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P15090

- FABP4_HUMAN

UniProt

P15090 - FABP4_HUMAN

Protein

Fatty acid-binding protein, adipocyte

Gene

FABP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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. lipid particle Source: Reactome
    3. nucleus Source: UniProtKB-SubCell

    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

    ArrayExpressiP15090.
    BgeeiP15090.
    CleanExiHS_FABP4.
    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. 7 interactions.
    MINTiMINT-1398507.
    STRINGi9606.ENSP00000256104.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    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

    MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI    50
    TIKSESTFKN TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG 100
    KSTTIKRKRE DDKLVVECVM KGVTSTRVYE RA 132
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6230.1.
    PIRi A33363. FZHUF.
    RefSeqi NP_001433.1. NM_001442.2.
    UniGenei Hs.391561.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TOU X-ray 2.00 A 2-132 [» ]
    1TOW X-ray 2.00 A 2-132 [» ]
    2HNX X-ray 1.50 A 1-132 [» ]
    2NNQ X-ray 1.80 A 2-132 [» ]
    3FR2 X-ray 2.20 A 2-132 [» ]
    3FR4 X-ray 2.16 A 1-132 [» ]
    3FR5 X-ray 2.20 A 2-132 [» ]
    3P6C X-ray 1.25 A 1-132 [» ]
    3P6D X-ray 1.06 A 1-132 [» ]
    3P6E X-ray 1.08 A 1-132 [» ]
    3P6F X-ray 1.20 A 1-132 [» ]
    3P6G X-ray 1.20 A 1-132 [» ]
    3P6H X-ray 1.15 A 1-132 [» ]
    3Q6L X-ray 1.40 A 1-132 [» ]
    3RZY X-ray 1.08 A 1-132 [» ]
    ProteinModelPortali P15090.
    SMRi P15090. Positions 1-132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108465. 10 interactions.
    IntActi P15090. 7 interactions.
    MINTi MINT-1398507.
    STRINGi 9606.ENSP00000256104.

    Chemistry

    BindingDBi P15090.
    ChEMBLi CHEMBL2083.

    PTM databases

    PhosphoSitei P15090.

    Polymorphism databases

    DMDMi 119781.

    2D gel databases

    UCD-2DPAGE P15090.

    Proteomic databases

    MaxQBi P15090.
    PaxDbi P15090.
    PeptideAtlasi P15090.
    PRIDEi P15090.

    Protocols and materials databases

    DNASUi 2167.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256104 ; ENSP00000256104 ; ENSG00000170323 .
    GeneIDi 2167.
    KEGGi hsa:2167.
    UCSCi uc003ycd.2. human.

    Organism-specific databases

    CTDi 2167.
    GeneCardsi GC08M082390.
    HGNCi HGNC:3559. FABP4.
    HPAi CAB024961.
    HPA002188.
    MIMi 600434. gene.
    neXtProti NX_P15090.
    PharmGKBi PA27960.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326764.
    HOGENOMi HOG000004829.
    HOVERGENi HBG005633.
    InParanoidi P15090.
    KOi K08753.
    OMAi GQEFDEI.
    OrthoDBi EOG7NW6BZ.
    PhylomeDBi P15090.
    TreeFami TF316894.

    Enzyme and pathway databases

    Reactomei REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

    Miscellaneous databases

    ChiTaRSi FABP4. human.
    EvolutionaryTracei P15090.
    GeneWikii Adipocyte_protein_2.
    GenomeRNAii 2167.
    NextBioi 8751.
    PROi P15090.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15090.
    Bgeei P15090.
    CleanExi HS_FABP4.
    Genevestigatori P15090.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00178. FATTYACIDBP.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00214. FABP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 148 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