1525-1535(2006) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT ASN-44; ASN-73; ASN-85; ASN-108 AND ASN-241, DISULFIDE BONDS. - Ref.11"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108. - Ref.12"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 11:1-17(2012) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION AT ASN-108, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.13"Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation."
Marx P.F., Brondijk T.H., Plug T., Romijn R.A., Hemrika W., Meijers J.C., Huizinga E.G.
Blood 112:2803-2809(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-423 ALONE AND IN COMPLEX WITH ZINC IONS AND INHIBITOR, GLYCOSYLATION AT ASN-44; ASN-73; ASN-85 AND ASN-108, ZINC-BINDING SITES, COFACTOR, ENZYME REGULATION, DISULFIDE BONDS.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 324 – 325 | Cleavage; by thrombin | 2 |
<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>Keywords - PTMi
Disulfide bond, Glycoprotein, ZymogenProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q96IY4 |
PeptideAtlas More...PeptideAtlasi | Q96IY4 |
PRoteomics IDEntifications database More...PRIDEi | Q96IY4 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 76868 76869 [Q96IY4-2] |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 699 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q96IY4 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q96IY4 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | Q96IY4 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | A8K464 |
<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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000080618 |
CleanEx database of gene expression profiles More...CleanExi | HS_CPB2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q96IY4 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q96IY4 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA004146 |
<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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107753, 6 interactors |
Protein interaction database and analysis system More...IntActi | Q96IY4, 1 interactor |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000181383 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q96IY4 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 26 – 31 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 36 – 48 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 51 – 58 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 59 – 61 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 68 – 73 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 74 – 76 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 77 – 87 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 91 – 96 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 98 – 107 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 108 – 110 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 117 – 121 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 126 – 139 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 141 – 143 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 144 – 151 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 157 – 163 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 172 – 177 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 186 – 201 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 202 – 204 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 206 – 214 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 215 – 221 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 225 – 233 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 255 – 257 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 262 – 265 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 269 – 271 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 287 – 298 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 299 – 302 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 303 – 319 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 321 – 325 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 330 – 347 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 354 – 358 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 359 – 362 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 369 – 374 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 375 – 377 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 380 – 387 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 389 – 392 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 393 – 395 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 398 – 400 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 401 – 422 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 22 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q96IY4 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q96IY4 |
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 | Q96IY4 |
<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
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 181 – 184 | Substrate bindingBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 4 | |
| <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>Regioni | 256 – 257 | Substrate bindingBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 2 | |
| <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>Regioni | 311 – 312 | Substrate bindingBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 2 |
<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
<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>Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2650 Eukaryota COG2866 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119103 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000252968 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG050815 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q96IY4 |
KEGG Orthology (KO) More...KOi | K01300 |
Identification of Orthologs from Complete Genome Data More...OMAi | EIYSWIE |
Database of Orthologous Groups More...OrthoDBi | EOG091G0HUI |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q96IY4 |
TreeFam database of animal gene trees More...TreeFami | TF317197 |
Family and domain databases
Conserved Domains Database More...CDDi | cd06246 M14_CPB2, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.70.340, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR033849 CPB2 IPR036990 M14A-like_propep IPR003146 M14A_act_pep IPR000834 Peptidase_M14 |
Pfam protein domain database More...Pfami | View protein in Pfam PF00246 Peptidase_M14, 1 hit PF02244 Propep_M14, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00765 CRBOXYPTASEA |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00631 Zn_pept, 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 basketAdded 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.
10 20 30 40 50
MKLCSLAVLV PIVLFCEQHV FAFQSGQVLA ALPRTSRQVQ VLQNLTTTYE
60 70 80 90 100
IVLWQPVTAD LIVKKKQVHF FVNASDVDNV KAHLNVSGIP CSVLLADVED
110 120 130 140 150
LIQQQISNDT VSPRASASYY EQYHSLNEIY SWIEFITERH PDMLTKIHIG
160 170 180 190 200
SSFEKYPLYV LKVSGKEQAA KNAIWIDCGI HAREWISPAF CLWFIGHITQ
210 220 230 240 250
FYGIIGQYTN LLRLVDFYVM PVVNVDGYDY SWKKNRMWRK NRSFYANNHC
260 270 280 290 300
IGTDLNRNFA SKHWCEEGAS SSSCSETYCG LYPESEPEVK AVASFLRRNI
310 320 330 340 350
NQIKAYISMH SYSQHIVFPY SYTRSKSKDH EELSLVASEA VRAIEKISKN
360 370 380 390 400
TRYTHGHGSE TLYLAPGGGD DWIYDLGIKY SFTIELRDTG TYGFLLPERY
410 420
IKPTCREAFA AVSKIAWHVI RNV
The sequence of this isoform differs from the canonical sequence as follows:
198-234: Missing.
384-423: IELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVIRNV → SNPPVEKLLPLSLK
10 20 30 40 50
MKLCSLAVLV PIVLFCEQHV FAFQSGQVLA ALPRTSRQVQ VLQNLTTTYE
60 70 80 90 100
IVLWQPVTAD LIVKKKQVHF FVNASDVDNV KAHLNVSGIP CSVLLADVED
110 120 130 140 150
LIQQQISNDT VSPRASASYY EQYHSLNEIY SWIEFITERH PDMLTKIHIG
160 170 180 190 200
SSFEKYPLYV LKVSGKEQAA KNAIWIDCGI HAREWISPAF CLWFIGHNRM
210 220 230 240 250
WRKNRSFYAN NHCIGTDLNR NFASKHWCEE GASSSSCSET YCGLYPESEP
260 270 280 290 300
EVKAVASFLR RNINQIKAYI SMHSYSQHIV FPYSYTRSKS KDHEELSLVA
310 320 330 340 350
SEAVRAIEKI SKNTRYTHGH GSETLYLAPG GGDDWIYDLG IKYSFTSNPP
360
VEKLLPLSLK
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 25 | S → T in BAA90475 (Ref. 2) Curated | 1 |
Natural variant
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_013446 | 198 – 234 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 37 | |
| <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_013447 | 384 – 423 | IELRD…VIRNV → SNPPVEKLLPLSLK in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 40 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M75106 mRNA Translation: AAA60042.1 AB011969 mRNA Translation: BAA90475.1 BT006936 mRNA Translation: AAP35582.1 AK290829 mRNA Translation: BAF83518.1 AY714780 Genomic DNA Translation: AAT97987.1 AL137141 Genomic DNA No translation available. AL157758 Genomic DNA No translation available. BC007057 mRNA Translation: AAH07057.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS9401.1 [Q96IY4-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A41204 |
NCBI Reference Sequences More...RefSeqi | NP_001265470.1, NM_001278541.1 NP_001863.3, NM_001872.4 [Q96IY4-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.512937 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000181383; ENSP00000181383; ENSG00000080618 [Q96IY4-1] ENST00000645658; ENSP00000496703; ENSG00000080618 [Q96IY4-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1361 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1361 |
UCSC genome browser More...UCSCi | uc001vaw.4 human [Q96IY4-1] |
<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>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q96IY4 | CPB2 isoform 2 | 424 | |||
| UPI000181D396 | 424 | ||||
| CPB2 isoform 1 | 423 | ||||
| Carboxypeptidase B2 | 423 | ||||
| Carboxypeptidase B2 | 423 | ||||
| +18 | |||||
| Q96IY4-2 | CPB2 isoform 1 | 387 | |||
| Carboxypeptidase B2 | 386 | ||||
| CPB2 isoform 2 | 386 | ||||
| Carboxypeptidase B2 | 386 | ||||
| Carboxypeptidase B2 | 386 | ||||
| +12 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q96IY4 | UPI000181D3A1 | 424 | |||
| CPB2 isoform 2 | 424 | ||||
| Carboxypeptidase B2 | 423 | ||||
| Carboxypeptidase B2 | 423 | ||||
| Carboxypeptidase B2 | 423 | ||||
| +212 | |||||
| Q96IY4-2 | CPB2 isoform 1 | 387 | |||
| Carboxypeptidase B2 | 386 | ||||
| Carboxypeptidase B2 | 386 | ||||
| Carboxypeptidase B2 | 386 | ||||
| UPI000C29D0DB | 386 | ||||
| +24 | |||||
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| SeattleSNPs |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M75106 mRNA Translation: AAA60042.1 AB011969 mRNA Translation: BAA90475.1 BT006936 mRNA Translation: AAP35582.1 AK290829 mRNA Translation: BAF83518.1 AY714780 Genomic DNA Translation: AAT97987.1 AL137141 Genomic DNA No translation available. AL157758 Genomic DNA No translation available. BC007057 mRNA Translation: AAH07057.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS9401.1 [Q96IY4-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A41204 |
NCBI Reference Sequences More...RefSeqi | NP_001265470.1, NM_001278541.1 NP_001863.3, NM_001872.4 [Q96IY4-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.512937 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 3D66 | X-ray | 3.10 | A/B/C | 24-423 | [»] | |
| 3D67 | X-ray | 3.40 | A/B/C | 24-423 | [»] | |
| 3D68 | X-ray | 2.80 | A/B/C | 24-423 | [»] | |
| 3LMS | X-ray | 2.50 | A | 115-423 | [»] | |
| 4P10 | X-ray | 2.00 | A | 23-423 | [»] | |
| 5HVF | X-ray | 2.85 | A | 23-423 | [»] | |
| 5HVG | X-ray | 3.05 | A/C | 23-423 | [»] | |
| 5HVH | X-ray | 3.00 | A | 23-423 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q96IY4 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q96IY4 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107753, 6 interactors |
Protein interaction database and analysis system More...IntActi | Q96IY4, 1 interactor |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000181383 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q96IY4 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3419 |
Drug and drug target database More...DrugBanki | DB05712 AZD-9684 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1594 |
Protein family/group databases
MEROPS protease database More...MEROPSi | M14.009 |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 699 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q96IY4 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q96IY4 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | Q96IY4 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 317373332 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q96IY4 |
PeptideAtlas More...PeptideAtlasi | Q96IY4 |
PRoteomics IDEntifications database More...PRIDEi | Q96IY4 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 76868 76869 [Q96IY4-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 1361 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000181383; ENSP00000181383; ENSG00000080618 [Q96IY4-1] ENST00000645658; ENSP00000496703; ENSG00000080618 [Q96IY4-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1361 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1361 |
UCSC genome browser More...UCSCi | uc001vaw.4 human [Q96IY4-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 1361 |
DisGeNET More...DisGeNETi | 1361 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000080618.13 |
GeneCards: human genes, protein and diseases More...GeneCardsi | CPB2 |
Human Gene Nomenclature Database More...HGNCi | HGNC:2300 CPB2 |
Human Protein Atlas More...HPAi | HPA004146 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 603101 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q96IY4 |
Open Targets More...OpenTargetsi | ENSG00000080618 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26822 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2650 Eukaryota COG2866 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119103 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000252968 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG050815 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q96IY4 |
KEGG Orthology (KO) More...KOi | K01300 |
Identification of Orthologs from Complete Genome Data More...OMAi | EIYSWIE |
Database of Orthologous Groups More...OrthoDBi | EOG091G0HUI |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q96IY4 |
TreeFam database of animal gene trees More...TreeFami | TF317197 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.17.20 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins R-HSA-977606 Regulation of Complement cascade |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | CPB2 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q96IY4 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Carboxypeptidase_B2 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 1361 |
CutDB - Proteolytic event database More...PMAP-CutDBi | A8K464 |
Protein Ontology More...PROi | PR:Q96IY4 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000080618 |
CleanEx database of gene expression profiles More...CleanExi | HS_CPB2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q96IY4 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q96IY4 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd06246 M14_CPB2, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.70.340, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR033849 CPB2 IPR036990 M14A-like_propep IPR003146 M14A_act_pep IPR000834 Peptidase_M14 |
Pfam protein domain database More...Pfami | View protein in Pfam PF00246 Peptidase_M14, 1 hit PF02244 Propep_M14, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00765 CRBOXYPTASEA |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00631 Zn_pept, 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 namei | CBPB2_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>Accessioni | Q96IY4Primary (citable) accession number: Q96IY4 Secondary accession number(s): A8K464 , Q15114, Q5T9K1, Q5T9K2, Q9P2Y6 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | April 26, 2005 |
| Last sequence update: | January 11, 2011 | |
| Last modified: | June 20, 2018 | |
| This is version 147 of the entry and version 2 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 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. | |
<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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 13
Human chromosome 13: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - 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 - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families
