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Protein

Fatty acid-binding protein, liver

Gene

FABP1

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

Functioni

Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (PubMed:25732850). Binds cholesterol (PubMed:25732850). 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 (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163586-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Chemistry databases

SwissLipidsiSLP:000001516.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:FABP1
Synonyms:FABPL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3555. FABP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi2168.
OpenTargetsiENSG00000163586.
PharmGKBiPA27956.

Chemistry databases

ChEMBLiCHEMBL5421.
DrugBankiDB02659. Cholic Acid.
DB04224. Oleic Acid.

Polymorphism and mutation databases

BioMutaiFABP1.
DMDMi119808.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000673341 – 127Fatty acid-binding protein, liverAdd BLAST127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei11PhosphoserineCombined sources1
Modified residuei31N6-succinyllysineBy similarity1
Modified residuei36N6-succinyllysineBy similarity1
Modified residuei39PhosphoserineBy similarity1
Modified residuei46N6-succinyllysineBy similarity1
Modified residuei51PhosphothreonineCombined sources1
Modified residuei56PhosphoserineCombined sources1
Modified residuei57N6-succinyllysineBy similarity1
Modified residuei78N6-succinyllysineBy similarity1
Modified residuei90N6-succinyllysineBy similarity1
Modified residuei100PhosphoserineBy similarity1
Modified residuei121N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP07148.
PeptideAtlasiP07148.
PRIDEiP07148.

2D gel databases

SWISS-2DPAGEP07148.

PTM databases

iPTMnetiP07148.
PhosphoSitePlusiP07148.

Expressioni

Gene expression databases

BgeeiENSG00000163586.
CleanExiHS_FABP1.
ExpressionAtlasiP07148. baseline and differential.
GenevisibleiP07148. HS.

Organism-specific databases

HPAiCAB002305.
HPA028275.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
FLNAP21333-23EBI-2115989,EBI-9641086

Protein-protein interaction databases

BioGridi108466. 7 interactors.
IntActiP07148. 2 interactors.
MINTiMINT-5002397.
STRINGi9606.ENSP00000295834.

Chemistry databases

BindingDBiP07148.

Structurei

Secondary structure

1127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Helixi15 – 21Combined sources7
Helixi26 – 32Combined sources7
Beta strandi38 – 44Combined sources7
Beta strandi47 – 54Combined sources8
Beta strandi57 – 64Combined sources8
Beta strandi67 – 72Combined sources6
Beta strandi74 – 76Combined sources3
Beta strandi78 – 82Combined sources5
Beta strandi84 – 87Combined sources4
Beta strandi90 – 95Combined sources6
Beta strandi98 – 105Combined sources8
Beta strandi108 – 115Combined sources8
Beta strandi118 – 126Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP07148.
SMRiP07148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07148.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00390000012034.
HOVERGENiHBG005633.
InParanoidiP07148.
KOiK08750.
OMAiFTLGEEC.
OrthoDBiEOG091G16BV.
PhylomeDBiP07148.
TreeFamiTF330348.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07148-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFSGKYQLQ SQENFEAFMK AIGLPEELIQ KGKDIKGVSE IVQNGKHFKF
60 70 80 90 100
TITAGSKVIQ NEFTVGEECE LETMTGEKVK TVVQLEGDNK LVTTFKNIKS
110 120
VTELNGDIIT NTMTLGDIVF KRISKRI
Length:127
Mass (Da):14,208
Last modified:April 1, 1988 - v1
Checksum:i065DCEFB08DAB6B6
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01466254A → T.Corresponds to variant rs1801273dbSNPEnsembl.1
Natural variantiVAR_02209394T → A Polymorphism; increases the binding for cholesterol; increases high density lipoprotein (HDL)- and low density lipoprotein (LDL)-mediated cholesterol uptake. 1 PublicationCorresponds to variant rs2241883dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10617 mRNA. Translation: AAA52419.1.
M10050 mRNA. Translation: AAA52418.1.
BC032801 mRNA. Translation: AAH32801.1.
CCDSiCCDS2001.1.
PIRiA22289. FZHUL.
RefSeqiNP_001434.1. NM_001443.2.
UniGeneiHs.380135.

Genome annotation databases

EnsembliENST00000295834; ENSP00000295834; ENSG00000163586.
GeneIDi2168.
KEGGihsa:2168.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10617 mRNA. Translation: AAA52419.1.
M10050 mRNA. Translation: AAA52418.1.
BC032801 mRNA. Translation: AAH32801.1.
CCDSiCCDS2001.1.
PIRiA22289. FZHUL.
RefSeqiNP_001434.1. NM_001443.2.
UniGeneiHs.380135.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP07148.
SMRiP07148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108466. 7 interactors.
IntActiP07148. 2 interactors.
MINTiMINT-5002397.
STRINGi9606.ENSP00000295834.

Chemistry databases

BindingDBiP07148.
ChEMBLiCHEMBL5421.
DrugBankiDB02659. Cholic Acid.
DB04224. Oleic Acid.
SwissLipidsiSLP:000001516.

PTM databases

iPTMnetiP07148.
PhosphoSitePlusiP07148.

Polymorphism and mutation databases

BioMutaiFABP1.
DMDMi119808.

2D gel databases

SWISS-2DPAGEP07148.

Proteomic databases

PaxDbiP07148.
PeptideAtlasiP07148.
PRIDEiP07148.

Protocols and materials databases

DNASUi2168.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295834; ENSP00000295834; ENSG00000163586.
GeneIDi2168.
KEGGihsa:2168.

Organism-specific databases

CTDi2168.
DisGeNETi2168.
GeneCardsiFABP1.
HGNCiHGNC:3555. FABP1.
HPAiCAB002305.
HPA028275.
MIMi134650. gene.
neXtProtiNX_P07148.
OpenTargetsiENSG00000163586.
PharmGKBiPA27956.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00390000012034.
HOVERGENiHBG005633.
InParanoidiP07148.
KOiK08750.
OMAiFTLGEEC.
OrthoDBiEOG091G16BV.
PhylomeDBiP07148.
TreeFamiTF330348.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163586-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Miscellaneous databases

ChiTaRSiFABP1. human.
EvolutionaryTraceiP07148.
GeneWikiiFABP1.
GenomeRNAii2168.
PROiP07148.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163586.
CleanExiHS_FABP1.
ExpressionAtlasiP07148. baseline and differential.
GenevisibleiP07148. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABPL_HUMAN
AccessioniPrimary (citable) accession number: P07148
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 2, 2016
This is version 166 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.