CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019039
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Far upstream element-binding protein 1 
Protein Synonyms/Alias
 FBP; FUSE-binding protein 1; DNA helicase V; hDH V 
Gene Name
 FUBP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
44RARQIAAKIGGDAGTubiquitination[1]
64DYGYGGQKRPLEDGDubiquitination[1]
76DGDQPDAKKVAPQNDubiquitination[1]
203KAGLVIGKGGETIKQubiquitination[1]
209GKGGETIKQLQERAGubiquitination[2]
312AGVRIQFKPDDGTTPubiquitination[1]
400GKGGETIKSISQQSGubiquitination[1]
446ARQLIEEKIGGPVNPubiquitination[2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription. 
Sequence Annotation
 DOMAIN 100 164 KH 1.
 DOMAIN 185 251 KH 2.
 DOMAIN 275 339 KH 3.
 DOMAIN 376 443 KH 4.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 140 140 Phosphoserine.
 MOD_RES 153 153 Phosphothreonine.
 MOD_RES 630 630 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 644 AA 
Protein Sequence
MADYSTVPPP SSGSAGGGGG GGGGGGVNDA FKDALQRARQ IAAKIGGDAG TSLNSNDYGY 60
GGQKRPLEDG DQPDAKKVAP QNDSFGTQLP PMHQQQSRSV MTEEYKVPDG MVGFIIGRGG 120
EQISRIQQES GCKIQIAPDS GGLPERSCML TGTPESVQSA KRLLDQIVEK GRPAPGFHHG 180
DGPGNAVQEI MIPASKAGLV IGKGGETIKQ LQERAGVKMV MIQDGPQNTG ADKPLRITGD 240
PYKVQQAKEM VLELIRDQGG FREVRNEYGS RIGGNEGIDV PIPRFAVGIV IGRNGEMIKK 300
IQNDAGVRIQ FKPDDGTTPE RIAQITGPPD RCQHAAEIIT DLLRSVQAGN PGGPGPGGRG 360
RGRGQGNWNM GPPGGLQEFN FIVPTGKTGL IIGKGGETIK SISQQSGARI ELQRNPPPNA 420
DPNMKLFTIR GTPQQIDYAR QLIEEKIGGP VNPLGPPVPH GPHGVPGPHG PPGPPGPGTP 480
MGPYNPAPYN PGPPGPAPHG PPAPYAPQGW GNAYPHWQQQ APPDPAKAGT DPNSAAWAAY 540
YAHYYQQQAQ PPPAAPAGAP TTTQTNGQGD QQNPAPAGQV DYTKAWEEYY KKMGQAVPAP 600
TGAPPGGQPD YSAAWAEYYR QQAAYYAQTS PQGMPQHPPA PQGQ 644 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
 GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR015096; DUF1897.
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1. 
Pfam
 PF09005; DUF1897
 PF00013; KH_1 
SMART
 SM00322; KH 
PROSITE
 PS50084; KH_TYPE_1 
PRINTS