CPLM-004040

Genbank Nucleotide ID

Fatty acid-binding protein, liver

Protein Synonyms/Alias

14 kDa selenium-binding protein; Fatty acid-binding protein 1; Liver-type fatty acid-binding protein; L-FABP

Mus musculus (Mouse)

Position	Peptide	Type	References
6	**MNFSGKYQLQSQE	acetylation	[1, 2]
6	**MNFSGKYQLQSQE	ubiquitination	[3]
20	ENFEPFMKAIGLPED	ubiquitination	[3]
31	LPEDLIQKGKDIKGV	acetylation	[4, 5, 6]
31	LPEDLIQKGKDIKGV	succinylation	[5]
31	LPEDLIQKGKDIKGV	ubiquitination	[3]
33	EDLIQKGKDIKGVSE	ubiquitination	[3]
36	IQKGKDIKGVSEIVH	acetylation	[1, 2, 5]
36	IQKGKDIKGVSEIVH	succinylation	[5]
36	IQKGKDIKGVSEIVH	ubiquitination	[3]
46	SEIVHEGKKIKLTIT	acetylation	[1, 2, 4, 5, 6, 7]
46	SEIVHEGKKIKLTIT	succinylation	[5]
46	SEIVHEGKKIKLTIT	ubiquitination	[3]
49	VHEGKKIKLTITYGP	acetylation	[5]
49	VHEGKKIKLTITYGP	succinylation	[5]
49	VHEGKKIKLTITYGP	ubiquitination	[3]
57	LTITYGPKVVRNEFT	acetylation	[4, 5, 6]
57	LTITYGPKVVRNEFT	succinylation	[5]
57	LTITYGPKVVRNEFT	ubiquitination	[3]
78	LETMTGEKVKAVVKL	acetylation	[5]
78	LETMTGEKVKAVVKL	succinylation	[5]
78	LETMTGEKVKAVVKL	ubiquitination	[3]
80	TMTGEKVKAVVKLEG	ubiquitination	[3]
84	EKVKAVVKLEGDNKM	acetylation	[1, 2, 4, 5, 6, 7, 8]
84	EKVKAVVKLEGDNKM	succinylation	[5]
84	EKVKAVVKLEGDNKM	ubiquitination	[3]
90	VKLEGDNKMVTTFKG	acetylation	[2, 4, 5, 6]
90	VKLEGDNKMVTTFKG	succinylation	[5]
90	VKLEGDNKMVTTFKG	ubiquitination	[3]
96	NKMVTTFKGIKSVTE	acetylation	[1, 2, 4, 5, 6]
96	NKMVTTFKGIKSVTE	phosphoglycerylation	[9]
96	NKMVTTFKGIKSVTE	succinylation	[5]
96	NKMVTTFKGIKSVTE	ubiquitination	[3]
99	VTTFKGIKSVTELNG	acetylation	[2]
99	VTTFKGIKSVTELNG	ubiquitination	[3]
121	TLGDIVYKRVSKRI*	acetylation	[5]
121	TLGDIVYKRVSKRI*	succinylation	[5]
121	TLGDIVYKRVSKRI*	ubiquitination	[3]

[1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
[2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[7] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
[8] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
[9] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
Moellering RE, Cravatt BF.
Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]

Functional Description

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. Also seems to bind selenium.

MOD_RES 1 1 N-acetylmethionine (By similarity).

Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Lipid-binding; Reference proteome; Selenium; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0045179; C:apical cortex; IEA:Compara.
GO:0005737; C:cytoplasm; IDA:MGI.
GO:0005829; C:cytosol; IEA:Compara.
GO:0005634; C:nucleus; IDA:MGI.
GO:0005782; C:peroxisomal matrix; IEA:Compara.
GO:0016209; F:antioxidant activity; IEA:Compara.
GO:0032052; F:bile acid binding; IEA:Compara.
GO:0003682; F:chromatin binding; IDA:MGI.
GO:0008144; F:drug binding; IEA:Compara.
GO:0005504; F:fatty acid binding; ISO:MGI.
GO:0005324; F:long-chain fatty acid transporter activity; IEA:Compara.
GO:0005543; F:phospholipid binding; IEA:Compara.
GO:0070301; P:cellular response to hydrogen peroxide; IEA:Compara.
GO:0071456; P:cellular response to hypoxia; IEA:Compara.
GO:0050892; P:intestinal absorption; IEA:Compara.
GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
GO:0032000; P:positive regulation of fatty acid beta-oxidation; IEA:Compara.
GO:0051345; P:positive regulation of hydrolase activity; IEA:Compara.

IPR012674; Calycin.
IPR011038; Calycin-like.
IPR000463; Fatty_acid-bd.
IPR000566; Lipocln_cytosolic_FA-bd_dom.

PR00178; FATTYACIDBP.