ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P15090


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name FABP4_HUMAN
Primary accession number P15090
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 87)
Name and origin of the protein
Protein name Fatty acid-binding protein, adipocyte
Synonyms A-FABP
AFABP
Fatty acid-binding protein 4
Adipocyte lipid-binding protein
ALBP
Gene name
Name: FABP4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00448a003; PubMed=2481498 [NCBI, ExPASy, EBI, Israel, Japan]
Baxa C.A., Sha R.S., Buelt M.K., Smith A.J., Matarese V., Chinander L.L., Boundy K.L., Bernlohr D.A.;
"Human adipocyte lipid-binding protein: purification of the protein and cloning of its complementary DNA.";
Biochemistry 28:8683-8690(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
VARIANT [LARGE SCALE ANALYSIS] ASP-23.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR.
DOI=10.1016/j.bmcl.2004.06.057; PubMed=15357969 [NCBI, ExPASy, EBI, Israel, Japan]
Lehmann F., Haile S., Axen E., Medina C., Uppenberg J., Svensson S., Lundbaeck T., Rondahl L., Barf T.;
"Discovery of inhibitors of human adipocyte fatty acid-binding protein, a potential type 2 diabetes target.";
Bioorg. Med. Chem. Lett. 14:4445-4448(2004).
[6]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID, SUBUNIT, PARTIAL PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
DOI=10.1107/S1744309106038656; PubMed=17077479 [NCBI, ExPASy, EBI, Israel, Japan]
Marr E., Tardie M., Carty M., Brown Phillips T., Wang I.-K., Soeller W., Qiu X., Karam G.;
"Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2).";
Acta Crystallogr. F 62:1058-1060(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J02874; AAA51689.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006809; AAP35455.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003672; AAH03672.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A33363; FZHUF.
RefSeq NP_001433.1; -.
UniGene Hs.391561
3D structure databases
PDB
1TOU; X-ray; 2.00 A; A=1-132.[ExPASy / RCSB / EBI]
1TOW; X-ray; 2.00 A; A=1-132.[ExPASy / RCSB / EBI]
2HNX; X-ray; 1.50 A; A=1-132.[ExPASy / RCSB / EBI]
2NNQ; X-ray; 1.80 A; A=2-132.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1TOU; -.
1TOW; -.
2HNX; -.
2NNQ; -.
ModBase P15090.
Protein-protein interaction databases
IntAct P15090; -.
PTM databases
PhosphoSite P15090; -.
Enzyme and pathway databases
Reactome REACT_602; Lipid and lipoprotein metabolism.
Organism-specific databases
H-InvDB HIX0007617; -.
HGNC HGNC:3559; FABP4.
GenAtlas FABP4.
HPA HPA002188; -.
MIM 600434; gene. [NCBI / EBI]
PharmGKB PA27960; -.
GeneCards P15090.
Gene expression databases
ArrayExpress P15090; -.
CleanEx HS_FABP4; -.
GermOnline ENSG00000170323; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from UniProtKB).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0005504; Molecular function: fatty acid binding (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR012674; Calycin.
IPR000463; Fatty_acid_bd.
IPR000566; Lipocln_cytFABP.
Graphical view of domain structure.
Gene3D G3DSA:2.40.128.20; Calycin; 1.
PANTHER PTHR11955; Fatty_acid_bd; 1.
Pfam PF00061; Lipocalin; 1.
Pfam graphical view of domain structure.
PRINTS PR00178; FATTYACIDBP.
PROSITE PS00214; FABP; 1.
BLOCKS P15090.
Proteomic databases
PeptideAtlas P15090; -.
Genome annotation databases
Ensembl ENSG00000170323; Homo sapiens. [Contig view]
GeneID 2167; -.
KEGG hsa:2167; -.
Phylogenomic databases
HOGENOM P15090; -.
HOVERGEN P15090; -.
Other
SOURCE FABP4; Homo sapiens.
ProtoNet P15090.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Lipid-binding; Nucleus; Phosphoprotein; Polymorphism; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   132  131     Fatty acid-binding protein, adipocyte. PRO_0000067366
REGION   127   129  3     Fatty acid binding. 
MOTIF   22    32  11     Nuclear localization signal (By similarity). 
MOD_RES   20    20        Phosphotyrosine; by Tyr-kinases (By similarity). 
VARIANT   23    23  1     E -> D (in a breast cancer sample; somatic mutation). VAR_036320 [3D]
STRAND   7    16  10      
HELIX   17    24  8      
HELIX   28    36  9      
STRAND   40    46  7      
STRAND   49    55  7      
STRAND   61    66  6      
STRAND   71    74  4      
STRAND   80    88  9      
STRAND   91    98  8      
STRAND   101   110  10      
STRAND   113   120  8      
STRAND   123   131  9      
Sequence information
Length: 132 AA [This is the length of the unprocessed precursor] Molecular weight: 14719 Da [This is the MW of the unprocessed precursor] CRC64: 819D788FF4BF7235 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI TIKSESTFKN 

        70         80         90        100        110        120 
TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG KSTTIKRKRE DDKLVVECVM 

       130 
KGVTSTRVYE RA 

P15090 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!