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Protein

Fatty acid-binding protein 5

Gene

FABP5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Intracellular carrier for long-chain fatty acids and related active lipids, such as the endocannabinoid, that regulates 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: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).By similarity2 Publications

Caution

While mouse FABP5 is found only in the monomeric form, human FABP5 can exist as a monomer as well as a domain-swapped dimer.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43Fatty acidCombined sources1 Publication1
Binding sitei56Fatty acidBy similarity1

GO - Molecular functioni

  • fatty acid binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • lipid binding Source: ProtInc
  • retinoic acid binding Source: Ensembl

GO - Biological processi

Keywordsi

Biological processTransport
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-163560 Triglyceride catabolism
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-6798695 Neutrophil degranulation

Protein family/group databases

TCDBi8.A.33.1.1 the fatty acid binding protein (fabp) family

Chemistry databases

SwissLipidsiSLP:000001104

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein 5
Alternative name(s):
Epidermal-type fatty acid-binding protein1 Publication
Short name:
E-FABP1 Publication
Fatty acid-binding protein, epidermal
Psoriasis-associated fatty acid-binding protein homolog
Short name:
PA-FABP
Gene namesi
Name:FABP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000164687.10
HGNCiHGNC:3560 FABP5
MIMi605168 gene
neXtProtiNX_Q01469

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Nucleus, Postsynaptic cell membrane, Secreted, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24K → A: Loss of ligand-induced nuclear import; when associated with A-33 and A-34. 1 Publication1
Mutagenesisi33R → A: Loss of ligand-induced nuclear import; when associated with A-24 and A-34. 1 Publication1
Mutagenesisi34K → A: Loss of ligand-induced nuclear import; when associated with A-24 and A-33. 1 Publication1

Organism-specific databases

DisGeNETi2171
OpenTargetsiENSG00000164687
PharmGKBiPA27961

Chemistry databases

ChEMBLiCHEMBL3674
DrugBankiDB03796 Palmitic Acid
GuidetoPHARMACOLOGYi2535

Polymorphism and mutation databases

BioMutaiFABP5
DMDMi232081

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000673772 – 135Fatty acid-binding protein 5Add BLAST134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei17N6-acetyllysineCombined sources1
Disulfide bondi120 ↔ 127Combined sources3 Publications
Modified residuei131PhosphotyrosineCombined sources1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ01469
MaxQBiQ01469
PaxDbiQ01469
PeptideAtlasiQ01469
PRIDEiQ01469
ProteomicsDBi57957
TopDownProteomicsiQ01469

2D gel databases

SWISS-2DPAGEiQ01469
UCD-2DPAGEiQ01469

PTM databases

iPTMnetiQ01469
PhosphoSitePlusiQ01469
SwissPalmiQ01469

Expressioni

Tissue specificityi

Keratinocytes; highly expressed in psoriatic skin.1 Publication

Gene expression databases

BgeeiENSG00000164687
CleanExiHS_FABP5
ExpressionAtlasiQ01469 baseline and differential
GenevisibleiQ01469 HS

Organism-specific databases

HPAiCAB017831
CAB040577
HPA051895

Interactioni

Subunit structurei

Monomer. Homodimer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108469, 40 interactors
IntActiQ01469, 3 interactors
STRINGi9606.ENSP00000297258

Chemistry databases

BindingDBiQ01469

Structurei

Secondary structure

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 7Combined sources4
Beta strandi9 – 18Combined sources10
Helixi19 – 25Combined sources7
Helixi30 – 38Combined sources9
Beta strandi42 – 48Combined sources7
Beta strandi51 – 57Combined sources7
Beta strandi63 – 68Combined sources6
Beta strandi73 – 76Combined sources4
Beta strandi78 – 80Combined sources3
Beta strandi82 – 90Combined sources9
Beta strandi93 – 100Combined sources8
Beta strandi103 – 112Combined sources10
Beta strandi115 – 122Combined sources8
Beta strandi125 – 134Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B56X-ray2.05A1-135[»]
1JJJNMR-A1-135[»]
4AZMX-ray2.75A/B1-135[»]
4AZRX-ray2.95A/B1-135[»]
4LKPX-ray1.67A1-135[»]
4LKTX-ray2.57A/B/C/D1-135[»]
5HZ5X-ray1.40A2-135[»]
5UR9X-ray2.20A/B/C/D/E/F/G/H1-135[»]
ProteinModelPortaliQ01469
SMRiQ01469
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01469

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni129 – 131Fatty acid bindingCombined sources3 Publications3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi24 – 34Nuclear localization signal1 PublicationAdd BLAST11

Domaini

Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015 Eukaryota
ENOG4111US8 LUCA
GeneTreeiENSGT00760000118898
HOGENOMiHOG000004829
HOVERGENiHBG005633
InParanoidiQ01469
KOiK08754
OMAiVECDMNG
OrthoDBiEOG091G0QSV
PhylomeDBiQ01469
TreeFamiTF316894

Family and domain databases

Gene3Di2.40.128.20, 1 hit
InterProiView protein in InterPro
IPR012674 Calycin
IPR000463 Fatty_acid-bd
IPR031259 ILBP
IPR000566 Lipocln_cytosolic_FA-bd_dom
PANTHERiPTHR11955 PTHR11955, 1 hit
PfamiView protein in Pfam
PF00061 Lipocalin, 1 hit
PRINTSiPR00178 FATTYACIDBP
SUPFAMiSSF50814 SSF50814, 1 hit
PROSITEiView protein in PROSITE
PS00214 FABP, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01469-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK
60 70 80 90 100
NLTIKTESTL KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW
110 120 130
DGKESTITRK LKDGKLVVEC VMNNVTCTRI YEKVE
Length:135
Mass (Da):15,164
Last modified:January 23, 2007 - v3
Checksum:i77D38F8806143D63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94856 mRNA Translation: AAA58467.1
BT007449 mRNA Translation: AAP36117.1
AK311856 mRNA Translation: BAG34797.1
CH471068 Genomic DNA Translation: EAW87088.1
BC019385 mRNA Translation: AAH19385.1
BC070303 mRNA Translation: AAH70303.1
CCDSiCCDS6228.1
PIRiI56326
RefSeqiNP_001435.1, NM_001444.2
UniGeneiHs.408061

Genome annotation databases

EnsembliENST00000297258; ENSP00000297258; ENSG00000164687
GeneIDi2171
KEGGihsa:2171
UCSCiuc003yca.3 human

Similar proteinsi

Entry informationi

Entry nameiFABP5_HUMAN
AccessioniPrimary (citable) accession number: Q01469
Secondary accession number(s): B2R4K0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 204 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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