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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, vibronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219, PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711). Have also 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 ‘Function’ 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 ‘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 sitei203Substrate1 Publication1
    Binding sitei204Substrate1 Publication1
    <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 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

    • dipeptidyl-peptidase activity Source: UniProtKB
    • endopeptidase activity Source: BHF-UCL
    • integrin binding Source: UniProtKB
    • metalloendopeptidase activity Source: UniProtKB
    • peptidase activity Source: UniProtKB
    • protease binding Source: BHF-UCL
    • protein dimerization activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • serine-type endopeptidase activity Source: UniProtKB
    • serine-type peptidase activity Source: UniProtKB

    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

    More...
    BRENDAi
    3.4.21.B28 2681

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q12884

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q12884

    Protein family/group databases

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

    More...
    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

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000078098.13

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:3590 FAP

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    600403 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q12884

    <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 Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    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

    More...
    DisGeNETi
    2191

    Open Targets

    More...
    OpenTargetsi
    ENSG00000078098

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA28003

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4683

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2365

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    FAP

    Domain mapping of disease mutations (DMDM)

    More...
    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.<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

    More...
    EPDi
    Q12884

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

    More...
    PaxDbi
    Q12884

    PeptideAtlas

    More...
    PeptideAtlasi
    Q12884

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q12884

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    59000
    59001 [Q12884-2]

    PTM databases

    GlyConnect protein glycosylation platform

    More...
    GlyConnecti
    1641

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q12884

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

    More...
    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 141 organ(s), highest expression level in body of uterus

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_FAP

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q12884 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q12884 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA059739

    <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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    108485, 16 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q12884, 10 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q12884

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000188790

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q12884

    <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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q12884

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

    More...
    SMRi
    Q12884

    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
    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

    More...
    eggNOGi
    KOG2100 Eukaryota
    COG1506 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000160454

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000231875

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG005527

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q12884

    KEGG Orthology (KO)

    More...
    KOi
    K08674

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    KHLYTHM

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0BU5

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q12884

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF313309

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.140.10.30, 1 hit
    3.40.50.1820, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029058 AB_hydrolase
    IPR031245 FAP/Dpf2
    IPR002471 Pept_S9_AS
    IPR001375 Peptidase_S9
    IPR002469 Peptidase_S9B_N
    IPR038554 Peptidase_S9B_N_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11731:SF136 PTHR11731:SF136, 1 hit

    Pfam protein domain database

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

    Superfamily database of structural and functional annotation

    More...
    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>.<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 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    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: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>
    A0A0D9SEN1A0A0D9SEN1_HUMAN
    Prolyl endopeptidase FAP
    FAP
    759Annotation 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>
    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>
    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. 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_0053671 – 521Missing in isoform 2. 1 PublicationAdd BLAST521

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    More...
    CCDSi
    CCDS33311.1 [Q12884-1]

    NCBI Reference Sequences

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

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.654370

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000188790; ENSP00000188790; ENSG00000078098 [Q12884-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    2191

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:2191

    UCSC genome browser

    More...
    UCSCi
    uc002ucd.3 human [Q12884-1]

    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

    <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]
    UniGeneiHs.654370

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1Z68X-ray2.60A/B39-757[»]
    ProteinModelPortaliQ12884
    SMRiQ12884
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108485, 16 interactors
    IntActiQ12884, 10 interactors
    MINTiQ12884
    STRINGi9606.ENSP00000188790

    Chemistry databases

    BindingDBiQ12884
    ChEMBLiCHEMBL4683
    GuidetoPHARMACOLOGYi2365

    Protein family/group databases

    ESTHERihuman-FAP DPP4N_Peptidase_S9
    MEROPSiS09.007

    PTM databases

    GlyConnecti1641
    iPTMnetiQ12884
    PhosphoSitePlusiQ12884
    SwissPalmiQ12884

    Polymorphism and mutation databases

    BioMutaiFAP
    DMDMi292495099

    Proteomic databases

    EPDiQ12884
    PaxDbiQ12884
    PeptideAtlasiQ12884
    PRIDEiQ12884
    ProteomicsDBi59000
    59001 [Q12884-2]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    2191
    DisGeNETi2191
    EuPathDBiHostDB:ENSG00000078098.13

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    FAP

    H-Invitational Database, human transcriptome db

    More...
    H-InvDBi
    HIX0002548
    HGNCiHGNC:3590 FAP
    HPAiHPA059739
    MIMi600403 gene
    neXtProtiNX_Q12884
    OpenTargetsiENSG00000078098
    PharmGKBiPA28003

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2100 Eukaryota
    COG1506 LUCA
    GeneTreeiENSGT00940000160454
    HOGENOMiHOG000231875
    HOVERGENiHBG005527
    InParanoidiQ12884
    KOiK08674
    OMAiKHLYTHM
    OrthoDBiEOG091G0BU5
    PhylomeDBiQ12884
    TreeFamiTF313309

    Enzyme and pathway databases

    BRENDAi3.4.21.B28 2681
    SABIO-RKiQ12884
    SIGNORiQ12884

    Miscellaneous databases

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

    More...
    ChiTaRSi
    FAP human
    EvolutionaryTraceiQ12884

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    Fibroblast_activation_protein,_alpha

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

    More...
    GenomeRNAii
    2191

    Protein Ontology

    More...
    PROi
    PR:Q12884

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000078098 Expressed in 141 organ(s), highest expression level in body of uterus
    CleanExiHS_FAP
    ExpressionAtlasiQ12884 baseline and differential
    GenevisibleiQ12884 HS

    Family and domain databases

    Gene3Di2.140.10.30, 1 hit
    3.40.50.1820, 1 hit
    InterProiView protein in InterPro
    IPR029058 AB_hydrolase
    IPR031245 FAP/Dpf2
    IPR002471 Pept_S9_AS
    IPR001375 Peptidase_S9
    IPR002469 Peptidase_S9B_N
    IPR038554 Peptidase_S9B_N_sf
    PANTHERiPTHR11731:SF136 PTHR11731:SF136, 1 hit
    PfamiView protein in Pfam
    PF00930 DPPIV_N, 1 hit
    PF00326 Peptidase_S9, 1 hit
    SUPFAMiSSF53474 SSF53474, 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 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: December 5, 2018
    This is version 181 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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