Search Results

Overview

Uniprot IDQ01469
Protein NameFatty acid-binding protein 5
Gene NameFABP5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
34 GVGIALRKMGAMAKP
55 DGKNLTIKTESTLKT
61 IKTESTLKTTQFSCT
72 FSCTLGEKFEETTAD
82 ETTADGRKTQTVCNF

Function

Intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids, that regulate the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors (PubMed:21395585, PubMed:22170058). Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (By similarity). May be involved in keratinocyte differentiation (PubMed:8092987)

Protein Sequence

10 MATVQQLEGR 20 WRLVDSKGFD 30 EYMKELGVGI 40 ALRKMGAMAK 50 PDCIITCDGK 60 NLTIKTESTL 70 KTTQFSCTLG 80 EKFEETTADG 90 RKTQTVCNFT 100 DGALVQHQEW 110 DGKESTITRK 120 LKDGKLVVEC 130 VMNNVTCTRI YEKVE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0035578 azurophil granule lumen
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0099524 postsynaptic cytosol
Cellular Component GO:0014069 postsynaptic density
Cellular Component GO:0099092 postsynaptic density, intracellular component
Cellular Component GO:0030667 secretory granule membrane
Cellular Component GO:0045202 synapse
Molecular Function GO:0005504 fatty acid binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0008289 lipid binding
Molecular Function GO:0005319 lipid transporter activity
Molecular Function GO:0005324 long-chain fatty acid transmembrane transporter activity
Molecular Function GO:0001972 retinoic acid binding
Biological Process GO:0008544 epidermis development
Biological Process GO:0015908 fatty acid transport
Biological Process GO:0006629 lipid metabolic process
Biological Process GO:1990379 lipid transport across blood-brain barrier
Biological Process GO:0015909 long-chain fatty acid transport
Biological Process GO:0120162 positive regulation of cold-induced thermogenesis
Biological Process GO:0035360 positive regulation of peroxisome proliferator activated receptor signaling pathway
Biological Process GO:0031392 regulation of prostaglandin biosynthetic process
Biological Process GO:0099178 regulation of retrograde trans-synaptic signaling by endocanabinoid
Biological Process GO:0051930 regulation of sensory perception of pain
Biological Process GO:0098921 retrograde trans-synaptic signaling by endocannabinoid
Biological Process GO:0019433 triglyceride catabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.