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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

  1. fatty acid binding Source: ProtInc
  2. transporter activity Source: InterPro

GO - Biological processi

  1. brown fat cell differentiation Source: Ensembl
  2. cellular response to lithium ion Source: Ensembl
  3. cholesterol homeostasis Source: Ensembl
  4. cytokine production Source: Ensembl
  5. negative regulation of protein kinase activity Source: Ensembl
  6. negative regulation of transcription, DNA-templated Source: Ensembl
  7. positive regulation of inflammatory response Source: Ensembl
  8. small molecule metabolic process Source: Reactome
  9. triglyceride catabolic process Source: Reactome
  10. white fat cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

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
ProteomesiUP000005640: 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

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. lipid particle Source: Reactome
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27960.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 132131Fatty acid-binding protein, adipocytePRO_0000067366Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteine1 Publication
Modified residuei20 – 201Phosphotyrosine; by Tyr-kinasesBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15090.
PaxDbiP15090.
PeptideAtlasiP15090.
PRIDEiP15090.

2D gel databases

UCD-2DPAGEP15090.

PTM databases

PhosphoSiteiP15090.

Expressioni

Gene expression databases

BgeeiP15090.
CleanExiHS_FABP4.
ExpressionAtlasiP15090. baseline and differential.
GenevestigatoriP15090.

Organism-specific databases

HPAiCAB024961.
HPA002188.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi108465. 10 interactions.
IntActiP15090. 8 interactions.
MINTiMINT-1398507.
STRINGi9606.ENSP00000256104.

Structurei

Secondary structure

1
132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 54Combined sources
Beta strandi7 – 1610Combined sources
Helixi17 – 248Combined sources
Helixi28 – 369Combined sources
Beta strandi40 – 467Combined sources
Beta strandi49 – 557Combined sources
Beta strandi61 – 655Combined sources
Beta strandi71 – 744Combined sources
Beta strandi80 – 889Combined sources
Beta strandi91 – 988Combined sources
Beta strandi101 – 11010Combined sources
Beta strandi113 – 1208Combined sources
Beta strandi123 – 1319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4NNTX-ray1.53A1-132[»]
ProteinModelPortaliP15090.
SMRiP15090. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15090.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 1293Fatty acid binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi22 – 3211Nuclear localization signalBy similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG326764.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP15090.
KOiK08753.
OMAiGQEFDEI.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP15090.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231E → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_036320

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.2. human.

Polymorphism databases

DMDMi119781.

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
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[»]
4NNTX-ray1.53A1-132[»]
ProteinModelPortaliP15090.
SMRiP15090. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108465. 10 interactions.
IntActiP15090. 8 interactions.
MINTiMINT-1398507.
STRINGi9606.ENSP00000256104.

Chemistry

BindingDBiP15090.
ChEMBLiCHEMBL2083.

PTM databases

PhosphoSiteiP15090.

Polymorphism databases

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.2. human.

Organism-specific databases

CTDi2167.
GeneCardsiGC08M082390.
HGNCiHGNC:3559. FABP4.
HPAiCAB024961.
HPA002188.
MIMi600434. gene.
neXtProtiNX_P15090.
PharmGKBiPA27960.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG326764.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP15090.
KOiK08753.
OMAiGQEFDEI.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP15090.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

ChiTaRSiFABP4. human.
EvolutionaryTraceiP15090.
GeneWikiiAdipocyte_protein_2.
GenomeRNAii2167.
NextBioi8751.
PROiP15090.
SOURCEiSearch...

Gene expression databases

BgeeiP15090.
CleanExiHS_FABP4.
ExpressionAtlasiP15090. baseline and differential.
GenevestigatoriP15090.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Human adipocyte lipid-binding protein: purification of the protein and cloning of its complementary DNA."
    Baxa C.A., Sha R.S., Buelt M.K., Smith A.J., Matarese V., Chinander L.L., Boundy K.L., Bernlohr D.A.
    Biochemistry 28:8683-8690(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Urinary bladder.
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  7. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-23.
  8. "Discovery of inhibitors of human adipocyte fatty acid-binding protein, a potential type 2 diabetes target."
    Lehmann F., Haile S., Axen E., Medina C., Uppenberg J., Svensson S., Lundbaeck T., Rondahl L., Barf T.
    Bioorg. Med. Chem. Lett. 14:4445-4448(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR.
  9. "Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2)."
    Marr E., Tardie M., Carty M., Brown Phillips T., Wang I.-K., Soeller W., Qiu X., Karam G.
    Acta Crystallogr. F 62:1058-1060(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID, SUBUNIT, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.

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: February 4, 2015
This is version 152 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

External Data

Dasty 3

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 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.