CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010700
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; GAP SH3 domain-binding protein 1; HDH-VIII 
Gene Name
 G3bp1 
Gene Synonyms/Alias
 G3bp 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
5***MVMEKPSPLLVGubiquitination[1]
50GGLDSNGKPADAVYGubiquitination[1]
76NFTNCHTKIRHVDAHacetylation[2]
123PEGSVANKFYVHNDIubiquitination[1]
351NLPHEVDKSELKDFFacetylation[3]
351NLPHEVDKSELKDFFubiquitination[1]
374LRINSGGKLPNFGFVacetylation[4]
374LRINSGGKLPNFGFVubiquitination[1]
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] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [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] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
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 338 413 RRM.
 MOD_RES 143 143 Phosphothreonine (By similarity).
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 266 266 Phosphothreonine.
 MOD_RES 371 371 Phosphoserine (By similarity).
 MOD_RES 374 374 N6-acetyllysine (By similarity).
 MOD_RES 433 433 Dimethylated arginine; alternate (By
 MOD_RES 433 433 Omega-N-methylarginine; alternate (By
 MOD_RES 445 445 Omega-N-methylated arginine (By
 MOD_RES 458 458 Dimethylated arginine; alternate (By
 MOD_RES 458 458 Omega-N-methylated arginine; alternate
 MOD_RES 464 464 Omega-N-methylated arginine (By  
Keyword
 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
 465 AA 
Protein Sequence
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY AHGGLDSNGK PADAVYGQKE 60
IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV 120
ANKFYVHNDI FRYQDEVFGG FVTEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQTVSN 180
DLEEHLEEPV VEPEPEPEPE PEPEPVSDIQ EDKPEAALEE AAPDDVQKST SPAPADVAPA 240
QEDLRTFSWA SVTSKNLPPS GAVPVTGTPP HVVKVPASQP RPESKPDSQI PPQRPQRDQR 300
VREQRINIPP QRGPRPIREA GEPGDVEPRR MVRHPDSHQL FIGNLPHEVD KSELKDFFQN 360
FGNVVELRIN SGGKLPNFGF VVFDDSEPVQ KVLSNRPIMF RGAVRLNVEE KKTRAAREGD 420
RRDNRLRGPG GPRGGPSGGM RGPPRGGMVQ KPGFGVGRGI TTPRQ 465 
Gene Ontology
 GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0003729; F:mRNA binding; IDA:MGI.
 GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IMP:MGI.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 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