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Reviewed, UniProtKB/Swiss-Prot P15090 (FABP4_HUMAN)

Last modified June 16, 2009. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fatty acid-binding protein, adipocyte
Alternative name(s):
    A-FABP
      Short name=AFABP
    Fatty acid-binding protein 4
    Adipocyte lipid-binding protein
      Short name=ALBP
Gene names
Name: FABP4
OrganismHomo sapiens (Human)
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.

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
   PTMPhosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processtransport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

soluble fraction Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionfatty acid binding Ref.1

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: IntAct

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

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 residue201Phosphotyrosine; by Tyr-kinases By similarity

Natural variations

Natural variant231E → D in a breast cancer sample; somatic mutation. Ref.4
VAR_036320

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P15090-1 [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: 2481498] [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]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Urinary bladder.
[4]"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: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-23.
[5]"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: 15357969] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR.
[6]"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: 17077479] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID, SUBUNIT, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

J02874 mRNA. Translation: AAA51689.1.
BT006809 mRNA. Translation: AAP35455.1.
BC003672 mRNA. Translation: AAH03672.1.
IPIIPI00215746.
PIRFZHUF. A33363.
RefSeqNP_001433.1.
UniGeneHs.391561

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TOUX-ray2.00A2-131[»]
1TOWX-ray2.00A2-132[»]
2HNXX-ray1.50A1-132[»]
2NNQX-ray1.80A2-131[»]
3FR2X-ray2.20A2-132[»]
3FR4X-ray2.16A1-132[»]
3FR5X-ray2.20A2-132[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP15090. 4 interactions.

PTM databases

PhosphoSiteP15090.

Proteomic databases

PeptideAtlasP15090.
PRIDEP15090.

Genome annotation databases

EnsemblENSG00000170323. Homo sapiens. [Contig view]
GeneID2167.
KEGGhsa:2167.

Organism-specific databases

GeneCardsGC08M082553.
H-InvDBHIX0007617.
HGNCHGNC:3559. FABP4.
HPAHPA002188.
MIM600434. gene.
PharmGKBPA27960.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP15090.
HOVERGENP15090.
OMAP15090. GQEFDEI.

Enzyme and pathway databases

ReactomeREACT_602. Lipid and lipoprotein metabolism.

Gene expression databases

ArrayExpressP15090.
BgeeP15090.
CleanExHS_FABP4.
GermOnlineENSG00000170323. Homo sapiens.

Family and domain databases

InterProIPR012674. Calycin.
IPR000463. Fatty_acid_bd.
IPR000566. Lipocln_cytFABP.
[Graphical view]
Gene3DG3DSA:2.40.128.20. Calycin. 1 hit.
PANTHERPTHR11955. Fatty_acid_bd. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio8751.
SOURCESearch...

Entry information

Entry nameFABP4_HUMAN
AccessionPrimary (citable) accession number: P15090
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 8

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents