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P05413

- FABPH_HUMAN

UniProt

P05413 - FABPH_HUMAN

Protein

Fatty acid-binding protein, heart

Gene

FABP3

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

    FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei127 – 1271Fatty acid
    Binding sitei129 – 1291Fatty acid

    GO - Molecular functioni

    1. cytoskeletal protein binding Source: UniProtKB
    2. icosatetraenoic acid binding Source: Ensembl
    3. long-chain fatty acid binding Source: BHF-UCL
    4. long-chain fatty acid transporter activity Source: Ensembl
    5. oleic acid binding Source: BHF-UCL
    6. protein binding Source: IntAct

    GO - Biological processi

    1. cholesterol homeostasis Source: BHF-UCL
    2. fatty acid metabolic process Source: Ensembl
    3. long-chain fatty acid import Source: BHF-UCL
    4. negative regulation of cell proliferation Source: ProtInc
    5. phospholipid homeostasis Source: BHF-UCL
    6. positive regulation of phospholipid biosynthetic process Source: BHF-UCL
    7. regulation of fatty acid oxidation Source: BHF-UCL
    8. response to drug Source: Ensembl
    9. response to fatty acid Source: Ensembl
    10. response to insulin Source: Ensembl

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid-binding protein, heart
    Alternative name(s):
    Fatty acid-binding protein 3
    Heart-type fatty acid-binding protein
    Short name:
    H-FABP
    Mammary-derived growth inhibitor
    Short name:
    MDGI
    Muscle fatty acid-binding protein
    Short name:
    M-FABP
    Gene namesi
    Name:FABP3
    Synonyms:FABP11, MDGI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3557. FABP3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: BHF-UCL
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. sarcoplasm Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27958.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 133132Fatty acid-binding protein, heartPRO_0000067321Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylvaline2 Publications
    Modified residuei20 – 201Phosphotyrosine; by Tyr-kinasesBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP05413.
    PaxDbiP05413.
    PeptideAtlasiP05413.
    PRIDEiP05413.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00219684.
    UCD-2DPAGEP05413.

    PTM databases

    PhosphoSiteiP05413.

    Expressioni

    Gene expression databases

    BgeeiP05413.
    CleanExiHS_FABP3.
    GenevestigatoriP05413.

    Organism-specific databases

    HPAiCAB017830.
    HPA055754.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ITGB1P055562EBI-704216,EBI-703066

    Protein-protein interaction databases

    BioGridi108468. 4 interactions.
    IntActiP05413. 11 interactions.
    MINTiMINT-1432076.
    STRINGi9606.ENSP00000362817.

    Structurei

    Secondary structure

    1
    133
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53
    Beta strandi7 – 1610
    Helixi17 – 248
    Helixi28 – 347
    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
    1G5WNMR-A2-133[»]
    1HMRX-ray1.40A2-133[»]
    1HMSX-ray1.40A2-133[»]
    1HMTX-ray1.40A2-133[»]
    2HMBX-ray2.10A2-133[»]
    3RSWX-ray2.60A/B1-133[»]
    3WBGX-ray2.15A/B/C/D1-133[»]
    ProteinModelPortaliP05413.
    SMRiP05413. Positions 2-132.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05413.

    Family & Domainsi

    Domaini

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG281572.
    HOGENOMiHOG000004829.
    HOVERGENiHBG005633.
    InParanoidiP05413.
    KOiK08752.
    OMAiGSVVCTR.
    OrthoDBiEOG7NW6BZ.
    PhylomeDBiP05413.
    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.

    P05413-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDAFLGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDIL    50
    TLKTHSTFKN TEISFKLGVE FDETTADDRK VKSIVTLDGG KLVHLQKWDG 100
    QETTLVRELI DGKLILTLTH GTAVCTRTYE KEA 133
    Length:133
    Mass (Da):14,858
    Last modified:January 23, 2007 - v4
    Checksum:i5FD396B1BE538A3C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21V → A in CAA71305. 1 PublicationCurated
    Sequence conflicti105 – 1051L → K AA sequence (PubMed:3421901)Curated
    Sequence conflicti125 – 1251C → S AA sequence (PubMed:3421901)Curated
    Sequence conflicti130 – 1301E → Q AA sequence (PubMed:2266954)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti53 – 531K → R.
    Corresponds to variant rs2228194 [ dbSNP | Ensembl ].
    VAR_061165

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56549 mRNA. Translation: CAA39889.1.
    Y10255 mRNA. Translation: CAA71305.1.
    U57623 Genomic DNA. Translation: AAB02555.1.
    AK314122 mRNA. Translation: BAG36813.1.
    U17081 Genomic DNA. Translation: AAC99800.1.
    S67314 mRNA. Translation: AAB29294.1.
    BT006727 mRNA. Translation: AAP35373.1.
    AL451070 Genomic DNA. Translation: CAH71850.1.
    CH471059 Genomic DNA. Translation: EAX07619.1.
    BC007021 mRNA. Translation: AAH07021.1.
    CCDSiCCDS342.1.
    PIRiS15432. FZHUC.
    RefSeqiNP_004093.1. NM_004102.3.
    UniGeneiHs.657242.

    Genome annotation databases

    EnsembliENST00000373713; ENSP00000362817; ENSG00000121769.
    GeneIDi2170.
    KEGGihsa:2170.
    UCSCiuc001bss.1. human.

    Polymorphism databases

    DMDMi119802.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56549 mRNA. Translation: CAA39889.1 .
    Y10255 mRNA. Translation: CAA71305.1 .
    U57623 Genomic DNA. Translation: AAB02555.1 .
    AK314122 mRNA. Translation: BAG36813.1 .
    U17081 Genomic DNA. Translation: AAC99800.1 .
    S67314 mRNA. Translation: AAB29294.1 .
    BT006727 mRNA. Translation: AAP35373.1 .
    AL451070 Genomic DNA. Translation: CAH71850.1 .
    CH471059 Genomic DNA. Translation: EAX07619.1 .
    BC007021 mRNA. Translation: AAH07021.1 .
    CCDSi CCDS342.1.
    PIRi S15432. FZHUC.
    RefSeqi NP_004093.1. NM_004102.3.
    UniGenei Hs.657242.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G5W NMR - A 2-133 [» ]
    1HMR X-ray 1.40 A 2-133 [» ]
    1HMS X-ray 1.40 A 2-133 [» ]
    1HMT X-ray 1.40 A 2-133 [» ]
    2HMB X-ray 2.10 A 2-133 [» ]
    3RSW X-ray 2.60 A/B 1-133 [» ]
    3WBG X-ray 2.15 A/B/C/D 1-133 [» ]
    ProteinModelPortali P05413.
    SMRi P05413. Positions 2-132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108468. 4 interactions.
    IntActi P05413. 11 interactions.
    MINTi MINT-1432076.
    STRINGi 9606.ENSP00000362817.

    Chemistry

    BindingDBi P05413.
    ChEMBLi CHEMBL3344.

    PTM databases

    PhosphoSitei P05413.

    Polymorphism databases

    DMDMi 119802.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00219684.
    UCD-2DPAGE P05413.

    Proteomic databases

    MaxQBi P05413.
    PaxDbi P05413.
    PeptideAtlasi P05413.
    PRIDEi P05413.

    Protocols and materials databases

    DNASUi 2170.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373713 ; ENSP00000362817 ; ENSG00000121769 .
    GeneIDi 2170.
    KEGGi hsa:2170.
    UCSCi uc001bss.1. human.

    Organism-specific databases

    CTDi 2170.
    GeneCardsi GC01M031838.
    HGNCi HGNC:3557. FABP3.
    HPAi CAB017830.
    HPA055754.
    MIMi 134651. gene.
    neXtProti NX_P05413.
    PharmGKBi PA27958.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG281572.
    HOGENOMi HOG000004829.
    HOVERGENi HBG005633.
    InParanoidi P05413.
    KOi K08752.
    OMAi GSVVCTR.
    OrthoDBi EOG7NW6BZ.
    PhylomeDBi P05413.
    TreeFami TF316894.

    Miscellaneous databases

    ChiTaRSi FABP3. human.
    EvolutionaryTracei P05413.
    GeneWikii Heart-type_fatty_acid_binding_protein.
    GenomeRNAii 2170.
    NextBioi 8763.
    PROi P05413.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05413.
    CleanExi HS_FABP3.
    Genevestigatori P05413.

    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. "Cloning of the cDNA encoding human skeletal-muscle fatty-acid-binding protein, its peptide sequence and chromosomal localization."
      Peeter R.A., Veerkamp J.H., Kanda T., Ono T., Geurts van Kessel A.
      Biochem. J. 276:203-207(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skeletal muscle.
    2. "Molecular cloning of human mammary-derived growth inhibitor (MDGI) reveals that its expression is associated with breast differentiation, but not with cancer progression."
      Hu Y.F., Ao X., Russo I.H., Russo J.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary gland.
    3. "Genomic organization and complete nucleotide sequence of the human cardiac fatty acid binding protein gene (FABP3), and identification of a closely related genomic sequence."
      Wu X., Arlt M., Goodfellow P.J., Rottman J.N.
      Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Hippocampus.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Liver.
    9. "Characterization and amino acid sequence of a fatty acid-binding protein from human heart."
      Offner G.D., Brecher P., Sawlivich W.B., Costello C.E., Troxler R.F.
      Biochem. J. 252:191-198(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-133.
    10. "Revision of the amino acid sequence of human heart fatty acid-binding protein."
      Boerchers T., Hoejrup P., Nielsen S.U., Roepstorff P., Spener F., Knudsen J.
      Mol. Cell. Biochem. 98:127-133(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-133, SEQUENCE REVISION.
    11. "Localization of the gene for human heart fatty acid binding protein to chromosome 1p32-1p33."
      Troxler R.F., Offner G.D., Jiang J.W., Wu B.L., Skare J.C., Milunsky A., Wyandt H.E.
      Hum. Genet. 92:563-566(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-133.
      Tissue: Heart.
    12. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 23-31; 46-53; 67-80; 98-107 AND 114-127, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    13. "The major protein expression profile and two-dimensional protein database of human heart."
      Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.
      Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-39.
      Tissue: Heart.
    14. "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 VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Three-dimensional structure of recombinant human muscle fatty acid-binding protein."
      Zanotti G., Scapin G., Spadon P., Veerkamp J.H., Sacchettini J.C.
      J. Biol. Chem. 267:18541-18550(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    16. "Structural studies on human muscle fatty acid binding protein at 1.4-A resolution: binding interactions with three C18 fatty acids."
      Young A.C.M., Scapin G., Kromminga A., Patel S.B., Veerkamp J.H., Sacchettini J.C.
      Structure 2:523-534(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH C18 FATTY ACID.
    17. "Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP)."
      Luecke C., Rademacher M., Zimmerman A.W., van Moerkerk H.T.B., Veerkamp J.H., Rueterjans H.
      Biochem. J. 354:259-266(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiFABPH_HUMAN
    AccessioniPrimary (citable) accession number: P05413
    Secondary accession number(s): B2RAB6, Q5VV93, Q99957
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 of the entry and version 4 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 1
      Human chromosome 1: 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