SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q01469

- FABP5_HUMAN

UniProt

Q01469 - FABP5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 acid By 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
Complete GO annotation...

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
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 – 11Removed1 Publication
Chaini2 – 135134Fatty acid-binding protein, epidermal
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ01469.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1313Fatty acid binding By 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

« 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(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: July 9, 2014
This is version 163 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