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Protein

Fatty acid-binding protein, adipocyte

Gene

Fabp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.3 Publications

GO - Molecular functioni

GO - Biological processi

  • brown fat cell differentiation Source: MGI
  • cellular response to lithium ion Source: MGI
  • cholesterol homeostasis Source: MGI
  • cytokine production Source: MGI
  • negative regulation of protein kinase activity Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • positive regulation of inflammatory response Source: MGI
  • white fat cell differentiation Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, adipocyte
Alternative name(s):
3T3-L1 lipid-binding protein
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
Myelin P2 protein homolog
P15
P2 adipocyte protein
Protein 422
Gene namesi
Name:Fabp4
Synonyms:Ap2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88038. 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.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221K → A: Abolishes ligand-induced translocation to the nucleus; when associated with A-31 and A-32. 1 Publication
Mutagenesisi31 – 311R → A: Abolishes ligand-induced translocation to the nucleus; when associated with A-22 and A-32. 1 Publication
Mutagenesisi32 – 321K → A: Abolishes ligand-induced translocation to the nucleus; when associated with A-22 and A-31. 1 Publication
Mutagenesisi58 – 581F → A: Abolishes ligand-induced translocation to the nucleus. 1 Publication
Mutagenesisi67 – 671L → A: Abolishes export from nucleus; when associated with A-87 and A-92. 2 Publications
Mutagenesisi87 – 871L → A: Abolishes export from nucleus; when associated with A-67 and A-92. 2 Publications
Mutagenesisi92 – 921L → A: Abolishes export from nucleus; when associated with A-67 and A-87. 2 Publications

Chemistry

ChEMBLiCHEMBL1075118.
GuidetoPHARMACOLOGYi2534.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity1 Publication
Chaini2 – 132131Fatty acid-binding protein, adipocytePRO_0000067367Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteineBy similarity
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei20 – 201Phosphotyrosine; by Tyr-kinasesBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP04117.
PaxDbiP04117.
PRIDEiP04117.

2D gel databases

SWISS-2DPAGEP04117.

PTM databases

iPTMnetiP04117.
PhosphoSiteiP04117.

Expressioni

Gene expression databases

BgeeiP04117.
CleanExiMM_FABP4.
ExpressionAtlasiP04117. baseline and differential.
GenevisibleiP04117. MM.

Interactioni

Subunit structurei

Monomer (By similarity). Homodimer. Interacts with PPARG.By similarity6 Publications

Protein-protein interaction databases

IntActiP04117. 1 interaction.
MINTiMINT-4094909.
STRINGi10090.ENSMUSP00000029041.

Structurei

Secondary structure

1
132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi7 – 1610Combined sources
Helixi17 – 248Combined sources
Helixi28 – 3710Combined sources
Beta strandi41 – 466Combined sources
Beta strandi49 – 546Combined sources
Beta strandi61 – 655Combined sources
Beta strandi67 – 693Combined sources
Beta strandi71 – 744Combined sources
Beta strandi80 – 889Combined sources
Beta strandi91 – 988Combined sources
Beta strandi101 – 11010Combined sources
Beta strandi113 – 1208Combined sources
Beta strandi123 – 1319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A18X-ray2.40A2-132[»]
1A2DX-ray2.40A/B2-132[»]
1AB0X-ray1.90A3-132[»]
1ACDX-ray2.70A3-132[»]
1ADLX-ray1.60A2-132[»]
1ALBX-ray2.50A2-132[»]
1G74X-ray1.70A2-132[»]
1G7NX-ray1.50A2-132[»]
1LIBX-ray1.70A2-132[»]
1LICX-ray1.60A2-132[»]
1LIDX-ray1.60A2-132[»]
1LIEX-ray1.60A2-132[»]
1LIFX-ray1.60A2-132[»]
2ANSX-ray2.50A/B2-132[»]
2Q9SX-ray2.30A1-132[»]
2QM9X-ray2.31A/B1-132[»]
3HK1X-ray1.70A2-132[»]
3JS1X-ray1.81A/B2-132[»]
3JSQX-ray2.30A2-132[»]
5C0NX-ray3.00A/B1-132[»]
5D8JX-ray3.00A1-132[»]
ProteinModelPortaliP04117.
SMRiP04117. Positions 2-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04117.

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi22 – 3211Nuclear localization signalAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP04117.
KOiK08753.
OMAiGQEFDEI.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP04117.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR033073. FABP4.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF83. PTHR11955:SF83. 1 hit.
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.

P04117-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDLV
60 70 80 90 100
TIRSESTFKN TEISFKLGVE FDEITADDRK VKSIITLDGG ALVQVQKWDG
110 120 130
KSTTIKRKRD GDKLVVECVM KGVTSTRVYE RA
Length:132
Mass (Da):14,650
Last modified:January 23, 2007 - v3
Checksum:iED08EDDBBE2D7E32
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401N → T in AAA39870 (PubMed:6206497).Curated
Sequence conflicti111 – 1111G → V in AAA39417 (PubMed:3520554).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02109 mRNA. Translation: AAA39416.1.
M13264
, M13261, M13262, M13263 Genomic DNA. Translation: AAA39870.1.
M13385 Genomic DNA. Translation: AAA39417.1.
AK003143 mRNA. Translation: BAB22601.1.
BC054426 mRNA. Translation: AAH54426.1.
M20497 Genomic DNA. Translation: AAA37188.1.
M28726 mRNA. Translation: AAA37112.1.
CCDSiCCDS17238.1.
PIRiB25952.
RefSeqiNP_077717.1. NM_024406.2.
UniGeneiMm.582.

Genome annotation databases

EnsembliENSMUST00000029041; ENSMUSP00000029041; ENSMUSG00000062515.
GeneIDi11770.
KEGGimmu:11770.
UCSCiuc008opl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02109 mRNA. Translation: AAA39416.1.
M13264
, M13261, M13262, M13263 Genomic DNA. Translation: AAA39870.1.
M13385 Genomic DNA. Translation: AAA39417.1.
AK003143 mRNA. Translation: BAB22601.1.
BC054426 mRNA. Translation: AAH54426.1.
M20497 Genomic DNA. Translation: AAA37188.1.
M28726 mRNA. Translation: AAA37112.1.
CCDSiCCDS17238.1.
PIRiB25952.
RefSeqiNP_077717.1. NM_024406.2.
UniGeneiMm.582.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A18X-ray2.40A2-132[»]
1A2DX-ray2.40A/B2-132[»]
1AB0X-ray1.90A3-132[»]
1ACDX-ray2.70A3-132[»]
1ADLX-ray1.60A2-132[»]
1ALBX-ray2.50A2-132[»]
1G74X-ray1.70A2-132[»]
1G7NX-ray1.50A2-132[»]
1LIBX-ray1.70A2-132[»]
1LICX-ray1.60A2-132[»]
1LIDX-ray1.60A2-132[»]
1LIEX-ray1.60A2-132[»]
1LIFX-ray1.60A2-132[»]
2ANSX-ray2.50A/B2-132[»]
2Q9SX-ray2.30A1-132[»]
2QM9X-ray2.31A/B1-132[»]
3HK1X-ray1.70A2-132[»]
3JS1X-ray1.81A/B2-132[»]
3JSQX-ray2.30A2-132[»]
5C0NX-ray3.00A/B1-132[»]
5D8JX-ray3.00A1-132[»]
ProteinModelPortaliP04117.
SMRiP04117. Positions 2-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04117. 1 interaction.
MINTiMINT-4094909.
STRINGi10090.ENSMUSP00000029041.

Chemistry

ChEMBLiCHEMBL1075118.
GuidetoPHARMACOLOGYi2534.

PTM databases

iPTMnetiP04117.
PhosphoSiteiP04117.

2D gel databases

SWISS-2DPAGEP04117.

Proteomic databases

EPDiP04117.
PaxDbiP04117.
PRIDEiP04117.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029041; ENSMUSP00000029041; ENSMUSG00000062515.
GeneIDi11770.
KEGGimmu:11770.
UCSCiuc008opl.2. mouse.

Organism-specific databases

CTDi2167.
MGIiMGI:88038. Fabp4.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP04117.
KOiK08753.
OMAiGQEFDEI.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP04117.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiR-MMU-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

EvolutionaryTraceiP04117.
NextBioi279545.
PROiP04117.
SOURCEiSearch...

Gene expression databases

BgeeiP04117.
CleanExiMM_FABP4.
ExpressionAtlasiP04117. baseline and differential.
GenevisibleiP04117. MM.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR033073. FABP4.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF83. PTHR11955:SF83. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of specific mRNAs during adipose differentiation: identification of an mRNA encoding a homologue of myelin P2 protein."
    Bernlohr D.A., Angus C.W., Lane M.D., Bolanowski M.A., Kelly T.J. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 81:5468-5472(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Adipocyte P2 gene: developmental expression and homology of 5'-flanking sequences among fat cell-specific genes."
    Hunt C.R., Ro J.H.-S., Dobson D.E., Min H.Y., Spiegelman B.M.
    Proc. Natl. Acad. Sci. U.S.A. 83:3786-3790(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of three genes participating in the adipose differentiation of 3T3 cells."
    Phillips M., Djian P., Green H.
    J. Biol. Chem. 261:10821-10827(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  6. "Purification of murine adipocyte lipid-binding protein. Characterization as a fatty acid- and retinoic acid-binding protein."
    Matarese V., Bernlohr D.A.
    J. Biol. Chem. 263:14544-14551(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-132.
  7. "Expression of the differentiation-induced gene for fatty acid-binding protein is activated by glucocorticoid and cAMP."
    Cook J.S., Lucas J.J., Sibley E., Bolanowski M.A., Christy R.J., Kelly T.J. Jr., Lane M.D.
    Proc. Natl. Acad. Sci. U.S.A. 85:2949-2953(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
  8. "Developmentally regulated mRNAs in 3T3-adipocytes: analysis of transcriptional control."
    Cook K.S., Hunt C.R., Spiegelman B.M.
    J. Cell Biol. 100:514-520(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-132.
  9. "Expression of fatty acid-binding proteins in the developing mouse mammary gland."
    Bansal M.P., Medina D.
    Biochem. Biophys. Res. Commun. 191:61-69(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-35; 37-51 AND 59-88.
    Tissue: Mammary gland.
  10. "Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription."
    Tan N.-S., Shaw N.S., Vinckenbosch N., Liu P., Yasmin R., Desvergne B., Wahli W., Noy N.
    Mol. Cell. Biol. 22:5114-5127(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPARG.
  11. "Adipocyte-type fatty acid-binding protein as inter-compartmental shuttle for peroxisome proliferator activated receptor gamma agonists in cultured cell."
    Adida A., Spener F.
    Biochim. Biophys. Acta 1761:172-181(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPARG.
  12. "Continuous nucleocytoplasmic shuttling underlies transcriptional activation of PPARgamma by FABP4."
    Ayers S.D., Nedrow K.L., Gillilan R.E., Noy N.
    Biochemistry 46:6744-6752(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-22; ARG-31; LYS-32; LEU-67; LEU-87 AND LEU-92.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  14. "Crystal structure of recombinant murine adipocyte lipid-binding protein."
    Xu Z., Bernlohr D.A., Banaszak L.J.
    Biochemistry 31:3484-3492(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  15. "The adipocyte lipid-binding protein at 1.6-A resolution. Crystal structures of the apoprotein and with bound saturated and unsaturated fatty acids."
    Xu Z., Bernlohr D.A., Banaszak L.J.
    J. Biol. Chem. 268:7874-7884(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  16. "Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1, 8-anilinonaphthalene-8-sulfonate."
    Ory J.J., Banaszak L.J.
    Biophys. J. 77:1107-1116(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  17. "X-ray crystallographic structures of adipocyte lipid-binding protein complexed with palmitate and hexadecanesulfonic acid. Properties of cavity binding sites."
    LaLonde J.M., Bernlohr D.A., Banaszak L.J.
    Biochemistry 33:4885-4895(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
  18. "Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and X-ray crystallographic studies."
    LaLonde J.M., Levenson M.A., Roe J.J., Bernlohr D.A., Banaszak L.J.
    J. Biol. Chem. 269:25339-25347(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
  19. "Specificity determinants for lipids bound to beta-barrel proteins."
    Reese A.J., Banaszak L.J.
    J. Lipid Res. 45:232-243(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
  20. "Structural basis for activation of fatty acid-binding protein 4."
    Gillilan R.E., Ayers S.D., Noy N.
    J. Mol. Biol. 372:1246-1260(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH TROGLITAZONE AND LINOLEIC ACID, SUBUNIT, MUTAGENESIS OF PHE-58; LEU-67; LEU-87 AND LEU-92, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFABP4_MOUSE
AccessioniPrimary (citable) accession number: P04117
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.