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Q01469

- FABP5_HUMAN

UniProt

Q01469 - FABP5_HUMAN

Protein

Fatty acid-binding protein, epidermal

Gene

FABP5

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

    High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091Fatty acidBy similarity

    GO - Molecular functioni

    1. fatty acid binding Source: ProtInc
    2. lipid binding Source: ProtInc
    3. protein binding Source: UniProtKB
    4. transporter activity Source: InterPro

    GO - Biological processi

    1. epidermis development Source: ProtInc
    2. glucose metabolic process Source: Ensembl
    3. glucose transport Source: Ensembl
    4. lipid metabolic process Source: ProtInc
    5. phosphatidylcholine biosynthetic process Source: Ensembl
    6. response to wounding Source: Ensembl

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Protein family/group databases

    TCDBi8.A.33.1.1. the fatty acid binding protein (fabp) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid-binding protein, epidermal
    Alternative name(s):
    Epidermal-type fatty acid-binding protein
    Short name:
    E-FABP
    Fatty acid-binding protein 5
    Psoriasis-associated fatty acid-binding protein homolog
    Short name:
    PA-FABP
    Gene namesi
    Name:FABP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3560. FABP5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27961.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 135134Fatty acid-binding protein, epidermalPRO_0000067377Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei17 – 171N6-acetyllysine1 Publication
    Disulfide bondi120 ↔ 1272 Publications
    Modified residuei131 – 1311Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ01469.
    PaxDbiQ01469.
    PRIDEiQ01469.

    2D gel databases

    SWISS-2DPAGEQ01469.
    UCD-2DPAGEQ01469.

    PTM databases

    PhosphoSiteiQ01469.

    Expressioni

    Tissue specificityi

    Keratinocytes; highly expressed in psoriatic skin.

    Gene expression databases

    BgeeiQ01469.
    CleanExiHS_FABP5.
    GenevestigatoriQ01469.

    Organism-specific databases

    HPAiCAB017831.
    CAB040577.

    Interactioni

    Protein-protein interaction databases

    BioGridi108469. 5 interactions.
    IntActiQ01469. 2 interactions.
    MINTiMINT-3024261.
    STRINGi9606.ENSP00000297258.

    Structurei

    Secondary structure

    1
    135
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 74
    Beta strandi9 – 1810
    Helixi19 – 268
    Helixi30 – 389
    Beta strandi42 – 487
    Beta strandi51 – 577
    Beta strandi62 – 687
    Beta strandi73 – 764
    Beta strandi78 – 803
    Beta strandi82 – 909
    Beta strandi93 – 1008
    Beta strandi103 – 11210
    Beta strandi115 – 1228
    Beta strandi125 – 1339

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B56X-ray2.05A1-135[»]
    1JJJNMR-A1-135[»]
    4AZMX-ray2.75A/B1-135[»]
    4AZRX-ray2.95A/B1-135[»]
    4LKPX-ray1.67A1-135[»]
    4LKTX-ray2.57A/B/C/D1-135[»]
    ProteinModelPortaliQ01469.
    SMRiQ01469. Positions 2-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01469.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 1313Fatty acid bindingBy similarity

    Domaini

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG309791.
    HOGENOMiHOG000004829.
    HOVERGENiHBG005633.
    InParanoidiQ01469.
    KOiK08754.
    OMAiVECDMNG.
    OrthoDBiEOG7NW6BZ.
    PhylomeDBiQ01469.
    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.

    Q01469-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK    50
    NLTIKTESTL KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW 100
    DGKESTITRK LKDGKLVVEC VMNNVTCTRI YEKVE 135
    Length:135
    Mass (Da):15,164
    Last modified:January 23, 2007 - v3
    Checksum:i77D38F8806143D63
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94856 mRNA. Translation: AAA58467.1.
    BT007449 mRNA. Translation: AAP36117.1.
    AK311856 mRNA. Translation: BAG34797.1.
    CH471068 Genomic DNA. Translation: EAW87088.1.
    BC019385 mRNA. Translation: AAH19385.1.
    BC070303 mRNA. Translation: AAH70303.1.
    CCDSiCCDS6228.1.
    PIRiI56326.
    RefSeqiNP_001435.1. NM_001444.2.
    UniGeneiHs.408061.

    Genome annotation databases

    EnsembliENST00000297258; ENSP00000297258; ENSG00000164687.
    GeneIDi2171.
    KEGGihsa:2171.
    UCSCiuc003yca.2. human.

    Polymorphism databases

    DMDMi232081.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94856 mRNA. Translation: AAA58467.1 .
    BT007449 mRNA. Translation: AAP36117.1 .
    AK311856 mRNA. Translation: BAG34797.1 .
    CH471068 Genomic DNA. Translation: EAW87088.1 .
    BC019385 mRNA. Translation: AAH19385.1 .
    BC070303 mRNA. Translation: AAH70303.1 .
    CCDSi CCDS6228.1.
    PIRi I56326.
    RefSeqi NP_001435.1. NM_001444.2.
    UniGenei Hs.408061.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B56 X-ray 2.05 A 1-135 [» ]
    1JJJ NMR - A 1-135 [» ]
    4AZM X-ray 2.75 A/B 1-135 [» ]
    4AZR X-ray 2.95 A/B 1-135 [» ]
    4LKP X-ray 1.67 A 1-135 [» ]
    4LKT X-ray 2.57 A/B/C/D 1-135 [» ]
    ProteinModelPortali Q01469.
    SMRi Q01469. Positions 2-135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108469. 5 interactions.
    IntActi Q01469. 2 interactions.
    MINTi MINT-3024261.
    STRINGi 9606.ENSP00000297258.

    Chemistry

    BindingDBi Q01469.
    ChEMBLi CHEMBL3674.

    Protein family/group databases

    TCDBi 8.A.33.1.1. the fatty acid binding protein (fabp) family.

    PTM databases

    PhosphoSitei Q01469.

    Polymorphism databases

    DMDMi 232081.

    2D gel databases

    SWISS-2DPAGE Q01469.
    UCD-2DPAGE Q01469.

    Proteomic databases

    MaxQBi Q01469.
    PaxDbi Q01469.
    PRIDEi Q01469.

    Protocols and materials databases

    DNASUi 2171.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297258 ; ENSP00000297258 ; ENSG00000164687 .
    GeneIDi 2171.
    KEGGi hsa:2171.
    UCSCi uc003yca.2. human.

    Organism-specific databases

    CTDi 2171.
    GeneCardsi GC08P082242.
    HGNCi HGNC:3560. FABP5.
    HPAi CAB017831.
    CAB040577.
    MIMi 605168. gene.
    neXtProti NX_Q01469.
    PharmGKBi PA27961.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309791.
    HOGENOMi HOG000004829.
    HOVERGENi HBG005633.
    InParanoidi Q01469.
    KOi K08754.
    OMAi VECDMNG.
    OrthoDBi EOG7NW6BZ.
    PhylomeDBi Q01469.
    TreeFami TF316894.

    Miscellaneous databases

    EvolutionaryTracei Q01469.
    GeneWikii FABP5.
    GenomeRNAii 2171.
    NextBioi 8767.
    PROi Q01469.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q01469.
    CleanExi HS_FABP5.
    Genevestigatori Q01469.

    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. "Molecular cloning and expression of a novel keratinocyte protein (psoriasis-associated fatty acid-binding protein [PA-FABP]) that is highly up-regulated in psoriatic skin and that shares similarity to fatty acid-binding proteins."
      Madsen P.S., Rasmussen H.H., Leffers H., Honore B., Celis J.E.
      J. Invest. Dermatol. 99:299-305(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Keratinocyte.
    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. "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: Tongue.
    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: Ovary.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2.
    7. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 18-33; 35-50; 62-103 AND 116-129, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    8. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-33; 39-50; 62-71; 83-101 AND 120-129.
      Tissue: Keratinocyte.
    9. "Purification and characterization of the human epidermal fatty acid-binding protein: localization during epidermal cell differentiation in vivo and in vitro."
      Siegenthaler G., Hotz R., Chatellard-Gruaz D., Didierjean L., Hellman U., Saurat J.-H.
      Biochem. J. 302:363-371(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 67-72 AND 104-110, CHARACTERIZATION.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Expression, purification and crystal structure determination of recombinant human epidermal-type fatty acid-binding protein."
      Hohoff C., Borchers T., Rustow B., Spener F., van Tilbeurgh H.
      Biochemistry 38:12229-12239(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FATTY ACID, DISULFIDE BOND.
    17. "Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP)."
      Gutierrez-Gonzalez L.H., Ludwig C., Hohoff C., Rademacher M., Hanhoff T., Rueterjans H., Spener F., Luecke C.
      Biochem. J. 364:725-737(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, DISULFIDE BOND.

    Entry informationi

    Entry nameiFABP5_HUMAN
    AccessioniPrimary (citable) accession number: Q01469
    Secondary accession number(s): B2R4K0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 164 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3