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

Written2014-08Erin 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

Abstract 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).

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Identity

Alias_namesfatty acid binding protein 5 (psoriasis-associated)
Alias_symbol (synonym)E-FABP
PA-FABP
KFABP
HGNC (Hugo) FABP5
LocusID (NCBI) 2171
Atlas_Id 49862
Location 8q21.13  [Link to chromosome band 8q21]
Location_base_pair Starts at 82192718 and ends at 82197012 bp from pter ( according to hg19-Feb_2009)  [Mapping FABP5.png]
Local_order PAG1FABP5 → PMP2.

DNA/RNA

 
  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.
Description 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).
Transcription 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).
Pseudogene 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.

Protein

Description 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).
Expression 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).
Localisation 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).
Function 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).
Homology 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).
 

Mutations

Note 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

Note
Entity Cancer
Note 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 Breast cancer
Note 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).
 
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 <0.01.
  
Entity Prostate cancer
Note 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 Other cancers
Note FABP5 is elevated in several other human malignancies where it influences tumorigenic potential by modulating proliferation, invasion, and drug resistance.
Cytoplasmic FABP5 levels are elevated in human head and neck squamous cell carcinomas (Han et al., 2009). Elevated cytoplasmic FABP5 levels have also been documented in advanced tongue carcinomas (Ohyama et al., 2014). Proteomic analysis revealed FABP5 as highly upregulated in oral squamous cell carcinoma (OSCC). Overexpression of FABP5 increased invasion, proliferation and production of matrix metalloproteinase-9 (MMP-9) in OSCC cell lines (Fang et al., 2010).
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 Psychiatric diseases
Note 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 Obesity, metabolic syndrome, atherosclerosis
Note 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 Diabetes
Note 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 Psoriasis
Note 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).
  

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The effects of Fabp7 and Fabp5 on postnatal hippocampal neurogenesis in the mouse.
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Stem Cells. 2012 Jul;30(7):1532-43. doi: 10.1002/stem.1124.
PMID 22581784
 
Epidermal-type FABP is a predictive marker of clinical response to systemic treatment and ultraviolet therapy in psoriatic skin lesions.
Miyake T, Ogawa E, Mikoshiba A, Kobayashi A, Hosoe H, Kashiwabara S, Uhara H, Owada Y, Okuyama R.
J Dermatol Sci. 2012 Dec;68(3):199-202. doi: 10.1016/j.jdermsci.2012.09.002. Epub 2012 Sep 21.
PMID 23039948
 
Expression of cutaneous fatty acid-binding protein (C-FABP) in prostate cancer: potential prognostic marker and target for tumourigenicity-suppression.
Morgan EA, Forootan SS, Adamson J, Foster CS, Fujii H, Igarashi M, Beesley C, Smith PH, Ke Y.
Int J Oncol. 2008 Apr;32(4):767-75.
PMID 18360704
 
The tumour-associated antigen EpCAM upregulates the fatty acid binding protein E-FABP.
Munz M, Zeidler R, Gires O.
Cancer Lett. 2005 Jul 8;225(1):151-7. Epub 2004 Dec 28.
PMID 15922867
 
Disulfide bonds in rat cutaneous fatty acid-binding protein.
Odani S, Namba Y, Ishii A, Ono T, Fujii H.
J Biochem. 2000 Sep;128(3):355-61.
PMID 10965032
 
Differential expression of fatty acid-binding proteins and pathological implications in the progression of tongue carcinoma.
Ohyama Y, Kawamoto Y, Chiba T, Kikuchi K, Sakashita H, Imai K.
Mol Clin Oncol. 2014 Jan;2(1):19-25. Epub 2013 Oct 3.
PMID 24649302
 
Altered water barrier function in epidermal-type fatty acid binding protein-deficient mice.
Owada Y, Takano H, Yamanaka H, Kobayashi H, Sugitani Y, Tomioka Y, Suzuki I, Suzuki R, Terui T, Mizugaki M, Tagami H, Noda T, Kondo H.
J Invest Dermatol. 2002 Mar;118(3):430-5.
PMID 11874481
 
Profiling protein markers associated with lymph node metastasis in prostate cancer by DIGE-based proteomics analysis.
Pang J, Liu WP, Liu XP, Li LY, Fang YQ, Sun QP, Liu SJ, Li MT, Su ZL, Gao X.
J Proteome Res. 2010 Jan;9(1):216-26. doi: 10.1021/pr900953s.
PMID 19894759
 
Crystallographic study of FABP5 as an intracellular endocannabinoid transporter.
Sanson B, Wang T, Sun J, Wang L, Kaczocha M, Ojima I, Deutsch D, Li H.
Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):290-8. doi: 10.1107/S1399004713026795. Epub 2014 Jan 29.
PMID 24531463
 
Fatty-acid-binding protein from bovine brain. Amino acid sequence and some properties.
Schoentgen F, Pignede G, Bonanno LM, Jolles P.
Eur J Biochem. 1989 Oct 20;185(1):35-40.
PMID 2806261
 
Overcoming retinoic acid-resistance of mammary carcinomas by diverting retinoic acid from PPARbeta/delta to RAR.
Schug TT, Berry DC, Toshkov IA, Cheng L, Nikitin AY, Noy N.
Proc Natl Acad Sci U S A. 2008 May 27;105(21):7546-51. doi: 10.1073/pnas.0709981105. Epub 2008 May 21.
PMID 18495924
 
Functional characterization of FABP3, 5 and 7 gene variants identified in schizophrenia and autism spectrum disorder and mouse behavioral studies.
Shimamoto C, Ohnishi T, Maekawa M, Watanabe A, Ohba H, Arai R, Iwayama Y, Hisano Y, Toyota T, Toyoshima M, Suzuki K, Shirayama Y, Nakamura K, Mori N, Owada Y, Kobayashi T, Yoshikawa T.
Hum Mol Genet. 2014 Jul 15. pii: ddu369. [Epub ahead of print]
PMID 25027319
 
Increased 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, Hutter G, Kottgen E, Dietel M, Schadendorf D, Lage H.
Electrophoresis. 1999 Oct;20(14):2952-60.
PMID 10546833
 
The human fatty acid-binding protein family: evolutionary divergences and functions.
Smathers RL, Petersen DR.
Hum Genomics. 2011 Mar;5(3):170-91. (REVIEW)
PMID 21504868
 
Critical roles of PPAR beta/delta in keratinocyte response to inflammation.
Tan NS, Michalik L, Noy N, Yasmin R, Pacot C, Heim M, Fluhmann B, Desvergne B, Wahli W.
Genes Dev. 2001 Dec 15;15(24):3263-77.
PMID 11751632
 
Lens epithelial cell mRNA, II. Expression of a mRNA encoding a lipid-binding protein in rat lens epithelial cells.
Wen Y, Li GW, Chen P, Wong E, Bekhor I.
Gene. 1995 Jun 9;158(2):269-74.
PMID 7607553
 
Fatty acid-binding protein 5 (FABP5) regulates cognitive function both by decreasing anandamide levels and by activating the nuclear receptor peroxisome proliferator-activated receptor beta/delta (PPARb/d) in the brain.
Yu S, Levi L, Casadesus G, Kunos G, Noy N.
J Biol Chem. 2014 May 2;289(18):12748-58. doi: 10.1074/jbc.M114.559062. Epub 2014 Mar 18.
PMID 24644281
 
New insights into the structure and function of fatty acid-binding proteins.
Zimmerman AW, Veerkamp JH.
Cell Mol Life Sci. 2002 Jul;59(7):1096-116. (REVIEW)
PMID 12222958
 

Citation

This paper should be referenced as such :
Balcom E, Liu RZ, Poon S, Godbout R
FABP5 (fatty acid binding protein 5 (psoriasis-associated));
Atlas Genet Cytogenet Oncol Haematol. in press
On line version : http://AtlasGeneticsOncology.org/Genes/FABP5ID49862ch8q21.html


External links

Nomenclature
HGNC (Hugo)FABP5   3560
Cards
AtlasFABP5ID49862ch8q21
Entrez_Gene (NCBI)FABP5  2171  fatty acid binding protein 5
AliasesE-FABP; EFABP; KFABP; PA-FABP; 
PAFABP
GeneCards (Weizmann)FABP5
Ensembl hg19 (Hinxton)ENSG00000164687 [Gene_View]  chr8:82192718-82197012 [Contig_View]  FABP5 [Vega]
Ensembl hg38 (Hinxton)ENSG00000164687 [Gene_View]  chr8:82192718-82197012 [Contig_View]  FABP5 [Vega]
ICGC DataPortalENSG00000164687
TCGA cBioPortalFABP5
AceView (NCBI)FABP5
Genatlas (Paris)FABP5
WikiGenes2171
SOURCE (Princeton)FABP5
Genetics Home Reference (NIH)FABP5
Genomic and cartography
GoldenPath hg19 (UCSC)FABP5  -     chr8:82192718-82197012 +  8q21.13   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)FABP5  -     8q21.13   [Description]    (hg38-Dec_2013)
EnsemblFABP5 - 8q21.13 [CytoView hg19]  FABP5 - 8q21.13 [CytoView hg38]
Mapping of homologs : NCBIFABP5 [Mapview hg19]  FABP5 [Mapview hg38]
OMIM605168   
Gene and transcription
Genbank (Entrez)AK226036 AK311856 BC019385 BC070303 BT007449
RefSeq transcript (Entrez)NM_001444
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)FABP5
Cluster EST : UnigeneHs.408061 [ NCBI ]
CGAP (NCI)Hs.408061
Alternative Splicing GalleryENSG00000164687
Gene ExpressionFABP5 [ NCBI-GEO ]   FABP5 [ EBI - ARRAY_EXPRESS ]   FABP5 [ SEEK ]   FABP5 [ MEM ]
Gene Expression Viewer (FireBrowse)FABP5 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2171
GTEX Portal (Tissue expression)FABP5
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ01469   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ01469  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ01469
Splice isoforms : SwissVarQ01469
PhosPhoSitePlusQ01469
Domaine pattern : Prosite (Expaxy)FABP (PS00214)   
Domains : Interpro (EBI)Calycin    Calycin-like    Fatty_acid-bd    iLBP    Lipocln_cytosolic_FA-bd_dom   
Domain families : Pfam (Sanger)Lipocalin (PF00061)   
Domain families : Pfam (NCBI)pfam00061   
Conserved Domain (NCBI)FABP5
DMDM Disease mutations2171
Blocks (Seattle)FABP5
PDB (SRS)1B56    1JJJ    4AZM    4AZR    4LKP    4LKT   
PDB (PDBSum)1B56    1JJJ    4AZM    4AZR    4LKP    4LKT   
PDB (IMB)1B56    1JJJ    4AZM    4AZR    4LKP    4LKT   
PDB (RSDB)1B56    1JJJ    4AZM    4AZR    4LKP    4LKT   
Structural Biology KnowledgeBase1B56    1JJJ    4AZM    4AZR    4LKP    4LKT   
SCOP (Structural Classification of Proteins)1B56    1JJJ    4AZM    4AZR    4LKP    4LKT   
CATH (Classification of proteins structures)1B56    1JJJ    4AZM    4AZR    4LKP    4LKT   
SuperfamilyQ01469
Human Protein AtlasENSG00000164687
Peptide AtlasQ01469
HPRD05524
IPIIPI00007797   IPI00788781   
Protein Interaction databases
DIP (DOE-UCLA)Q01469
IntAct (EBI)Q01469
FunCoupENSG00000164687
BioGRIDFABP5
STRING (EMBL)FABP5
ZODIACFABP5
Ontologies - Pathways
QuickGOQ01469
Ontology : AmiGOtransporter activity  fatty acid binding  protein binding  nucleoplasm  cytoplasm  cytosol  glucose metabolic process  lipid metabolic process  phosphatidylcholine biosynthetic process  lipid binding  epidermis development  response to wounding  glucose transport  triglyceride catabolic process  extracellular exosome  
Ontology : EGO-EBItransporter activity  fatty acid binding  protein binding  nucleoplasm  cytoplasm  cytosol  glucose metabolic process  lipid metabolic process  phosphatidylcholine biosynthetic process  lipid binding  epidermis development  response to wounding  glucose transport  triglyceride catabolic process  extracellular exosome  
Pathways : KEGGPPAR signaling pathway   
REACTOMEQ01469 [protein]
REACTOME PathwaysR-HSA-6798695 [pathway]
NDEx NetworkFABP5
Atlas of Cancer Signalling NetworkFABP5
Wikipedia pathwaysFABP5
Orthology - Evolution
OrthoDB2171
GeneTree (enSembl)ENSG00000164687
Phylogenetic Trees/Animal Genes : TreeFamFABP5
HOVERGENQ01469
HOGENOMQ01469
Homologs : HomoloGeneFABP5
Homology/Alignments : Family Browser (UCSC)FABP5
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerFABP5 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)FABP5
dbVarFABP5
ClinVarFABP5
1000_GenomesFABP5 
Exome Variant ServerFABP5
ExAC (Exome Aggregation Consortium)FABP5 (select the gene name)
Genetic variants : HAPMAP2171
Genomic Variants (DGV)FABP5 [DGVbeta]
DECIPHER (Syndromes)8:82192718-82197012  ENSG00000164687
CONAN: Copy Number AnalysisFABP5 
Mutations
ICGC Data PortalFABP5 
TCGA Data PortalFABP5 
Broad Tumor PortalFABP5
OASIS PortalFABP5 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICFABP5  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDFABP5
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch FABP5
DgiDB (Drug Gene Interaction Database)FABP5
DoCM (Curated mutations)FABP5 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)FABP5 (select a term)
intoGenFABP5
NCG5 (London)FABP5
Cancer3DFABP5(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM605168   
Orphanet
MedgenFABP5
Genetic Testing Registry FABP5
NextProtQ01469 [Medical]
TSGene2171
GENETestsFABP5
Huge Navigator FABP5 [HugePedia]
snp3D : Map Gene to Disease2171
BioCentury BCIQFABP5
ClinGenFABP5
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD2171
Chemical/Pharm GKB GenePA27961
Clinical trialFABP5
Miscellaneous
canSAR (ICR)FABP5 (select the gene name)
Probes
Litterature
PubMed72 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineFABP5
EVEXFABP5
GoPubMedFABP5
iHOPFABP5
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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