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Protein

Fatty acid-binding protein, epidermal

Gene

FABP5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei109Fatty acidBy similarity1

GO - Molecular functioni

  • fatty acid binding Source: ProtInc
  • lipid binding Source: ProtInc
  • transporter activity Source: InterPro

GO - Biological processi

  • epidermis development Source: ProtInc
  • glucose metabolic process Source: Ensembl
  • glucose transport Source: Ensembl
  • lipid metabolic process Source: ProtInc
  • phosphatidylcholine biosynthetic process Source: Ensembl
  • response to wounding Source: Ensembl
  • triglyceride catabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164687-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
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, epidermal
Alternative name(s):
Epidermal-type fatty acid-binding protein
Short name:
E-FABP
Fatty acid-binding protein 5
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

HGNCiHGNC:3560. FABP5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi2171.
OpenTargetsiENSG00000164687.
PharmGKBiPA27961.

Chemistry databases

ChEMBLiCHEMBL3674.
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, epidermalAdd BLAST134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei17N6-acetyllysineCombined sources1
Disulfide bondi120 ↔ 1272 Publications
Modified residuei131PhosphotyrosineCombined sources1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ01469.
MaxQBiQ01469.
PaxDbiQ01469.
PeptideAtlasiQ01469.
PRIDEiQ01469.
TopDownProteomicsiQ01469.

2D gel databases

SWISS-2DPAGEQ01469.
UCD-2DPAGEQ01469.

PTM databases

iPTMnetiQ01469.
PhosphoSitePlusiQ01469.
SwissPalmiQ01469.

Expressioni

Tissue specificityi

Keratinocytes; highly expressed in psoriatic skin.

Gene expression databases

BgeeiENSG00000164687.
CleanExiHS_FABP5.
ExpressionAtlasiQ01469. baseline and differential.
GenevisibleiQ01469. HS.

Organism-specific databases

HPAiCAB017831.
CAB040577.
HPA051895.

Interactioni

Protein-protein interaction databases

BioGridi108469. 37 interactors.
IntActiQ01469. 2 interactors.
MINTiMINT-3024261.
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 – 26Combined sources8
Helixi30 – 38Combined sources9
Beta strandi42 – 48Combined sources7
Beta strandi51 – 57Combined sources7
Beta strandi62 – 68Combined sources7
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 – 133Combined sources9

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[»]
ProteinModelPortaliQ01469.
SMRiQ01469.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01469.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni129 – 131Fatty acid bindingBy similarity3

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.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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[»]
ProteinModelPortaliQ01469.
SMRiQ01469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108469. 37 interactors.
IntActiQ01469. 2 interactors.
MINTiMINT-3024261.
STRINGi9606.ENSP00000297258.

Chemistry databases

BindingDBiQ01469.
ChEMBLiCHEMBL3674.
GuidetoPHARMACOLOGYi2535.
SwissLipidsiSLP:000001104.

Protein family/group databases

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

PTM databases

iPTMnetiQ01469.
PhosphoSitePlusiQ01469.
SwissPalmiQ01469.

Polymorphism and mutation databases

BioMutaiFABP5.
DMDMi232081.

2D gel databases

SWISS-2DPAGEQ01469.
UCD-2DPAGEQ01469.

Proteomic databases

EPDiQ01469.
MaxQBiQ01469.
PaxDbiQ01469.
PeptideAtlasiQ01469.
PRIDEiQ01469.
TopDownProteomicsiQ01469.

Protocols and materials databases

DNASUi2171.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2171.
DisGeNETi2171.
GeneCardsiFABP5.
HGNCiHGNC:3560. FABP5.
HPAiCAB017831.
CAB040577.
HPA051895.
MIMi605168. gene.
neXtProtiNX_Q01469.
OpenTargetsiENSG00000164687.
PharmGKBiPA27961.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164687-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-5362517. Signaling by Retinoic Acid.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiQ01469.
GeneWikiiFABP5.
GenomeRNAii2171.
PROiQ01469.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164687.
CleanExiHS_FABP5.
ExpressionAtlasiQ01469. baseline and differential.
GenevisibleiQ01469. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABP5_HUMAN
AccessioniPrimary (citable) accession number: Q01469
Secondary accession number(s): B2R4K0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 188 of the entry and version 3 of the sequence. [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

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.