CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019332
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Far upstream element-binding protein 3 
Protein Synonyms/Alias
 FUSE-binding protein 3 
Gene Name
 FUBP3 
Gene Synonyms/Alias
 FBP3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15QSAPVGMKAEGFVDAubiquitination[1, 2, 3]
32RVRQIAAKIDSIPHLacetylation[4]
32RVRQIAAKIDSIPHLubiquitination[2]
57VYGYGVQKRPLDDGVubiquitination[2, 3, 5, 6]
83TVITEEFKVPDKMVGubiquitination[2]
87EEFKVPDKMVGFIIGubiquitination[2, 3, 5, 6, 7]
138PESIEQAKRLLGQIVubiquitination[2]
186GRGGETIKQLQERTGubiquitination[2, 8]
195LQERTGVKMVMIQDGubiquitination[2]
220RITGDAFKVQQAREMubiquitination[2, 3]
378GKGGENIKSINQQSGubiquitination[3, 5, 6, 7]
525KAWEDYYKKQSHAASubiquitination[1, 5, 6, 7]
526AWEDYYKKQSHAASAubiquitination[1, 2, 3]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [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] 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]
 [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] 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
Functional Description
 May interact with single-stranded DNA from the far- upstream element (FUSE). May activate gene expression. 
Sequence Annotation
 DOMAIN 77 141 KH 1.
 DOMAIN 162 228 KH 2.
 DOMAIN 253 317 KH 3.
 DOMAIN 354 421 KH 4.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 76 76 Phosphothreonine.
 MOD_RES 296 296 Phosphoserine.
 MOD_RES 539 539 Phosphoserine.
 MOD_RES 569 569 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 572 AA 
Protein Sequence
MAELVQGQSA PVGMKAEGFV DALHRVRQIA AKIDSIPHLN NSTPLVDPSV YGYGVQKRPL 60
DDGVGNQLGA LVHQRTVITE EFKVPDKMVG FIIGRGGEQI SRIQAESGCK IQIASESSGI 120
PERPCVLTGT PESIEQAKRL LGQIVDRCRN GPGFHNDIDS NSTIQEILIP ASKVGLVIGR 180
GGETIKQLQE RTGVKMVMIQ DGPLPTGADK PLRITGDAFK VQQAREMVLE IIREKDQADF 240
RGVRGDFNSR MGGGSIEVSV PRFAVGIVIG RNGEMIKKIQ NDAGVRIQFK PDDGISPERA 300
AQVMGPPDRC QHAAHIISEL ILTAQERDGF GGLAAARGRG RGRGDWSVGA PGGVQEITYT 360
VPADKCGLVI GKGGENIKSI NQQSGAHVEL QRNPPPNSDP NLRRFTIRGV PQQIEVARQL 420
IDEKVGGTNL GAPGAFGQSP FSQPPAPPHQ NTFPPRSSGC FPNMAAKVNG NPHSTPVSGP 480
PAFLTQGWGS TYQAWQQPTQ QVPSQQSQPQ SSQPNYSKAW EDYYKKQSHA ASAAPQASSP 540
PDYTMAWAEY YRQQVAFYGQ TLGQAQAHSQ EQ 572 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IDA:UniProtKB. 
Interpro
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1. 
Pfam
 PF00013; KH_1 
SMART
 SM00322; KH 
PROSITE
 PS50084; KH_TYPE_1 
PRINTS