CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010853
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fatty acid-binding protein, epidermal 
Protein Synonyms/Alias
 Epidermal-type fatty acid-binding protein; E-FABP; Fatty acid-binding protein 5; Psoriasis-associated fatty acid-binding protein homolog; PA-FABP 
Gene Name
 FABP5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17RWRLVDSKGFDEYMKacetylation[1, 2, 3, 4]
17RWRLVDSKGFDEYMKubiquitination[4, 5, 6, 7]
24KGFDEYMKELGVGIAubiquitination[4, 5, 6, 7, 8, 9, 10]
34GVGIALRKMGAMAKPubiquitination[4, 6, 7, 9]
61IKTESTLKTTQFSCTubiquitination[5, 7]
72FSCTLGEKFEETTADubiquitination[7]
82ETTADGRKTQTVCNFubiquitination[5, 7]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [8] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation. 
Sequence Annotation
 REGION 129 131 Fatty acid binding (By similarity).
 BINDING 109 109 Fatty acid (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 17 17 N6-acetyllysine.
 MOD_RES 131 131 Phosphotyrosine.
 DISULFID 120 127  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Lipid-binding; Phosphoprotein; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 135 AA 
Protein Sequence
MATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK NLTIKTESTL 60
KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW DGKESTITRK LKDGKLVVEC 120
VMNNVTCTRI YEKVE 135 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0005504; F:fatty acid binding; TAS:ProtInc.
 GO:0005215; F:transporter activity; IEA:InterPro.
 GO:0008544; P:epidermis development; TAS:ProtInc.
 GO:0006006; P:glucose metabolic process; IEA:Compara.
 GO:0015758; P:glucose transport; IEA:Compara.
 GO:0006629; P:lipid metabolic process; TAS:ProtInc.
 GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Compara. 
Interpro
 IPR012674; Calycin.
 IPR011038; Calycin-like.
 IPR000463; Fatty_acid-bd.
 IPR000566; Lipocln_cytosolic_FA-bd_dom. 
Pfam
 PF00061; Lipocalin 
SMART
  
PROSITE
 PS00214; FABP 
PRINTS
 PR00178; FATTYACIDBP.