EIF3B_MOUSE - dbPTM
EIF3B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3B_MOUSE
UniProt AC Q8JZQ9
Protein Name Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001}
Gene Name Eif3b
Organism Mus musculus (Mouse).
Sequence Length 803
Subcellular Localization Cytoplasm .
Protein Description RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression..
Protein Sequence MQDAENVAVPEAAEERAEPARQQPASESPPTDEAAGSGGSEVGQTEDAEEDAEAGPEPEVRAKPAAQSEEETATSPAASPTPQSAERSPSQEPSAPGKAEAVGEQARGHPSAGAEEEGGSDGSAAEAEPRALENGEADEPSFSDPEDFVDDVSEEELLGDVLKDRPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKIINDYYPEEDGKTKGYIFLEYASPAHAVDAVKNADGYKLDKQHTFRVNLFTDFDKYMTISDEWDIPEKQPFKDLGNLRYWLEEAECRDQYSVIFESGDRTSIFWNDVKDPVSIEERARWTETYVRWSPKGTYLATFHQRGIALWGGDKFKQIQRFSHQGVQLIDFSPCERYLVTFSPLMDTQDDPQAIIIWDILTGHKKRGFHCESSAHWPIFKWSHDGKFFARMTLDTLSIYETPSMGLLDKKSLKISGIKDFSWSPGGNIIAFWVPEDKDIPARVTLMQLPTRQEIRVRNLFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKETIIAFAWEPNGSKFAVLHGEAPRISVSFYHVKSNGKIELIKMFDKQQANTIFWSPQGQFVVLAGLRSMNGALAFVDTSDCTVMNIAEHYMASDVEWDPTGRYVVTSVSWWSHKVDNAYWLWTFQGRLLQKNNKDRFCQLLWRPRPPTLLSQDQIKQIKKDLKKYSKIFEQKDRLSQSKASKELVERRRTMMEDFRQYRKMAQELYMKQKNERLELRGGVDTDELDSNVDDWEEETIEFFVTEEVIPLGSQE
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
1Acetylation-------MQDAENVA
-------CCCHHHCC		8.00-
26PhosphorylationPARQQPASESPPTDE
HHHCCCCCCCCCCCC		45.3425619855
28PhosphorylationRQQPASESPPTDEAA
HCCCCCCCCCCCCCC		33.4127087446
31PhosphorylationPASESPPTDEAAGSG
CCCCCCCCCCCCCCC		50.2724723360
37PhosphorylationPTDEAAGSGGSEVGQ
CCCCCCCCCCCCCCC		34.9427087446
40PhosphorylationEAAGSGGSEVGQTED
CCCCCCCCCCCCCCC		32.4127087446
45PhosphorylationGGSEVGQTEDAEEDA
CCCCCCCCCCHHHHH		29.8827087446
68PhosphorylationRAKPAAQSEEETATS
CCCCCCCCCCHHCCC		42.1024925903
72PhosphorylationAAQSEEETATSPAAS
CCCCCCHHCCCCCCC		38.2224925903
74PhosphorylationQSEEETATSPAASPT
CCCCHHCCCCCCCCC		42.5424925903
75PhosphorylationSEEETATSPAASPTP
CCCHHCCCCCCCCCC		15.3024925903
79PhosphorylationTATSPAASPTPQSAE
HCCCCCCCCCCCCCC		31.2627087446
81PhosphorylationTSPAASPTPQSAERS
CCCCCCCCCCCCCCC		31.3127087446
84PhosphorylationAASPTPQSAERSPSQ
CCCCCCCCCCCCCCC		33.0427087446
88PhosphorylationTPQSAERSPSQEPSA
CCCCCCCCCCCCCCC		22.0225521595
90PhosphorylationQSAERSPSQEPSAPG
CCCCCCCCCCCCCCC		48.7127087446
94PhosphorylationRSPSQEPSAPGKAEA
CCCCCCCCCCCCHHH		46.4727742792
98UbiquitinationQEPSAPGKAEAVGEQ
CCCCCCCCHHHHCHH		41.8327667366
111PhosphorylationEQARGHPSAGAEEEG
HHCCCCCCCCCCCCC		33.3927087446
120PhosphorylationGAEEEGGSDGSAAEA
CCCCCCCCCCCCCCC		50.0527087446
123PhosphorylationEEGGSDGSAAEAEPR
CCCCCCCCCCCCCCC		29.3327087446
141PhosphorylationNGEADEPSFSDPEDF
CCCCCCCCCCCHHHH		35.0222942356
143PhosphorylationEADEPSFSDPEDFVD
CCCCCCCCCHHHHCC		57.5027087446
153PhosphorylationEDFVDDVSEEELLGD
HHHCCCCCHHHHHHH		46.4122942356
191UbiquitinationVGPDRLEKLKNVIHK
CCHHHHHHHHHHHHH		70.16-
198AcetylationKLKNVIHKIFSKFGK
HHHHHHHHHHHHHHH		34.03-
198UbiquitinationKLKNVIHKIFSKFGK
HHHHHHHHHHHHHHH		34.03-
201PhosphorylationNVIHKIFSKFGKIIN
HHHHHHHHHHHHHHH		30.4630387612
202UbiquitinationVIHKIFSKFGKIIND
HHHHHHHHHHHHHHH		47.6027667366
205AcetylationKIFSKFGKIINDYYP
HHHHHHHHHHHHCCC		43.4722826441
205UbiquitinationKIFSKFGKIINDYYP
HHHHHHHHHHHHCCC		43.47-
217AcetylationYYPEEDGKTKGYIFL
CCCCCCCCEEEEEEE		60.4323954790
226PhosphorylationKGYIFLEYASPAHAV
EEEEEEEECCHHHHH		17.9623984901
228PhosphorylationYIFLEYASPAHAVDA
EEEEEECCHHHHHHH		23.0126745281
237UbiquitinationAHAVDAVKNADGYKL
HHHHHHHHCCCCCCC		48.41-
242PhosphorylationAVKNADGYKLDKQHT
HHHCCCCCCCCCCCE		14.6630387612
246UbiquitinationADGYKLDKQHTFRVN
CCCCCCCCCCEEEEE		55.1827667366
246MalonylationADGYKLDKQHTFRVN
CCCCCCCCCCEEEEE		55.1826320211
265PhosphorylationFDKYMTISDEWDIPE
HHHCCCCCCCCCCCC		21.9525338131
273UbiquitinationDEWDIPEKQPFKDLG
CCCCCCCCCCCCCCC		58.90-
277UbiquitinationIPEKQPFKDLGNLRY
CCCCCCCCCCCCHHH		59.74-
277AcetylationIPEKQPFKDLGNLRY
CCCCCCCCCCCCHHH		59.74-
295PhosphorylationEAECRDQYSVIFESG
HHHCCCEEEEEEECC		14.8123567750
296PhosphorylationAECRDQYSVIFESGD
HHCCCEEEEEEECCC		11.7823567750
305PhosphorylationIFESGDRTSIFWNDV
EEECCCCCEEEECCC		30.8023567750
313UbiquitinationSIFWNDVKDPVSIEE
EEEECCCCCCCCHHH		60.2127667366
327PhosphorylationERARWTETYVRWSPK
HHHHCEEEEEEECCC		21.6825367039
328PhosphorylationRARWTETYVRWSPKG
HHHCEEEEEEECCCC		5.0425367039
353UbiquitinationIALWGGDKFKQIQRF
EEEECCHHHHCHHHH		58.71-
353AcetylationIALWGGDKFKQIQRF
EEEECCHHHHCHHHH		58.7122826441
373GlutathionylationQLIDFSPCERYLVTF
EEEECCCCCEEEEEE		4.5024333276
409GlutathionylationHKKRGFHCESSAHWP
CCCCCCCCCCCCCCC		5.1824333276
436PhosphorylationRMTLDTLSIYETPSM
EEEECHHEEEECCCC		25.8025367039
438PhosphorylationTLDTLSIYETPSMGL
EECHHEEEECCCCCC		15.4618563927
440PhosphorylationDTLSIYETPSMGLLD
CHHEEEECCCCCCCC		12.0517203969
448UbiquitinationPSMGLLDKKSLKISG
CCCCCCCCCCCEECC		44.20-
483PhosphorylationKDIPARVTLMQLPTR
CCCCCEEEEEECCCC		15.8028059163
489PhosphorylationVTLMQLPTRQEIRVR
EEEEECCCCHHEHHH		54.2818779572
505UbiquitinationLFNVVDCKLHWQKNG
CCCEEECEEECEECC		38.63-
514PhosphorylationHWQKNGDYLCVKVDR
ECEECCCEEEEEECC		11.91-
524UbiquitinationVKVDRTPKGTQGVVT
EEECCCCCCCCCEEE		74.1727667366
524AcetylationVKVDRTPKGTQGVVT
EEECCCCCCCCCEEE		74.1723806337
541UbiquitinationEIFRMREKQVPVDVV
EEEEECCCCCCCEEE		46.3527667366
541AcetylationEIFRMREKQVPVDVV
EEEEECCCCCCCEEE		46.3523806337
593AcetylationNGKIELIKMFDKQQA
CCEEEEEEEECHHHC		46.2522826441
633PhosphorylationFVDTSDCTVMNIAEH
EEECCCCCEEEHHHH		27.99-
641PhosphorylationVMNIAEHYMASDVEW
EEEHHHHHHCCCCEE		5.96-
702PhosphorylationPRPPTLLSQDQIKQI
CCCCCCCCHHHHHHH		34.5218779572
716PhosphorylationIKKDLKKYSKIFEQK
HHHHHHHHHHHHHHH		17.3828059163
718UbiquitinationKDLKKYSKIFEQKDR
HHHHHHHHHHHHHHH		48.61-
718MalonylationKDLKKYSKIFEQKDR
HHHHHHHHHHHHHHH		48.6126320211
723MalonylationYSKIFEQKDRLSQSK
HHHHHHHHHHHCHHH		37.3026320211
727PhosphorylationFEQKDRLSQSKASKE
HHHHHHHCHHHHHHH		33.05-
733AcetylationLSQSKASKELVERRR
HCHHHHHHHHHHHHH		60.9823806337
733UbiquitinationLSQSKASKELVERRR
HCHHHHHHHHHHHHH		60.9827667366
759UbiquitinationMAQELYMKQKNERLE
HHHHHHHHHHHHHCE		44.5627667366
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 EIF3B_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3B_MOUSE !!
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 EIF3B_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EIF3B_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EIF3B_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 THR-74; SER-75; SER-79;SER-120 AND SER-123, AND MASS SPECTROMETRY.
"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-75 AND SER-79, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, ANDMASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-120 AND SER-123,AND MASS SPECTROMETRY.
"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-68; THR-74; SER-75;SER-79; SER-90; SER-120 AND SER-123, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, ANDMASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASSSPECTROMETRY.
"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 THR-440, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND MASSSPECTROMETRY.

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