CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023230
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ras GTPase-activating protein-binding protein 2 
Protein Synonyms/Alias
 G3BP-2; GAP SH3 domain-binding protein 2 
Gene Name
 G3BP2 
Gene Synonyms/Alias
 KIAA0660 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MVMEKPSPLLVGubiquitination[1, 2, 3]
25QYYTLLNKAPEYLHRubiquitination[2, 3, 4, 5, 6, 7]
64GQNDIHHKVLSLNFSubiquitination[6]
76NFSECHTKIRHVDAHubiquitination[5]
107NSGQPERKFMQTFVLubiquitination[2, 3, 6, 7]
370NTKGVGGKLPNFGFVubiquitination[4, 6, 8]
392VQRILIAKPIMFRGEubiquitination[3, 6]
Reference
 [1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [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]
 [3] 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]
 [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] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Probable scaffold protein that may be involved in mRNA transport (Potential). 
Sequence Annotation
 DOMAIN 11 133 NTF2.
 DOMAIN 331 409 RRM.
 MOD_RES 141 141 Phosphoserine.
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 225 225 Phosphoserine (By similarity).
 MOD_RES 227 227 Phosphothreonine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; mRNA transport; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 482 AA 
Protein Sequence
MVMEKPSPLL VGREFVRQYY TLLNKAPEYL HRFYGRNSSY VHGGVDASGK PQEAVYGQND 60
IHHKVLSLNF SECHTKIRHV DAHATLSDGV VVQVMGLLSN SGQPERKFMQ TFVLAPEGSV 120
PNKFYVHNDM FRYEDEVFGD SEPELDEESE DEVEEEQEER QPSPEPVQEN ANSGYYEAHP 180
VTNGIEEPLE ESSHEPEPEP ESETKTEELK PQVEEKNLEE LEEKSTTPPP AEPVSLPQEP 240
PKAFSWASVT SKNLPPSGTV SSSGIPPHVK APVSQPRVEA KPEVQSQPPR VREQRPRERP 300
GFPPRGPRPG RGDMEQNDSD NRRIIRYPDS HQLFVGNLPH DIDENELKEF FMSFGNVVEL 360
RINTKGVGGK LPNFGFVVFD DSEPVQRILI AKPIMFRGEV RLNVEEKKTR AARERETRGG 420
GDDRRDIRRN DRGPGGPRGI VGGGMMRDRD GRGPPPRGGM AQKLGSGRGT GQMEGRFTGQ 480
RR 482 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
 GO:0003723; F:RNA binding; NAS:UniProtKB.
 GO:0007253; P:cytoplasmic sequestering of NF-kappaB; NAS:UniProtKB.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0007265; P:Ras protein signal transduction; NAS:UniProtKB.
 GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. 
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