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P07148 (FABPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid-binding protein, liver
Alternative name(s):
Fatty acid-binding protein 1
Liver-type fatty acid-binding protein
Short name=L-FABP
Gene names
Name:FABP1
Synonyms:FABPL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport.

Subcellular location

Cytoplasm.

Domain

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

Sequence similarities

Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandLipid-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to hydrogen peroxide

Inferred from direct assay PubMed 16175609. Source: UniProtKB

cellular response to hypoxia

Inferred from direct assay PubMed 16175609. Source: UniProtKB

intestinal absorption

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 16175609. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 16175609. Source: UniProtKB

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of fatty acid beta-oxidation

Inferred from electronic annotation. Source: Ensembl

positive regulation of hydrolase activity

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentapical cortex

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

peroxisomal matrix

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionantioxidant activity

Inferred from direct assay PubMed 16175609. Source: UniProtKB

bile acid binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from electronic annotation. Source: Ensembl

drug binding

Inferred from electronic annotation. Source: Ensembl

fatty acid binding

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid transporter activity

Inferred from electronic annotation. Source: Ensembl

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 127127Fatty acid-binding protein, liver
PRO_0000067334

Amino acid modifications

Modified residue11N-acetylmethionine
Modified residue311N6-succinyllysine By similarity
Modified residue361N6-succinyllysine By similarity
Modified residue461N6-succinyllysine By similarity
Modified residue571N6-succinyllysine By similarity
Modified residue781N6-succinyllysine By similarity
Modified residue901N6-succinyllysine By similarity
Modified residue1211N6-succinyllysine By similarity

Natural variations

Natural variant541A → T.
Corresponds to variant rs1801273 [ dbSNP | Ensembl ].
VAR_014662
Natural variant941T → A. Ref.2
Corresponds to variant rs2241883 [ dbSNP | Ensembl ].
VAR_022093

Secondary structure

............................ 127
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07148 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 065DCEFB08DAB6B6

FASTA12714,208
        10         20         30         40         50         60 
MSFSGKYQLQ SQENFEAFMK AIGLPEELIQ KGKDIKGVSE IVQNGKHFKF TITAGSKVIQ 

        70         80         90        100        110        120 
NEFTVGEECE LETMTGEKVK TVVQLEGDNK LVTTFKNIKS VTELNGDIIT NTMTLGDIVF 


KRISKRI 

« Hide

References

« Hide 'large scale' references
[1]"Human liver fatty acid binding protein cDNA and amino acid sequence. Functional and evolutionary implications."
Chan L., Wei C.-F., Li W.-H., Yang C.-Y., Ratner P., Pownall H., Gotto A.M. Jr., Smith L.C.
J. Biol. Chem. 260:2629-2632(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human liver fatty acid binding protein. Isolation of a full length cDNA and comparative sequence analyses of orthologous and paralogous proteins."
Lowe J.B., Boguski M.S., Sweetser D.A., Elshourbagy N.A., Taylor J.M., Gordon J.I.
J. Biol. Chem. 260:3413-3417(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-94.
[3]"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: Colon, Kidney and Stomach.
[4]"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].
[5]"Rapid data collection for protein structure determination by NMR spectroscopy."
Xu Y., Long D., Yang D.
J. Am. Chem. Soc. 129:7722-7723(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[6]"Crystal structure of human FABP1."
Structural genomics consortium (SGC)
Submitted (DEC-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10617 mRNA. Translation: AAA52419.1.
M10050 mRNA. Translation: AAA52418.1.
BC032801 mRNA. Translation: AAH32801.1.
PIRFZHUL. A22289.
RefSeqNP_001434.1. NM_001443.2.
UniGeneHs.380135.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F73X-ray2.50A/B/C/D/E/F/G/H1-127[»]
2L67NMR-A2-127[»]
2L68NMR-A2-127[»]
2LKKNMR-A2-127[»]
2PY1NMR-A1-127[»]
3B2HX-ray1.55A2-127[»]
3B2IX-ray1.86A2-127[»]
3B2JX-ray2.00A2-127[»]
3B2KX-ray1.73A2-127[»]
3B2LX-ray2.25A2-127[»]
3STKX-ray1.55A2-127[»]
3STMX-ray2.22X2-127[»]
3STNX-ray2.60A2-127[»]
3VG2X-ray2.40A2-127[»]
3VG3X-ray2.22A2-127[»]
3VG4X-ray2.50A2-127[»]
3VG5X-ray2.00A2-127[»]
3VG6X-ray2.22A2-127[»]
3VG7X-ray1.44A2-127[»]
ProteinModelPortalP07148.
SMRP07148. Positions 2-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108466. 4 interactions.
IntActP07148. 1 interaction.
MINTMINT-5002397.
STRING9606.ENSP00000295834.

Chemistry

BindingDBP07148.
ChEMBLCHEMBL5421.

PTM databases

PhosphoSiteP07148.

Polymorphism databases

DMDM119808.

2D gel databases

SWISS-2DPAGEP07148.

Proteomic databases

PaxDbP07148.
PRIDEP07148.

Protocols and materials databases

DNASU2168.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295834; ENSP00000295834; ENSG00000163586.
GeneID2168.
KEGGhsa:2168.
UCSCuc002sst.2. human.

Organism-specific databases

CTD2168.
GeneCardsGC02M088422.
HGNCHGNC:3555. FABP1.
HPACAB002305.
HPA028275.
MIM134650. gene.
neXtProtNX_P07148.
PharmGKBPA27956.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317209.
HOVERGENHBG005633.
InParanoidP07148.
KOK08750.
OMAQNEFTLG.
PhylomeDBP07148.
TreeFamTF330348.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP07148.
BgeeP07148.
CleanExHS_FABP1.
GenevestigatorP07148.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFABP1. human.
EvolutionaryTraceP07148.
GeneWikiFABP1.
GenomeRNAi2168.
NextBio8755.
PROP07148.
SOURCESearch...

Entry information

Entry nameFABPL_HUMAN
AccessionPrimary (citable) accession number: P07148
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: March 19, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM