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FAP Gene(Protein Coding)

Fibroblast Activation Protein Alpha

GCID:
GC02M162170
GIFtS:
60
Genes Participants
UDN Logo

Aliases for FAP Gene

Aliases for FAP Gene

  • Fibroblast Activation Protein Alpha 2 3 4 5
  • Seprase 2 3 4
  • 170 KDa Melanoma Membrane-Bound Gelatinase 3 4
  • Gelatine Degradation Protease FAP 3 4
  • Integral Membrane Serine 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
  • Fibroblast Activation Protein, Alpha 2
  • Serine Integral Membrane Protease 4
  • Prolyl Endopeptidase FAP 3
  • EC 3.4.21.26 4
  • EC 3.4.14.5 4
  • EC 3.4.21.- 4
  • DPPIV 3
  • FAPA 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 Breast Ductal Carcinoma. GO annotations related to this gene include protein homodimerization activity and serine-type endopeptidase 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 CIViC summary , Tocris Summary , PharmGKB "VIP" Summary , fRNAdb sequence ontologies and piRNA Summary for FAP Gene

Genomics for FAP Gene

Products:

  1. Regulatory Element

Regulatory Elements for FAP Gene

Enhancers for FAP Gene
GeneHancer Identifier Enhancer Score Enhancer Sources Gene-Enhancer Score TSS distance (kb) Number of Genes Away Size (kb) Transcription Factor Binding Sites within enhancer Gene Targets for Enhancer
GH02G162196 0.8 ENCODE dbSUPER 17 +46.8 46783 3.5 JUND HLF FOS MAFK NFE2L2 FAP LOC101929532 GCG
GH02G162220 1 ENCODE dbSUPER 11.8 +24.4 24394 1.1 CTCF ZNF654 RNF2 MTA2 TRIM22 ARID4B ZNF644 RAD21 CEBPA ZNF580 FAP GCG
GH02G162316 1.3 ENCODE dbSUPER 4.9 -73.7 -73659 4.1 HDGF PKNOX1 ATF1 WRNIP1 ARID4B SIN3A ZNF48 YY1 ZNF766 CBX5 FAP GCA PIR31305
GH02G162240 1.2 Ensembl ENCODE dbSUPER 5.3 +1.3 1327 6.8 SOX5 SOX13 FOXA2 JUN SIN3A CEBPB EP300 JUND STAT3 FOS FAP GCG
GH02G162260 1 Ensembl ENCODE dbSUPER 5.4 -16.4 -16392 1.5 JUND JUNB FOS ZNF7 GABPA FAP GC02P162270 LOC105373724
- Elite enhancer and/or Elite enhancer-gene association Download GeneHancer data dump

Enhancers around FAP on UCSC Golden Path with GeneCards custom track

Transcription factor binding sites by QIAGEN in the FAP gene promoter:

Genomic Location for FAP Gene

Chromosome:
2
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

Genes around FAP on UCSC Golden Path with GeneCards custom track

Cytogenetic band:
FAP Gene in genomic location: bands according to Ensembl, locations according to GeneLoc (and/or Entrez Gene and/or Ensembl if different)
Genomic Location for FAP Gene
GeneLoc Logo Genomic Neighborhood • Exon Structure • Gene Density

RefSeq DNA sequence for FAP Gene

Proteins for FAP Gene

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  • 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

Protein Expression for FAP Gene

See protein expression from ProteomicsDB, MOPED, PaxDb, and MaxQB

Post-translational modifications for FAP Gene

Other Protein References for FAP Gene

ENSEMBL proteins:
REFSEQ proteins:

Antibody Products

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

No data available for DME Specific Peptides for FAP Gene

Domains & Families for FAP Gene

Gene Families for FAP Gene

HGNC:

Protein Domains for FAP Gene

InterPro:
Blocks:
ProtoNet:

Suggested Antigen Peptide Sequences for FAP Gene

GenScript: Design optimal peptide antigens:

Graphical View of Domain Structure for InterPro Entry

Q12884

UniProtKB/Swiss-Prot:

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

Function for FAP Gene

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  2. CRISPR
  3. miRNA
  4. Inhibitory RNA
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  7. Flow Cytometry

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 IEA,IDA 10593948
GO:0005178 integrin binding IPI 10455171
genes like me logo Genes that share ontologies with FAP: view
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

Inhibitory RNA Products

Flow Cytometry Products

No data available for Human Phenotype Ontology , miRNA , Transcription Factor Targets 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
Extracellular space Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi Apparatus Nucleus Mitochondrion 0 1 2 3 4 5 Confidence
COMPARTMENTS Subcellular localization image for FAP gene
Compartment Confidence
plasma membrane 5
extracellular 5
golgi apparatus 2
endoplasmic reticulum 1
cytosol 1
lysosome 1

Gene Ontology (GO) - Cellular Components for FAP Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0005576 extracellular region IEA --
GO:0005615 extracellular space IDA 17317851
GO:0005737 cytoplasm IEA --
GO:0005886 plasma membrane NAS 10455171
GO:0005925 focal adhesion IDA 21423176
genes like me logo Genes that share ontologies with FAP: view

Pathways & Interactions for FAP Gene

SuperPathways for FAP Gene

PathCards logo More details on SuperPathways for FAP
No Data Available

Gene Ontology (GO) - Biological Process for FAP Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0001525 angiogenesis IEA --
GO:0006508 proteolysis IEA,IDA 10455171
GO:0006915 apoptotic process IEA --
GO:0007155 cell adhesion IEA --
GO:0010710 regulation of collagen catabolic process IDA 10455171
genes like me logo Genes that share ontologies with FAP: view

No data available for Pathways by source and SIGNOR curated interactions for FAP Gene

Drugs & Compounds for FAP Gene

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(14) Drugs for FAP Gene - From: ClinicalTrials and Novoseek

Name Status Disease Links Group Role Mechanism of Action Clinical Trials
Celecoxib Approved, Investigational Pharma Inhibition, Inhibitor Selective cyclooxygenase-2 (COX-2) inhibitor 444
Analgesics Pharma 11733
Analgesics, Non-Narcotic Pharma 6501
Anti-Inflammatory Agents Pharma 10729
Anti-Inflammatory Agents, Non-Steroidal Pharma 4443

(2) Additional Compounds for FAP Gene - From: Novoseek

Name Synonyms Role CAS Number PubChem IDs PubMed IDs
genes like me logo Genes that share compounds with FAP: view

Transcripts for FAP Gene

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  1. CRISPR
  2. miRNA
  3. Inhibitory RNA
  4. Clone
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mRNA/cDNA for FAP Gene

(5) REFSEQ mRNAs :
(9) Additional mRNA sequences :
(103) Selected AceView cDNA sequences:
(14) Ensembl transcripts including schematic representations, and UCSC links where relevant :

Unigene Clusters for FAP Gene

Fibroblast activation protein, alpha:
Representative Sequences:

CRISPR Products

Inhibitory RNA 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

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  1. Primer

mRNA expression in normal human tissues from GTEx, Illumina, BioGPS, and CGAP SAGE for FAP Gene

mRNA expression in normal human tissues for FAP Gene
mRNA expression by BioGPS for FAP GenemRNA expression by GTEx 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 (x4.9).

Protein differential expression in normal tissues from HIPED for FAP Gene

This gene is overexpressed in Serum (18.7), Uterus (18.7), Islet of Langerhans (8.7), and Plasma (6.2).

Integrated Proteomics: protein expression in normal tissues and cell lines from ProteomicsDB, PaxDb, and MOPED for FAP Gene



NURSA nuclear receptor signaling pathways regulating expression of FAP Gene:

FAP

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.

Evidence on tissue expression from TISSUES for FAP Gene

  • Bone marrow(4)
  • Pancreas(2.4)
  • Skin(2.4)
  • Intestine(2.2)
  • Nervous system(2.2)
genes like me logo Genes that share expression patterns with FAP: view

Primer Products

No data available for Protein tissue co-expression partners and Phenotype-based relationships between genes and organs from Gene ORGANizer for FAP Gene

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 34 35
  • 99.69 (n)
cow
(Bos Taurus)
 Mammalia FAP 34 35
  • 93.99 (n)
dog
(Canis familiaris)
 Mammalia FAP 34 35
  • 93.99 (n)
mouse
(Mus musculus)
 Mammalia Fap 34 16 35
  • 89.43 (n)
rat
(Rattus norvegicus)
 Mammalia Fap 34
  • 88.2 (n)
oppossum
(Monodelphis domestica)
 Mammalia FAP 35
  • 87 (a)
 OneToOne
platypus
(Ornithorhynchus anatinus)
 Mammalia FAP 35
  • 84 (a)
 OneToOne
chicken
(Gallus gallus)
 Aves FAP 34 35
  • 75.1 (n)
lizard
(Anolis carolinensis)
 Reptilia FAP 35
  • 66 (a)
 OneToOne
tropical clawed frog
(Silurana tropicalis)
 Amphibia fap 34
  • 66.58 (n)
African clawed frog
(Xenopus laevis)
 Amphibia fap-A 34
zebrafish
(Danio rerio)
 Actinopterygii fap 35
  • 51 (a)
 ManyToMany
dpp4 35
  • 48 (a)
 ManyToMany
fruit fly
(Drosophila melanogaster)
 Insecta ome 35 34
  • 46.05 (n)
 ManyToMany
CG11319 36 35
  • 35 (a)
CG11034 36 35
  • 31 (a)
CG17684 35
  • 26 (a)
 ManyToMany
CG9059 35
  • 21 (a)
 ManyToMany
African malaria mosquito
(Anopheles gambiae)
 Insecta AgaP_AGAP011584 34
  • 45.29 (n)
worm
(Caenorhabditis elegans)
 Secernentea C27C12.7 36
  • 30 (a)
T23F1.7b 36
  • 30 (a)
T23F1.7a 36
  • 29 (a)
dpf-2 35
  • 25 (a)
 ManyToMany
dpf-1 35
  • 24 (a)
 ManyToMany
baker's yeast
(Saccharomyces cerevisiae)
 Saccharomycetes DAP2 35
  • 26 (a)
 ManyToMany
STE13 35
  • 21 (a)
 ManyToMany
sea squirt
(Ciona savignyi)
 Ascidiacea -- 35
  • 41 (a)
 ManyToMany
-- 35
  • 35 (a)
 ManyToMany
-- 35
  • 34 (a)
 ManyToMany
-- 35
  • 23 (a)
 ManyToMany
Species where no ortholog for FAP was found in the sources mined by GeneCards:
  • 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

(3) 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
rs1000079893 -- 162,202,561(+) GAAAC(G/T)TGTTC intron-variant
rs1000097199 -- 162,226,857(+) CTGGC(C/T)GGAAA intron-variant
rs1000116460 -- 162,206,926(+) TTTTC(G/T)AATTC intron-variant
rs1000124096 -- 162,176,048(+) TTTTA(A/G)GACCT intron-variant
rs1000127007 -- 162,226,753(+) GAACT(C/T)CTATC intron-variant

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

Variant ID Type Subtype PubMed ID
dgv749e214 CNV gain 21293372
esv3593177 CNV loss 21293372
nsv3009 CNV insertion 18451855
nsv472079 CNV novel sequence insertion 20440878
nsv834439 CNV gain 17160897
nsv834440 CNV gain 17160897

Variation tolerance for FAP Gene

Residual Variation Intolerance Score: 10.2% of all genes are more intolerant (likely to be disease-causing)
Gene Damage Index Score: 2.77; 47.19% of all genes are more intolerant (likely to be disease-causing)

Relevant External Links for FAP Gene

Human Gene Mutation Database (HGMD)
FAP
SNPedia medical, phenotypic, and genealogical associations of SNPs for
FAP

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

Disorders for FAP Gene

MalaCards: The human disease database

(4) MalaCards diseases for FAP Gene - From: DISEASES, Novoseek, and GeneCards

Disorder Aliases PubMed IDs
infiltrative basal cell carcinoma
  • skin infiltrating basal cell carcinoma
breast ductal carcinoma
  • duct carcinoma, nos
melanoma
  • malignant melanoma
glioma
- elite association - COSMIC cancer census association via MalaCards
Search FAP in MalaCards View complete list of genes associated with diseases

Relevant External Links for FAP

Genetic Association Database (GAD)
FAP
Human Genome Epidemiology (HuGE) Navigator
FAP
Atlas of Genetics and Cytogenetics in Oncology and Haematology:
FAP
genes like me logo Genes that share disorders with FAP: view

No data available for UniProtKB/Swiss-Prot and Genatlas 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 22 64
  2. Fibroblast activation protein peptide substrates identified from human collagen I derived gelatin cleavage sites. (PMID: 18095711) Aggarwal S. … Denmeade S.R. (Biochemistry 2008) 3 4 22 64
  3. Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity. (PMID: 16410248) Edosada C.Y. … Wolf B.B. (J. Biol. Chem. 2006) 3 4 22 64
  4. Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein. (PMID: 16223769) Lee K.N. … McKee P.A. (Blood 2006) 3 4 22 64
  5. The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices. (PMID: 16651416) Ghersi G. … Chen W.T. (Cancer Res. 2006) 3 4 22 64

Products for FAP Gene

Sources for FAP Gene

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