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P07148

- FABPL_HUMAN

UniProt

P07148 - FABPL_HUMAN

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Protein

Fatty acid-binding protein, liver

Gene

FABP1

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

Functioni

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.

GO - Molecular functioni

  1. antioxidant activity Source: UniProtKB
  2. bile acid binding Source: Ensembl
  3. chromatin binding Source: Ensembl
  4. drug binding Source: Ensembl
  5. fatty acid binding Source: Ensembl
  6. long-chain fatty acid transporter activity Source: Ensembl
  7. phospholipid binding Source: Ensembl

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. cellular response to hydrogen peroxide Source: UniProtKB
  3. cellular response to hypoxia Source: UniProtKB
  4. intestinal absorption Source: Ensembl
  5. negative regulation of apoptotic process Source: UniProtKB
  6. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  7. positive regulation of cell proliferation Source: Ensembl
  8. positive regulation of fatty acid beta-oxidation Source: Ensembl
  9. positive regulation of hydrolase activity Source: Ensembl
  10. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3555. FABP1.

Subcellular locationi

GO - Cellular componenti

  1. apical cortex Source: Ensembl
  2. cytosol Source: Ensembl
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. peroxisomal matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27956.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Fatty acid-binding protein, liverPRO_0000067334Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei31 – 311N6-succinyllysineBy similarity
Modified residuei36 – 361N6-succinyllysineBy similarity
Modified residuei46 – 461N6-succinyllysineBy similarity
Modified residuei57 – 571N6-succinyllysineBy similarity
Modified residuei78 – 781N6-succinyllysineBy similarity
Modified residuei90 – 901N6-succinyllysineBy similarity
Modified residuei121 – 1211N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP07148.
PaxDbiP07148.
PRIDEiP07148.

2D gel databases

SWISS-2DPAGEP07148.

PTM databases

PhosphoSiteiP07148.

Expressioni

Gene expression databases

BgeeiP07148.
CleanExiHS_FABP1.
ExpressionAtlasiP07148. baseline and differential.
GenevestigatoriP07148.

Organism-specific databases

HPAiCAB002305.
HPA028275.

Interactioni

Protein-protein interaction databases

BioGridi108466. 4 interactions.
IntActiP07148. 1 interaction.
MINTiMINT-5002397.
STRINGi9606.ENSP00000295834.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Helixi15 – 217Combined sources
Helixi26 – 327Combined sources
Beta strandi38 – 447Combined sources
Beta strandi47 – 548Combined sources
Beta strandi57 – 648Combined sources
Beta strandi67 – 726Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 825Combined sources
Beta strandi84 – 874Combined sources
Beta strandi90 – 956Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi108 – 1158Combined sources
Beta strandi118 – 1269Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07148.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG317209.
HOVERGENiHBG005633.
InParanoidiP07148.
KOiK08750.
OMAiDTITNTM.
PhylomeDBiP07148.
TreeFamiTF330348.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541A → T.
Corresponds to variant rs1801273 [ dbSNP | Ensembl ].
VAR_014662
Natural varianti94 – 941T → A.1 Publication
Corresponds to variant rs2241883 [ dbSNP | Ensembl ].
VAR_022093

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.
UCSCiuc002sst.2. human.

Polymorphism databases

DMDMi119808.

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 .
CCDSi CCDS2001.1.
PIRi A22289. FZHUL.
RefSeqi NP_001434.1. NM_001443.2.
UniGenei Hs.380135.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2F73 X-ray 2.50 A/B/C/D/E/F/G/H 1-127 [» ]
2L67 NMR - A 2-127 [» ]
2L68 NMR - A 2-127 [» ]
2LKK NMR - A 2-127 [» ]
2PY1 NMR - A 1-127 [» ]
3B2H X-ray 1.55 A 2-127 [» ]
3B2I X-ray 1.86 A 2-127 [» ]
3B2J X-ray 2.00 A 2-127 [» ]
3B2K X-ray 1.73 A 2-127 [» ]
3B2L X-ray 2.25 A 2-127 [» ]
3STK X-ray 1.55 A 2-127 [» ]
3STM X-ray 2.22 X 2-127 [» ]
3STN X-ray 2.60 A 2-127 [» ]
3VG2 X-ray 2.40 A 2-127 [» ]
3VG3 X-ray 2.22 A 2-127 [» ]
3VG4 X-ray 2.50 A 2-127 [» ]
3VG5 X-ray 2.00 A 2-127 [» ]
3VG6 X-ray 2.22 A 2-127 [» ]
3VG7 X-ray 1.44 A 2-127 [» ]
ProteinModelPortali P07148.
SMRi P07148. Positions 2-127.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108466. 4 interactions.
IntActi P07148. 1 interaction.
MINTi MINT-5002397.
STRINGi 9606.ENSP00000295834.

Chemistry

BindingDBi P07148.
ChEMBLi CHEMBL5421.

PTM databases

PhosphoSitei P07148.

Polymorphism databases

DMDMi 119808.

2D gel databases

SWISS-2DPAGE P07148.

Proteomic databases

MaxQBi P07148.
PaxDbi P07148.
PRIDEi P07148.

Protocols and materials databases

DNASUi 2168.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295834 ; ENSP00000295834 ; ENSG00000163586 .
GeneIDi 2168.
KEGGi hsa:2168.
UCSCi uc002sst.2. human.

Organism-specific databases

CTDi 2168.
GeneCardsi GC02M088422.
HGNCi HGNC:3555. FABP1.
HPAi CAB002305.
HPA028275.
MIMi 134650. gene.
neXtProti NX_P07148.
PharmGKBi PA27956.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG317209.
HOVERGENi HBG005633.
InParanoidi P07148.
KOi K08750.
OMAi DTITNTM.
PhylomeDBi P07148.
TreeFami TF330348.

Enzyme and pathway databases

Reactomei REACT_116145. PPARA activates gene expression.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Miscellaneous databases

ChiTaRSi FABP1. human.
EvolutionaryTracei P07148.
GeneWikii FABP1.
GenomeRNAii 2168.
NextBioi 8755.
PROi P07148.
SOURCEi Search...

Gene expression databases

Bgeei P07148.
CleanExi HS_FABP1.
ExpressionAtlasi P07148. baseline and differential.
Genevestigatori P07148.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
[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. "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], ACETYLATION AT MET-1.
  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. 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).

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 26, 2014
This is version 146 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

External Data

Dasty 3