Q01469 (FABP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

FABP5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	135 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subcellular location	Cytoplasm.
Tissue specificity	Keratinocytes; highly expressed in psoriatic skin.
Domain	Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Sequence similarities	Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm
Ligand	Lipid-binding
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	epidermis development Traceable author statement Ref.1. Source: ProtInc glucose metabolic process Inferred from electronic annotation. Source: Compara glucose transport Inferred from electronic annotation. Source: Compara lipid metabolic process Traceable author statement Ref.9. Source: ProtInc phosphatidylcholine biosynthetic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Traceable author statement PubMed 16130169. Source: UniProtKB
Molecular_function	fatty acid binding Traceable author statement Ref.9. Source: ProtInc transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 135

134

Fatty acid-binding protein, epidermal

PRO_0000067377

Regions

Region

129 – 131

3

Fatty acid binding By similarity

Sites

Binding site

109

1

Fatty acid By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

17

1

N6-acetyllysine Ref.11

Modified residue

131

1

Phosphotyrosine Ref.10

Disulfide bond

120 ↔ 127

Ref.13 Ref.14

Secondary structure

1

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135

Helix Strand Turn

Details...

Helix

4 – 7

4

Beta strand

9 – 15

7

Helix

19 – 26

8

Helix

30 – 38

9

Beta strand

42 – 48

7

Beta strand

51 – 57

7

Beta strand

62 – 68

7

Beta strand

73 – 76

4

Beta strand

78 – 80

3

Beta strand

82 – 90

9

Beta strand

93 – 100

8

Beta strand

103 – 112

10

Beta strand

115 – 122

8

Beta strand

125 – 133

9

Sequences

	Sequence		Length	Mass (Da)
	Q01469 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 77D38F8806143D63	FASTA	135	15,164
	10 20 30 40 50 60 MATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK NLTIKTESTL 70 80 90 100 110 120 KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW DGKESTITRK LKDGKLVVEC 130 VMNNVTCTRI YEKVE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, 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, MASS SPECTROMETRY.
[11]	"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, MASS SPECTROMETRY.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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.
[14]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00007797.

PIR

I56326.

RefSeq

NP_001435.1. NM_001444.2.

UniGene

Hs.408061.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B56	X-ray	2.05	A	1-135	[»]
1JJJ	NMR	-	A	1-135	[»]

ProteinModelPortal

Q01469.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q01469. 1 interaction.

STRING

9606.ENSP00000297258.

Protein family/group databases

TCDB

8.A.33.1.1. fatty acid binding protein (FABP) family.

PTM databases

PhosphoSite

Q01469.

Polymorphism databases

DMDM

232081.

2D gel databases

SWISS-2DPAGE

Q01469.

UCD-2DPAGE

Q01469.

Proteomic databases

PaxDb

Q01469.

PRIDE

Q01469.

Protocols and materials databases

DNASU

2171.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000297258; ENSP00000297258; ENSG00000164687.

GeneID

2171.

KEGG

hsa:2171.

UCSC

uc003yca.2. human.

Organism-specific databases

CTD

2171.

GeneCards

GC08P082242.

HGNC

HGNC:3560. FABP5.

HPA

CAB017831.
CAB040577.

MIM

605168. gene.

neXtProt

NX_Q01469.

PharmGKB

PA27961.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG309791.

HOGENOM

HOG000004829.

HOVERGEN

HBG005633.

InParanoid

Q01469.

KO

K08754.

OMA

KMGSMAK.

OrthoDB

EOG4V1724.

PhylomeDB

Q01469.

Gene expression databases

ArrayExpress

Q01469.

Bgee

Q01469.

CleanEx

HS_FABP5.

Genevestigator

Q01469.

GermOnline

ENSG00000164687. Homo sapiens.
ENSG00000166899. Homo sapiens.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR00178. FATTYACIDBP.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00214. FABP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q01469.

ChEMBL

CHEMBL3674.

EvolutionaryTrace

Q01469.

GenomeRNAi

2171.

NextBio

8767.

SOURCE

Search...

Entry information

Entry name

FABP5_HUMAN

Accession

Primary (citable) accession number: Q01469
Secondary accession number(s): B2R4K0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 149 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.