EIF3C_MOUSE - dbPTM
EIF3C_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3C_MOUSE
UniProt AC Q8R1B4
Protein Name Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002}
Gene Name Eif3c
Organism Mus musculus (Mouse).
Sequence Length 911
Subcellular Localization Cytoplasm .
Protein Description 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 MSRFFTTGSDSESESSLSGEELVTKPVSGNYGKQPLLLSEDEEDTKRVVRSAKDKRFEELTNLIRTIRNAMKIRDVTKCLEEFELLGKAYGKAKSIVDKEGVPRFYIRILADLEDYLNELWEDKEGKKKMNKNNAKALSTLRQKIRKYNRDFESHITNYKQNPEQSADEDAEKNEEDSEGSSDEDEDEDGVGNTTFLKKKQESSGESRKFHKKMEDDDEDSEDSEDEEWDTSSTSSDSDSEEEEGKQTVLASKFLKKAPTTEEDKKAAEKKREDKAKKKHDRKSKRLDEEEEDNEGGEWERVRGGVPLVKEKPKMFAKGTEITHAVVIKKLNEILQVRGKKGTDRATQIELLQLLVQIAAENNLGVGVIVKIKFNIIASLYDYNPNLATYMKPEMWQMCLDCINELMDTLVAHSNIFVGENILEESENLHNFDQPLRVRGCILTLVERMDEEFTKIMQNTDPHSQEYVEHLKDEAQVCAIIERVQRYLEEKGTTEEICQIYLRRILHTYYKFDYKAHQRQLTPPEGSSKSEQDQAENEGEDSAVLMERLCKYIYAKDRTDRIRTCAILCHIYHHALHSRWYQARDLMLMSHLQDNIQHADPPVQILYNRTMVQLGICAFRQGLTKDAHNALLDIQSSGRAKELLGQGLLLRSLQERNQEQEKVERRRQVPFHLHINLELLECVYLVSAMLLEIPYMAAHESDARRRMISKQFHHQLRVGERQPLLGPPESMREHVVAASKAMKMGDWKTCHSFIINEKMNGKVWDLFPEADKVRTMLVRKIQEESLRTYLFTYSSVYDSISMETLSDMFELDLPTVHSIISKMIINEELMASLDQPTQTVVMHRTEPTAQQNLALQLAEKLGSLVENNERVFDHKQGTYGGYFRDQKDGYRKNEGYMRRGGYRQQQSQTAY
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
2Phosphorylation------MSRFFTTGS
------CCCCCCCCC		37.4826643407
6Phosphorylation--MSRFFTTGSDSES
--CCCCCCCCCCCCC		27.7720531401
7Phosphorylation-MSRFFTTGSDSESE
-CCCCCCCCCCCCCC		29.5421082442
9PhosphorylationSRFFTTGSDSESESS
CCCCCCCCCCCCCCC		35.5522942356
11PhosphorylationFFTTGSDSESESSLS
CCCCCCCCCCCCCCC		44.7321082442
13PhosphorylationTTGSDSESESSLSGE
CCCCCCCCCCCCCCC		46.8921082442
15PhosphorylationGSDSESESSLSGEEL
CCCCCCCCCCCCCCE		45.9521082442
16PhosphorylationSDSESESSLSGEELV
CCCCCCCCCCCCCEE		23.6221082442
18PhosphorylationSESESSLSGEELVTK
CCCCCCCCCCCEEEC		46.2122942356
24PhosphorylationLSGEELVTKPVSGNY
CCCCCEEECCCCCCC		42.1125619855
28PhosphorylationELVTKPVSGNYGKQP
CEEECCCCCCCCCCC		29.8325619855
31PhosphorylationTKPVSGNYGKQPLLL
ECCCCCCCCCCCCCC		29.2625619855
39PhosphorylationGKQPLLLSEDEEDTK
CCCCCCCCCCHHHHH		42.8624925903
45PhosphorylationLSEDEEDTKRVVRSA
CCCCHHHHHHHHHHH		24.8324925903
51PhosphorylationDTKRVVRSAKDKRFE
HHHHHHHHHHHHHHH		28.23-
79S-nitrosylationKIRDVTKCLEEFELL
HHHHHHHHHHHHHHH		4.1720925432
79S-nitrosocysteineKIRDVTKCLEEFELL
HHHHHHHHHHHHHHH		4.17-
95PhosphorylationKAYGKAKSIVDKEGV
HHHCCHHHCCCCCCC		32.4829514104
99AcetylationKAKSIVDKEGVPRFY
CHHHCCCCCCCCHHH		45.5323806337
132AcetylationEGKKKMNKNNAKALS
HHHHHCCHHHHHHHH		48.347712021
136AcetylationKMNKNNAKALSTLRQ
HCCHHHHHHHHHHHH		52.577712031
139PhosphorylationKNNAKALSTLRQKIR
HHHHHHHHHHHHHHH		30.2023737553
140PhosphorylationNNAKALSTLRQKIRK
HHHHHHHHHHHHHHH		27.1523737553
166PhosphorylationYKQNPEQSADEDAEK
CCCCHHHCCCHHHHH		35.7125521595
178PhosphorylationAEKNEEDSEGSSDED
HHHCHHCCCCCCCCC		47.3321082442
181PhosphorylationNEEDSEGSSDEDEDE
CHHCCCCCCCCCCCC		30.4825521595
182PhosphorylationEEDSEGSSDEDEDED
HHCCCCCCCCCCCCC		56.7421082442
194PhosphorylationDEDGVGNTTFLKKKQ
CCCCCCCCHHHHHHH		17.0021659605
195PhosphorylationEDGVGNTTFLKKKQE
CCCCCCCHHHHHHHC		30.8525159016
253AcetylationKQTVLASKFLKKAPT
HHHHHHHHHHHCCCC		49.4623954790
260PhosphorylationKFLKKAPTTEEDKKA
HHHHCCCCCHHHHHH		52.2629899451
261PhosphorylationFLKKAPTTEEDKKAA
HHHCCCCCHHHHHHH		36.0024719451
329UbiquitinationITHAVVIKKLNEILQ
EEHHHHHHHHHHHHH		39.3327667366
441S-palmitoylationQPLRVRGCILTLVER
CCHHHHHHHHHHHHH		1.2928526873
441GlutathionylationQPLRVRGCILTLVER
CCHHHHHHHHHHHHH		1.2924333276
522PhosphorylationKAHQRQLTPPEGSSK
HHHHCCCCCCCCCCH		28.5825521595
527PhosphorylationQLTPPEGSSKSEQDQ
CCCCCCCCCHHHHHH		32.6927841257
528PhosphorylationLTPPEGSSKSEQDQA
CCCCCCCCHHHHHHH		51.5722802335
529UbiquitinationTPPEGSSKSEQDQAE
CCCCCCCHHHHHHHH		60.7622790023
530PhosphorylationPPEGSSKSEQDQAEN
CCCCCCHHHHHHHHH		42.3021183079
556UbiquitinationLCKYIYAKDRTDRIR
HHHHHHHCCCCHHHH		30.6727667366
617S-palmitoylationTMVQLGICAFRQGLT
HHHHHHHHHHHCCCC		2.5126165157
625MalonylationAFRQGLTKDAHNALL
HHHCCCCCHHHHHHH		58.9426320211
641AcetylationIQSSGRAKELLGQGL
HHCCCHHHHHHHHHH		47.7523806337
641MalonylationIQSSGRAKELLGQGL
HHCCCHHHHHHHHHH		47.7526320211
641UbiquitinationIQSSGRAKELLGQGL
HHCCCHHHHHHHHHH		47.7527667366
684PhosphorylationLELLECVYLVSAMLL
HHHHHHHHHHHHHHH		17.0325777480
687PhosphorylationLECVYLVSAMLLEIP
HHHHHHHHHHHHHCC		12.8325777480
695PhosphorylationAMLLEIPYMAAHESD
HHHHHCCHHHCCCHH		12.6825777480
701PhosphorylationPYMAAHESDARRRMI
CHHHCCCHHHHHHHH		27.0625777480
710MalonylationARRRMISKQFHHQLR
HHHHHHHHHHHHHCC		46.1626320211
710UbiquitinationARRRMISKQFHHQLR
HHHHHHHHHHHHHCC		46.1627667366
758UbiquitinationHSFIINEKMNGKVWD
EEEEEEHHHCCCHHH		32.9322790023
762UbiquitinationINEKMNGKVWDLFPE
EEHHHCCCHHHCCCC		34.8422790023
845PhosphorylationQTVVMHRTEPTAQQN
CEEEEECCCCHHHHH		31.4726239621
860UbiquitinationLALQLAEKLGSLVEN
HHHHHHHHHHHHHHC		53.17-
863PhosphorylationQLAEKLGSLVENNER
HHHHHHHHHHHCCCC		39.4128066266
875UbiquitinationNERVFDHKQGTYGGY
CCCEECCCCCCCCCC		52.8722790023
878PhosphorylationVFDHKQGTYGGYFRD
EECCCCCCCCCCCCC		19.2522345495
879PhosphorylationFDHKQGTYGGYFRDQ
ECCCCCCCCCCCCCC		18.5122817900
882PhosphorylationKQGTYGGYFRDQKDG
CCCCCCCCCCCCCCC		7.35-
892UbiquitinationDQKDGYRKNEGYMRR
CCCCCCCCCCCCCCC		51.36-
892MalonylationDQKDGYRKNEGYMRR
CCCCCCCCCCCCCCC		51.3626320211
907PhosphorylationGGYRQQQSQTAY---
CCCCCCCCCCCC---		25.7625521595
909PhosphorylationYRQQQSQTAY-----
CCCCCCCCCC-----		32.9225521595
911PhosphorylationQQQSQTAY-------
CCCCCCCC-------		23.6023984901
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 EIF3C_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3C_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 EIF3C_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EIF3C_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EIF3C_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-39, 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-39, 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-178; SER-181 ANDSER-182, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.
"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-39, 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 SER-166, AND MASSSPECTROMETRY.

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