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Entry version 198 (29 Sep 2021)
Sequence version 5 (23 Mar 2010)
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Protein

Prolyl endopeptidase FAP

Gene

FAP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

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>

<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

Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769, PubMed:16480718, PubMed:16410248, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721).

Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219, PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711).

Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16651416, PubMed:16410248, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288).

Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817).

The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.

By similarity21 Publications

<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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Gelatinase activity is inhibited by serine-protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF), 4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride (AEBSF), 4-amidino phenylsulfonyl fluoride (APSF) and diisopropyl fluorophosphate (DFP), N-ethylmaleimide (NEM) and phenylmethylsulfonyl fluoride (PMSF). Dipeptidyl peptidase activity is inhibited by 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), diisopropylfluorophosphate (DFP). Prolyl endopeptidase activity is inhibited by the boronic acid peptide Ac-Gly-BoroPro, Ac-Gly-Pro-chloromethyl ketone and Thr-Ser-Gly-chloromethyl ketone.6 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.46 mM for Ala-Pro (Dipeptidyl peptidase activity)1 Publication
  2. KM=0.9 mM for Lys-Pro (Dipeptidyl peptidase activity)1 Publication
  3. KM=1.15 mM for Gly-Pro (Dipeptidyl peptidase activity)1 Publication
  4. KM=0.25 mM for Gly-Pro (Dipeptidyl peptidase activity)1 Publication
  5. KM=0.24 mM for Ala-Pro (Dipeptidyl peptidase activity)1 Publication
  6. KM=0.10 mM for Ile-Pro (Dipeptidyl peptidase activity)1 Publication
  7. KM=0.24 mM for Phe-Pro (Dipeptidyl peptidase activity)1 Publication
  8. KM=0.24 mM for Gly-Pro (Dipeptidyl peptidase activity)1 Publication
  9. KM=0.33 mM for Ac-Gly-Pro (Prolyl endopeptidase activity)2 Publications
  10. KM=1.3 µM for Thr-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity)1 Publication
  11. KM=2.2 µM for Ala-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity)1 Publication
  12. KM=0.7 µM for Thr-Ala-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity)1 Publication
  13. KM=1.9 µM for Thr-Ser-Gly-Pro-Ser-Gln (Prolyl endopeptidase activity)1 Publication
  14. KM=2.2 µM for Thr-Ser-Gly-Pro-Asn-Ser (Prolyl endopeptidase activity)1 Publication
  15. KM=4.3 µM for Ala-Ser-Gly-Pro-Ser-Ser (Prolyl endopeptidase activity)1 Publication
  16. KM=0.101 mM for Gly-Pro (FAP form, prolyl endopeptidase activity)1 Publication
  17. KM=0.124 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble form, prolyl endopeptidase activity)1 Publication
  18. KM=0.323 mM for Gly-Pro (FAP form, dipeptidyl peptidase activity)1 Publication
  19. KM=0.272 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble form, dipeptidyl peptidase activity)1 Publication
  20. KM=0.029 mM for Arg-Gly-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu (FAP form, prolyl endopeptidase activity)1 Publication
  21. KM=0.026 mM for Arg-Gly-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu (Antiplasmin-cleaving enzyme FAP soluble form, prolyl endopeptidase activity)1 Publication

pH dependencei

Optimum pH is 6-8.4 for gelatinase activity. At pH lower than 5 inhibited gelatinase activity.2 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius for gelatinase activity. Temperatures above 50 degrees Celsius inhibit gelatinase activity.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei203Substrate1 Publication1
Binding sitei204Substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei624Charge relay systemPROSITE-ProRule annotation1 Publication1
Active sitei702Charge relay system1 Publication1
Active sitei734Charge relay system1 Publication1

<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

GO - Biological processi

<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 functionHydrolase, Protease, Serine protease
Biological processAngiogenesis, Apoptosis, Cell adhesion

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.4.21.B28, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
Q12884

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
Q12884

SIGNOR Signaling Network Open Resource

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SIGNORi
Q12884

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

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ESTHERi
human-FAP, DPP4N_Peptidase_S9

MEROPS protease database

More...
MEROPSi
S09.007

<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:
Prolyl endopeptidase FAPCurated (EC:3.4.21.261 Publication)
Alternative name(s):
170 kDa melanoma membrane-bound gelatinase2 Publications
Dipeptidyl peptidase FAPCurated (EC:3.4.14.51 Publication)
Fibroblast activation protein alpha1 Publication
Short name:
FAPalphaBy similarity
Gelatine degradation protease FAPCurated (EC:3.4.21.-1 Publication)
Integral membrane serine protease1 Publication
Post-proline cleaving enzymeCurated
Serine integral membrane protease1 Publication
Short name:
SIMP1 Publication
Surface-expressed protease1 Publication
Short name:
Seprase1 Publication
Cleaved into the following chain:
Antiplasmin-cleaving enzyme FAP, soluble form1 Publication (EC:3.4.14.52 Publications, EC:3.4.21.-2 Publications, EC:3.4.21.262 Publications)
Short name:
APCE1 Publication
<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:FAPImported
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:3590, FAP

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600403, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q12884

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000078098

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 4Cytoplasmic1 PublicationSequence analysis4
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei5 – 25Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini26 – 760Extracellular1 PublicationSequence analysisAdd BLAST735

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi123R → A, M or E: Reduces dipeptidyl peptidase and endopeptidase activities. 1 Publication1
Mutagenesisi203E → A, D or Q: Reduces dipeptidyl peptidase and endopeptidase activities. Does not inhibit cell adhesion, migration and invasion. Inhibits dipeptidyl peptidase and endopeptidase activities; when associated with A-204. 2 Publications1
Mutagenesisi204E → A, D or Q: Reduces dipeptidyl peptidase and endopeptidase activities. Does not inhibit cell adhesion, migration and invasion. Inhibits dipeptidyl peptidase and endopeptidase activities; when associated with A-203. 2 Publications1
Mutagenesisi624S → A: Reduces dipeptidyl peptidase and gelatinolytic activities. Does not inhibit cell adhesion, migration and invasion. 2 Publications1
Mutagenesisi656Y → F: Reduces dipeptidyl peptidase and endopeptidase activities. 1 Publication1
Mutagenesisi657A → D or N: Inhibits endopeptidase activity. Increases dipeptidyl peptidase activity. 1 Publication1
Mutagenesisi657A → F or V: Reduces dipeptidyl peptidase and endopeptidase activities. 1 Publication1
Mutagenesisi657A → Q: Inhibits endopeptidase activity. No change in dipeptidyl peptidase activity. 1 Publication1
Mutagenesisi657A → S or T: Reduces strongly endopeptidase activity. No change in dipeptidyl peptidase activity. 1 Publication1
Mutagenesisi704N → A: Reduces dipeptidyl peptidase and endopeptidase activities. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
2191

Open Targets

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OpenTargetsi
ENSG00000078098

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28003

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q12884, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4683

Drug and drug target database

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DrugBanki
DB06474, Sibrotuzumab

DrugCentral

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DrugCentrali
Q12884

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2365

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
FAP

Domain mapping of disease mutations (DMDM)

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DMDMi
292495099

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001224241 – 760Prolyl endopeptidase FAPCuratedAdd BLAST760
ChainiPRO_000043064324 – 760Antiplasmin-cleaving enzyme FAP, soluble form1 PublicationAdd BLAST737

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi49N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi92N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi99N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi227N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation2 Publications1
Glycosylationi314N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
<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 bondi321 ↔ 3321 Publication
Disulfide bondi438 ↔ 4411 Publication
Disulfide bondi448 ↔ 4661 Publication
Disulfide bondi643 ↔ 7551 Publication
Glycosylationi679N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

<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

N-glycosylated.4 Publications
The N-terminus may be blocked.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei23 – 24Cleavage1 Publication2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q12884

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q12884

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q12884

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q12884

PeptideAtlas

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PeptideAtlasi
Q12884

PRoteomics IDEntifications database

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PRIDEi
Q12884

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
59000 [Q12884-1]
59001 [Q12884-2]

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1641, 12 N-Linked glycans (3 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
Q12884, 6 sites, 12 N-linked glycans (3 sites)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q12884

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q12884

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q12884

<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

Expressed in adipose tissue. Expressed in the dermal fibroblasts in the fetal skin. Expressed in the granulation tissue of healing wounds and on reactive stromal fibroblast in epithelial cancers. Expressed in activated fibroblast-like synoviocytes from inflamed synovial tissues. Expressed in activated hepatic stellate cells (HSC) and myofibroblasts from cirrhotic liver, but not detected in normal liver. Expressed in glioma cells (at protein level). Expressed in glioblastomas and glioma cells. Isoform 1 and isoform 2 are expressed in melanoma, carcinoma and fibroblast cell lines.8 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

In fibroblasts at times and sites of tissue remodeling during development, tissue repair and carcinogenesis. Up-regulated upon tumor stem cell differentiation. Up-regulated by transforming growth factor-beta, 12-O-tetradecanoyl phorbol-13-acetate and retinoids.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000078098, Expressed in stromal cell of endometrium and 157 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q12884, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q12884, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000078098, Tissue enhanced (endometrium)

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; homodimerization is required for activity of both plasma membrane and soluble forms. The monomer is inactive. Heterodimer with DPP4.

Interacts with PLAUR; the interaction occurs at the cell surface of invadopodia membranes.

Interacts with ITGB1.

Interacts with ITGA3. Associates with integrin alpha-3/beta-1; the association occurs in a collagen-dependent manner at the cell surface of invadopodia membranes.

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
108485, 18 interactors

Protein interaction database and analysis system

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IntActi
Q12884, 10 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000188790

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q12884

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q12884, protein

<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

1760
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q12884

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q12884

<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

<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

Belongs to the peptidase S9B family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2100, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000160454

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q12884

Identification of Orthologs from Complete Genome Data

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OMAi
NHGIYGG

Database of Orthologous Groups

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OrthoDBi
269253at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q12884

TreeFam database of animal gene trees

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TreeFami
TF313309

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029058, AB_hydrolase
IPR031245, FAP-alpha
IPR002471, Pept_S9_AS
IPR001375, Peptidase_S9
IPR002469, Peptidase_S9B_N

The PANTHER Classification System

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PANTHERi
PTHR11731:SF136, PTHR11731:SF136, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00930, DPPIV_N, 1 hit
PF00326, Peptidase_S9, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53474, SSF53474, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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 basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q12884-1) [UniParc]FASTAAdd to basket
Also known as: L, seprase-I1 Publication

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MKTWVKIVFG VATSAVLALL VMCIVLRPSR VHNSEENTMR ALTLKDILNG
60 70 80 90 100
TFSYKTFFPN WISGQEYLHQ SADNNIVLYN IETGQSYTIL SNRTMKSVNA
110 120 130 140 150
SNYGLSPDRQ FVYLESDYSK LWRYSYTATY YIYDLSNGEF VRGNELPRPI
160 170 180 190 200
QYLCWSPVGS KLAYVYQNNI YLKQRPGDPP FQITFNGREN KIFNGIPDWV
210 220 230 240 250
YEEEMLATKY ALWWSPNGKF LAYAEFNDTD IPVIAYSYYG DEQYPRTINI
260 270 280 290 300
PYPKAGAKNP VVRIFIIDTT YPAYVGPQEV PVPAMIASSD YYFSWLTWVT
310 320 330 340 350
DERVCLQWLK RVQNVSVLSI CDFREDWQTW DCPKTQEHIE ESRTGWAGGF
360 370 380 390 400
FVSTPVFSYD AISYYKIFSD KDGYKHIHYI KDTVENAIQI TSGKWEAINI
410 420 430 440 450
FRVTQDSLFY SSNEFEEYPG RRNIYRISIG SYPPSKKCVT CHLRKERCQY
460 470 480 490 500
YTASFSDYAK YYALVCYGPG IPISTLHDGR TDQEIKILEE NKELENALKN
510 520 530 540 550
IQLPKEEIKK LEVDEITLWY KMILPPQFDR SKKYPLLIQV YGGPCSQSVR
560 570 580 590 600
SVFAVNWISY LASKEGMVIA LVDGRGTAFQ GDKLLYAVYR KLGVYEVEDQ
610 620 630 640 650
ITAVRKFIEM GFIDEKRIAI WGWSYGGYVS SLALASGTGL FKCGIAVAPV
660 670 680 690 700
SSWEYYASVY TERFMGLPTK DDNLEHYKNS TVMARAEYFR NVDYLLIHGT
710 720 730 740 750
ADDNVHFQNS AQIAKALVNA QVDFQAMWYS DQNHGLSGLS TNHLYTHMTH
760
FLKQCFSLSD
Note: Major isoform.
Length:760
Mass (Da):87,713
Last modified:March 23, 2010 - v5
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7FF817B5A4F75142
GO
Isoform 21 Publication (identifier: Q12884-2) [UniParc]FASTAAdd to basket
Also known as: S, Truncated, seprase-s1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-521: Missing.

Note: Upstream open reading frames ORF(s)-containing region inhibits the translation of its downstream ORF.1 Publication
Show »
Length:239
Mass (Da):26,954
Checksum:i853731E1DF446AC6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B4DLR2B4DLR2_HUMAN
Prolyl endopeptidase FAP
FAP
735Annotation score:

Annotation score:2 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>
A0A0D9SEN1A0A0D9SEN1_HUMAN
Prolyl endopeptidase FAP
FAP
759Annotation score:

Annotation score:2 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>
C9J131C9J131_HUMAN
Prolyl endopeptidase FAP
FAP
155Annotation score:

Annotation score:1 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>
F8WF29F8WF29_HUMAN
Prolyl endopeptidase FAP
FAP
121Annotation score:

Annotation score:1 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>
H0YG61H0YG61_HUMAN
Prolyl endopeptidase FAP
FAP
47Annotation score:

Annotation score:1 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>
H7C4D9H7C4D9_HUMAN
Prolyl endopeptidase FAP
FAP
25Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti207A → P in AAB49652 (PubMed:7911242).Curated1
Sequence conflicti229T → K in AAB49652 (PubMed:7911242).Curated1
Sequence conflicti354T → R in AAB49652 (PubMed:7911242).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071264363S → L Decreased plasma membrane expression; loss of homodimerization and dipeptidyl peptidase activity; mislocalized with the calnexin in the endoplasmic reticulum; causes induction of the unfolded protein response (UPR). 2 PublicationsCorresponds to variant dbSNP:rs762738740Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0053671 – 521Missing in isoform 2. 1 PublicationAdd BLAST521

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U09278 mRNA Translation: AAB49652.1
U76833 mRNA Translation: AAC51668.1
AF007822 mRNA Translation: AAF21600.1
AC007750 Genomic DNA Translation: AAY24205.1
CH471058 Genomic DNA Translation: EAX11353.1
BC026250 mRNA Translation: AAH26250.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS33311.1 [Q12884-1]

NCBI Reference Sequences

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RefSeqi
NP_001278736.1, NM_001291807.2
NP_004451.2, NM_004460.4 [Q12884-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000188790; ENSP00000188790; ENSG00000078098 [Q12884-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
2191

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2191

UCSC genome browser

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UCSCi
uc002ucd.3, human [Q12884-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09278 mRNA Translation: AAB49652.1
U76833 mRNA Translation: AAC51668.1
AF007822 mRNA Translation: AAF21600.1
AC007750 Genomic DNA Translation: AAY24205.1
CH471058 Genomic DNA Translation: EAX11353.1
BC026250 mRNA Translation: AAH26250.1
CCDSiCCDS33311.1 [Q12884-1]
RefSeqiNP_001278736.1, NM_001291807.2
NP_004451.2, NM_004460.4 [Q12884-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z68X-ray2.60A/B39-757[»]
6Y0FX-ray2.92A/B/C/D36-757[»]
SMRiQ12884
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi108485, 18 interactors
IntActiQ12884, 10 interactors
STRINGi9606.ENSP00000188790

Chemistry databases

BindingDBiQ12884
ChEMBLiCHEMBL4683
DrugBankiDB06474, Sibrotuzumab
DrugCentraliQ12884
GuidetoPHARMACOLOGYi2365

Protein family/group databases

ESTHERihuman-FAP, DPP4N_Peptidase_S9
MEROPSiS09.007

PTM databases

GlyConnecti1641, 12 N-Linked glycans (3 sites)
GlyGeniQ12884, 6 sites, 12 N-linked glycans (3 sites)
iPTMnetiQ12884
PhosphoSitePlusiQ12884
SwissPalmiQ12884

Genetic variation databases

BioMutaiFAP
DMDMi292495099

Proteomic databases

EPDiQ12884
jPOSTiQ12884
MassIVEiQ12884
PaxDbiQ12884
PeptideAtlasiQ12884
PRIDEiQ12884
ProteomicsDBi59000 [Q12884-1]
59001 [Q12884-2]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
Q12884, 31 sequenced antibodies

Antibodypedia a portal for validated antibodies

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Antibodypediai
33750, 654 antibodies

The DNASU plasmid repository

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DNASUi
2191

Genome annotation databases

EnsembliENST00000188790; ENSP00000188790; ENSG00000078098 [Q12884-1]
GeneIDi2191
KEGGihsa:2191
UCSCiuc002ucd.3, human [Q12884-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2191
DisGeNETi2191

GeneCards: human genes, protein and diseases

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GeneCardsi
FAP
HGNCiHGNC:3590, FAP
HPAiENSG00000078098, Tissue enhanced (endometrium)
MIMi600403, gene
neXtProtiNX_Q12884
OpenTargetsiENSG00000078098
PharmGKBiPA28003
VEuPathDBiHostDB:ENSG00000078098

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2100, Eukaryota
GeneTreeiENSGT00940000160454
InParanoidiQ12884
OMAiNHGIYGG
OrthoDBi269253at2759
PhylomeDBiQ12884
TreeFamiTF313309

Enzyme and pathway databases

BRENDAi3.4.21.B28, 2681
PathwayCommonsiQ12884
SABIO-RKiQ12884
SIGNORiQ12884

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
2191, 8 hits in 1007 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
FAP, human
EvolutionaryTraceiQ12884

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Fibroblast_activation_protein,_alpha

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
2191
PharosiQ12884, Tchem

Protein Ontology

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PROi
PR:Q12884
RNActiQ12884, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000078098, Expressed in stromal cell of endometrium and 157 other tissues
ExpressionAtlasiQ12884, baseline and differential
GenevisibleiQ12884, HS

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR031245, FAP-alpha
IPR002471, Pept_S9_AS
IPR001375, Peptidase_S9
IPR002469, Peptidase_S9B_N
PANTHERiPTHR11731:SF136, PTHR11731:SF136, 1 hit
PfamiView protein in Pfam
PF00930, DPPIV_N, 1 hit
PF00326, Peptidase_S9, 1 hit
SUPFAMiSSF53474, SSF53474, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiSEPR_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>AccessioniPrimary (citable) accession number: Q12884
Secondary accession number(s): O00199
, Q53TP5, Q86Z29, Q99998, Q9UID4
<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 historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 23, 2010
Last modified: September 29, 2021
This is version 198 of the entry and version 5 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with genetic variants
    List of human entries with genetic variants
  4. Human variants curated from literature reports
    Index of human variants curated from literature reports
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
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