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P51161

- FABP6_HUMAN

UniProt

P51161 - FABP6_HUMAN

Protein

Gastrotropin

Gene

FABP6

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

    Ileal protein which stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. Isoform 2 is essential for the survival of colon cancer cells to bile acid-induced apoptosis.1 Publication

    GO - Molecular functioni

    1. lipid binding Source: ProtInc
    2. transporter activity Source: InterPro

    GO - Biological processi

    1. bile acid and bile salt transport Source: Reactome
    2. bile acid metabolic process Source: Reactome
    3. lipid metabolic process Source: ProtInc
    4. negative regulation of cell proliferation Source: ProtInc
    5. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_11042. Recycling of bile acids and salts.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gastrotropin
    Short name:
    GT
    Alternative name(s):
    Fatty acid-binding protein 6
    Ileal lipid-binding protein
    Short name:
    ILBP
    Intestinal 15 kDa protein
    Short name:
    I-15P
    Intestinal bile acid-binding protein
    Short name:
    I-BABP
    Gene namesi
    Name:FABP6
    Synonyms:ILBP, ILLBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:3561. FABP6.

    Subcellular locationi

    Isoform 2 : Cytoplasm
    Note: Localized close to nucleus on the apical side of both normal and neoplastic cells.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27962.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 128127GastrotropinPRO_0000067380Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP51161.
    PaxDbiP51161.
    PRIDEiP51161.

    PTM databases

    PhosphoSiteiP51161.

    Expressioni

    Tissue specificityi

    Isoform 2 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform 1 is expressed in the jejunum, ileum, cecum and ascending colon intestine. Isoform 2 is expressed in the gallbladder, duodenum, jejunum, ileum, cecum, ascending, transverse and descending colon, sigmoid colon and rectum.1 Publication

    Inductioni

    Isoform 1 is up-regulated by chenodeoxycholic acid (CDCA) via the FXR transcription pathway. Isoform 2 is up-regulated by NF-kappa-B and in all stages of colorectal adenocarcinoma. Isoform 1 is not up-regulated in all stages of colorectal adenocarcinoma.1 Publication

    Gene expression databases

    ArrayExpressiP51161.
    BgeeiP51161.
    CleanExiHS_FABP6.
    GenevestigatoriP51161.

    Organism-specific databases

    HPAiCAB024713.
    HPA012601.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000377549.

    Structurei

    Secondary structure

    1
    128
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1411
    Helixi15 – 228
    Helixi26 – 338
    Beta strandi38 – 425
    Beta strandi47 – 548
    Beta strandi57 – 659
    Turni66 – 683
    Beta strandi70 – 723
    Beta strandi75 – 784
    Beta strandi80 – 823
    Beta strandi88 – 947
    Beta strandi99 – 1046
    Beta strandi106 – 11712
    Beta strandi119 – 1268

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O1UNMR-A2-128[»]
    1O1VNMR-A2-128[»]
    2MM3NMR-A2-128[»]
    ProteinModelPortaliP51161.
    SMRiP51161. Positions 2-128.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51161.

    Family & Domainsi

    Domaini

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG275686.
    HOGENOMiHOG000004830.
    HOVERGENiHBG005633.
    InParanoidiP51161.
    KOiK08755.
    OMAiFKATVKM.
    OrthoDBiEOG7HB5C9.
    PhylomeDBiP51161.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform 1 (identifier: P51161-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAFTGKFEME SEKNYDEFMK LLGISSDVIE KARNFKIVTE VQQDGQDFTW    50
    SQHYSGGHTM TNKFTVGKES NIQTMGGKTF KATVQMEGGK LVVNFPNYHQ 100
    TSEIVGDKLV EVSTIGGVTY ERVSKRLA 128
    Length:128
    Mass (Da):14,371
    Last modified:January 23, 2007 - v2
    Checksum:i173CBC5DBEDADDE1
    GO
    Isoform 2 (identifier: P51161-2) [UniParc]FASTAAdd to Basket

    Also known as: IBABP-L

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MKTVTMMMVVEMQALTQVLRAVLSACTWVSRKGDLQRMKQTHKGKPPSSM

    Show »
    Length:177
    Mass (Da):19,874
    Checksum:i0ACBAE8E7DF65BF0
    GO

    Sequence cautioni

    The sequence AAH22489.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331R → H.1 Publication
    Corresponds to variant rs17856662 [ dbSNP | Ensembl ].
    VAR_039578
    Natural varianti55 – 551S → Y.1 Publication
    Corresponds to variant rs17852045 [ dbSNP | Ensembl ].
    VAR_039579
    Natural varianti79 – 791T → M.
    Corresponds to variant rs1130435 [ dbSNP | Ensembl ].
    VAR_039580

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MKTVTMMMVVEMQALTQVLR AVLSACTWVSRKGDLQRMKQ THKGKPPSSM in isoform 2. 1 PublicationVSP_038039

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19869 mRNA. Translation: AAB82751.1.
    X90908 mRNA. Translation: CAA62415.1.
    DQ132786 mRNA. Translation: ABA12611.1.
    AC008609 Genomic DNA. No translation available.
    AC112191 Genomic DNA. No translation available.
    BC022489 mRNA. Translation: AAH22489.1. Different initiation.
    AJ250902 Genomic DNA. Translation: CAB65728.1.
    CCDSiCCDS43393.1. [P51161-2]
    CCDS4349.1. [P51161-1]
    PIRiS63983.
    RefSeqiNP_001035532.1. NM_001040442.1. [P51161-2]
    NP_001124430.1. NM_001130958.1. [P51161-2]
    NP_001436.1. NM_001445.2. [P51161-1]
    XP_006714891.1. XM_006714828.1. [P51161-2]
    XP_006714893.1. XM_006714830.1. [P51161-1]
    UniGeneiHs.519719.

    Genome annotation databases

    EnsembliENST00000393980; ENSP00000377549; ENSG00000170231. [P51161-2]
    ENST00000402432; ENSP00000385433; ENSG00000170231. [P51161-1]
    GeneIDi2172.
    KEGGihsa:2172.
    UCSCiuc003lxx.1. human. [P51161-2]
    uc003lya.1. human. [P51161-1]

    Polymorphism databases

    DMDMi1708457.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19869 mRNA. Translation: AAB82751.1 .
    X90908 mRNA. Translation: CAA62415.1 .
    DQ132786 mRNA. Translation: ABA12611.1 .
    AC008609 Genomic DNA. No translation available.
    AC112191 Genomic DNA. No translation available.
    BC022489 mRNA. Translation: AAH22489.1 . Different initiation.
    AJ250902 Genomic DNA. Translation: CAB65728.1 .
    CCDSi CCDS43393.1. [P51161-2 ]
    CCDS4349.1. [P51161-1 ]
    PIRi S63983.
    RefSeqi NP_001035532.1. NM_001040442.1. [P51161-2 ]
    NP_001124430.1. NM_001130958.1. [P51161-2 ]
    NP_001436.1. NM_001445.2. [P51161-1 ]
    XP_006714891.1. XM_006714828.1. [P51161-2 ]
    XP_006714893.1. XM_006714830.1. [P51161-1 ]
    UniGenei Hs.519719.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1O1U NMR - A 2-128 [» ]
    1O1V NMR - A 2-128 [» ]
    2MM3 NMR - A 2-128 [» ]
    ProteinModelPortali P51161.
    SMRi P51161. Positions 2-128.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000377549.

    PTM databases

    PhosphoSitei P51161.

    Polymorphism databases

    DMDMi 1708457.

    Proteomic databases

    MaxQBi P51161.
    PaxDbi P51161.
    PRIDEi P51161.

    Protocols and materials databases

    DNASUi 2172.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393980 ; ENSP00000377549 ; ENSG00000170231 . [P51161-2 ]
    ENST00000402432 ; ENSP00000385433 ; ENSG00000170231 . [P51161-1 ]
    GeneIDi 2172.
    KEGGi hsa:2172.
    UCSCi uc003lxx.1. human. [P51161-2 ]
    uc003lya.1. human. [P51161-1 ]

    Organism-specific databases

    CTDi 2172.
    GeneCardsi GC05P159573.
    HGNCi HGNC:3561. FABP6.
    HPAi CAB024713.
    HPA012601.
    MIMi 600422. gene.
    neXtProti NX_P51161.
    PharmGKBi PA27962.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG275686.
    HOGENOMi HOG000004830.
    HOVERGENi HBG005633.
    InParanoidi P51161.
    KOi K08755.
    OMAi FKATVKM.
    OrthoDBi EOG7HB5C9.
    PhylomeDBi P51161.
    TreeFami TF330348.

    Enzyme and pathway databases

    Reactomei REACT_11042. Recycling of bile acids and salts.

    Miscellaneous databases

    ChiTaRSi FABP6. human.
    EvolutionaryTracei P51161.
    GeneWikii FABP6.
    GenomeRNAii 2172.
    NextBioi 8771.
    PROi P51161.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51161.
    Bgeei P51161.
    CleanExi HS_FABP6.
    Genevestigatori P51161.

    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. "Cloning and chromosomal localization of the human ileal lipid-binding protein."
      Oelkers P., Dawson P.A.
      Biochim. Biophys. Acta 1257:199-202(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Ileum.
    2. "Molecular cloning, expression, and characterization of a human intestinal 15-kDa protein."
      Fujita M., Fujii H., Kanda T., Sato E., Hatakeyama K., Ono T.
      Eur. J. Biochem. 233:406-413(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Ileum.
    3. "A novel variant of ileal bile acid binding protein is up-regulated through nuclear factor-kappaB activation in colorectal adenocarcinoma."
      Fang C., Dean J., Smith J.W.
      Cancer Res. 67:9039-9046(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE PROMOTER USAGE, INDUCTION, TISSUE SPECIFICITY.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      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: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS HIS-33 AND TYR-55.
      Tissue: Brain.
    6. "The human ileal bile acid binding protein gene: promoter sequence and effects of CDX2 on expression."
      Barley N.F., Shaw-Smith C.J., Chakravarty P., Howard A., Legon S., Walters J.R.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19 (ISOFORM 1).
    7. "Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures."
      Kurz M., Brachvogel V., Matter H., Stengelin S., Thuering H., Kramer W.
      Proteins 50:312-328(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR IN COMPLEX WITH BILE ACID.

    Entry informationi

    Entry nameiFABP6_HUMAN
    AccessioniPrimary (citable) accession number: P51161
    Secondary accession number(s): Q07DR7, Q8TBI3, Q9UGI7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 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 5
      Human chromosome 5: 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