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Protein

Fatty acid-binding protein, epidermal

Gene

FABP5

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

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. 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
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_267785. Signaling by Retinoic Acid.

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 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3560. FABP5.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleoplasm Source: Reactome
Complete GO annotation...

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.
ExpressionAtlasiQ01469. baseline.
GenevestigatoriQ01469.

Organism-specific databases

HPAiCAB017831.
CAB040577.
HPA051895.

Interactioni

Protein-protein interaction databases

BioGridi108469. 8 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 – 74Combined sources
Beta strandi9 – 1810Combined sources
Helixi19 – 268Combined sources
Helixi30 – 389Combined sources
Beta strandi42 – 487Combined sources
Beta strandi51 – 577Combined sources
Beta strandi62 – 687Combined sources
Beta strandi73 – 764Combined sources
Beta strandi78 – 803Combined sources
Beta strandi82 – 909Combined sources
Beta strandi93 – 1008Combined sources
Beta strandi103 – 11210Combined sources
Beta strandi115 – 1228Combined sources
Beta strandi125 – 1339Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118898.
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

        10         20         30         40         50
MATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK
60 70 80 90 100
NLTIKTESTL KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW
110 120 130
DGKESTITRK LKDGKLVVEC VMNNVTCTRI YEKVE
Length:135
Mass (Da):15,164
Last modified:January 23, 2007 - v3
Checksum:i77D38F8806143D63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi108469. 8 interactions.
IntActiQ01469. 2 interactions.
MINTiMINT-3024261.
STRINGi9606.ENSP00000297258.

Chemistry

BindingDBiQ01469.
ChEMBLiCHEMBL3674.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ01469.

Polymorphism databases

DMDMi232081.

2D gel databases

SWISS-2DPAGEQ01469.
UCD-2DPAGEQ01469.

Proteomic databases

MaxQBiQ01469.
PaxDbiQ01469.
PRIDEiQ01469.

Protocols and materials databases

DNASUi2171.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2171.
GeneCardsiGC08P082242.
HGNCiHGNC:3560. FABP5.
HPAiCAB017831.
CAB040577.
HPA051895.
MIMi605168. gene.
neXtProtiNX_Q01469.
PharmGKBiPA27961.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG309791.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiQ01469.
KOiK08754.
OMAiVECDMNG.
OrthoDBiEOG7NW6BZ.
PhylomeDBiQ01469.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiREACT_267785. Signaling by Retinoic Acid.

Miscellaneous databases

EvolutionaryTraceiQ01469.
GeneWikiiFABP5.
GenomeRNAii2171.
NextBioi8767.
PROiQ01469.
SOURCEiSearch...

Gene expression databases

BgeeiQ01469.
CleanExiHS_FABP5.
ExpressionAtlasiQ01469. baseline.
GenevestigatoriQ01469.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1991) [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 (APR-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(2003) [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(2003) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (NOV-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(1991) [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(1993) [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(2004) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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(2008) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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(1998) [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(2001) [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: April 1, 2015
This is version 169 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.