EIF3J_HUMAN - dbPTM
EIF3J_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3J_HUMAN
UniProt AC O75822
Protein Name Eukaryotic translation initiation factor 3 subunit J {ECO:0000255|HAMAP-Rule:MF_03009}
Gene Name EIF3J {ECO:0000255|HAMAP-Rule:MF_03009}
Organism Homo sapiens (Human).
Sequence Length 258
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. [PubMed: 25849773]
Protein Sequence MAAAAAAAGDSDSWDADAFSVEDPVRKVGGGGTAGGDRWEGEDEDEDVKDNWDDDDDEKKEEAEVKPEVKISEKKKIAEKIKEKERQQKKRQEEIKKRLEEPEEPKVLTPEEQLADKLRLKKLQEESDLELAKETFGVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISLEIDDLKKITNSLTVLCSEKQKQEKQSKAKKKKKGVVPGGGLKATMKDDLADYGGYDGGYVQDYEDFM
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
2Acetylation------MAAAAAAAG
------CCHHHHHCC		13.0517322308
11PhosphorylationAAAAAGDSDSWDADA
HHHHCCCCCCCCCCC		32.4029255136
13PhosphorylationAAAGDSDSWDADAFS
HHCCCCCCCCCCCCC		30.7029255136
20PhosphorylationSWDADAFSVEDPVRK
CCCCCCCCCCCCCEE		26.7322167270
27UbiquitinationSVEDPVRKVGGGGTA
CCCCCCEECCCCCCC		45.53-
27AcetylationSVEDPVRKVGGGGTA
CCCCCCEECCCCCCC		45.5321339330
33PhosphorylationRKVGGGGTAGGDRWE
EECCCCCCCCCCCCC		25.9625159151
38MethylationGGTAGGDRWEGEDED
CCCCCCCCCCCCCCC		36.30-
60 (in isoform 3)Phosphorylation-59.7525159151
72PhosphorylationVKPEVKISEKKKIAE
CCCCCCHHHHHHHHH		37.3325159151
74AcetylationPEVKISEKKKIAEKI
CCCCHHHHHHHHHHH		53.2125953088
80AcetylationEKKKIAEKIKEKERQ
HHHHHHHHHHHHHHH		50.4825953088
106SumoylationLEEPEEPKVLTPEEQ
HCCCCCCCCCCHHHH		53.8328112733
106AcetylationLEEPEEPKVLTPEEQ
HCCCCCCCCCCHHHH		53.8323236377
106AcetylationLEEPEEPKVLTPEEQ
HCCCCCCCCCCHHHH		53.83-
109PhosphorylationPEEPKVLTPEEQLAD
CCCCCCCCHHHHHHH		31.4819664994
112UbiquitinationPKVLTPEEQLADKLR
CCCCCHHHHHHHHHH		52.69-
117UbiquitinationPEEQLADKLRLKKLQ
HHHHHHHHHHHHHHH		29.87-
117AcetylationPEEQLADKLRLKKLQ
HHHHHHHHHHHHHHH		29.87-
117UbiquitinationPEEQLADKLRLKKLQ
HHHHHHHHHHHHHHH		29.87-
1172-HydroxyisobutyrylationPEEQLADKLRLKKLQ
HHHHHHHHHHHHHHH		29.87-
117MalonylationPEEQLADKLRLKKLQ
HHHHHHHHHHHHHHH		29.8726320211
117UbiquitinationPEEQLADKLRLKKLQ
HHHHHHHHHHHHHHH		29.87-
117AcetylationPEEQLADKLRLKKLQ
HHHHHHHHHHHHHHH		29.8723954790
122UbiquitinationADKLRLKKLQEESDL
HHHHHHHHHHHHHCH		61.05-
127PhosphorylationLKKLQEESDLELAKE
HHHHHHHHCHHHHHH		46.9029255136
127 (in isoform 2)Phosphorylation-46.9029507054
133UbiquitinationESDLELAKETFGVNN
HHCHHHHHHHHCCCC		70.66-
135PhosphorylationDLELAKETFGVNNAV
CHHHHHHHHCCCCCE		25.6122210691
143PhosphorylationFGVNNAVYGIDAMNP
HCCCCCEECCCCCCC		13.1222210691
148SulfoxidationAVYGIDAMNPSSRDD
CEECCCCCCCCCCCC		7.2230846556
151PhosphorylationGIDAMNPSSRDDFTE
CCCCCCCCCCCCHHH		32.7622210691
152PhosphorylationIDAMNPSSRDDFTEF
CCCCCCCCCCCHHHH		40.7722210691
157PhosphorylationPSSRDDFTEFGKLLK
CCCCCCHHHHHHHHH		37.08-
161UbiquitinationDDFTEFGKLLKDKIT
CCHHHHHHHHHHHHH		56.8421890473
1612-HydroxyisobutyrylationDDFTEFGKLLKDKIT
CCHHHHHHHHHHHHH		56.84-
166UbiquitinationFGKLLKDKITQYEKS
HHHHHHHHHHHHHHH		46.17-
1662-HydroxyisobutyrylationFGKLLKDKITQYEKS
HHHHHHHHHHHHHHH		46.17-
168PhosphorylationKLLKDKITQYEKSLY
HHHHHHHHHHHHHHH		30.7328152594
170PhosphorylationLKDKITQYEKSLYYA
HHHHHHHHHHHHHHH		19.3728152594
175PhosphorylationTQYEKSLYYASFLEV
HHHHHHHHHHHHHHH		12.2222817900
197AcetylationSLEIDDLKKITNSLT
CCCHHHHHHHHHHHH		49.4726051181
198AcetylationLEIDDLKKITNSLTV
CCHHHHHHHHHHHHH		63.1626051181
200PhosphorylationIDDLKKITNSLTVLC
HHHHHHHHHHHHHHC		27.8627732954
202PhosphorylationDLKKITNSLTVLCSE
HHHHHHHHHHHHCCH		19.4327732954
204PhosphorylationKKITNSLTVLCSEKQ
HHHHHHHHHHCCHHH		15.9727732954
207GlutathionylationTNSLTVLCSEKQKQE
HHHHHHHCCHHHHHH		4.2522555962
207S-nitrosylationTNSLTVLCSEKQKQE
HHHHHHHCCHHHHHH		4.2519483679
207S-nitrosocysteineTNSLTVLCSEKQKQE
HHHHHHHCCHHHHHH		4.25-
208PhosphorylationNSLTVLCSEKQKQEK
HHHHHHCCHHHHHHH		43.6025159151
210AcetylationLTVLCSEKQKQEKQS
HHHHCCHHHHHHHHH		46.6425953088
220AcetylationQEKQSKAKKKKKGVV
HHHHHHHHHHCCCCC		69.7130588407
221AcetylationEKQSKAKKKKKGVVP
HHHHHHHHHCCCCCC		74.7630588413
222AcetylationKQSKAKKKKKGVVPG
HHHHHHHHCCCCCCC		60.0430588419
223AcetylationQSKAKKKKKGVVPGG
HHHHHHHCCCCCCCC		64.7330588425
224UbiquitinationSKAKKKKKGVVPGGG
HHHHHHCCCCCCCCC		66.86-
233MethylationVVPGGGLKATMKDDL
CCCCCCHHHCCCCHH		45.12-
233UbiquitinationVVPGGGLKATMKDDL
CCCCCCHHHCCCCHH		45.12-
235PhosphorylationPGGGLKATMKDDLAD
CCCCHHHCCCCHHHH		24.1427642862
237MethylationGGLKATMKDDLADYG
CCHHHCCCCHHHHHC		43.68-
243PhosphorylationMKDDLADYGGYDGGY
CCCHHHHHCCCCCCC		13.5726552605
246PhosphorylationDLADYGGYDGGYVQD
HHHHHCCCCCCCCCC		13.6726552605
250PhosphorylationYGGYDGGYVQDYEDF
HCCCCCCCCCCHHHH		10.6426552605
254PhosphorylationDGGYVQDYEDFM---
CCCCCCCHHHHC---		10.5828112733
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
127SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3J_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPYL2_HUMANDPYSL2physical
22863883
TTC1_HUMANTTC1physical
22863883
HNRPU_HUMANHNRNPUphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EIF3J_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11; SER-13 AND THR-109, AND MASS SPECTROMETRY.
"Structural characterization of the human eukaryotic initiation factor3 protein complex by mass spectrometry.";
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
Mol. Cell. Proteomics 6:1135-1146(2007).
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,PHOSPHORYLATION AT SER-11; SER-13; SER-20 AND THR-109, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109; SER-127 ANDTYR-254, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11; SER-13 AND THR-109, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109 AND SER-127, ANDMASS SPECTROMETRY.
"Structural characterization of the human eukaryotic initiation factor3 protein complex by mass spectrometry.";
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
Mol. Cell. Proteomics 6:1135-1146(2007).
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,PHOSPHORYLATION AT SER-11; SER-13; SER-20 AND THR-109, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-13, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND MASSSPECTROMETRY.

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