IF2P_MOUSE - dbPTM
IF2P_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF2P_MOUSE
UniProt AC Q05D44
Protein Name Eukaryotic translation initiation factor 5B
Gene Name Eif5b
Organism Mus musculus (Mouse).
Sequence Length 1216
Subcellular Localization Cytoplasm .
Protein Description Plays a role in translation initiation. Translational GTPase that catalyzes the joining of the 40S and 60S subunits to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. GTP binding and hydrolysis induces conformational changes in the enzyme that renders it active for productive interactions with the ribosome. The release of the enzyme after formation of the initiation complex is a prerequisite to form elongation-competent ribosomes..
Protein Sequence MGKKQKNKSEDSTKDDTDLGALAAEIEGAGAAKEQEPQKSKGKKKKEKKKQDFDENDILRELEELSLEAQGIRADRDAAAVKPTENNEEESASKQDKKKKGQKGKKTSFDENDSEELEDKDSKSKKTARPNSEAPLSGSEDADDSNKLSKKGKKAQKSTKKRDGSEEDEDNSKRSKERSRVNSSGESGGESDEFLQSRKGQKKNQKNKSVPTVDSGNEDDDSSFKIKTVAQKKAEKKEREKKKRDEEKAKLRKMKEKEELEKGKKEQSKQREPQKRPEEEVLTLRGTPDTGAASEEKGDTAAALEDDNEGDKKKKDKKKKKTEKDEKEKEKKKGPSKSTVKAIQEALAKLKEEEERQKREEEERIKRLEELEAKRKEEERLEQEKRERKKQKEKERKERLKKEGKLLTKSQREARARAEVTLRHLQAQGVEVPSKDSLPKKRPVYEDKKKKKTPQQLESKEVSETLEISAPVEAVDQGGPEKEETPPSVEPEEEEDTEDAGLDDWEAMASDEEREKEGNMIHIEVEENPEEEEEEEEEEEEEESEDEEEEGDSEGSDGDEEDCKLSDEKDSGKAGDTKPSKDASSDSEYDSDDDRTKEERAYDKAKRRIEKRRLEHGKNVNTEKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDEFEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKDDEIPVLKDELIHELKQTLNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKMKILPQYIFNSRDPIVIGVTVEAGQVKQGTPMCVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPGESPKMFGRHFEATDILVSKISRQSIDALKDWFRDEMQKSDWQLIVELKKVFEII
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
9PhosphorylationGKKQKNKSEDSTKDD
CCCCCCCCCCCCCCC		56.9025338131
12PhosphorylationQKNKSEDSTKDDTDL
CCCCCCCCCCCCCHH		33.0525338131
13PhosphorylationKNKSEDSTKDDTDLG
CCCCCCCCCCCCHHH		51.3025338131
17PhosphorylationEDSTKDDTDLGALAA
CCCCCCCCHHHHHHH		43.1722817900
66PhosphorylationLRELEELSLEAQGIR
HHHHHHHHHHHHCCC		27.6925521595
91PhosphorylationTENNEEESASKQDKK
CCCCHHHHCCHHHHH		40.9123684622
93PhosphorylationNNEEESASKQDKKKK
CCHHHHCCHHHHHHH		39.8825521595
107PhosphorylationKGQKGKKTSFDENDS
HCCCCCCCCCCCCCH		37.8025521595
108PhosphorylationGQKGKKTSFDENDSE
CCCCCCCCCCCCCHH		39.3125521595
114PhosphorylationTSFDENDSEELEDKD
CCCCCCCHHHHCCCC		44.5527087446
122PhosphorylationEELEDKDSKSKKTAR
HHHCCCCCCCCCCCC		44.5625619855
127PhosphorylationKDSKSKKTARPNSEA
CCCCCCCCCCCCCCC		31.4727087446
132PhosphorylationKKTARPNSEAPLSGS
CCCCCCCCCCCCCCC		37.5127087446
137PhosphorylationPNSEAPLSGSEDADD
CCCCCCCCCCCCCCC		38.9327087446
139PhosphorylationSEAPLSGSEDADDSN
CCCCCCCCCCCCCCC		29.0027087446
145PhosphorylationGSEDADDSNKLSKKG
CCCCCCCCCHHCHHH		36.0927742792
149PhosphorylationADDSNKLSKKGKKAQ
CCCCCHHCHHHHHHH		33.6527742792
165PhosphorylationSTKKRDGSEEDEDNS
CCCCCCCCCCCCCCH		41.9427087446
172PhosphorylationSEEDEDNSKRSKERS
CCCCCCCHHHHHHHH		41.5925159016
175PhosphorylationDEDNSKRSKERSRVN
CCCCHHHHHHHHCCC		42.4729899451
179PhosphorylationSKRSKERSRVNSSGE
HHHHHHHHCCCCCCC		41.4927087446
183PhosphorylationKERSRVNSSGESGGE
HHHHCCCCCCCCCCC		36.5425521595
184PhosphorylationERSRVNSSGESGGES
HHHCCCCCCCCCCCC		41.1827087446
187PhosphorylationRVNSSGESGGESDEF
CCCCCCCCCCCCHHH		56.4725521595
191PhosphorylationSGESGGESDEFLQSR
CCCCCCCCHHHHHHH		45.7927087446
197PhosphorylationESDEFLQSRKGQKKN
CCHHHHHHHCCCCCC		37.8025619855
209PhosphorylationKKNQKNKSVPTVDSG
CCCCCCCCCCCCCCC		42.6024925903
212PhosphorylationQKNKSVPTVDSGNED
CCCCCCCCCCCCCCC		34.4924925903
215PhosphorylationKSVPTVDSGNEDDDS
CCCCCCCCCCCCCCC		38.9024925903
222PhosphorylationSGNEDDDSSFKIKTV
CCCCCCCCCCHHHHH		44.6725521595
223PhosphorylationGNEDDDSSFKIKTVA
CCCCCCCCCHHHHHH		37.2425521595
283PhosphorylationRPEEEVLTLRGTPDT
CCHHHHHEECCCCCC		21.4225521595
287PhosphorylationEVLTLRGTPDTGAAS
HHHEECCCCCCCCCC		16.1425521595
290PhosphorylationTLRGTPDTGAASEEK
EECCCCCCCCCCCCC		29.8925619855
294PhosphorylationTPDTGAASEEKGDTA
CCCCCCCCCCCCCCC		45.8425521595
300PhosphorylationASEEKGDTAAALEDD
CCCCCCCCCHHHCCC		27.1925619855
349UbiquitinationAIQEALAKLKEEEER
HHHHHHHHHHHHHHH		62.0222790023
410PhosphorylationEGKLLTKSQREARAR
HHHCCCHHHHHHHHH		29.2729514104
434PhosphorylationAQGVEVPSKDSLPKK
HCCCCCCCCCCCCCC		55.0326643407
437PhosphorylationVEVPSKDSLPKKRPV
CCCCCCCCCCCCCCC		50.7526824392
459PhosphorylationKTPQQLESKEVSETL
CCHHHHHCCHHHHCE		42.5829514104
463PhosphorylationQLESKEVSETLEISA
HHHCCHHHHCEEECC		26.4223649490
485PhosphorylationGGPEKEETPPSVEPE
CCCCCCCCCCCCCCC		41.4125195567
488PhosphorylationEKEETPPSVEPEEEE
CCCCCCCCCCCCCCC		40.0724925903
497PhosphorylationEPEEEEDTEDAGLDD
CCCCCCCCCCCCCCH		38.7622324799
510PhosphorylationDDWEAMASDEEREKE
CHHHHHCCHHHHHHH		32.2524925903
544PhosphorylationEEEEEEESEDEEEEG
HHHHHHHCCHHHHCC		54.34-
553PhosphorylationDEEEEGDSEGSDGDE
HHHHCCCCCCCCCCH		55.50-
556PhosphorylationEEGDSEGSDGDEEDC
HCCCCCCCCCCHHHH		34.08-
571PhosphorylationKLSDEKDSGKAGDTK
CCCCCCCCCCCCCCC		53.9427818261
577PhosphorylationDSGKAGDTKPSKDAS
CCCCCCCCCCCCCCC		43.8929472430
580PhosphorylationKAGDTKPSKDASSDS
CCCCCCCCCCCCCCC		44.7325159016
584PhosphorylationTKPSKDASSDSEYDS
CCCCCCCCCCCCCCC		44.8227087446
585PhosphorylationKPSKDASSDSEYDSD
CCCCCCCCCCCCCCC		47.0425521595
587PhosphorylationSKDASSDSEYDSDDD
CCCCCCCCCCCCCCC		39.7525521595
589PhosphorylationDASSDSEYDSDDDRT
CCCCCCCCCCCCCCH		25.3825159016
591PhosphorylationSSDSEYDSDDDRTKE
CCCCCCCCCCCCHHH		41.8825521595
596PhosphorylationYDSDDDRTKEERAYD
CCCCCCCHHHHHHHH		50.2125159016
631S-nitrosocysteineKLRAPIICVLGHVDT
HHCCCEEEEEECCCC		1.82-
631S-nitrosylationKLRAPIICVLGHVDT
HHCCCEEEEEECCCC		1.8220925432
631S-palmitoylationKLRAPIICVLGHVDT
HHCCCEEEEEECCCC		1.8226165157
762UbiquitinationDRLYDWKKSPDSDVA
HHHCCCCCCCCCCHH		64.0722790023
773MalonylationSDVAVTLKKQKKNTK
CCHHHHHCCCCCCCH		43.7426320211
849S-palmitoylationLSKRLAHCEELRAQV
HHHHHHHHHHHHHHH		3.4626165157
1011UbiquitinationINIGPVHKKDVMKAS
CEECCCCHHHHHHHH		51.40-
1011MalonylationINIGPVHKKDVMKAS
CEECCCCHHHHHHHH		51.4026320211
1091AcetylationAVFPCKMKILPQYIF
EEEECCCCCCHHHHH		26.9622826441
1164PhosphorylationIEPIPGESPKMFGRH
EEECCCCCCCHHCCC		35.4225521595
1181UbiquitinationATDILVSKISRQSID
HHHHHHHHHHHHHHH		36.9022790023
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 IF2P_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF2P_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 IF2P_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of IF2P_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF2P_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-114; SER-137; SER-139AND SER-215, 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-165 AND SER-215, ANDMASS SPECTROMETRY.
"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-114; SER-137; SER-165;SER-183; SER-184; SER-187 AND SER-191, AND MASS 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-137, 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-114; SER-137; SER-139;SER-187; SER-191 AND SER-215, 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-179; SER-183; SER-184;SER-187; SER-191; SER-584; SER-585 AND SER-591, 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-114 AND SER-215, ANDMASS SPECTROMETRY.
"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 SER-215, AND MASSSPECTROMETRY.

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