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Aliases for FAP Gene

Aliases for FAP Gene

  • Fibroblast Activation Protein, Alpha 2 3
  • Seprase 2 3 4
  • 170 KDa Melanoma Membrane-Bound Gelatinase 3 4
  • Gelatine Degradation Protease FAP 3 4
  • Integral Membrane Serine Protease 3 4
  • Serine Integral Membrane Protease 3 4
  • Post-Proline Cleaving Enzyme 3 4
  • Surface-Expressed Protease 3 4
  • Dipeptidyl Peptidase FAP 3 4
  • FAPalpha 3 4
  • SIMP 3 4
  • FAPA 3 6
  • Fibroblast Activation Protein Alpha 4
  • Prolyl Endopeptidase FAP 3
  • EC 3.4.21.26 4
  • EC 3.4.14.5 4
  • EC 3.4.21.- 4
  • DPPIV 3

External Ids for FAP Gene

Previous GeneCards Identifiers for FAP Gene

  • GC02M161080
  • GC02M161555
  • GC02M162991
  • GC02M163229
  • GC02M162852
  • GC02M162735
  • GC02M154909
  • GC02M163027

Summaries for FAP Gene

Entrez Gene Summary for FAP Gene

  • The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. It is selectively expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. This protein is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2014]

GeneCards Summary for FAP Gene

FAP (Fibroblast Activation Protein, Alpha) is a Protein Coding gene. Diseases associated with FAP include infiltrative basal cell carcinoma and pharyngitis. GO annotations related to this gene include protein homodimerization activity and protein dimerization activity. An important paralog of this gene is DPP4.

UniProtKB/Swiss-Prot for FAP Gene

  • 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.

Gene Wiki entry for FAP Gene

No data available for Tocris Summary , PharmGKB "VIP" Summary , fRNAdb sequence ontologies and piRNA Summary for FAP Gene

Genomics for FAP Gene

Regulatory Elements for FAP Gene

Genomic Location for FAP Gene

Start:
162,170,684 bp from pter
End:
162,245,151 bp from pter
Size:
74,468 bases
Orientation:
Minus strand

Genomic View for FAP Gene

UCSC Golden Path with GeneCards custom track
Cytogenetic band:
Genomic Location for FAP Gene
GeneLoc Logo Genomic Neighborhood Exon StructureGene Density

RefSeq DNA sequence for FAP Gene

Proteins for FAP Gene

  • Protein details for FAP Gene (UniProtKB/Swiss-Prot)

    Protein Symbol:
    Q12884-SEPR_HUMAN
    Recommended name:
    Prolyl endopeptidase FAP
    Protein Accession:
    Q12884
    Secondary Accessions:
    • O00199
    • Q53TP5
    • Q86Z29
    • Q99998
    • Q9UID4

    Protein attributes for FAP Gene

    Size:
    760 amino acids
    Molecular mass:
    87713 Da
    Quaternary structure:
    • 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.

    Three dimensional structures from OCA and Proteopedia for FAP Gene

    Alternative splice isoforms for FAP Gene

    UniProtKB/Swiss-Prot:

neXtProt entry for FAP Gene

Proteomics data for FAP Gene at MOPED

Post-translational modifications for FAP Gene

Other Protein References for FAP Gene

Antibody Products

  • R&D Systems Antibodies for FAP (Fibroblast Activation Protein alpha/FAP)

No data available for DME Specific Peptides for FAP Gene

Domains for FAP Gene

Suggested Antigen Peptide Sequences for FAP Gene

Graphical View of Domain Structure for InterPro Entry

Q12884

UniProtKB/Swiss-Prot:

SEPR_HUMAN :
  • Q12884
Family:
  • Belongs to the peptidase S9B family.
genes like me logo Genes that share domains with FAP: view

No data available for Gene Families for FAP Gene

Function for FAP Gene

Molecular function for FAP Gene

GENATLAS Biochemistry: fibroblast activation protein alpha (95kDa),expressed in epithelial cancer stroma,same gene as seprase
UniProtKB/Swiss-Prot BiophysicochemicalProperties: Kinetic parameters: KM=0.46 mM for Ala-Pro (Dipeptidyl peptidase activity) {ECO:0000269 PubMed:10593948}; KM=0.9 mM for Lys-Pro (Dipeptidyl peptidase activity) {ECO:0000269 PubMed:10593948}; KM=1.15 mM for Gly-Pro (Dipeptidyl peptidase activity) {ECO:0000269 PubMed:10593948}; KM=0.25 mM for Gly-Pro (Dipeptidyl peptidase activity) {ECO:0000269 PubMed:17381073}; KM=0.24 mM for Ala-Pro (Dipeptidyl peptidase activity) {ECO:0000269 PubMed:16410248}; KM=0.10 mM for Ile-Pro (Dipeptidyl peptidase activity) {ECO:0000269 PubMed:16410248}; KM=0.24 mM for Phe-Pro (Dipeptidyl peptidase activity) {ECO:0000269 PubMed:16410248}; KM=0.24 mM for Gly-Pro (Dipeptidyl peptidase activity) {ECO:0000269 PubMed:16410248}; KM=0.33 mM for Ac-Gly-Pro (Prolyl endopeptidase activity) {ECO:0000269 PubMed:16410248, ECO:0000269 PubMed:17381073}; KM=1.3 uM for Thr-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity) {ECO:0000269 PubMed:16480718}; KM=2.2 uM for Ala-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity) {ECO:0000269 PubMed:16480718}; KM=0.7 uM for Thr-Ala-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity) {ECO:0000269 PubMed:16480718}; KM=1.9 uM for Thr-Ser-Gly-Pro-Ser-Gln (Prolyl endopeptidase activity) {ECO:0000269 PubMed:16480718}; KM=2.2 uM for Thr-Ser-Gly-Pro-Asn-Ser (Prolyl endopeptidase activity) {ECO:0000269 PubMed:16480718}; KM=4.3 uM for Ala-Ser-Gly-Pro-Ser-Ser (Prolyl endopeptidase activity) {ECO:0000269 PubMed:16480718}; KM=0.101 mM for Gly-Pro (FAP form, prolyl endopeptidase activity) {ECO:0000269 PubMed:16223769}; KM=0.124 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble form, prolyl endopeptidase activity) {ECO:0000269 PubMed:16223769}; KM=0.323 mM for Gly-Pro (FAP form, dipeptidyl peptidase activity) {ECO:0000269 PubMed:16223769}; KM=0.272 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble form, dipeptidyl peptidase activity) {ECO:0000269 PubMed:16223769}; KM=0.029 mM for Arg-Gly-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu (FAP form, prolyl endopeptidase activity) {ECO:0000269 PubMed:16223769}; 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) {ECO:0000269 PubMed:16223769}; pH dependence: Optimum pH is 6-8.4 for gelatinase activity. At pH lower than 5 inhibited gelatinase activity. {ECO:0000269 PubMed:2172980, ECO:0000269 PubMed:9065413}; Temperature dependence: Optimum temperature is 37 degrees Celsius for gelatinase activity. Temperatures above 50 degrees Celsius inhibit gelatinase activity. {ECO:0000269 PubMed:2172980, ECO:0000269 PubMed:9065413};
UniProtKB/Swiss-Prot CatalyticActivity: Hydrolysis of Pro- -Xaa >> Ala- -Xaa in oligopeptides.
UniProtKB/Swiss-Prot CatalyticActivity: Release of an N-terminal dipeptide, Xaa-Yaa- -Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
UniProtKB/Swiss-Prot EnzymeRegulation: 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.
UniProtKB/Swiss-Prot Function: 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.
UniProtKB/Swiss-Prot Induction: 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.

Enzyme Numbers (IUBMB) for FAP Gene

Gene Ontology (GO) - Molecular Function for FAP Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0002020 protease binding IPI 17317851
GO:0004175 endopeptidase activity IDA 17317851
GO:0004222 metalloendopeptidase activity TAS 9065413
GO:0004252 serine-type endopeptidase activity IDA 10593948
GO:0005178 integrin binding IPI 10455171
genes like me logo Genes that share ontologies with FAP: view

Phenotypes for FAP Gene

MGI mutant phenotypes for FAP:
inferred from 2 alleles
genes like me logo Genes that share phenotypes with FAP: view

Animal Models for FAP Gene

MGI Knock Outs for FAP:

Animal Model Products

CRISPR Products

No data available for miRNA , Transcription Factor Targeting and HOMER Transcription for FAP Gene

Localization for FAP Gene

Subcellular locations from UniProtKB/Swiss-Prot for FAP Gene

Prolyl endopeptidase FAP: Cell surface. Cell membrane; Single-pass type II membrane protein. Cell projection, lamellipodium membrane; Single-pass type II membrane protein. Cell projection, invadopodium membrane; Single-pass type II membrane protein. Cell projection, ruffle membrane; Single-pass type II membrane protein. Membrane; Single-pass type II membrane protein. Note=Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin. {ECO:0000269 PubMed:10593948, ECO:0000269 PubMed:12376466, ECO:0000269 PubMed:16175601, ECO:0000269 PubMed:16651416, ECO:0000269 PubMed:17105646, ECO:0000269 PubMed:2172980, ECO:0000269 PubMed:24717288, ECO:0000269 PubMed:7911242, ECO:0000269 PubMed:7923219, ECO:0000269 PubMed:9065413, ECO:0000303 PubMed:10455171}.
Antiplasmin-cleaving enzyme FAP, soluble form: Secreted. Note=Found in blood plasma and serum. {ECO:0000269 PubMed:14751930, ECO:0000269 PubMed:16223769, ECO:0000269 PubMed:24371721}.
Isoform 2: Cytoplasm.

Subcellular locations from

COMPARTMENTS
Jensen Localization Image for FAP Gene COMPARTMENTS Subcellular localization image for FAP gene
Compartment Confidence
plasma membrane 5
extracellular 4
golgi apparatus 2
endoplasmic reticulum 1
lysosome 1

Gene Ontology (GO) - Cellular Components for FAP Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0005615 extracellular space IDA 17317851
GO:0005737 cytoplasm IEA --
GO:0005886 plasma membrane NAS 10455171
GO:0005925 focal adhesion IDA 21423176
GO:0009986 cell surface ISS --
genes like me logo Genes that share ontologies with FAP: view

Pathways for FAP Gene

SuperPathways for FAP Gene

No Data Available

PCR Array Products

  • Pathway & Disease-focused RT² Profiler PCR Arrays

Gene Ontology (GO) - Biological Process for FAP Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0001525 angiogenesis IEA --
GO:0006508 proteolysis IDA 10455171
GO:0007155 cell adhesion IEA --
GO:0010710 regulation of collagen catabolic process IDA 10455171
GO:0010716 negative regulation of extracellular matrix disassembly IDA 16651416
genes like me logo Genes that share ontologies with FAP: view

No data available for Pathways by source for FAP Gene

Compounds for FAP Gene

(4) Novoseek inferred chemical compound relationships for FAP Gene

Compound -log(P) Hits PubMed IDs
dpps 74.7 1
serine 71.4 54
proline 25.3 2
matrigel 17.4 2
genes like me logo Genes that share compounds with FAP: view

Transcripts for FAP Gene

Unigene Clusters for FAP Gene

Fibroblast activation protein, alpha:
Representative Sequences:

CRISPR Products

miRNA Products

Inhibitory RNA Products

  • Predesigned siRNA for gene silencing in human,mouse,rat for FAP

Primer Products

Flow Cytometry Products

Alternative Splicing Database (ASD) splice patterns (SP) for FAP Gene

ExUns: 1 ^ 2a · 2b ^ 3 ^ 4 ^ 5 ^ 6 ^ 7 ^ 8a · 8b ^ 9 ^ 10 ^ 11 ^ 12 ^ 13 ^ 14 ^ 15 ^ 16a · 16b · 16c ^ 17 ^ 18 ^ 19a · 19b ^ 20 ^ 21 ^
SP1: - - - - - -
SP2: - - -
SP3:
SP4:
SP5: - -
SP6:
SP7: - - -
SP8:

ExUns: 22a · 22b ^ 23 ^ 24a · 24b ^ 25a · 25b ^ 26a · 26b ^ 27 ^ 28 ^ 29 ^ 30
SP1: - - -
SP2: - - -
SP3:
SP4:
SP5: -
SP6: -
SP7:
SP8:

Relevant External Links for FAP Gene

GeneLoc Exon Structure for
FAP
ECgene alternative splicing isoforms for
FAP

Expression for FAP Gene

mRNA expression in normal human tissues for FAP Gene

mRNA expression in embryonic tissues and stem cells from LifeMap Discovery

mRNA differential expression in normal tissues according to GTEx for FAP Gene

This gene is overexpressed in Uterus (4.9).

Integrated Proteomics: protein expression from ProteomicsDB, PaxDb, and MOPED for FAP Gene

SOURCE GeneReport for Unigene cluster for FAP Gene Hs.654370

mRNA Expression by UniProt/SwissProt for FAP Gene

Q12884-SEPR_HUMAN
Tissue specificity: 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.
genes like me logo Genes that share expressions with FAP: view

In Situ Assay Products

Orthologs for FAP Gene

This gene was present in the common ancestor of animals and fungi.

Orthologs for FAP Gene

Organism Taxonomy Gene Similarity Type Details
chimpanzee
(Pan troglodytes)
Mammalia FAP 35
  • 99.69 (n)
  • 100 (a)
FAP 36
  • 100 (a)
OneToOne
cow
(Bos Taurus)
Mammalia FAP 35
  • 93.99 (n)
  • 93.95 (a)
FAP 36
  • 94 (a)
OneToOne
dog
(Canis familiaris)
Mammalia FAP 35
  • 93.99 (n)
  • 93.29 (a)
FAP 36
  • 93 (a)
OneToOne
mouse
(Mus musculus)
Mammalia Fap 35
  • 89.43 (n)
  • 89.61 (a)
Fap 16
Fap 36
  • 89 (a)
OneToOne
oppossum
(Monodelphis domestica)
Mammalia FAP 36
  • 87 (a)
OneToOne
platypus
(Ornithorhynchus anatinus)
Mammalia FAP 36
  • 84 (a)
OneToOne
rat
(Rattus norvegicus)
Mammalia Fap 35
  • 88.2 (n)
  • 88.95 (a)
chicken
(Gallus gallus)
Aves FAP 35
  • 75.1 (n)
  • 73.65 (a)
FAP 36
  • 74 (a)
OneToOne
lizard
(Anolis carolinensis)
Reptilia FAP 36
  • 66 (a)
OneToOne
African clawed frog
(Xenopus laevis)
Amphibia fap-A 35
tropical clawed frog
(Silurana tropicalis)
Amphibia fap 35
  • 66.58 (n)
  • 61.19 (a)
zebrafish
(Danio rerio)
Actinopterygii dpp4 36
  • 48 (a)
ManyToMany
fap 36
  • 51 (a)
ManyToMany
African malaria mosquito
(Anopheles gambiae)
Insecta AgaP_AGAP011584 35
  • 45.29 (n)
  • 39.13 (a)
fruit fly
(Drosophila melanogaster)
Insecta CG11034 36
  • 30 (a)
ManyToMany
CG11319 36
  • 26 (a)
ManyToMany
CG17684 36
  • 26 (a)
ManyToMany
CG9059 36
  • 21 (a)
ManyToMany
ome 35
  • 46.05 (n)
  • 36.38 (a)
ome 36
  • 24 (a)
ManyToMany
CG11319 37
  • 35 (a)
CG11034 37
  • 31 (a)
worm
(Caenorhabditis elegans)
Secernentea dpf-1 36
  • 24 (a)
ManyToMany
dpf-2 36
  • 25 (a)
ManyToMany
T23F1.7b 37
  • 30 (a)
C27C12.7 37
  • 30 (a)
T23F1.7a 37
  • 29 (a)
baker's yeast
(Saccharomyces cerevisiae)
Saccharomycetes DAP2 36
  • 26 (a)
ManyToMany
STE13 36
  • 21 (a)
ManyToMany
sea squirt
(Ciona savignyi)
Ascidiacea -- 36
  • 34 (a)
ManyToMany
-- 36
  • 41 (a)
ManyToMany
-- 36
  • 23 (a)
ManyToMany
-- 36
  • 35 (a)
ManyToMany
Species with no ortholog for FAP:
  • A. gosspyii yeast (Ashbya gossypii)
  • Actinobacteria (Mycobacterium tuberculosis)
  • Alicante grape (Vitis vinifera)
  • alpha proteobacteria (Wolbachia pipientis)
  • amoeba (Dictyostelium discoideum)
  • Archea (Pyrococcus horikoshii)
  • barley (Hordeum vulgare)
  • beta proteobacteria (Neisseria meningitidis)
  • bread mold (Neurospora crassa)
  • Chromalveolata (Phytophthora infestans)
  • common water flea (Daphnia pulex)
  • corn (Zea mays)
  • E. coli (Escherichia coli)
  • filamentous fungi (Aspergillus nidulans)
  • Firmicute bacteria (Streptococcus pneumoniae)
  • fission yeast (Schizosaccharomyces pombe)
  • green algae (Chlamydomonas reinhardtii)
  • honey bee (Apis mellifera)
  • K. lactis yeast (Kluyveromyces lactis)
  • loblloly pine (Pinus taeda)
  • malaria parasite (Plasmodium falciparum)
  • medicago trunc (Medicago Truncatula)
  • moss (Physcomitrella patens)
  • orangutan (Pongo pygmaeus)
  • pig (Sus scrofa)
  • rainbow trout (Oncorhynchus mykiss)
  • rice (Oryza sativa)
  • rice blast fungus (Magnaporthe grisea)
  • schistosome parasite (Schistosoma mansoni)
  • sea anemone (Nematostella vectensis)
  • sea urchin (Strongylocentrotus purpuratus)
  • sorghum (Sorghum bicolor)
  • soybean (Glycine max)
  • stem rust fungus (Puccinia graminis)
  • sugarcane (Saccharum officinarum)
  • thale cress (Arabidopsis thaliana)
  • tomato (Lycopersicon esculentum)
  • toxoplasmosis (Toxoplasma gondii)
  • Trichoplax (Trichoplax adhaerens)
  • wheat (Triticum aestivum)

Evolution for FAP Gene

ENSEMBL:
Gene Tree for FAP (if available)
TreeFam:
Gene Tree for FAP (if available)

Paralogs for FAP Gene

Paralogs for FAP Gene

Selected SIMAP similar genes for FAP Gene using alignment to 6 proteins:

genes like me logo Genes that share paralogs with FAP: view

Variants for FAP Gene

Sequence variations from dbSNP and Humsavar for FAP Gene

SNP ID Clin Chr 02 pos Sequence Context AA Info Type MAF
rs977907 -- 162,221,345(+) gccaa(A/T)atgga intron-variant
rs980012 -- 162,223,975(+) TTTCC(C/T)TTCAT intron-variant
rs1030093 -- 162,183,629(+) ataat(A/T)ttatC intron-variant
rs1126507 -- 162,203,132(-) TTCAA(C/G)ACCAG reference, missense
rs1468916 -- 162,194,905(+) CACTT(C/T)TAAGT intron-variant

Structural Variations from Database of Genomic Variants (DGV) for FAP Gene

Variant ID Type Subtype PubMed ID
nsv834439 CNV Gain 17160897
nsv834440 CNV Gain 17160897
nsv3009 CNV Insertion 18451855

Relevant External Links for FAP Gene

HapMap Linkage Disequilibrium report
FAP
Human Gene Mutation Database (HGMD)
FAP

No data available for Polymorphic Variants from UniProtKB/Swiss-Prot for FAP Gene

Disorders for FAP Gene

MalaCards: The human disease database

MalaCards: The human disease database. (3) Diseases for FAP Gene including...

Search for FAP Gene in MalaCards »

(1) University of Copenhagen DISEASES for FAP Gene

(19) Novoseek inferred disease relationships for FAP Gene

Disease -log(P) Hits PubMed IDs
stromal tumors 73.5 6
epithelial tumor 48.7 5
metastasis 47 25
melanoma 46.7 21
cancer 44.1 43

Relevant External Links for FAP

Genetic Association Database (GAD)
FAP
Human Genome Epidemiology (HuGE) Navigator
FAP
genes like me logo Genes that share disorders with FAP: view

No data available for UniProtKB/Swiss-Prot for FAP Gene

Publications for FAP Gene

  1. Molecular cloning of seprase: a serine integral membrane protease from human melanoma. (PMID: 9247085) Goldstein L.A. … Chen W.-T. (Biochim. Biophys. Acta 1997) 2 3 4 23
  2. A novel protease-docking function of integrin at invadopodia. (PMID: 10455171) Mueller S.C. … Chen W.T. (J. Biol. Chem. 1999) 3 4 23
  3. Fibroblast activation protein, a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts. (PMID: 10593948) Park J.E. … Rettig W.J. (J. Biol. Chem. 1999) 3 4 23
  4. Molecular cloning of fibroblast activation protein alpha, a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers. (PMID: 7911242) Scanlan M.J. … Rettig W.J. (Proc. Natl. Acad. Sci. U.S.A. 1994) 3 4 23
  5. Fibroblast activation protein: purification, epitope mapping and induction by growth factors. (PMID: 7519584) Rettig W.J. … Old L.J. (Int. J. Cancer 1994) 3 4 23

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