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P07148

- FABPL_HUMAN

UniProt

P07148 - FABPL_HUMAN

Protein

Fatty acid-binding protein, liver

Gene

FABP1

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

    Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport.

    GO - Molecular functioni

    1. antioxidant activity Source: UniProtKB
    2. bile acid binding Source: Ensembl
    3. chromatin binding Source: Ensembl
    4. drug binding Source: Ensembl
    5. fatty acid binding Source: Ensembl
    6. long-chain fatty acid transporter activity Source: Ensembl
    7. phospholipid binding Source: Ensembl

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. cellular response to hydrogen peroxide Source: UniProtKB
    3. cellular response to hypoxia Source: UniProtKB
    4. intestinal absorption Source: Ensembl
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    7. positive regulation of cell proliferation Source: Ensembl
    8. positive regulation of fatty acid beta-oxidation Source: Ensembl
    9. positive regulation of hydrolase activity Source: Ensembl
    10. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid-binding protein, liver
    Alternative name(s):
    Fatty acid-binding protein 1
    Liver-type fatty acid-binding protein
    Short name:
    L-FABP
    Gene namesi
    Name:FABP1
    Synonyms:FABPL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3555. FABP1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical cortex Source: Ensembl
    2. cytosol Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. nucleoplasm Source: Reactome
    5. peroxisomal matrix Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27956.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 127127Fatty acid-binding protein, liverPRO_0000067334Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei31 – 311N6-succinyllysineBy similarity
    Modified residuei36 – 361N6-succinyllysineBy similarity
    Modified residuei46 – 461N6-succinyllysineBy similarity
    Modified residuei57 – 571N6-succinyllysineBy similarity
    Modified residuei78 – 781N6-succinyllysineBy similarity
    Modified residuei90 – 901N6-succinyllysineBy similarity
    Modified residuei121 – 1211N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP07148.
    PaxDbiP07148.
    PRIDEiP07148.

    2D gel databases

    SWISS-2DPAGEP07148.

    PTM databases

    PhosphoSiteiP07148.

    Expressioni

    Gene expression databases

    ArrayExpressiP07148.
    BgeeiP07148.
    CleanExiHS_FABP1.
    GenevestigatoriP07148.

    Organism-specific databases

    HPAiCAB002305.
    HPA028275.

    Interactioni

    Protein-protein interaction databases

    BioGridi108466. 4 interactions.
    IntActiP07148. 1 interaction.
    MINTiMINT-5002397.
    STRINGi9606.ENSP00000295834.

    Structurei

    Secondary structure

    1
    127
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 1410
    Helixi15 – 217
    Helixi26 – 327
    Beta strandi38 – 447
    Beta strandi47 – 548
    Beta strandi57 – 648
    Beta strandi67 – 726
    Beta strandi74 – 763
    Beta strandi78 – 825
    Beta strandi84 – 874
    Beta strandi90 – 956
    Beta strandi98 – 1058
    Beta strandi108 – 1158
    Beta strandi118 – 1269

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F73X-ray2.50A/B/C/D/E/F/G/H1-127[»]
    2L67NMR-A2-127[»]
    2L68NMR-A2-127[»]
    2LKKNMR-A2-127[»]
    2PY1NMR-A1-127[»]
    3B2HX-ray1.55A2-127[»]
    3B2IX-ray1.86A2-127[»]
    3B2JX-ray2.00A2-127[»]
    3B2KX-ray1.73A2-127[»]
    3B2LX-ray2.25A2-127[»]
    3STKX-ray1.55A2-127[»]
    3STMX-ray2.22X2-127[»]
    3STNX-ray2.60A2-127[»]
    3VG2X-ray2.40A2-127[»]
    3VG3X-ray2.22A2-127[»]
    3VG4X-ray2.50A2-127[»]
    3VG5X-ray2.00A2-127[»]
    3VG6X-ray2.22A2-127[»]
    3VG7X-ray1.44A2-127[»]
    ProteinModelPortaliP07148.
    SMRiP07148. Positions 2-127.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07148.

    Family & Domainsi

    Domaini

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG317209.
    HOVERGENiHBG005633.
    InParanoidiP07148.
    KOiK08750.
    OMAiDTITNTM.
    PhylomeDBiP07148.
    TreeFamiTF330348.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    [Graphical view]
    PRINTSiPR00178. FATTYACIDBP.
    SUPFAMiSSF50814. SSF50814. 1 hit.
    PROSITEiPS00214. FABP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07148-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFSGKYQLQ SQENFEAFMK AIGLPEELIQ KGKDIKGVSE IVQNGKHFKF    50
    TITAGSKVIQ NEFTVGEECE LETMTGEKVK TVVQLEGDNK LVTTFKNIKS 100
    VTELNGDIIT NTMTLGDIVF KRISKRI 127
    Length:127
    Mass (Da):14,208
    Last modified:April 1, 1988 - v1
    Checksum:i065DCEFB08DAB6B6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541A → T.
    Corresponds to variant rs1801273 [ dbSNP | Ensembl ].
    VAR_014662
    Natural varianti94 – 941T → A.1 Publication
    Corresponds to variant rs2241883 [ dbSNP | Ensembl ].
    VAR_022093

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10617 mRNA. Translation: AAA52419.1.
    M10050 mRNA. Translation: AAA52418.1.
    BC032801 mRNA. Translation: AAH32801.1.
    CCDSiCCDS2001.1.
    PIRiA22289. FZHUL.
    RefSeqiNP_001434.1. NM_001443.2.
    UniGeneiHs.380135.

    Genome annotation databases

    EnsembliENST00000295834; ENSP00000295834; ENSG00000163586.
    GeneIDi2168.
    KEGGihsa:2168.
    UCSCiuc002sst.2. human.

    Polymorphism databases

    DMDMi119808.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10617 mRNA. Translation: AAA52419.1 .
    M10050 mRNA. Translation: AAA52418.1 .
    BC032801 mRNA. Translation: AAH32801.1 .
    CCDSi CCDS2001.1.
    PIRi A22289. FZHUL.
    RefSeqi NP_001434.1. NM_001443.2.
    UniGenei Hs.380135.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F73 X-ray 2.50 A/B/C/D/E/F/G/H 1-127 [» ]
    2L67 NMR - A 2-127 [» ]
    2L68 NMR - A 2-127 [» ]
    2LKK NMR - A 2-127 [» ]
    2PY1 NMR - A 1-127 [» ]
    3B2H X-ray 1.55 A 2-127 [» ]
    3B2I X-ray 1.86 A 2-127 [» ]
    3B2J X-ray 2.00 A 2-127 [» ]
    3B2K X-ray 1.73 A 2-127 [» ]
    3B2L X-ray 2.25 A 2-127 [» ]
    3STK X-ray 1.55 A 2-127 [» ]
    3STM X-ray 2.22 X 2-127 [» ]
    3STN X-ray 2.60 A 2-127 [» ]
    3VG2 X-ray 2.40 A 2-127 [» ]
    3VG3 X-ray 2.22 A 2-127 [» ]
    3VG4 X-ray 2.50 A 2-127 [» ]
    3VG5 X-ray 2.00 A 2-127 [» ]
    3VG6 X-ray 2.22 A 2-127 [» ]
    3VG7 X-ray 1.44 A 2-127 [» ]
    ProteinModelPortali P07148.
    SMRi P07148. Positions 2-127.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108466. 4 interactions.
    IntActi P07148. 1 interaction.
    MINTi MINT-5002397.
    STRINGi 9606.ENSP00000295834.

    Chemistry

    BindingDBi P07148.
    ChEMBLi CHEMBL5421.

    PTM databases

    PhosphoSitei P07148.

    Polymorphism databases

    DMDMi 119808.

    2D gel databases

    SWISS-2DPAGE P07148.

    Proteomic databases

    MaxQBi P07148.
    PaxDbi P07148.
    PRIDEi P07148.

    Protocols and materials databases

    DNASUi 2168.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295834 ; ENSP00000295834 ; ENSG00000163586 .
    GeneIDi 2168.
    KEGGi hsa:2168.
    UCSCi uc002sst.2. human.

    Organism-specific databases

    CTDi 2168.
    GeneCardsi GC02M088422.
    HGNCi HGNC:3555. FABP1.
    HPAi CAB002305.
    HPA028275.
    MIMi 134650. gene.
    neXtProti NX_P07148.
    PharmGKBi PA27956.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG317209.
    HOVERGENi HBG005633.
    InParanoidi P07148.
    KOi K08750.
    OMAi DTITNTM.
    PhylomeDBi P07148.
    TreeFami TF330348.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

    Miscellaneous databases

    ChiTaRSi FABP1. human.
    EvolutionaryTracei P07148.
    GeneWikii FABP1.
    GenomeRNAii 2168.
    NextBioi 8755.
    PROi P07148.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07148.
    Bgeei P07148.
    CleanExi HS_FABP1.
    Genevestigatori P07148.

    Family and domain databases

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

    Publicationsi

    1. "Human liver fatty acid binding protein cDNA and amino acid sequence. Functional and evolutionary implications."
      Chan L., Wei C.-F., Li W.-H., Yang C.-Y., Ratner P., Pownall H., Gotto A.M. Jr., Smith L.C.
      J. Biol. Chem. 260:2629-2632(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT MET-1.
    2. "Human liver fatty acid binding protein. Isolation of a full length cDNA and comparative sequence analyses of orthologous and paralogous proteins."
      Lowe J.B., Boguski M.S., Sweetser D.A., Elshourbagy N.A., Taylor J.M., Gordon J.I.
      J. Biol. Chem. 260:3413-3417(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-94.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon, Kidney and Stomach.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "Rapid data collection for protein structure determination by NMR spectroscopy."
      Xu Y., Long D., Yang D.
      J. Am. Chem. Soc. 129:7722-7723(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    6. "Crystal structure of human FABP1."
      Structural genomics consortium (SGC)
      Submitted (DEC-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiFABPL_HUMAN
    AccessioniPrimary (citable) accession number: P07148
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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