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Protein Page:
FABP4 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
FABP4 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. Homodimer. Interacts with PPARG. Monomer. Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family. Note: This description may include information from UniProtKB.
Protein type: Lipid binding protein
Cellular Component: cytoplasm; lipid particle; nucleus
Molecular Function: transporter activity; fatty acid binding
Biological Process: cholesterol homeostasis; transport; white fat cell differentiation; triacylglycerol catabolic process; brown fat cell differentiation; cytokine production; negative regulation of protein kinase activity; negative regulation of transcription, DNA-dependent; positive regulation of inflammatory response
Reference #:  P15090 (UniProtKB)
Alt. Names/Synonyms: A-FABP; Adipocyte lipid-binding protein; Adipocyte-type fatty acid-binding protein; AFABP; ALBP; aP2; FABP4; fatty acid binding protein 4, adipocyte; Fatty acid-binding protein 4; Fatty acid-binding protein, adipocyte
Gene Symbols: FABP4
Molecular weight: 14,719 Da
Basal Isoelectric point: 6.59  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

FABP4

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S13 VGTWKLVSSENFDDy
2 3 Y20-p SSENFDDyMKEVGVG
0 4 K22 ENFDDyMKEVGVGFA
0 1 T30 EVGVGFATRKVAGMA
0 1 K32 GVGFATRKVAGMAKP
0 1 K38 RKVAGMAKPNMIISV
0 1 T57 ITIKSESTFKNTEIS
0 2 K59 IKSESTFKNTEISFI
0 1 K59 IKSESTFKNTEISFI
0 2 T75 GQEFDEVTADDRKVK
0 1 K80 EVTADDRKVKSTITL
0 1 K97 GVLVHVQKWDGkStt
0 1 K101-ac HVQKWDGkSttIKRK
0 1 K101 HVQKWDGKSttIKRK
0 1 T103-p QKWDGkSttIKRKRE
0 1 T104-p KWDGkSttIKRKRED
0 1 K113 KRKREDDKLVVECVM
0 2 K121 LVVECVMKGVTSTRV
0 3 K121 LVVECVMKGVTSTRV
0 2 Y129-p GVTSTRVyERA____
  mouse

 
S13-p VGTWKLVsSENFDDy
Y20-p sSENFDDyMkEVGVG
K22-ub ENFDDyMkEVGVGFA
T30-p EVGVGFAtRkVAGMA
K32-ub GVGFAtRkVAGMAkP
K38-ub RkVAGMAkPNMIISV
T57-p VTIRSEStFkNTEIS
K59-ac IRSEStFkNTEISFK
K59-ub IRSEStFkNTEISFK
T75-p GVEFDEItADDRkVK
K80-ub EItADDRkVKSIITL
K97-ub GALVQVQkWDGkSTT
K101 QVQkWDGKSTTIKRK
K101-ub QVQkWDGkSTTIKRK
T103 QkWDGkSTTIKRKRD
T104 kWDGkSTTIKRKRDG
K113-ub KRKRDGDkLVVECVM
K121-ac LVVECVMkGVTSTRV
K121-ub LVVECVMkGVTSTRV
Y129 GVTSTRVYERA____
  rat

 
S13 VGTWKLVSSENFDDY
Y20 SSENFDDYMKEVGVG
K22 ENFDDYMKEVGVGFA
T30 EVGVGFATRKVAGMA
K32 GVGFATRKVAGMAKP
K38 RKVAGMAKPNLIISV
T57 VVIRSESTFKNTEIS
K59 IRSESTFKNTEISFK
K59 IRSESTFKNTEISFK
T75 GVEFDEITPDDRKVK
K80 EITPDDRKVKSIITL
K97 GVLVHVQKWDGKSTT
K101 HVQKWDGKSTTIKKR
K101 HVQKWDGKSTTIKKR
T103 QKWDGKSTTIKKRRD
T104 KWDGKSTTIKKRRDG
K113 KKRRDGDKLVVECVM
K121 LVVECVMKGVTSTRV
K121 LVVECVMKGVTSTRV
Y129 GVTSTRVYERA____
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