FABP5 (fatty acid binding protein 5 (psoriasis-associated))

2014-08-01   Erin Balcom , Rong-Zong Liu , Stanley Poon , Roseline Godbout 

Department of Oncology, University of Alberta, Cross Cancer Institute, 11560 University Avenue, Edmonton, Alberta, T6G 1Z2 Canada




The FABP5 gene encodes a member of the fatty acid binding protein family which is also known as epidermal or cutaneous FABP. Overexpression of FABP5 is associated with a number of cancers including breast and prostate cancers, as well as psychiatric disorders and diabetes. FABP5 can bind retinoic acid as well as polyunsaturated and saturated fatty acids. Transport of FABP5 ligands such as arachidonic acid and retinoic acid to the nucleus is believed to activate the nuclear receptor peroxisome proliferator-activated receptor beta\/delta (PPARβ\/δ).


Atlas Image
FABP 5 gene. The FABP5 gene is located on chromosome 8 in the region of q21.13 on the positive strand. Neighbouring genes are indicated.


The FABP5 gene spans approximately 4.3 kb and has 4 exons, all of which contain coding sequences.
Ten SNPs have been validated in the coding region of FABP5, 7 missense and 3 synonymous (not affecting the amino acid sequence). Two SNPs in the regulatory region of FABP5 have been identified in association with type 2 diabetes mellitus (T2DM): rs454550 showed significant association with T2DM in a non-Hispanic White sample, and a newly reported SNP at genomic position 82354416 was associated with T2DM in both non-Hispanic White and African sample populations (Bu et al., 2011). A missense 340G>C (Gly114Arg) SNP in the coding region of FABP5 has been linked to autism (Maekawa et al., 2010). FABP5 SNPs are described at the following site (http://www.ncbi.nlm.nih.gov/snp).


The transcript is approximately 750 nucleotides with an open reading frame of 408 nucleotides, a 5 untranslated region of 113 nucleotides and a 3 untranslated region of 209 nucleotides excluding the poly-A tail.
Based on Expressed Sequence Tag (EST) data, FABP5 RNA is present in a wide range of human tissues, with highest levels in the uterus, pharynx, bone, and heart. FABP5 transcripts have been identified in normal mammalian cells, including adipocytes, tongue epithelia, lens (Wen et al., 1995), developing retina, lung and mammary gland epithelia (Zimmerman and Veerkamp, 2002), macrophages, kidney, liver, and skeletal muscle (Smathers and Petersen, 2011). Immunohistochemistry has confirmed the presence of FABP5 in endothelial cells of the placenta, heart, small intestine, and renal medulla (Masouyé et al., 1997).
Nerve growth factor (NGF) positively regulates FABP5 expression in PC12 cells (pheochromocytoma of rat adrenal medulla) through a MEK-dependent pathway (Liu et al., 2008). FABP5 is a known target of c-Myc (Coller et al., 2000), and epithelial cell adhesion molecule epCAM has been demonstrated to upregulate FABP5 expression, presumably via induction of c-Myc (Münz et al., 2005). The promoter region of FABP5 contains two cognate response elements (CREs) to transcription factor NF-κB (Kannan-Thulasiraman et al., 2010). Epidermal growth factor receptor (EGFR) activation directly increases FABP5 expression through the ERK and phosphatidylinositol-3-kinase cascades and subsequent activation of NF-κB (Kannan-Thulasiraman et al., 2010). Ligands of peroxisome proliferator-activated receptors (PPARs) have been shown to influence FABP5 expression: PPARα and PPARγ agonists upregulate FABP5 expression, whereas PPARβ activation decreases FABP5 expression (Hyder et al., 2010). In contrast to FABP7, mRNA length for FABP5 does not vary throughout the body, limiting the likelihood of post-transcriptional modification (Zimmerman and Veerkamp, 2002).


The human genome contains 14 pseudogenes similar to the FABP5 locus.
Predicted pseudogenes are listed here: http://www.ncbi.nlm.nih.gov/gene/?Term=related_functional_gene_2171%5Bgroup%5D.



FABP5 is a member of the intracellular lipid binding protein family. FABP5 is a 135 amino acid protein with an estimated molecular mass of 15.1 kDa. Similar to other FABPs, FABP5 has a beta-clam (beta barrel) structure composed of 10 anti-parallel beta sheets and two N-terminal alpha helices, with low backbone motility (Gutiérrez-González et al., 2002). Six cysteine residues and a disulfide bridge between Cys120 and Cys127 contribute to protein stability and are hypothesized to relieve oxidative stress by thiol disulfide interchange reaction (Odani et al., 2000). Hydrophobic ligands are bound within the water-filled central cavity formed by the beta barrel. The carboxylic head group of linoleic acid forms a salt bridge with Arg-129 and hydrogen bonds with the hydroxyl groups of Tyr-131 and Arg-109 in the binding pocket of FABP5 (Armstrong et al., 2014). Hydrophobic residues within the binding pocket such as Cys-120 also facilitate ligand binding. FABP5 contains ligand-sensitive tertiary nuclear localization sequences in the α1 and α2 helices and a putative nuclear export signal located at the edge of the β-barrel. The putative NES consists of Lys-69, Lys-94, and Phe-89 residues (Armstrong et al., 2014).


FABP5 was first identified as a low molecular weight protein highly upregulated in human psoriatic skin (Madsen et al., 1992). FABP5 is expressed in numerous normal adult epithelial tissues, including those of the reproductive and urinary tracts, mammary glands, lungs, tongue, and lens. FABP5 is also expressed in macrophages, bone, and skeletal muscle (Smathers and Petersen, 2011).
The expression of FABP5 during mammalian neurogenesis has been investigated using rodent models, with similar results obtained in mouse and rat. FABP5 transcripts are detected in mid-term embryonic rat brain, peaking at birth and gradually decreasing from P1 to P21, with expression virtually undetectable in the adult brain (Owada et al., 2002), except during regeneration in response to neuronal injury (Allen et al., 2001). FABP5 is critical in post-natal hippocampal dentate gyrus neurogenesis in mice (Matsumata et al., 2012).


The FABP5 protein has a nuclear or cytoplasmic localization that is dependent upon ligand binding and cell type. Retinoic acid (RA), linoleic acid and arachidonic acid (AA) have been shown to elicit nuclear translocation through allosteric interaction between the ligand-sensing β2 loop and nuclear localization sequence (NLS) in the alpha helix (Tan et al., 2001; Schug et al., 2007; Armstrong et al., 2014).


Unique to brain-expressed FABPs, both human and rat FABP5 have a high affinity for saturated fatty acids such as stearic acid, with a Kd of 168.1 nM as determined by 1-anili-nonapthalene-8-sulfonic acid (ANS) assay (Liu et al., 2010), and 290 nM as determined by the Lipidex assay (see Table) (Liu et al., 2010). FABP5 has a broad range of saturated and unsaturated hydrophobic ligands, including linoleic acid, eicosapentanenoic acid (EPA), docosahexaenoic acid (DHA), AA and their derivatives (Sanson et al., 2014). Nuclear localization upon binding to linoleic acid and AA is thought to influence gene expression through activation of the nuclear receptor PPARβ/δ (Tan et al., 2001), which controls the expression of genes involved in lipid and glucose metabolism, differentiation, and survival (Schug et al., 2007).
FABP5 expression during development is associated with neurite outgrowth (Allen et al., 2001), with an important role in post-natal hippocampal dentate gyrus neurogenesis through nuclear transport of RA to activate PPARβ/δ (Matsumata et al., 2012). The hippocampi of FABP5-null mice contain excess neuronal progenitors and are deficient in mature neurons (Yu et al., 2012). FABP5 knockout mice do not have a brain phenotype, perhaps as a result of compensation by other FABP members.
FABP5 has been shown to facilitate nociception in mice through transport of adandamide (AEA), an anti-nociceptive lipid that is hydrolyzed into AA within the cell. FABP5 knockout mice accumulate AEA, which results in PPARβ/δ inactivation (Yu et al., 2014). Pharmacological inhibition of FABP5 reduces inflammatory, visceral, and neuropathic pain in mice (Kaczocha et al., 2014).
FABP5 knockout mice exhibit reduced basal transepithelial water loss (TEWL) and delayed recovery in TEWL upon disruption of the lipid barrier, suggesting that FABP5 plays a critical role in maintenance of the water permeability barrier of the skin (Owada et al., 2002).
Several cell types in the immune system, including macrophages, thymic epithelial cells, and subsets of lymphocytes express FABP5, and animal studies indicate that FABP5 plays a role in immune regulation (Grau et al., 2003; Adachi et al., 2012). Production of cytokines IL-7 and IL-18 is increased in stromal cells over-expressing FABP5 (Adachi et al., 2012), while ablation of FABP5 results in increased macrophage and neutrophil infiltration during influenza A infection (Gally et al., 2013). Lung epithelial cells initially downregulate FABP5 expression during the onset of the anti-viral response, and recover pre-infection levels upon attenuation of inflammation. Deficiency in FABP5 correlates with increased oxidative damage and lipid peroxidation over the course of infection, indicating that FABP5 is required for the prevention of tissue damage resulting from excessive inflammation (Gally et al., 2013).


The human FABP5 amino acid sequence is 64.8% identical to chicken FABP5 and 80% identical to mouse FABP5 isoform 1. Human FABP5 shows variable sequence identity with the other FABP paralogues, with the highest identity to FABP8/PMP2 (59%) and the lowest identity to FABP2 and FABP6 (27%). FABP5 is phylogenetically related to FABP3 and FABP7, which are also expressed in the brain (Schoentgen et al., 1989; Godbout, 1993; Bennett et al., 1994; Feng et al., 1994) and shows 51% and 46% amino acid sequence identity with FABP3 and FABP7, respectively. FABP5 also has sequence identity to other lipid binding proteins, with 36% identity to human cellular retinoic acid binding protein 1 (CRABP1).
Atlas Image
Ligand affinities for FABP5. Abbreviations: Rn= Rattus norvegicus, Ms= Mus musculus, Hs= Homo sapiens.



Several variants of FABP5 have been linked to human diseases, including type 2 diabetes. Nine MGI mutant phenotypes in mice have been reported, with disruption in FABP5 resulting in defects in epithelial water balance and resistance to obesity.

Implicated in

Entity name
FABP5 is involved in signaling pathways controlling differentiation, metabolism, proliferation, and resistance to apoptosis (Tan et al., 2001) and is highly expressed in several human tumors including breast, prostate, oral, and hepatocellular carcinomas (Adamson et al., 2003; Fujii et al., 2005; Fang et al., 2010). The majority of malignancies associated with elevated FABP5 are of apparent epithelial origin, where FABP5 is believed to contribute to proliferation, metastasis, and resistance to therapy.
Entity name
Breast cancer
In 2001, FABP5 overexpression was shown to induce metastasis in rat mammary epithelial cells through induction of the vascular endothelial growth factor (VEGF) (Jing et al., 2001). FABP5 can also be upregulated by EGFR signaling in breast cancer cells and serves as a critical mediator of EGFR-induced cell proliferation (Kannan-Thulasiraman et al., 2010). Analysis of a cohort of 120 breast cancer patients revealed an association between elevated levels of cytoplasmic FABP5, high tumor grade, reduced recurrence-free survival and poor prognosis in triple-negative breast cancer (Liu et al., 2011) (see Figure). Recently, genetic ablation of FABP5 was shown to suppress Her-2-induced mammary tumorigenesis, indicating a potential role for FABP5 as a chemotherapeutic target (Levi et al., 2013).
Manipulation of FABP5 levels in human breast cancer cell lines and cell lines generated from breast cancer mouse models demonstrates a correlation between FABP5 levels and response to RA treatment (Schug et al., 2007; Schug et al., 2008; Liu et al., 2011). It has been hypothesized that FABP5 confers resistance to RA therapy through competition with CRABP2 for RA, with FABP5 promoting proliferation and survival through activation of PPARβ and CRABP2 inhibiting proliferation through activation of the nuclear retinoic acid receptor (RAR) (Schug et al., 2007; Schug et al., 2008; Liu et al., 2011).
Atlas Image
FABP5 mRNA levels in molecular and histological subtypes of breast cancer based on gene profiling data. FABP5 mRNA levels were determined by gene expression microarray analysis of 176 treatment-naïve primary human breast tumors. Signal intensity values were normalized and log-transformed. Statistically significant differences between groups (indicated by stars) were determined using the student t-test. ** denotes p
Entity name
Prostate cancer
Elevated FABP5 protein levels are linked to increased tumor size and invasiveness in prostate cancer (Adamson et al., 2003). Depletion of FABP5 decreases VEGF and microvessel density in prostatic tumors in nude mice and suppresses proliferation and invasion in prostatic carcinoma cells (Adamson et al., 2003). High levels of FABP5 are associated with a poorer prognosis in prostate cancer (Morgan et al., 2008; Forootan et al., 2014). Significantly higher levels of FABP5 protein were found in the serum of patients with lymph node metastatic prostate cancer compared to patients with localized prostate cancer (Pang et al., 2010). As in other cancers, FABP5 appears to influence tumor progression through PPARβ, and levels of both FABP5 and PPARβ correlate with the tumorigenic potential of prostate cancer cell lines by inducing the expression of genes which promote anchorage independence and proliferation (Morgan et al., 2008). FABP5 has been shown to be a direct target of PPARβ in prostate cancer cell lines and it has been suggested that targeting the PPARβ/FABP5 pathway may represent a new strategy for the treatment of prostate cancer (Morgan et al., 2008).
Entity name
Other cancers
FABP5 is elevated in several other human malignancies where it influences tumorigenic potential by modulating proliferation, invasion, and drug resistance.
Drug-resistant adenocarcinoma of the pancreas is associated with high levels of FABP5, with FABP5 proposed to facilitate the sequestration and removal of cytotoxic drugs in these tumors (Sinha et al., 1999). In keeping with other types of cancers, a high ratio of FABP5 to CRABP2 in pancreatic ductal adenocarcinoma cell lines correlates with poor response to RA, whereas CRABP2 expression in the absence of FABP5 correlates with growth inhibition in the presence of RA (Gupta et al., 2012).
A number of RA signaling proteins, including FABP5, are highly expressed in high-grade astrocytomas, with FABP5 expression correlating with an undifferentiated tumor phenotype (Campos et al., 2011). The ratio of FABP5 to CRABP2 was found to correlate with survival time in grade IV astrocytoma patients, with a high FABP5 to CRABP2 ratio associated with shorter term survival (Barbus et al., 2011).
Entity name
Psychiatric diseases
Abnormalities in lipid metabolism are linked to several psychiatric illnesses. Several rare non-synonymous polymorphisms in FABP5 have been identified in patients with schizophrenia and autism spectrum disorder. Altered FABP5 mRNA expression levels were detected in schizophrenic brain (Shimamoto et al., 2014). Variants in the FABP5 gene were found in autistic patients, but no significant genetic association between FABP5 and autism has been established (Maekawa et al., 2010).
Entity name
Obesity, metabolic syndrome, atherosclerosis
Due to their role in lipid homeostasis, FABPs have been implicated in obesity, metabolic syndrome, and atherosclerosis. Increased serum levels of FABP5 correlate with age, waist circumference, blood pressure, and insulin resistance in human adults (Ishimura et al., 2013). Combined deficiency in FABP5 and FABP4 in mice protects against atherosclerosis and metabolic syndrome (Babaev et al., 2011). In a population study of 806 individuals with type 2 diabetes, levels of FABP4 and FABP5 in adipocytes and macrophages independently correlated with incidence of metabolic syndrome and the presence of coronary artery calcium, a marker for coronary heart disease (Bagheri et al., 2010). FABP4 and FABP5 may contribute to the pathogenesis and serve as biomarkers for metabolic syndrome and cardiovascular disease risk factors.
Entity name
Two single nucleotide polymorphisms in the regulatory region of FABP5 are associated with type 2 diabetes in humans (Bu et al., 2011). Human islet cells and insulin-secreting rat INS1E β-cells express FABP5 (Hyder et al., 2010). Targeted depletion of FABP5 protected mice from insulin resistance and diabetes when administered a high fat diet (Maeda et al., 2005). High glucose increased FABP5 expression in human islet and rat β-cells, indicating that FABP5 contributes to pancreatic function and glucose metabolism in mammals (Hyder et al., 2010).
Entity name
FABP5 was first identified as a gene highly upregulated in human psoriatic skin lesions (Madsen et al., 1992). Psoriasis is caused by a defect in the differentiation of keratinocytes, and FABP5 modulates differentiation of normal and psoriatic human keratinocytes (Dallaglio et al., 2013). It has been proposed that FABP5 overexpression contributes to the pathogenesis of psoriasis by promoting the proliferation and survival of keratinocytes and disrupting the uptake and metabolism of fatty acids in the epidermis. In psoriasis patients, depletion of FABP5 in the epidermis upon TNF-α or narrow-band ultraviolet B treatment corresponded with response to therapy (Miyake et al., 2012).


Pubmed IDLast YearTitleAuthors
225850402012Fatty acid-binding protein 4 (FABP4) and FABP5 modulate cytokine production in the mouse thymic epithelial cells.Adachi Y et al
127435982003High-level expression of cutaneous fatty acid-binding protein in prostatic carcinomas and its effect on tumorigenicity.Adamson J et al
117463572001Induction and axonal localization of epithelial/epidermal fatty acid-binding protein in retinal ganglion cells are associated with axon development and regeneration.Allen GW et al
246925512014Structural basis for ligand regulation of the fatty acid-binding protein 5, peroxisome proliferator-activated receptor β/δ (FABP5-PPARβ/δ) signaling pathway.Armstrong EH et al
214748282011Macrophage Mal1 deficiency suppresses atherosclerosis in low-density lipoprotein receptor-null mice by activating peroxisome proliferator-activated receptor-γ-regulated genes.Babaev VR et al
209206502010Relation of plasma fatty acid binding proteins 4 and 5 with the metabolic syndrome, inflammation and coronary calcium in patients with type-2 diabetes mellitus.Bagheri R et al
213462262011Differential retinoic acid signaling in tumors of long- and short-term glioblastoma survivors.Barbus S et al
79313181994Cloning and characterization of a cDNA encoding a novel fatty acid binding protein from rat brain.Bennett E et al
212885882011Polymorphisms in fatty acid binding protein 5 show association with type 2 diabetes.Bu L et al
215144132011Aberrant expression of retinoic acid signaling molecules influences patient survival in astrocytic gliomas.Campos B et al
107377922000Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion.Coller HA et al
235282102013E-FABP induces differentiation in normal human keratinocytes and modulates the differentiation process in psoriatic keratinocytes in vitro.Dallaglio K et al
200400212010Fatty-acid-binding protein 5 promotes cell proliferation and invasion in oral squamous cell carcinoma.Fang LY et al
81614591994Brain lipid-binding protein (BLBP): a novel signaling system in the developing mammalian CNS.Feng L et al
241896402014The expression of C-FABP and PPARγ and their prognostic significance in prostate cancer.Forootan FS et al
157510052005Proteomic study of human hepatocellular carcinoma using two-dimensional difference gel electrophoresis with saturation cysteine dye.Fujii K et al
236247872013FABP5 deficiency enhances susceptibility to H1N1 influenza A virus-induced lung inflammation.Gally F et al
79166961993Identification and characterization of transcripts present at elevated levels in the undifferentiated chick retina.Godbout R et al
126403102003Induction of epidermal fatty acid binding protein in intravascular monocytes of renal allografts.Grau V et al
220102132012Molecular determinants of retinoic acid sensitivity in pancreatic cancer.Gupta S et al
120496372002Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP).Gutiérrez-González LH et al
196022322009Identification of potential therapeutic targets in human head & neck squamous cell carcinoma.Han J et al
210993112010Expression of fatty acid binding proteins 3 and 5 genes in rat pancreatic islets and INS-1E cells: regulation by fatty acids and glucose.Hyder A et al
242784212013Circulating levels of fatty acid-binding protein family and metabolic phenotype in the general population.Ishimura S et al
113890602001Human cutaneous fatty acid-binding protein induces metastasis by up-regulating the expression of vascular endothelial growth factor gene in rat Rama 37 model cells.Jing C et al
247053802014Inhibition of fatty acid binding proteins elevates brain anandamide levels and produces analgesia.Kaczocha M et al
204241642010Fatty acid-binding protein 5 and PPARbeta/delta are critical mediators of epidermal growth factor receptor-induced carcinoma cell growth.Kannan-Thulasiraman P et al
237225462013Genetic ablation of the fatty acid-binding protein FABP5 suppresses HER2-induced mammary tumorigenesis.Levi L et al
185133722008Expression of E-FABP in PC12 cells increases neurite extension during differentiation: involvement of n-3 and n-6 fatty acids.Liu JW et al
213563532011Association of FABP5 expression with poor survival in triple-negative breast cancer: implication for retinoic acid therapy.Liu RZ et al
205639942010Fatty acid binding proteins in brain development and disease.Liu RZ et al
15124661992Molecular cloning and expression of a novel keratinocyte protein (psoriasis-associated fatty acid-binding protein [PA-FABP]) that is highly up-regulated in psoriatic skin and that shares similarity to fatty acid-binding proteins.Madsen P et al
160540522005Adipocyte/macrophage fatty acid binding proteins control integrated metabolic responses in obesity and diabetes.Maeda K et al
200575062010Polymorphism screening of brain-expressed FABP7, 5 and 3 genes and association studies in autism and schizophrenia in Japanese subjects.Maekawa M et al
92856301997Endothelial cells of the human microvasculature express epidermal fatty acid-binding protein.Masouyé I et al
225817842012The effects of Fabp7 and Fabp5 on postnatal hippocampal neurogenesis in the mouse.Matsumata M et al
230399482012Epidermal-type FABP is a predictive marker of clinical response to systemic treatment and ultraviolet therapy in psoriatic skin lesions.Miyake T et al
183607042008Expression of cutaneous fatty acid-binding protein (C-FABP) in prostate cancer: potential prognostic marker and target for tumourigenicity-suppression.Morgan EA et al
159228672005The tumour-associated antigen EpCAM upregulates the fatty acid binding protein E-FABP.Münz M et al
109650322000Disulfide bonds in rat cutaneous fatty acid-binding protein.Odani S et al
246493022014Differential expression of fatty acid-binding proteins and pathological implications in the progression of tongue carcinoma.Ohyama Y et al
118744812002Altered water barrier function in epidermal-type fatty acid binding protein-deficient mice.Owada Y et al
198947592010Profiling protein markers associated with lymph node metastasis in prostate cancer by DIGE-based proteomics analysis.Pang J et al
245314632014Crystallographic study of FABP5 as an intracellular endocannabinoid transporter.Sanson B et al
28062611989Fatty-acid-binding protein from bovine brain. Amino acid sequence and some properties.Schoentgen F et al
184959242008Overcoming retinoic acid-resistance of mammary carcinomas by diverting retinoic acid from PPARbeta/delta to RAR.Schug TT et al
250273192014Functional characterization of FABP3, 5 and 7 gene variants identified in schizophrenia and autism spectrum disorder and mouse behavioral studies.Shimamoto C et al
105468331999Increased expression of epidermal fatty acid binding protein, cofilin, and 14-3-3-sigma (stratifin) detected by two-dimensional gel electrophoresis, mass spectrometry and microsequencing of drug-resistant human adenocarcinoma of the pancreas.Sinha P et al
215048682011The human fatty acid-binding protein family: evolutionary divergences and functions.Smathers RL et al
117516322001Critical roles of PPAR beta/delta in keratinocyte response to inflammation.Tan NS et al
76075531995Lens epithelial cell mRNA, II. Expression of a mRNA encoding a lipid-binding protein in rat lens epithelial cells.Wen Y et al
246442812014Fatty acid-binding protein 5 (FABP5) regulates cognitive function both by decreasing anandamide levels and by activating the nuclear receptor peroxisome proliferator-activated receptor β/δ (PPARβ/δ) in the brain.Yu S et al
122229582002New insights into the structure and function of fatty acid-binding proteins.Zimmerman AW et al

Other Information

Locus ID:

NCBI: 2171
MIM: 605168
HGNC: 3560
Ensembl: ENSG00000164687


dbSNP: 2171
ClinVar: 2171
TCGA: ENSG00000164687


Gene IDTranscript IDUniprot

Expression (GTEx)



PathwaySourceExternal ID
PPAR signaling pathwayKEGGko03320
PPAR signaling pathwayKEGGhsa03320
Immune SystemREACTOMER-HSA-168256
Innate Immune SystemREACTOMER-HSA-168249
Signal TransductionREACTOMER-HSA-162582
Signaling by Retinoic AcidREACTOMER-HSA-5362517
Metabolism of lipids and lipoproteinsREACTOMER-HSA-556833
Lipid digestion, mobilization, and transportREACTOMER-HSA-73923
Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysisREACTOMER-HSA-163560
Neutrophil degranulationREACTOMER-HSA-6798695

Protein levels (Protein atlas)

Not detected


Pubmed IDYearTitleCitations
213563532011Association of FABP5 expression with poor survival in triple-negative breast cancer: implication for retinoic acid therapy.47
204241642010Fatty acid-binding protein 5 and PPARbeta/delta are critical mediators of epidermal growth factor receptor-induced carcinoma cell growth.38
205639942010Fatty acid binding proteins in brain development and disease.38
183607042008Expression of cutaneous fatty acid-binding protein (C-FABP) in prostate cancer: potential prognostic marker and target for tumourigenicity-suppression.32
246925512014Structural basis for ligand regulation of the fatty acid-binding protein 5, peroxisome proliferator-activated receptor β/δ (FABP5-PPARβ/δ) signaling pathway.31
220102132012Molecular determinants of retinoic acid sensitivity in pancreatic cancer.22
265929762015Saturated fatty acids regulate retinoic acid signalling and suppress tumorigenesis by targeting fatty acid-binding protein 5.21
200400212010Fatty-acid-binding protein 5 promotes cell proliferation and invasion in oral squamous cell carcinoma.20
250273192014Functional characterization of FABP3, 5 and 7 gene variants identified in schizophrenia and autism spectrum disorder and mouse behavioral studies.20
241896402014The expression of C-FABP and PPARγ and their prognostic significance in prostate cancer.19


Erin Balcom ; Rong-Zong Liu ; Stanley Poon ; Roseline Godbout

FABP5 (fatty acid binding protein 5 (psoriasis-associated))

Atlas Genet Cytogenet Oncol Haematol. 2014-08-01

Online version: http://atlasgeneticsoncology.org/gene/49862/fabp5