G3BP1_MOUSE - dbPTM
G3BP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID G3BP1_MOUSE
UniProt AC P97855
Protein Name Ras GTPase-activating protein-binding protein 1
Gene Name G3bp1
Organism Mus musculus (Mouse).
Sequence Length 465
Subcellular Localization Cytoplasm, cytosol . Perikaryon . Cytoplasm, Stress granule . Nucleus . Cytoplasmic in proliferating cells, can be recruited to the plasma membrane in exponentially growing cells. Cytosolic and partially nuclear in resting cells. Recruited to stress
Protein Description ATP- and magnesium-dependent helicase (By similarity). 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 (By similarity). Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency (By similarity). Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA (By similarity). Phosphorylation-dependent sequence-specific endoribonuclease in vitro. [PubMed: 11604510 Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR]
Protein Sequence MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYAHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQTVSNDLEEHLEEPVVEPEPEPEPEPEPEPVSDIQEDKPEAALEEAAPDDVQKSTSPAPADVAPAQEDLRTFSWASVTSKNLPPSGAVPVTGTPPHVVKVPASQPRPESKPDSQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEPGDVEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQNFGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGAVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGPSGGMRGPPRGGMVQKPGFGVGRGITTPRQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
5Ubiquitination---MVMEKPSPLLVG
---CCCCCCCCCEEC		32.4722790023
7Phosphorylation-MVMEKPSPLLVGRE
-CCCCCCCCCEECHH		38.9730482847
36UbiquitinationMLHRFYGKNSSYAHG
HHHHHHCCCCCCCCC		42.13-
47PhosphorylationYAHGGLDSNGKPADA
CCCCCCCCCCCCCHH		53.1522345495
50UbiquitinationGGLDSNGKPADAVYG
CCCCCCCCCCHHHCC		41.0822790023
56PhosphorylationGKPADAVYGQKEIHR
CCCCHHHCCHHHHHH		18.6322817900
67PhosphorylationEIHRKVMSQNFTNCH
HHHHHHHHCCCCCCC		25.5925338131
73S-nitrosocysteineMSQNFTNCHTKIRHV
HHCCCCCCCCEEEEE		3.81-
73S-nitrosylationMSQNFTNCHTKIRHV
HHCCCCCCCCEEEEE		3.8120925432
73GlutathionylationMSQNFTNCHTKIRHV
HHCCCCCCCCEEEEE		3.8124333276
76MalonylationNFTNCHTKIRHVDAH
CCCCCCCEEEEEECC		17.6826320211
76AcetylationNFTNCHTKIRHVDAH
CCCCCCCEEEEEECC		17.6822826441
123UbiquitinationPEGSVANKFYVHNDI
CCCCHHCEEEEECCH		28.4722790023
125PhosphorylationGSVANKFYVHNDIFR
CCHHCEEEEECCHHH		11.4726745281
133PhosphorylationVHNDIFRYQDEVFGG
EECCHHHCCCCCCCC		15.0125619855
143PhosphorylationEVFGGFVTEPQEESE
CCCCCCCCCCCCCCH		39.4224925903
149PhosphorylationVTEPQEESEEEVEEP
CCCCCCCCHHHCCCH		49.9424925903
162PhosphorylationEPEERQQTPEVVPDD
CHHHHHCCCCCCCCC		17.0624453211
207PhosphorylationEPEPEPVSDIQEDKP
CCCCCCCCCCCCCCH		39.4523649490
229PhosphorylationAPDDVQKSTSPAPAD
CCCCHHHCCCCCCCC		19.6124925903
230PhosphorylationPDDVQKSTSPAPADV
CCCHHHCCCCCCCCC		45.8524925903
231PhosphorylationDDVQKSTSPAPADVA
CCHHHCCCCCCCCCC		26.5924925903
246PhosphorylationPAQEDLRTFSWASVT
CCHHHHHCEECCCCC		29.3523984901
248PhosphorylationQEDLRTFSWASVTSK
HHHHHCEECCCCCCC		22.5625521595
251PhosphorylationLRTFSWASVTSKNLP
HHCEECCCCCCCCCC		21.4825521595
253PhosphorylationTFSWASVTSKNLPPS
CEECCCCCCCCCCCC		31.3323984901
254PhosphorylationFSWASVTSKNLPPSG
EECCCCCCCCCCCCC		19.8623984901
260PhosphorylationTSKNLPPSGAVPVTG
CCCCCCCCCCCCCCC		37.1325619855
266O-linked_GlycosylationPSGAVPVTGTPPHVV
CCCCCCCCCCCCCEE		29.3063812699
266PhosphorylationPSGAVPVTGTPPHVV
CCCCCCCCCCCCCEE		29.3022942356
268PhosphorylationGAVPVTGTPPHVVKV
CCCCCCCCCCCEEEC		25.0426824392
351UbiquitinationNLPHEVDKSELKDFF
CCCCCCCHHHHHHHH		51.5122790023
351AcetylationNLPHEVDKSELKDFF
CCCCCCCHHHHHHHH		51.5123236377
371PhosphorylationVVELRINSGGKLPNF
EEEEEECCCCCCCCE		46.6926745281
374UbiquitinationLRINSGGKLPNFGFV
EEECCCCCCCCEEEE		65.3822790023
374AcetylationLRINSGGKLPNFGFV
EEECCCCCCCCEEEE		65.3823806337
391UbiquitinationDDSEPVQKVLSNRPI
CCCHHHHHHHHCCCE		45.43-
427MethylationDRRDNRLRGPGGPRG
CCCCCCCCCCCCCCC		46.12-
427Asymmetric dimethylarginineDRRDNRLRGPGGPRG
CCCCCCCCCCCCCCC		46.12-
433MethylationLRGPGGPRGGPSGGM
CCCCCCCCCCCCCCC		67.0124129315
433Asymmetric dimethylarginineLRGPGGPRGGPSGGM
CCCCCCCCCCCCCCC		67.01-
445MethylationGGMRGPPRGGMVQKP
CCCCCCCCCCCCCCC		58.3924129315
445DimethylationGGMRGPPRGGMVQKP
CCCCCCCCCCCCCCC		58.39-
458MethylationKPGFGVGRGITTPRQ
CCCCCCCCCCCCCCC		30.8224129315
458DimethylationKPGFGVGRGITTPRQ
CCCCCCCCCCCCCCC		30.82-
464MethylationGRGITTPRQ------
CCCCCCCCC------		53.39-
464DimethylationGRGITTPRQ------
CCCCCCCCC------		53.39-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of G3BP1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
149SPhosphorylation

11604510
149SPhosphorylation

11604510
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of G3BP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELAV4_MOUSEElavl4physical
15086518
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of G3BP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-231 ANDTHR-266, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.
"RasGAP-associated endoribonuclease G3Bp: selective RNA degradationand phosphorylation-dependent localization.";
Tourriere H., Gallouzi I.-E., Chebli K., Capony J.-P., Mouaikel J.,van der Geer P., Tazi J.;
Mol. Cell. Biol. 21:7747-7760(2001).
Cited for: ENDORIBONUCLEASE ACTIVITY, AND PHOSPHORYLATION AT SER-149 AND SER-231.

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