CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001013
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endothelial differentiation-related factor 1 
Protein Synonyms/Alias
 EDF-1; Multiprotein-bridging factor 1; MBF1 
Gene Name
 EDF1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
25TAAQAKSKQAILAAQubiquitination[1, 2]
79RVTLEVGKVIQQGRQacetylation[3]
79RVTLEVGKVIQQGRQubiquitination[4]
93QSKGLTQKDLATKINacetylation[5]
93QSKGLTQKDLATKINubiquitination[5]
102LATKINEKPQVIADYubiquitination[2, 5, 6, 7]
123PNNQVLGKIERAIGLacetylation[3, 5, 8, 9]
143DIGKPIEKGPRAK**ubiquitination[4, 5, 10, 11]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] 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]
 [6] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Transcriptional coactivator stimulating NR5A1 and ligand-dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. May function in endothelial cells differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism. 
Sequence Annotation
 DOMAIN 81 135 HTH cro/C1-type.
 DNA_BIND 92 111 H-T-H motif (Potential).
 REGION 37 113 Interaction with NR5A2, PPARG and NR1H3.
 REGION 69 108 Interaction with TBP and NR5A1.
 MOTIF 81 88 IQ motif.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; Calmodulin-binding; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 148 AA 
Protein Sequence
MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK 60
LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV 120
LGKIERAIGL KLRGKDIGKP IEKGPRAK 148 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005634; C:nucleus; IMP:UniProtKB.
 GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
 GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
 GO:0045446; P:endothelial cell differentiation; TAS:UniProtKB.
 GO:0007275; P:multicellular organismal development; TAS:ProtInc.
 GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; TAS:UniProtKB.
 GO:0019216; P:regulation of lipid metabolic process; TAS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001387; HTH.
 IPR010982; Lambda_DNA-bd_dom.
 IPR013729; MBF1_N. 
Pfam
 PF01381; HTH_3
 PF08523; MBF1 
SMART
 SM00530; HTH_XRE 
PROSITE
 PS50943; HTH_CROC1 
PRINTS