EIF3B_HUMAN - dbPTM
EIF3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3B_HUMAN
UniProt AC P55884
Protein Name Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001}
Gene Name EIF3B {ECO:0000255|HAMAP-Rule:MF_03001}
Organism Homo sapiens (Human).
Sequence Length 814
Subcellular Localization Cytoplasm .
Protein Description RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. [PubMed: 9388245]
Protein Sequence MQDAENVAVPEAAEERAEPGQQQPAAEPPPAEGLLRPAGPGAPEAAGTEASSEEVGIAEAGPESEVRTEPAAEAEAASGPSESPSPPAAEELPGSHAEPPVPAQGEAPGEQARDERSDSRAQAVSEDAGGNEGRAAEAEPRALENGDADEPSFSDPEDFVDDVSEEELLGDVLKDRPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKITNDFYPEEDGKTKGYIFLEYASPAHAVDAVKNADGYKLDKQHTFRVNLFTDFDKYMTISDEWDIPEKQPFKDLGNLRYWLEEAECRDQYSVIFESGDRTSIFWNDVKDPVSIEERARWTETYVRWSPKGTYLATFHQRGIALWGGEKFKQIQRFSHQGVQLIDFSPCERYLVTFSPLMDTQDDPQAIIIWDILTGHKKRGFHCESSAHWPIFKWSHDGKFFARMTLDTLSIYETPSMGLLDKKSLKISGIKDFSWSPGGNIIAFWVPEDKDIPARVTLMQLPTRQEIRVRNLFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKETIIAFAWEPNGSKFAVLHGEAPRISVSFYHVKNNGKIELIKMFDKQQANTIFWSPQGQFVVLAGLRSMNGALAFVDTSDCTVMNIAEHYMASDVEWDPTGRYVVTSVSWWSHKVDNAYWLWTFQGRLLQKNNKDRFCQLLWRPRPPTLLSQEQIKQIKKDLKKYSKIFEQKDRLSQSKASKELVERRRTMMEDFRKYRKMAQELYMEQKNERLELRGGVDTDELDSNVDDWEEETIEFFVTEEIIPLGNQE
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
1Acetylation-------MQDAENVA
-------CCCHHHCC		8.0022223895
68PhosphorylationGPESEVRTEPAAEAE
CCCCCCCCCCHHHHH		52.0430278072
78PhosphorylationAAEAEAASGPSESPS
HHHHHHHCCCCCCCC		59.2823927012
81PhosphorylationAEAASGPSESPSPPA
HHHHCCCCCCCCCCH		54.9923927012
83PhosphorylationAASGPSESPSPPAAE
HHCCCCCCCCCCHHH		34.7125159151
85PhosphorylationSGPSESPSPPAAEEL
CCCCCCCCCCHHHCC		53.4423927012
95PhosphorylationAAEELPGSHAEPPVP
HHHCCCCCCCCCCCC		19.9930278072
117PhosphorylationEQARDERSDSRAQAV
HHHCCCCCCHHHHHH		37.5825159151
119PhosphorylationARDERSDSRAQAVSE
HCCCCCCHHHHHHHH		30.6620201521
125PhosphorylationDSRAQAVSEDAGGNE
CHHHHHHHHCCCCCC		32.5429255136
152PhosphorylationNGDADEPSFSDPEDF
CCCCCCCCCCCHHHH		35.0225159151
154PhosphorylationDADEPSFSDPEDFVD
CCCCCCCCCHHHHCC		57.5025159151
164PhosphorylationEDFVDDVSEEELLGD
HHHCCCCCHHHHHHH		46.4125159151
174AcetylationELLGDVLKDRPQEAD
HHHHHHHHCCCCCCC		52.09-
185PhosphorylationQEADGIDSVIVVDNV
CCCCCCCEEEEEECC		16.3028464451
202AcetylationVGPDRLEKLKNVIHK
CCHHHHHHHHHHHHH		70.1626051181
202UbiquitinationVGPDRLEKLKNVIHK
CCHHHHHHHHHHHHH		70.1621906983
202 (in isoform 1)Ubiquitination-70.1621890473
202 (in isoform 2)Ubiquitination-70.1621890473
204AcetylationPDRLEKLKNVIHKIF
HHHHHHHHHHHHHHH		61.3026210075
204UbiquitinationPDRLEKLKNVIHKIF
HHHHHHHHHHHHHHH		61.30-
209AcetylationKLKNVIHKIFSKFGK
HHHHHHHHHHHHHCC		34.0319608861
209UbiquitinationKLKNVIHKIFSKFGK
HHHHHHHHHHHHHCC		34.0321890473
209 (in isoform 1)Ubiquitination-34.0321890473
209 (in isoform 2)Ubiquitination-34.0321890473
212PhosphorylationNVIHKIFSKFGKITN
HHHHHHHHHHCCCCC		30.4624719451
213AcetylationVIHKIFSKFGKITND
HHHHHHHHHCCCCCC		47.6023749302
213UbiquitinationVIHKIFSKFGKITND
HHHHHHHHHCCCCCC		47.6021906983
213 (in isoform 1)Ubiquitination-47.6021890473
213 (in isoform 2)Ubiquitination-47.6021890473
216AcetylationKIFSKFGKITNDFYP
HHHHHHCCCCCCCCC		49.8725953088
216UbiquitinationKIFSKFGKITNDFYP
HHHHHHCCCCCCCCC		49.8721906983
216 (in isoform 1)Ubiquitination-49.8721890473
216 (in isoform 2)Ubiquitination-49.8721890473
218PhosphorylationFSKFGKITNDFYPEE
HHHHCCCCCCCCCCC		32.02-
228AcetylationFYPEEDGKTKGYIFL
CCCCCCCCEEEEEEE		60.4325953088
228MalonylationFYPEEDGKTKGYIFL
CCCCCCCCEEEEEEE		60.4326320211
228UbiquitinationFYPEEDGKTKGYIFL
CCCCCCCCEEEEEEE		60.43-
228 (in isoform 1)Ubiquitination-60.4321890473
228 (in isoform 2)Ubiquitination-60.4321890473
229PhosphorylationYPEEDGKTKGYIFLE
CCCCCCCEEEEEEEE		34.92-
230SumoylationPEEDGKTKGYIFLEY
CCCCCCEEEEEEEEE		53.88-
230UbiquitinationPEEDGKTKGYIFLEY
CCCCCCEEEEEEEEE		53.8821890473
230 (in isoform 1)Ubiquitination-53.8821890473
230 (in isoform 2)Ubiquitination-53.8821890473
232PhosphorylationEDGKTKGYIFLEYAS
CCCCEEEEEEEEECC		7.0528152594
232 (in isoform 2)Phosphorylation-7.0527642862
237PhosphorylationKGYIFLEYASPAHAV
EEEEEEEECCHHHHH		17.9628387310
237 (in isoform 2)Phosphorylation-17.9627642862
239PhosphorylationYIFLEYASPAHAVDA
EEEEEECCHHHHHHH		23.0130266825
248AcetylationAHAVDAVKNADGYKL
HHHHHHHHCCCCCCC		48.4126051181
248UbiquitinationAHAVDAVKNADGYKL
HHHHHHHHCCCCCCC		48.41-
253PhosphorylationAVKNADGYKLDKQHT
HHHCCCCCCCCCCCE		14.6628152594
254AcetylationVKNADGYKLDKQHTF
HHCCCCCCCCCCCEE		56.5925953088
254MalonylationVKNADGYKLDKQHTF
HHCCCCCCCCCCCEE		56.5926320211
254UbiquitinationVKNADGYKLDKQHTF
HHCCCCCCCCCCCEE		56.59-
254 (in isoform 1)Ubiquitination-56.5921890473
254 (in isoform 2)Ubiquitination-56.5921890473
257AcetylationADGYKLDKQHTFRVN
CCCCCCCCCCEEEEE		55.1823236377
257UbiquitinationADGYKLDKQHTFRVN
CCCCCCCCCCEEEEE		55.1821890473
257 (in isoform 1)Ubiquitination-55.1821890473
257 (in isoform 2)Ubiquitination-55.1821890473
267PhosphorylationTFRVNLFTDFDKYMT
EEEEEEECCHHHCCC		38.63-
272PhosphorylationLFTDFDKYMTISDEW
EECCHHHCCCCCCCC		11.01-
272 (in isoform 2)Phosphorylation-11.0127642862
284UbiquitinationDEWDIPEKQPFKDLG
CCCCCCCCCCCCCCC		58.9021906983
284 (in isoform 1)Ubiquitination-58.9021890473
284 (in isoform 2)Ubiquitination-58.9021890473
288AcetylationIPEKQPFKDLGNLRY
CCCCCCCCCCCCHHH		59.7419608861
288UbiquitinationIPEKQPFKDLGNLRY
CCCCCCCCCCCCHHH		59.7421890473
288 (in isoform 1)Ubiquitination-59.7421890473
288 (in isoform 2)Ubiquitination-59.7421890473
295 (in isoform 2)Phosphorylation-19.9427642862
306PhosphorylationEAECRDQYSVIFESG
HHHCCCEEEEEEECC		14.8128796482
306 (in isoform 2)Phosphorylation-14.8127642862
312PhosphorylationQYSVIFESGDRTSIF
EEEEEEECCCCCEEE		34.9321712546
317PhosphorylationFESGDRTSIFWNDVK
EECCCCCEEEECCCC		19.3825367160
324AcetylationSIFWNDVKDPVSIEE
EEEECCCCCCCCHHH		60.2126051181
324UbiquitinationSIFWNDVKDPVSIEE
EEEECCCCCCCCHHH		60.2120972266
324 (in isoform 1)Ubiquitination-60.2121890473
324 (in isoform 2)Ubiquitination-60.2121890473
328PhosphorylationNDVKDPVSIEERARW
CCCCCCCCHHHHHHC		29.6625367160
338PhosphorylationERARWTETYVRWSPK
HHHHCEEEEEEECCC		21.6827273156
339PhosphorylationRARWTETYVRWSPKG
HHHCEEEEEEECCCC		5.0428152594
343PhosphorylationTETYVRWSPKGTYLA
EEEEEEECCCCCEEE		13.2324719451
345AcetylationTYVRWSPKGTYLATF
EEEEECCCCCEEEEE		59.3726051181
345UbiquitinationTYVRWSPKGTYLATF
EEEEECCCCCEEEEE		59.3721890473
345 (in isoform 1)Ubiquitination-59.3721890473
345 (in isoform 2)Ubiquitination-59.3721890473
347PhosphorylationVRWSPKGTYLATFHQ
EEECCCCCEEEEEEC		22.8428152594
348PhosphorylationRWSPKGTYLATFHQR
EECCCCCEEEEEECC		11.7428152594
364AcetylationIALWGGEKFKQIQRF
EEEECCHHHHHHHHH		62.2219608861
364UbiquitinationIALWGGEKFKQIQRF
EEEECCHHHHHHHHH		62.2219608861
364 (in isoform 1)Ubiquitination-62.2221890473
364 (in isoform 2)Ubiquitination-62.2221890473
366 (in isoform 2)Ubiquitination-58.52-
372PhosphorylationFKQIQRFSHQGVQLI
HHHHHHHCCCCEEEE		19.6527050516
390PhosphorylationPCERYLVTFSPLMDT
CCCEEEEEECCCCCC		18.7927362937
392PhosphorylationERYLVTFSPLMDTQD
CEEEEEECCCCCCCC		14.0427362937
397PhosphorylationTFSPLMDTQDDPQAI
EECCCCCCCCCCCEE		21.6727362937
416MethylationILTGHKKRGFHCESS
CCCCCCCCCCCCCCC		58.79-
422PhosphorylationKRGFHCESSAHWPIF
CCCCCCCCCCCCCEE		37.9120873877
423PhosphorylationRGFHCESSAHWPIFK
CCCCCCCCCCCCEEE		11.2320873877
436AcetylationFKWSHDGKFFARMTL
EEECCCCCEEEEEEE		43.2819608861
442PhosphorylationGKFFARMTLDTLSIY
CCEEEEEEECHHEEE		18.8728102081
445PhosphorylationFARMTLDTLSIYETP
EEEEEECHHEEEECC		26.0528442448
447PhosphorylationRMTLDTLSIYETPSM
EEEECHHEEEECCCC		25.8026356563
449NitrationTLDTLSIYETPSMGL
EECHHEEEECCCCCC		15.46-
449PhosphorylationTLDTLSIYETPSMGL
EECHHEEEECCCCCC		15.4627273156
449 (in isoform 2)Phosphorylation-15.4627642862
451PhosphorylationDTLSIYETPSMGLLD
CHHEEEECCCCCCCC		12.0526356563
453PhosphorylationLSIYETPSMGLLDKK
HEEEECCCCCCCCCC		32.6628442448
459AcetylationPSMGLLDKKSLKISG
CCCCCCCCCCCEECC		44.2026051181
459UbiquitinationPSMGLLDKKSLKISG
CCCCCCCCCCCEECC		44.20-
460UbiquitinationSMGLLDKKSLKISGI
CCCCCCCCCCEECCC		61.77-
460 (in isoform 2)Ubiquitination-61.77-
461PhosphorylationMGLLDKKSLKISGIK
CCCCCCCCCEECCCC		40.41-
463AcetylationLLDKKSLKISGIKDF
CCCCCCCEECCCCCC		41.7525953088
463MalonylationLLDKKSLKISGIKDF
CCCCCCCEECCCCCC		41.7526320211
463UbiquitinationLLDKKSLKISGIKDF
CCCCCCCEECCCCCC		41.75-
463 (in isoform 2)Ubiquitination-41.75-
465PhosphorylationDKKSLKISGIKDFSW
CCCCCEECCCCCCCC		32.64-
473PhosphorylationGIKDFSWSPGGNIIA
CCCCCCCCCCCCEEE		16.69-
487UbiquitinationAFWVPEDKDIPARVT
EEECCCCCCCCCEEE		56.76-
496SulfoxidationIPARVTLMQLPTRQE
CCCEEEEEECCCCHH		2.5521406390
500PhosphorylationVTLMQLPTRQEIRVR
EEEEECCCCHHEHHH		54.2820068231
515GlutathionylationNLFNVVDCKLHWQKN
HCCCEEECEEECEEC		3.2322555962
516AcetylationLFNVVDCKLHWQKNG
CCCEEECEEECEECC		38.6325953088
516UbiquitinationLFNVVDCKLHWQKNG
CCCEEECEEECEECC		38.6321890473
516 (in isoform 1)Ubiquitination-38.6321890473
516 (in isoform 2)Ubiquitination-38.6321890473
521AcetylationDCKLHWQKNGDYLCV
ECEEECEECCCEEEE		58.6725953088
521UbiquitinationDCKLHWQKNGDYLCV
ECEEECEECCCEEEE		58.67-
521 (in isoform 2)Ubiquitination-58.67-
525PhosphorylationHWQKNGDYLCVKVDR
ECEECCCEEEEEECC		11.9128152594
529AcetylationNGDYLCVKVDRTPKG
CCCEEEEEECCCCCC		37.1025953088
529UbiquitinationNGDYLCVKVDRTPKG
CCCEEEEEECCCCCC		37.10-
529 (in isoform 2)Ubiquitination-37.10-
535UbiquitinationVKVDRTPKGTQGVVT
EEECCCCCCCCCEEE		74.1721139048
535 (in isoform 1)Ubiquitination-74.1721890473
535 (in isoform 2)Ubiquitination-74.1721890473
537PhosphorylationVDRTPKGTQGVVTNF
ECCCCCCCCCEEECE		28.4227050516
552AcetylationEIFRMREKQVPVDVV
EEEEECCCCCCCEEE		46.3525953088
552UbiquitinationEIFRMREKQVPVDVV
EEEEECCCCCCCEEE		46.3521890473
552 (in isoform 1)Ubiquitination-46.3521890473
552 (in isoform 2)Ubiquitination-46.3521890473
561SulfoxidationVPVDVVEMKETIIAF
CCCEEEECCCEEEEE		3.0030846556
575PhosphorylationFAWEPNGSKFAVLHG
EEECCCCCEEEEEEC		31.1020068231
595MalonylationSVSFYHVKNNGKIEL
EEEEEEEEECCEEEE		31.2326320211
599AcetylationYHVKNNGKIELIKMF
EEEEECCEEEEEEEC		34.8226051181
599UbiquitinationYHVKNNGKIELIKMF
EEEEECCEEEEEEEC		34.8221906983
599 (in isoform 1)Ubiquitination-34.8221890473
599 (in isoform 2)Ubiquitination-34.8221890473
604AcetylationNGKIELIKMFDKQQA
CCEEEEEEECCHHHC		46.2526051181
604UbiquitinationNGKIELIKMFDKQQA
CCEEEEEEECCHHHC		46.2521890473
604 (in isoform 1)Ubiquitination-46.2521890473
604 (in isoform 2)Ubiquitination-46.2521890473
608UbiquitinationELIKMFDKQQANTIF
EEEEECCHHHCCEEE		32.8021906983
608 (in isoform 1)Ubiquitination-32.8021890473
608 (in isoform 2)Ubiquitination-32.8021890473
693AcetylationFQGRLLQKNNKDRFC
EHHHHHHHCCCCCCH		63.5625953088
693UbiquitinationFQGRLLQKNNKDRFC
EHHHHHHHCCCCCCH		63.56-
710PhosphorylationLWRPRPPTLLSQEQI
HCCCCCCCCCCHHHH		42.9123312004
713PhosphorylationPRPPTLLSQEQIKQI
CCCCCCCCHHHHHHH		34.4823312004
718AcetylationLLSQEQIKQIKKDLK
CCCHHHHHHHHHHHH		45.7426051181
718UbiquitinationLLSQEQIKQIKKDLK
CCCHHHHHHHHHHHH		45.7421890473
718 (in isoform 1)Ubiquitination-45.7421890473
718 (in isoform 2)Ubiquitination-45.7421890473
726UbiquitinationQIKKDLKKYSKIFEQ
HHHHHHHHHHHHHHH		63.15-
726 (in isoform 2)Ubiquitination-63.15-
727PhosphorylationIKKDLKKYSKIFEQK
HHHHHHHHHHHHHHH		17.3820068231
728PhosphorylationKKDLKKYSKIFEQKD
HHHHHHHHHHHHHHH		28.3120068231
729AcetylationKDLKKYSKIFEQKDR
HHHHHHHHHHHHHHH		48.6125953088
729UbiquitinationKDLKKYSKIFEQKDR
HHHHHHHHHHHHHHH		48.6121890473
729 (in isoform 1)Ubiquitination-48.6121890473
729 (in isoform 2)Ubiquitination-48.6121890473
734AcetylationYSKIFEQKDRLSQSK
HHHHHHHHHHHCHHH		37.3025953088
734UbiquitinationYSKIFEQKDRLSQSK
HHHHHHHHHHHCHHH		37.30-
734 (in isoform 2)Ubiquitination-37.30-
738PhosphorylationFEQKDRLSQSKASKE
HHHHHHHCHHHHHHH		33.0523403867
740PhosphorylationQKDRLSQSKASKELV
HHHHHCHHHHHHHHH		27.1523403867
741UbiquitinationKDRLSQSKASKELVE
HHHHCHHHHHHHHHH		49.39-
743PhosphorylationRLSQSKASKELVERR
HHCHHHHHHHHHHHH		30.3323403867
744AcetylationLSQSKASKELVERRR
HCHHHHHHHHHHHHH		60.9820167786
744UbiquitinationLSQSKASKELVERRR
HCHHHHHHHHHHHHH		60.9821890473
744 (in isoform 1)Ubiquitination-60.9821890473
744 (in isoform 2)Ubiquitination-60.9821890473
752PhosphorylationELVERRRTMMEDFRK
HHHHHHHHHHHHHHH		21.0428555341
758DimethylationRTMMEDFRKYRKMAQ
HHHHHHHHHHHHHHH		47.63-
758MethylationRTMMEDFRKYRKMAQ
HHHHHHHHHHHHHHH		47.63-
762UbiquitinationEDFRKYRKMAQELYM
HHHHHHHHHHHHHHH		35.1821906983
762 (in isoform 1)Ubiquitination-35.1821890473
762 (in isoform 2)Ubiquitination-35.1821890473
763SulfoxidationDFRKYRKMAQELYME
HHHHHHHHHHHHHHH		3.2630846556
768PhosphorylationRKMAQELYMEQKNER
HHHHHHHHHHHHHHH		9.61-
768 (in isoform 2)Phosphorylation-9.6127642862
769SulfoxidationKMAQELYMEQKNERL
HHHHHHHHHHHHHHH		7.4130846556
772UbiquitinationQELYMEQKNERLELR
HHHHHHHHHHHHEEC		47.682190698
772 (in isoform 1)Ubiquitination-47.6821890473
772 (in isoform 2)Ubiquitination-47.6821890473
789PhosphorylationVDTDELDSNVDDWEE
CCHHHHCCCCCCCHH		51.9122468782
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 EIF3B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3B_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 EIF3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4A1_HUMANEIF4A1physical
16541103
IF4B_HUMANEIF4Bphysical
16286006
IF4E_HUMANEIF4Ephysical
16541103
IF4G1_HUMANEIF4G1physical
16541103
MTOR_HUMANMTORphysical
16286006
RS6_HUMANRPS6physical
16286006
KS6B1_HUMANRPS6KB1physical
16286006
EIF3A_HUMANEIF3Aphysical
16541103
EIF3C_HUMANEIF3Cphysical
15946946
EIF3I_HUMANEIF3Iphysical
16541103
EIF3J_HUMANEIF3Jphysical
15946946
RPTOR_HUMANRPTORphysical
16286006
EIF3G_HUMANEIF3Gphysical
9822659
EIF3E_HUMANEIF3Ephysical
18599441
EIF3F_HUMANEIF3Fphysical
18599441
EIF3H_HUMANEIF3Hphysical
18599441
EIF3K_HUMANEIF3Kphysical
18599441
EIF3L_HUMANEIF3Lphysical
18599441
EIF3M_HUMANEIF3Mphysical
18599441
MTOR_HUMANMTORphysical
21045808
RPTOR_HUMANRPTORphysical
21045808
EIF3F_HUMANEIF3Fphysical
19245811
EIF3C_HUMANEIF3Cphysical
19245811
EIF3A_HUMANEIF3Aphysical
19245811
EIF3I_HUMANEIF3Iphysical
22939629
EIF3G_HUMANEIF3Gphysical
22939629
EIF3C_HUMANEIF3Cphysical
22939629
EIF3H_HUMANEIF3Hphysical
22939629
EIF3F_HUMANEIF3Fphysical
22939629
EIF3D_HUMANEIF3Dphysical
22939629
EIF3E_HUMANEIF3Ephysical
22939629
EIF3K_HUMANEIF3Kphysical
22939629
EIF3L_HUMANEIF3Lphysical
22939629
IF5_HUMANEIF5physical
22939629
EIF3M_HUMANEIF3Mphysical
22939629
EIF3A_HUMANEIF3Aphysical
18628297
EIF3C_HUMANEIF3Cphysical
18628297
EIF3D_HUMANEIF3Dphysical
18628297
DDX3X_HUMANDDX3Xphysical
18628297
EIF3E_HUMANEIF3Ephysical
18628297
EIF3F_HUMANEIF3Fphysical
18628297
EIF3G_HUMANEIF3Gphysical
18628297
EIF3H_HUMANEIF3Hphysical
18628297
EIF3I_HUMANEIF3Iphysical
18628297
EIF3J_HUMANEIF3Jphysical
18628297
EIF3K_HUMANEIF3Kphysical
18628297
KS6B1_HUMANRPS6KB1physical
18423201
MTOR_HUMANMTORphysical
18423201
NCBP1_HUMANNCBP1physical
18423201
IF4E_HUMANEIF4Ephysical
18423201
ATLA3_HUMANATL3physical
26344197
VA0D1_HUMANATP6V0D1physical
26344197
EIF3D_HUMANEIF3Dphysical
26344197
EIF3I_HUMANEIF3Iphysical
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 EIF3B_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-78 AND SER-85, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209; LYS-288; LYS-364 ANDLYS-436, AND MASS 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-152; SER-154 ANDSER-164, AND MASS SPECTROMETRY.
"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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-78 AND SER-85, 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-78; SER-81; SER-83;SER-85; SER-125 AND SER-239, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.
"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, ACETYLATION, PHOSPHORYLATION AT SER-83; SER-85; SER-119;SER-125; SER-152; SER-154 AND SER-164, AND MASS SPECTROMETRY.
"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-152; SER-154 ANDSER-164, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85 AND SER-125,AND MASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-525, AND MASSSPECTROMETRY.

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