EIF3K_HUMAN - dbPTM
EIF3K_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3K_HUMAN
UniProt AC Q9UBQ5
Protein Name Eukaryotic translation initiation factor 3 subunit K {ECO:0000255|HAMAP-Rule:MF_03010}
Gene Name EIF3K {ECO:0000255|HAMAP-Rule:MF_03010}
Organism Homo sapiens (Human).
Sequence Length 218
Subcellular Localization Nucleus . 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: 17581632]
Protein Sequence MAMFEQMRANVGKLLKGIDRYNPENLATLERYVETQAKENAYDLEANLAVLKLYQFNPAFFQTTVTAQILLKALTNLPHTDFTLCKCMIDQAHQEERPIRQILYLGDLLETCHFQAFWQALDENMDLLEGITGFEDSVRKFICHVVGITYQHIDRWLLAEMLGDLSDSQLKVWMSKYGWSADESGQIFICSQEESIKPKNIVEKIDFDSVSSIMASSQ
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------MAMFEQMRA
------CHHHHHHHH		16.0417322308
13AcetylationQMRANVGKLLKGIDR
HHHHHHHHHHHCHHH		46.49-
13UbiquitinationQMRANVGKLLKGIDR
HHHHHHHHHHHCHHH		46.4921890473
13SumoylationQMRANVGKLLKGIDR
HHHHHHHHHHHCHHH		46.49-
13MalonylationQMRANVGKLLKGIDR
HHHHHHHHHHHCHHH		46.4926320211
13AcetylationQMRANVGKLLKGIDR
HHHHHHHHHHHCHHH		46.4923749302
13SumoylationQMRANVGKLLKGIDR
HHHHHHHHHHHCHHH		46.49-
13UbiquitinationQMRANVGKLLKGIDR
HHHHHHHHHHHCHHH		46.4921890473
132-HydroxyisobutyrylationQMRANVGKLLKGIDR
HHHHHHHHHHHCHHH		46.49-
16UbiquitinationANVGKLLKGIDRYNP
HHHHHHHHCHHHCCH		65.3421906983
16UbiquitinationANVGKLLKGIDRYNP
HHHHHHHHCHHHCCH		65.3421890473
16AcetylationANVGKLLKGIDRYNP
HHHHHHHHCHHHCCH		65.3427452117
21PhosphorylationLLKGIDRYNPENLAT
HHHCHHHCCHHHHHH		31.1828152594
28PhosphorylationYNPENLATLERYVET
CCHHHHHHHHHHHHH		32.1128450419
32PhosphorylationNLATLERYVETQAKE
HHHHHHHHHHHHHHH		8.0226074081
35PhosphorylationTLERYVETQAKENAY
HHHHHHHHHHHHHCC		24.6326074081
38UbiquitinationRYVETQAKENAYDLE
HHHHHHHHHHCCHHH		41.5021890473
38UbiquitinationRYVETQAKENAYDLE
HHHHHHHHHHCCHHH		41.5021890473
42PhosphorylationTQAKENAYDLEANLA
HHHHHHCCHHHHHHH		32.4226074081
52SumoylationEANLAVLKLYQFNPA
HHHHHHHHHHHCCCH		38.25-
86UbiquitinationHTDFTLCKCMIDQAH
CCCHHHHHHHHHHHH		29.92-
140UbiquitinationGFEDSVRKFICHVVG
CCHHHHHHHHHHHHC		36.6021890473
140AcetylationGFEDSVRKFICHVVG
CCHHHHHHHHHHHHC		36.6026051181
166PhosphorylationAEMLGDLSDSQLKVW
HHHHCCCCHHHHHHH		39.70-
197UbiquitinationCSQEESIKPKNIVEK
ECCCCCCCCCCHHHH		60.25-
199UbiquitinationQEESIKPKNIVEKID
CCCCCCCCCHHHHCC		55.06-
204SumoylationKPKNIVEKIDFDSVS
CCCCHHHHCCHHHHH		36.36-
204UbiquitinationKPKNIVEKIDFDSVS
CCCCHHHHCCHHHHH		36.36-
209PhosphorylationVEKIDFDSVSSIMAS
HHHCCHHHHHHHHHC		24.7220873877
211PhosphorylationKIDFDSVSSIMASSQ
HCCHHHHHHHHHCCC		20.3520068231
212PhosphorylationIDFDSVSSIMASSQ-
CCHHHHHHHHHCCC-		17.7720068231
216PhosphorylationSVSSIMASSQ-----
HHHHHHHCCC-----		16.3430266825
217PhosphorylationVSSIMASSQ------
HHHHHHCCC------		30.3025159151
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 EIF3K_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3K_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 EIF3K_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3L_HUMANEIF3Lphysical
16189514
CCND3_HUMANCCND3physical
15327989
EIF3J_HUMANEIF3Jphysical
14519125
EIF3G_HUMANEIF3Gphysical
14519125
EIF3C_HUMANEIF3Cphysical
14519125
EIF3B_HUMANEIF3Bphysical
18599441
EIF3L_HUMANEIF3Lphysical
22939629
EIF3M_HUMANEIF3Mphysical
22939629
RACK1_HUMANGNB2L1physical
22863883
LARP1_HUMANLARP1physical
22863883
MTAP2_HUMANMAP2physical
22863883
WNK1_HUMANWNK1physical
22863883
YBOX1_HUMANYBX1physical
22863883
EIF3L_HUMANEIF3Lphysical
25416956
EIF3B_HUMANEIF3Bphysical
26344197
EIF3C_HUMANEIF3Cphysical
26344197
EIFCL_HUMANEIF3CLphysical
26344197
EIF3D_HUMANEIF3Dphysical
26344197
UTP15_HUMANUTP15physical
26344197
EIF3L_HUMANEIF3Lphysical
21516116
GELS_HUMANGSNphysical
27173435
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EIF3K_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-217, 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, ANDMASS SPECTROMETRY.
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 SER-217, 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-217, 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 SER-217, 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-217, AND MASSSPECTROMETRY.

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