EIF3J_YEAST - dbPTM
EIF3J_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3J_YEAST
UniProt AC Q05775
Protein Name Eukaryotic translation initiation factor 3 subunit J {ECO:0000255|HAMAP-Rule:MF_03009}
Gene Name HCR1 {ECO:0000255|HAMAP-Rule:MF_03009}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 265
Subcellular Localization Cytoplasm .
Protein Description Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation..
Protein Sequence MSWDDEAINGSMGNDDAVLMDSWDAEIGDDEPVMQSWDAEEEEKKPAPKPKKEQPKKVKKGKESSADRALLDIDTLDEKTRKELIKKAEMESDLNNAADLFAGLGVAEEHPRARALQKEQEEQALKRPAFTKDTPIETHPLFNAETKREYQDLRKALTAAITPMNKKSPLNYSSSLAIDLIRDVAKPMSIESIRQTVATLNVLIKDKEREERQARLARVRGGTATGGAGKKKVKGKTNLGGAFKKDQDFDLDGPDDFEFGDDDFM
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
64PhosphorylationKVKKGKESSADRALL
CCCCCCCCHHHHHHH		34.0225521595
65PhosphorylationVKKGKESSADRALLD
CCCCCCCHHHHHHHC		34.9722369663
75PhosphorylationRALLDIDTLDEKTRK
HHHHCHHHCCHHHHH		36.1222369663
79AcetylationDIDTLDEKTRKELIK
CHHHCCHHHHHHHHH		53.9824489116
92PhosphorylationIKKAEMESDLNNAAD
HHHHHHHHHHHHHHH		46.1922369663
118UbiquitinationPRARALQKEQEEQAL
HHHHHHHHHHHHHHH		63.3123749301
126AcetylationEQEEQALKRPAFTKD
HHHHHHHHCCCCCCC		60.3924489116
131PhosphorylationALKRPAFTKDTPIET
HHHCCCCCCCCCCCC		30.0724961812
132AcetylationLKRPAFTKDTPIETH
HHCCCCCCCCCCCCC		53.8224489116
134PhosphorylationRPAFTKDTPIETHPL
CCCCCCCCCCCCCCC		27.9324961812
138PhosphorylationTKDTPIETHPLFNAE
CCCCCCCCCCCCCCC		29.5224961812
146PhosphorylationHPLFNAETKREYQDL
CCCCCCCCHHHHHHH		32.7528889911
147AcetylationPLFNAETKREYQDLR
CCCCCCCHHHHHHHH		34.4424489116
158PhosphorylationQDLRKALTAAITPMN
HHHHHHHHHHHCCCC		20.9222369663
162PhosphorylationKALTAAITPMNKKSP
HHHHHHHCCCCCCCC		16.2622369663
168PhosphorylationITPMNKKSPLNYSSS
HCCCCCCCCCCCCHH		35.9122369663
173PhosphorylationKKSPLNYSSSLAIDL
CCCCCCCCHHHHHHH		16.6330377154
174PhosphorylationKSPLNYSSSLAIDLI
CCCCCCCHHHHHHHH		21.0030377154
175PhosphorylationSPLNYSSSLAIDLIR
CCCCCCHHHHHHHHH		18.8430377154
186AcetylationDLIRDVAKPMSIESI
HHHHHHHCCCCHHHH		40.8924489116
189PhosphorylationRDVAKPMSIESIRQT
HHHHCCCCHHHHHHH		31.5622369663
192PhosphorylationAKPMSIESIRQTVAT
HCCCCHHHHHHHHHH		22.7722369663
237PhosphorylationKKKVKGKTNLGGAFK
CCCCCCCCCCCCCCC		44.3221551504
244AcetylationTNLGGAFKKDQDFDL
CCCCCCCCCCCCCCC		55.7125381059
2442-HydroxyisobutyrylationTNLGGAFKKDQDFDL
CCCCCCCCCCCCCCC		55.71-
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 EIF3J_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3J_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 EIF3J_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3B_YEASTPRT1physical
11179233
EIF3A_YEASTRPG1physical
11179233
EIF3G_YEASTTIF35physical
11179233
IF5_YEASTTIF5physical
11179233
SUI1_YEASTSUI1physical
11179233
EIF3A_YEASTRPG1genetic
10488093
EIF3C_YEASTNIP1physical
16429126
EIF3A_YEASTRPG1physical
16429126
RS18A_YEASTRPS18Aphysical
16429126
RS18B_YEASTRPS18Aphysical
16429126
RS8A_YEASTRPS8Aphysical
16429126
RS8B_YEASTRPS8Aphysical
16429126
EIF3G_YEASTTIF35physical
16429126
EIF3B_YEASTPRT1physical
16429126
EIF3B_YEASTPRT1physical
16581774
RIC1_YEASTRIC1genetic
19061648
YPT6_YEASTYPT6genetic
19061648
IF2A_YEASTSUI2genetic
19061648
NMD5_YEASTNMD5genetic
19061648
CSI1_YEASTCSI1genetic
19061648
FKBP_YEASTFPR1genetic
19061648
H2AZ_YEASTHTZ1genetic
19547744
SAC3_YEASTSAC3genetic
19547744
SLA1_YEASTSLA1genetic
20093466
RS14A_YEASTRPS14Agenetic
20093466
RL29_YEASTRPL29genetic
20093466
AAKG_YEASTSNF4genetic
20093466
PEX8_YEASTPEX8genetic
20093466
DBF2_YEASTDBF2genetic
20093466
ASK10_YEASTASK10genetic
20093466
FYV4_YEASTFYV4genetic
20093466
RPN10_YEASTRPN10genetic
20093466
PIR5_YEASTYJL160Cgenetic
20093466
PGM1_YEASTPGM1genetic
20093466
RM39_YEASTMRPL39genetic
20093466
MDM12_YEASTMDM12genetic
20093466
SHE4_YEASTSHE4genetic
20093466
SUR1_YEASTSUR1genetic
20093466
RS2_YEASTRPS2physical
20060839
RS23A_YEASTRPS23Aphysical
20060839
RS23B_YEASTRPS23Aphysical
20060839
IF1A_YEASTTIF11genetic
20060839
EIF3B_YEASTPRT1physical
20060839
EIF3A_YEASTRPG1physical
20584985
RPB4_YEASTRPB4physical
21074047
RPB7_YEASTRPB7physical
21074047
EIF3C_YEASTNIP1genetic
22123745
RS8A_YEASTRPS8Aphysical
23604635
RS8B_YEASTRPS8Aphysical
23604635
RLI1_YEASTRLI1genetic
24278036
EIF3A_YEASTRPG1physical
24278036
ERF3_YEASTSUP35physical
24278036
RLI1_YEASTRLI1physical
24278036
ERF1_YEASTSUP45physical
24278036
EIF3G_YEASTTIF35physical
24278036
ERF1_YEASTSUP45genetic
24278036
RL29_YEASTRPL29genetic
27708008
RL9A_YEASTRPL9Agenetic
27708008
SLA1_YEASTSLA1genetic
27708008
HAP3_YEASTHAP3genetic
27708008
MCFS2_YEASTEHT1genetic
27708008
RV161_YEASTRVS161genetic
27708008
RS14A_YEASTRPS14Agenetic
27708008
MTU1_YEASTSLM3genetic
27708008
PMP3_YEASTPMP3genetic
27708008
SNF1_YEASTSNF1genetic
27708008
AAKG_YEASTSNF4genetic
27708008
ATC1_YEASTPMR1genetic
27708008
MDM34_YEASTMDM34genetic
27708008
RTG2_YEASTRTG2genetic
27708008
PEX8_YEASTPEX8genetic
27708008
DBF2_YEASTDBF2genetic
27708008
RPN10_YEASTRPN10genetic
27708008
VPS53_YEASTVPS53genetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
MET5_YEASTMET5genetic
27708008
PGM1_YEASTPGM1genetic
27708008
RM49_YEASTMRP49genetic
27708008
COX12_YEASTCOX12genetic
27708008
ARPC3_YEASTARC18genetic
27708008
VIP1_YEASTVIP1genetic
27708008
RM39_YEASTMRPL39genetic
27708008
MSS1_YEASTMSS1genetic
27708008
PEX12_YEASTPEX12genetic
27708008
SCS7_YEASTSCS7genetic
27708008
EOS1_YEASTEOS1genetic
27708008
BRE5_YEASTBRE5genetic
27708008
MDM12_YEASTMDM12genetic
27708008
SUR1_YEASTSUR1genetic
27708008
RTC6_YEASTRTC6genetic
27708008
TMC1_YEASTTMC1genetic
27226598
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EIF3J_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; THR-75 AND SER-189,AND MASS SPECTROMETRY.
"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-65, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, AND MASSSPECTROMETRY.

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