IF2P_YEAST - dbPTM
IF2P_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF2P_YEAST
UniProt AC P39730
Protein Name Eukaryotic translation initiation factor 5B {ECO:0000305|PubMed:12507428}
Gene Name FUN12 {ECO:0000303|PubMed:8076820}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1002
Subcellular Localization Cytoplasm .
Protein Description Plays a role in translation initiation. [PubMed: 9624054 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]
Protein Sequence MAKKSKKNQQNYWDEEFEEDAAQNEEISATPTPNPESSAGADDTSREASASAEGAEAIEGDFMSTLKQSKKKQEKKVIEEKKDGKPILKSKKEKEKEKKEKEKQKKKEQAARKKAQQQAQKEKNKELNKQNVEKAAAEKAAAEKSQKSKGESDKPSASAKKPAKKVPAGLAALRRQLELKKQLEEQEKLEREEEERLEKEEEERLANEEKMKEEAKAAKKEKEKAKREKRKAEGKLLTRKQKEEKKLLERRRAALLSSGNVKVAGLAKKDGEENKPKKVVYSKKKKRTTQENASEAIKSDSKKDSEVVPDDELKESEDVLIDDWENLALGDDDEEGTNEETQESTASHENEDQNQGEEEEEGEEEEEEEEERAHVHEVAKSTPAATPAATPTPSSASPNKKDLRSPICCILGHVDTGKTKLLDKIRQTNVQGGEAGGITQQIGATYFPIDAIKAKTKVMAEYEKQTFDVPGLLVIDTPGHESFSNLRSRGSSLCNIAILVIDIMHGLEQQTIESIKLLRDRKAPFVVALNKIDRLYDWKAIPNNSFRDSFAKQSRAVQEEFQSRYSKIQLELAEQGLNSELYFQNKNMSKYVSIVPTSAVTGEGVPDLLWLLLELTQKRMSKQLMYLSHVEATILEVKVVEGFGTTIDVILSNGYLREGDRIVLCGMNGPIVTNIRALLTPQPLRELRLKSEYVHHKEVKAALGVKIAANDLEKAVSGSRLLVVGPEDDEDELMDDVMDDLTGLLDSVDTTGKGVVVQASTLGSLEALLDFLKDMKIPVMSIGLGPVYKRDVMKASTMLEKAPEYAVMLCFDVKVDKEAEQYAEQEGIKIFNADVIYHLFDSFTAYQEKLLEERRKDFLDYAIFPCVLQTLQIINKRGPMIIGVDVLEGTLRVGTPICAVKTDPTTKERQTLILGKVISLEINHQPVQEVKKGQTAAGVAVRLEDPSGQQPIWGRHVDENDTLYSLVSRRSIDTLKDKAFRDQVARSDWLLLKKLKVVFGIE
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
49PhosphorylationDDTSREASASAEGAE
CCCCCHHHHHHHHHH		20.2919779198
51PhosphorylationTSREASASAEGAEAI
CCCHHHHHHHHHHHH		25.1019779198
64PhosphorylationAIEGDFMSTLKQSKK
HHCCCHHHHHHHHHH		30.4928889911
67UbiquitinationGDFMSTLKQSKKKQE
CCHHHHHHHHHHHHH		53.2517644757
89AcetylationKDGKPILKSKKEKEK
CCCCCCCCCHHHHHH		62.0325381059
235AcetylationEKRKAEGKLLTRKQK
HHHHHHHHHCCHHHH		31.6524489116
257PhosphorylationRRRAALLSSGNVKVA
HHHHHHHHCCCEEEE		36.7324909858
258PhosphorylationRRAALLSSGNVKVAG
HHHHHHHCCCEEEEE		34.0624909858
288PhosphorylationYSKKKKRTTQENASE
EECCCCCCCHHHHHH		41.5327717283
289PhosphorylationSKKKKRTTQENASEA
ECCCCCCCHHHHHHH		37.6123749301
294PhosphorylationRTTQENASEAIKSDS
CCCHHHHHHHHHCCC		38.8623749301
298UbiquitinationENASEAIKSDSKKDS
HHHHHHHHCCCCCCC		56.0823749301
299PhosphorylationNASEAIKSDSKKDSE
HHHHHHHCCCCCCCC		40.7925521595
301PhosphorylationSEAIKSDSKKDSEVV
HHHHHCCCCCCCCCC		49.0119823750
305PhosphorylationKSDSKKDSEVVPDDE
HCCCCCCCCCCCCHH		40.9628889911
380AcetylationAHVHEVAKSTPAATP
HHHHHHHHCCCCCCC		61.1025381059
381PhosphorylationHVHEVAKSTPAATPA
HHHHHHHCCCCCCCC		29.8622369663
382PhosphorylationVHEVAKSTPAATPAA
HHHHHHCCCCCCCCC		19.0822369663
386PhosphorylationAKSTPAATPAATPTP
HHCCCCCCCCCCCCC		18.6322369663
390PhosphorylationPAATPAATPTPSSAS
CCCCCCCCCCCCCCC		29.7822369663
392PhosphorylationATPAATPTPSSASPN
CCCCCCCCCCCCCCC		31.2922369663
394PhosphorylationPAATPTPSSASPNKK
CCCCCCCCCCCCCCH		40.8022369663
395PhosphorylationAATPTPSSASPNKKD
CCCCCCCCCCCCCHH		33.6922890988
397PhosphorylationTPTPSSASPNKKDLR
CCCCCCCCCCCHHCC		30.8422369663
405PhosphorylationPNKKDLRSPICCILG
CCCHHCCCCEEEEEC		26.3912507428
424UbiquitinationGKTKLLDKIRQTNVQ
CHHHHHHHHHHHCCC		39.4917644757
453UbiquitinationYFPIDAIKAKTKVMA
ECCHHHHHHHHHHHH		45.6217644757
453AcetylationYFPIDAIKAKTKVMA
ECCHHHHHHHHHHHH		45.6224489116
457UbiquitinationDAIKAKTKVMAEYEK
HHHHHHHHHHHHHHH		29.3423749301
531AcetylationPFVVALNKIDRLYDW
CEEEEECCCCCCCCC		47.0024489116
539AcetylationIDRLYDWKAIPNNSF
CCCCCCCCCCCCCCH		33.2724489116
680PhosphorylationTNIRALLTPQPLREL
EEHHHHHCCHHHHHH		22.2622369663
714UbiquitinationIAANDLEKAVSGSRL
EEHHHHHHHHCCCEE		62.4823749301
714AcetylationIAANDLEKAVSGSRL
EEHHHHHHHHCCCEE		62.4824489116
781PhosphorylationDMKIPVMSIGLGPVY
HCCCCEEEECCCHHH		17.4619823750
788PhosphorylationSIGLGPVYKRDVMKA
EECCCHHHHHHHHHH		11.9319823750
789AcetylationIGLGPVYKRDVMKAS
ECCCHHHHHHHHHHH		42.2124489116
794UbiquitinationVYKRDVMKASTMLEK
HHHHHHHHHHHHHHH		38.7522106047
817UbiquitinationCFDVKVDKEAEQYAE
EEEECCCHHHHHHHH		62.9123749301
817AcetylationCFDVKVDKEAEQYAE
EEEECCCHHHHHHHH		62.9124489116
895PhosphorylationEGTLRVGTPICAVKT
CCEEECCCCEEEEEC		13.4627214570
907UbiquitinationVKTDPTTKERQTLIL
EECCCCCHHHHHEEE		54.0723749301
916UbiquitinationRQTLILGKVISLEIN
HHHEEEEEEEEEEEC		32.7117644757
919PhosphorylationLILGKVISLEINHQP
EEEEEEEEEEECCCC		23.9623749301
931AcetylationHQPVQEVKKGQTAAG
CCCHHHHHCCCCEEE		50.8924489116
931UbiquitinationHQPVQEVKKGQTAAG
CCCHHHHHCCCCEEE		50.8917644757
932UbiquitinationQPVQEVKKGQTAAGV
CCHHHHHCCCCEEEE		62.5217644757
971PhosphorylationYSLVSRRSIDTLKDK
HHHHHHHCHHHHHCH		24.5723749301
976SuccinylationRRSIDTLKDKAFRDQ
HHCHHHHHCHHHHHH		60.3123954790
976AcetylationRRSIDTLKDKAFRDQ
HHCHHHHHCHHHHHH		60.3124489116
978AcetylationSIDTLKDKAFRDQVA
CHHHHHCHHHHHHHH		48.0824489116
993AcetylationRSDWLLLKKLKVVFG
HCHHHHHHHHHHHHC		56.9024489116
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_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF2P_YEAST !!
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_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBF5_YEASTCBF5physical
11805826
C1TM_YEASTMIS1physical
11805826
EIF3C_YEASTNIP1physical
11805826
FBRL_YEASTNOP1physical
11805826
EIF3B_YEASTPRT1physical
11805826
PUF6_YEASTPUF6physical
11805826
GATF_YEASTGTF1physical
11805826
IF1A_YEASTTIF11physical
10982835
IMDH3_YEASTIMD3physical
16429126
EIF3C_YEASTNIP1physical
16429126
RS22A_YEASTRPS22Aphysical
16429126
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RS22B_YEASTRPS22Bphysical
16429126
CBF5_YEASTCBF5physical
16429126
IMDH2_YEASTIMD2physical
16429126
C1TM_YEASTMIS1physical
16429126
FBRL_YEASTNOP1physical
16429126
RL13B_YEASTRPL13Bphysical
16429126
RL2A_YEASTRPL2Aphysical
16429126
RL2B_YEASTRPL2Aphysical
16429126
RL36A_YEASTRPL36Aphysical
16429126
RRP5_YEASTRRP5physical
16429126
PUF6_YEASTPUF6physical
16429126
RL10_YEASTRPL10physical
16429126
RL13A_YEASTRPL13Aphysical
16429126
RL27A_YEASTRPL27Aphysical
16429126
RLA0_YEASTRPP0physical
16429126
RL3_YEASTRPL3physical
16429126
RL30_YEASTRPL30physical
16429126
RL8A_YEASTRPL8Aphysical
16429126
RL8B_YEASTRPL8Bphysical
16429126
RS3_YEASTRPS3physical
16429126
RS5_YEASTRPS5physical
16429126
EIF3B_YEASTPRT1physical
16429126
RL7A_YEASTRPL7Aphysical
16429126
PUF6_YEASTPUF6physical
18413716
IF1A_YEASTTIF11physical
17242201
IF2A_YEASTSUI2physical
20485439
IF2B_YEASTSUI3physical
20485439
IF2G_YEASTGCD11physical
20485439
IF1A_YEASTTIF11physical
21636924
NOP3_YEASTNPL3genetic
24100011
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF2P_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; THR-386 ANDTHR-390, AND MASS SPECTROMETRY.

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