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Protein

Fatty acid-binding protein, adipocyte

Gene

FABP4

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

Functioni

Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity).By similarity

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000133055-MONOMER.
ZFISH:ENSG00000170323-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
SIGNORiP15090.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, adipocyte
Alternative name(s):
Adipocyte lipid-binding protein
Short name:
ALBP
Adipocyte-type fatty acid-binding protein
Short name:
A-FABP
Short name:
AFABP
Fatty acid-binding protein 4
Gene namesi
Name:FABP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3559. FABP4.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • lipid particle Source: Reactome
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi2167.
OpenTargetsiENSG00000170323.
PharmGKBiPA27960.

Chemistry databases

ChEMBLiCHEMBL2083.
DrugBankiDB04224. Oleic Acid.
GuidetoPHARMACOLOGYi2534.

Polymorphism and mutation databases

BioMutaiFABP4.
DMDMi119781.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000673662 – 132Fatty acid-binding protein, adipocyteAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylcysteineCombined sources1
Modified residuei13PhosphoserineBy similarity1
Modified residuei20Phosphotyrosine; by Tyr-kinasesBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15090.
PaxDbiP15090.
PeptideAtlasiP15090.
PRIDEiP15090.

2D gel databases

UCD-2DPAGEP15090.

PTM databases

iPTMnetiP15090.
PhosphoSitePlusiP15090.
SwissPalmiP15090.

Expressioni

Gene expression databases

BgeeiENSG00000170323.
CleanExiHS_FABP4.
ExpressionAtlasiP15090. baseline and differential.
GenevisibleiP15090. HS.

Organism-specific databases

HPAiCAB024961.
HPA002188.

Interactioni

Subunit structurei

Homodimer. Interacts with PPARG (By similarity). Monomer.By similarity2 Publications

Protein-protein interaction databases

BioGridi108465. 12 interactors.
IntActiP15090. 8 interactors.
MINTiMINT-1398507.
STRINGi9606.ENSP00000256104.

Chemistry databases

BindingDBiP15090.

Structurei

Secondary structure

1132
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 5Combined sources4
Beta strandi7 – 16Combined sources10
Helixi17 – 24Combined sources8
Helixi28 – 36Combined sources9
Beta strandi40 – 46Combined sources7
Beta strandi49 – 55Combined sources7
Beta strandi61 – 65Combined sources5
Beta strandi71 – 74Combined sources4
Beta strandi80 – 88Combined sources9
Beta strandi91 – 98Combined sources8
Beta strandi101 – 110Combined sources10
Beta strandi113 – 120Combined sources8
Beta strandi123 – 131Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TOUX-ray2.00A2-132[»]
1TOWX-ray2.00A2-132[»]
2HNXX-ray1.50A1-132[»]
2NNQX-ray1.80A2-132[»]
3FR2X-ray2.20A2-132[»]
3FR4X-ray2.16A1-132[»]
3FR5X-ray2.20A2-132[»]
3P6CX-ray1.25A1-132[»]
3P6DX-ray1.06A1-132[»]
3P6EX-ray1.08A1-132[»]
3P6FX-ray1.20A1-132[»]
3P6GX-ray1.20A1-132[»]
3P6HX-ray1.15A1-132[»]
3Q6LX-ray1.40A1-132[»]
3RZYX-ray1.08A1-132[»]
4NNSX-ray1.53A1-132[»]
4NNTX-ray1.53A1-132[»]
5D45X-ray1.65A1-132[»]
5D47X-ray1.70A1-132[»]
5D48X-ray1.81A1-132[»]
5D4AX-ray1.70A1-132[»]
5EDBX-ray1.18A1-132[»]
5EDCX-ray1.29A1-132[»]
ProteinModelPortaliP15090.
SMRiP15090.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15090.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni127 – 129Fatty acid binding3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi22 – 32Nuclear localization signalBy similarityAdd BLAST11

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP15090.
KOiK08753.
OMAiGQEFDEI.
OrthoDBiEOG091G0QSV.
PhylomeDBiP15090.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR033073. FABP4.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF83. PTHR11955:SF83. 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.

P15090-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI
60 70 80 90 100
TIKSESTFKN TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG
110 120 130
KSTTIKRKRE DDKLVVECVM KGVTSTRVYE RA
Length:132
Mass (Da):14,719
Last modified:January 23, 2007 - v3
Checksum:i819D788FF4BF7235
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03632023E → D in a breast cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02874 mRNA. Translation: AAA51689.1.
BT006809 mRNA. Translation: AAP35455.1.
CR456903 mRNA. Translation: CAG33184.1.
CH471068 Genomic DNA. Translation: EAW87092.1.
BC003672 mRNA. Translation: AAH03672.1.
CCDSiCCDS6230.1.
PIRiA33363. FZHUF.
RefSeqiNP_001433.1. NM_001442.2.
UniGeneiHs.391561.

Genome annotation databases

EnsembliENST00000256104; ENSP00000256104; ENSG00000170323.
GeneIDi2167.
KEGGihsa:2167.
UCSCiuc003ycd.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02874 mRNA. Translation: AAA51689.1.
BT006809 mRNA. Translation: AAP35455.1.
CR456903 mRNA. Translation: CAG33184.1.
CH471068 Genomic DNA. Translation: EAW87092.1.
BC003672 mRNA. Translation: AAH03672.1.
CCDSiCCDS6230.1.
PIRiA33363. FZHUF.
RefSeqiNP_001433.1. NM_001442.2.
UniGeneiHs.391561.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TOUX-ray2.00A2-132[»]
1TOWX-ray2.00A2-132[»]
2HNXX-ray1.50A1-132[»]
2NNQX-ray1.80A2-132[»]
3FR2X-ray2.20A2-132[»]
3FR4X-ray2.16A1-132[»]
3FR5X-ray2.20A2-132[»]
3P6CX-ray1.25A1-132[»]
3P6DX-ray1.06A1-132[»]
3P6EX-ray1.08A1-132[»]
3P6FX-ray1.20A1-132[»]
3P6GX-ray1.20A1-132[»]
3P6HX-ray1.15A1-132[»]
3Q6LX-ray1.40A1-132[»]
3RZYX-ray1.08A1-132[»]
4NNSX-ray1.53A1-132[»]
4NNTX-ray1.53A1-132[»]
5D45X-ray1.65A1-132[»]
5D47X-ray1.70A1-132[»]
5D48X-ray1.81A1-132[»]
5D4AX-ray1.70A1-132[»]
5EDBX-ray1.18A1-132[»]
5EDCX-ray1.29A1-132[»]
ProteinModelPortaliP15090.
SMRiP15090.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108465. 12 interactors.
IntActiP15090. 8 interactors.
MINTiMINT-1398507.
STRINGi9606.ENSP00000256104.

Chemistry databases

BindingDBiP15090.
ChEMBLiCHEMBL2083.
DrugBankiDB04224. Oleic Acid.
GuidetoPHARMACOLOGYi2534.

PTM databases

iPTMnetiP15090.
PhosphoSitePlusiP15090.
SwissPalmiP15090.

Polymorphism and mutation databases

BioMutaiFABP4.
DMDMi119781.

2D gel databases

UCD-2DPAGEP15090.

Proteomic databases

MaxQBiP15090.
PaxDbiP15090.
PeptideAtlasiP15090.
PRIDEiP15090.

Protocols and materials databases

DNASUi2167.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256104; ENSP00000256104; ENSG00000170323.
GeneIDi2167.
KEGGihsa:2167.
UCSCiuc003ycd.3. human.

Organism-specific databases

CTDi2167.
DisGeNETi2167.
GeneCardsiFABP4.
HGNCiHGNC:3559. FABP4.
HPAiCAB024961.
HPA002188.
MIMi600434. gene.
neXtProtiNX_P15090.
OpenTargetsiENSG00000170323.
PharmGKBiPA27960.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP15090.
KOiK08753.
OMAiGQEFDEI.
OrthoDBiEOG091G0QSV.
PhylomeDBiP15090.
TreeFamiTF316894.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000133055-MONOMER.
ZFISH:ENSG00000170323-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
SIGNORiP15090.

Miscellaneous databases

ChiTaRSiFABP4. human.
EvolutionaryTraceiP15090.
GeneWikiiAdipocyte_protein_2.
GenomeRNAii2167.
PROiP15090.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000170323.
CleanExiHS_FABP4.
ExpressionAtlasiP15090. baseline and differential.
GenevisibleiP15090. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR033073. FABP4.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF83. PTHR11955:SF83. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABP4_HUMAN
AccessioniPrimary (citable) accession number: P15090
Secondary accession number(s): Q6IBA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 171 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.