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P15090 (FABP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FABP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homodimer. Interacts with PPARG By similarity. Monomer. Ref.9

Subcellular location

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.

Domain

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

Sequence similarities

Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbrown fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

cholesterol homeostasis

Inferred from electronic annotation. Source: Ensembl

cytokine production

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride catabolic process

Traceable author statement. Source: Reactome

white fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

lipid particle

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfatty acid binding

Traceable author statement Ref.1. Source: ProtInc

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 132131Fatty acid-binding protein, adipocyte
PRO_0000067366

Regions

Region127 – 1293Fatty acid binding
Motif22 – 3211Nuclear localization signal By similarity

Amino acid modifications

Modified residue21N-acetylcysteine Ref.6
Modified residue201Phosphotyrosine; by Tyr-kinases By similarity

Natural variations

Natural variant231E → D in a breast cancer sample; somatic mutation. Ref.7
VAR_036320

Secondary structure

.......................... 132
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15090 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 819D788FF4BF7235

FASTA13214,719
        10         20         30         40         50         60 
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI TIKSESTFKN 

        70         80         90        100        110        120 
TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG KSTTIKRKRE DDKLVVECVM 

       130 
KGVTSTRVYE RA 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6230.1.
PIRFZHUF. A33363.
RefSeqNP_001433.1. NM_001442.2.
UniGeneHs.391561.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP15090.
SMRP15090. Positions 1-132.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108465. 10 interactions.
IntActP15090. 7 interactions.
MINTMINT-1398507.
STRING9606.ENSP00000256104.

Chemistry

BindingDBP15090.
ChEMBLCHEMBL2083.

PTM databases

PhosphoSiteP15090.

Polymorphism databases

DMDM119781.

2D gel databases

UCD-2DPAGEP15090.

Proteomic databases

MaxQBP15090.
PaxDbP15090.
PeptideAtlasP15090.
PRIDEP15090.

Protocols and materials databases

DNASU2167.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256104; ENSP00000256104; ENSG00000170323.
GeneID2167.
KEGGhsa:2167.
UCSCuc003ycd.2. human.

Organism-specific databases

CTD2167.
GeneCardsGC08M082390.
HGNCHGNC:3559. FABP4.
HPACAB024961.
HPA002188.
MIM600434. gene.
neXtProtNX_P15090.
PharmGKBPA27960.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326764.
HOGENOMHOG000004829.
HOVERGENHBG005633.
InParanoidP15090.
KOK08753.
OMAGQEFDEI.
OrthoDBEOG7NW6BZ.
PhylomeDBP15090.
TreeFamTF316894.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpressP15090.
BgeeP15090.
CleanExHS_FABP4.
GenevestigatorP15090.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFABP4. human.
EvolutionaryTraceP15090.
GeneWikiAdipocyte_protein_2.
GenomeRNAi2167.
NextBio8751.
PROP15090.
SOURCESearch...

Entry information

Entry nameFABP4_HUMAN
AccessionPrimary (citable) accession number: P15090
Secondary accession number(s): Q6IBA1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM