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P15090

- FABP4_HUMAN

UniProt

P15090 - FABP4_HUMAN

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Protein

Fatty acid-binding protein, adipocyte

Gene
FABP4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus By similarity.

GO - Molecular functioni

  1. fatty acid binding Source: ProtInc
  2. transporter activity Source: InterPro

GO - Biological processi

  1. brown fat cell differentiation Source: Ensembl
  2. cellular response to lithium ion Source: Ensembl
  3. cholesterol homeostasis Source: Ensembl
  4. cytokine production Source: Ensembl
  5. negative regulation of protein kinase activity Source: Ensembl
  6. negative regulation of transcription, DNA-templated Source: Ensembl
  7. positive regulation of inflammatory response Source: Ensembl
  8. small molecule metabolic process Source: Reactome
  9. triglyceride catabolic process Source: Reactome
  10. white fat cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, adipocyte
Alternative name(s):
Adipocyte lipid-binding protein
Short name:
ALBP
Adipocyte-type fatty acid-binding protein
Short name:
A-FABP
Short name:
AFABP
Fatty acid-binding protein 4
Gene namesi
Name:FABP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:3559. FABP4.

Subcellular locationi

Cytoplasm. Nucleus
Note: Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. lipid particle Source: Reactome
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27960.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 132131Fatty acid-binding protein, adipocytePRO_0000067366Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteine1 Publication
Modified residuei20 – 201Phosphotyrosine; by Tyr-kinases By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15090.
PaxDbiP15090.
PeptideAtlasiP15090.
PRIDEiP15090.

2D gel databases

UCD-2DPAGEP15090.

PTM databases

PhosphoSiteiP15090.

Expressioni

Gene expression databases

ArrayExpressiP15090.
BgeeiP15090.
CleanExiHS_FABP4.
GenevestigatoriP15090.

Organism-specific databases

HPAiCAB024961.
HPA002188.

Interactioni

Subunit structurei

Homodimer. Interacts with PPARG By similarity. Monomer.1 Publication

Protein-protein interaction databases

BioGridi108465. 10 interactions.
IntActiP15090. 7 interactions.
MINTiMINT-1398507.
STRINGi9606.ENSP00000256104.

Structurei

Secondary structure

1
132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 54
Beta strandi7 – 1610
Helixi17 – 248
Helixi28 – 369
Beta strandi40 – 467
Beta strandi49 – 557
Beta strandi61 – 655
Beta strandi71 – 744
Beta strandi80 – 889
Beta strandi91 – 988
Beta strandi101 – 11010
Beta strandi113 – 1208
Beta strandi123 – 1319

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TOUX-ray2.00A2-132[»]
1TOWX-ray2.00A2-132[»]
2HNXX-ray1.50A1-132[»]
2NNQX-ray1.80A2-132[»]
3FR2X-ray2.20A2-132[»]
3FR4X-ray2.16A1-132[»]
3FR5X-ray2.20A2-132[»]
3P6CX-ray1.25A1-132[»]
3P6DX-ray1.06A1-132[»]
3P6EX-ray1.08A1-132[»]
3P6FX-ray1.20A1-132[»]
3P6GX-ray1.20A1-132[»]
3P6HX-ray1.15A1-132[»]
3Q6LX-ray1.40A1-132[»]
3RZYX-ray1.08A1-132[»]
ProteinModelPortaliP15090.
SMRiP15090. Positions 1-132.

Miscellaneous databases

EvolutionaryTraceiP15090.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 1293Fatty acid binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi22 – 3211Nuclear localization signal By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG326764.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP15090.
KOiK08753.
OMAiGQEFDEI.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP15090.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15090-1 [UniParc]FASTAAdd to Basket

« Hide

MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI    50
TIKSESTFKN TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG 100
KSTTIKRKRE DDKLVVECVM KGVTSTRVYE RA 132
Length:132
Mass (Da):14,719
Last modified:January 23, 2007 - v3
Checksum:i819D788FF4BF7235
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231E → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_036320

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02874 mRNA. Translation: AAA51689.1.
BT006809 mRNA. Translation: AAP35455.1.
CR456903 mRNA. Translation: CAG33184.1.
CH471068 Genomic DNA. Translation: EAW87092.1.
BC003672 mRNA. Translation: AAH03672.1.
CCDSiCCDS6230.1.
PIRiA33363. FZHUF.
RefSeqiNP_001433.1. NM_001442.2.
UniGeneiHs.391561.

Genome annotation databases

EnsembliENST00000256104; ENSP00000256104; ENSG00000170323.
GeneIDi2167.
KEGGihsa:2167.
UCSCiuc003ycd.2. human.

Polymorphism databases

DMDMi119781.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02874 mRNA. Translation: AAA51689.1 .
BT006809 mRNA. Translation: AAP35455.1 .
CR456903 mRNA. Translation: CAG33184.1 .
CH471068 Genomic DNA. Translation: EAW87092.1 .
BC003672 mRNA. Translation: AAH03672.1 .
CCDSi CCDS6230.1.
PIRi A33363. FZHUF.
RefSeqi NP_001433.1. NM_001442.2.
UniGenei Hs.391561.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TOU X-ray 2.00 A 2-132 [» ]
1TOW X-ray 2.00 A 2-132 [» ]
2HNX X-ray 1.50 A 1-132 [» ]
2NNQ X-ray 1.80 A 2-132 [» ]
3FR2 X-ray 2.20 A 2-132 [» ]
3FR4 X-ray 2.16 A 1-132 [» ]
3FR5 X-ray 2.20 A 2-132 [» ]
3P6C X-ray 1.25 A 1-132 [» ]
3P6D X-ray 1.06 A 1-132 [» ]
3P6E X-ray 1.08 A 1-132 [» ]
3P6F X-ray 1.20 A 1-132 [» ]
3P6G X-ray 1.20 A 1-132 [» ]
3P6H X-ray 1.15 A 1-132 [» ]
3Q6L X-ray 1.40 A 1-132 [» ]
3RZY X-ray 1.08 A 1-132 [» ]
ProteinModelPortali P15090.
SMRi P15090. Positions 1-132.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108465. 10 interactions.
IntActi P15090. 7 interactions.
MINTi MINT-1398507.
STRINGi 9606.ENSP00000256104.

Chemistry

BindingDBi P15090.
ChEMBLi CHEMBL2083.

PTM databases

PhosphoSitei P15090.

Polymorphism databases

DMDMi 119781.

2D gel databases

UCD-2DPAGE P15090.

Proteomic databases

MaxQBi P15090.
PaxDbi P15090.
PeptideAtlasi P15090.
PRIDEi P15090.

Protocols and materials databases

DNASUi 2167.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256104 ; ENSP00000256104 ; ENSG00000170323 .
GeneIDi 2167.
KEGGi hsa:2167.
UCSCi uc003ycd.2. human.

Organism-specific databases

CTDi 2167.
GeneCardsi GC08M082390.
HGNCi HGNC:3559. FABP4.
HPAi CAB024961.
HPA002188.
MIMi 600434. gene.
neXtProti NX_P15090.
PharmGKBi PA27960.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG326764.
HOGENOMi HOG000004829.
HOVERGENi HBG005633.
InParanoidi P15090.
KOi K08753.
OMAi GQEFDEI.
OrthoDBi EOG7NW6BZ.
PhylomeDBi P15090.
TreeFami TF316894.

Enzyme and pathway databases

Reactomei REACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

ChiTaRSi FABP4. human.
EvolutionaryTracei P15090.
GeneWikii Adipocyte_protein_2.
GenomeRNAii 2167.
NextBioi 8751.
PROi P15090.
SOURCEi Search...

Gene expression databases

ArrayExpressi P15090.
Bgeei P15090.
CleanExi HS_FABP4.
Genevestigatori P15090.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[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 adipocyte lipid-binding protein: purification of the protein and cloning of its complementary DNA."
    Baxa C.A., Sha R.S., Buelt M.K., Smith A.J., Matarese V., Chinander L.L., Boundy K.L., Bernlohr D.A.
    Biochemistry 28:8683-8690(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. 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: Urinary bladder.
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  7. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-23.
  8. "Discovery of inhibitors of human adipocyte fatty acid-binding protein, a potential type 2 diabetes target."
    Lehmann F., Haile S., Axen E., Medina C., Uppenberg J., Svensson S., Lundbaeck T., Rondahl L., Barf T.
    Bioorg. Med. Chem. Lett. 14:4445-4448(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR.
  9. "Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2)."
    Marr E., Tardie M., Carty M., Brown Phillips T., Wang I.-K., Soeller W., Qiu X., Karam G.
    Acta Crystallogr. F 62:1058-1060(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID, SUBUNIT, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFABP4_HUMAN
AccessioniPrimary (citable) accession number: P15090
Secondary accession number(s): Q6IBA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 147 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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

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