CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012049
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ras GTPase-activating protein-binding protein 1 
Protein Synonyms/Alias
 G3BP-1; ATP-dependent DNA helicase VIII; hDH VIII; GAP SH3 domain-binding protein 1 
Gene Name
 G3BP1 
Gene Synonyms/Alias
 G3BP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MVMEKPSPLLVGubiquitination[1, 2]
36MLHRFYGKNSSYVHGubiquitination[1, 2, 3, 4, 5, 6]
50GGLDSNGKPADAVYGubiquitination[1, 2, 3, 4, 6]
59ADAVYGQKEIHRKVMubiquitination[1, 2, 3, 6]
64GQKEIHRKVMSQNFTubiquitination[2]
76NFTNCHTKIRHVDAHubiquitination[1, 2, 5]
123PEGSVANKFYVHNDIubiquitination[2, 6]
353NLPHEVDKSELKDFFacetylation[7]
353NLPHEVDKSELKDFFubiquitination[1]
376LRINSGGKLPNFGFVacetylation[7]
376LRINSGGKLPNFGFVubiquitination[2, 4, 6]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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] 
Functional Description
 May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium- dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA. 
Sequence Annotation
 DOMAIN 11 133 NTF2.
 DOMAIN 340 415 RRM.
 MOD_RES 143 143 Phosphothreonine.
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 232 232 Phosphoserine.
 MOD_RES 268 268 Phosphothreonine (By similarity).
 MOD_RES 373 373 Phosphoserine.
 MOD_RES 376 376 N6-acetyllysine.
 MOD_RES 435 435 Dimethylated arginine; alternate.
 MOD_RES 435 435 Omega-N-methylarginine; alternate.
 MOD_RES 460 460 Dimethylated arginine; alternate.
 MOD_RES 460 460 Omega-N-methylated arginine; alternate.  
Keyword
 3D-structure; Acetylation; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Endonuclease; Helicase; Hydrolase; Membrane; Methylation; Nuclease; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 466 AA 
Protein Sequence
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK PADAVYGQKE 60
IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV 120
ANKFYVHNDI FRYQDEVFGG FVTEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQAVVS 180
NDMEEHLEEP VAEPEPDPEP EPEQEPVSEI QEEKPEPVLE ETAPEDAQKS SSPAPADIAQ 240
TVQEDLRTFS WASVTSKNLP PSGAVPVTGI PPHVVKVPAS QPRPESKPES QIPPQRPQRD 300
QRVREQRINI PPQRGPRPIR EAGEQGDIEP RRMVRHPDSH QLFIGNLPHE VDKSELKDFF 360
QSYGNVVELR INSGGKLPNF GFVVFDDSEP VQKVLSNRPI MFRGEVRLNV EEKKTRAARE 420
GDRRDNRLRG PGGPRGGLGG GMRGPPRGGM VQKPGFGVGR GLAPRQ 466 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0010494; C:cytoplasmic stress granule; IEA:Compara.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; TAS:ProtInc.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
 GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
 GO:0003729; F:mRNA binding; IEA:Compara.
 GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IEA:Compara.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
 GO:0006810; P:transport; IEA:UniProtKB-KW. 
Interpro
 IPR002075; NTF2.
 IPR018222; Nuclear_transport_factor_2_euk.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF02136; NTF2
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50177; NTF2_DOMAIN
 PS50102; RRM 
PRINTS