EIF3M_HUMAN - dbPTM
EIF3M_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3M_HUMAN
UniProt AC Q7L2H7
Protein Name Eukaryotic translation initiation factor 3 subunit M {ECO:0000255|HAMAP-Rule:MF_03012}
Gene Name EIF3M {ECO:0000255|HAMAP-Rule:MF_03012}
Organism Homo sapiens (Human).
Sequence Length 374
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: 17403899]
Protein Sequence MSVPAFIDISEEDQAAELRAYLKSKGAEISEENSEGGLHVDLAQIIEACDVCLKEDDKDVESVMNSVVSLLLILEPDKQEALIESLCEKLVKFREGERPSLRLQLLSNLFHGMDKNTPVRYTVYCSLIKVAASCGAIQYIPTELDQVRKWISDWNLTTEKKHTLLRLLYEALVDCKKSDAASKVMVELLGSYTEDNASQARVDAHRCIVRALKDPNAFLFDHLLTLKPVKFLEGELIHDLLTIFVSAKLASYVKFYQNNKDFIDSLGLLHEQNMAKMRLLTFMGMAVENKEISFDTMQQELQIGADDVEAFVIDAVRTKMVYCKIDQTQRKVVVSHSTHRTFGKQQWQQLYDTLNAWKQNLNKVKNSLLSLSDT
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------MSVPAFIDI
------CCCCCEEEC		36.4919664995
2Phosphorylation------MSVPAFIDI
------CCCCCEEEC		36.4925693802
10PhosphorylationVPAFIDISEEDQAAE
CCCEEECCHHHHHHH		31.0522199227
17UbiquitinationSEEDQAAELRAYLKS
CHHHHHHHHHHHHHH		41.63-
17UbiquitinationSEEDQAAELRAYLKS
CHHHHHHHHHHHHHH		41.6321890473
23UbiquitinationAELRAYLKSKGAEIS
HHHHHHHHHCCCCCC		37.1327667366
28UbiquitinationYLKSKGAEISEENSE
HHHHCCCCCCCHHCC		56.57-
28UbiquitinationYLKSKGAEISEENSE
HHHHCCCCCCCHHCC		56.5721963094
29UbiquitinationLKSKGAEISEENSEG
HHHCCCCCCCHHCCC		6.60-
29UbiquitinationLKSKGAEISEENSEG
HHHCCCCCCCHHCCC		6.6022817900
44UbiquitinationGLHVDLAQIIEACDV
CCCCCHHHHHHHHCH		44.48-
44UbiquitinationGLHVDLAQIIEACDV
CCCCCHHHHHHHHCH		44.4821963094
45UbiquitinationLHVDLAQIIEACDVC
CCCCHHHHHHHHCHH		2.27-
45UbiquitinationLHVDLAQIIEACDVC
CCCCHHHHHHHHCHH		2.2722817900
51UbiquitinationQIIEACDVCLKEDDK
HHHHHHCHHCCCCCC		4.07-
51UbiquitinationQIIEACDVCLKEDDK
HHHHHHCHHCCCCCC		4.0722817900
52UbiquitinationIIEACDVCLKEDDKD
HHHHHCHHCCCCCCC		2.6123000965
81AcetylationLEPDKQEALIESLCE
CCCCHHHHHHHHHHH		16.02-
81UbiquitinationLEPDKQEALIESLCE
CCCCHHHHHHHHHHH		16.02-
81AcetylationLEPDKQEALIESLCE
CCCCHHHHHHHHHHH		16.0219608861
81UbiquitinationLEPDKQEALIESLCE
CCCCHHHHHHHHHHH		16.0221963094
86UbiquitinationQEALIESLCEKLVKF
HHHHHHHHHHHHHHH		2.5821890473
89UbiquitinationLIESLCEKLVKFREG
HHHHHHHHHHHHCCC		58.5529967540
95UbiquitinationEKLVKFREGERPSLR
HHHHHHCCCCCCHHH		69.41-
95UbiquitinationEKLVKFREGERPSLR
HHHHHHCCCCCCHHH		69.4121963094
97UbiquitinationLVKFREGERPSLRLQ
HHHHCCCCCCHHHHH		57.5821963094
98UbiquitinationVKFREGERPSLRLQL
HHHCCCCCCHHHHHH		36.6422817900
113UbiquitinationLSNLFHGMDKNTPVR
HHHHHCCCCCCCCCC		5.0721963094
114UbiquitinationSNLFHGMDKNTPVRY
HHHHCCCCCCCCCCH		45.7222817900
115UbiquitinationNLFHGMDKNTPVRYT
HHHCCCCCCCCCCHH		54.5521890473
115AcetylationNLFHGMDKNTPVRYT
HHHCCCCCCCCCCHH		54.5525953088
115UbiquitinationNLFHGMDKNTPVRYT
HHHCCCCCCCCCCHH		54.5523000965
116UbiquitinationLFHGMDKNTPVRYTV
HHCCCCCCCCCCHHH		45.4023000965
120UbiquitinationMDKNTPVRYTVYCSL
CCCCCCCCHHHHHHH		23.7022817900
121PhosphorylationDKNTPVRYTVYCSLI
CCCCCCCHHHHHHHH		10.7828152594
122UbiquitinationKNTPVRYTVYCSLIK
CCCCCCHHHHHHHHH		8.40-
122AcetylationKNTPVRYTVYCSLIK
CCCCCCHHHHHHHHH		8.4019608861
122PhosphorylationKNTPVRYTVYCSLIK
CCCCCCHHHHHHHHH		8.4028152594
122UbiquitinationKNTPVRYTVYCSLIK
CCCCCCHHHHHHHHH		8.4023000965
126PhosphorylationVRYTVYCSLIKVAAS
CCHHHHHHHHHHHHH		18.5524719451
128UbiquitinationYTVYCSLIKVAASCG
HHHHHHHHHHHHHCC		1.62-
128UbiquitinationYTVYCSLIKVAASCG
HHHHHHHHHHHHHCC		1.6223000965
139PhosphorylationASCGAIQYIPTELDQ
HHCCCHHCCCCCHHH		11.6228152594
142PhosphorylationGAIQYIPTELDQVRK
CCHHCCCCCHHHHHH		39.3528152594
144UbiquitinationIQYIPTELDQVRKWI
HHCCCCCHHHHHHHH		6.5029967540
149UbiquitinationTELDQVRKWISDWNL
CCHHHHHHHHHCCCC		50.4521890473
149AcetylationTELDQVRKWISDWNL
CCHHHHHHHHHCCCC		50.4526051181
149UbiquitinationTELDQVRKWISDWNL
CCHHHHHHHHHCCCC		50.4522817900
150UbiquitinationELDQVRKWISDWNLT
CHHHHHHHHHCCCCC		5.6921890473
152PhosphorylationDQVRKWISDWNLTTE
HHHHHHHHCCCCCHH		35.1422617229
157PhosphorylationWISDWNLTTEKKHTL
HHHCCCCCHHHHHHH		29.6926074081
158PhosphorylationISDWNLTTEKKHTLL
HHCCCCCHHHHHHHH		49.3126074081
1602-HydroxyisobutyrylationDWNLTTEKKHTLLRL
CCCCCHHHHHHHHHH		48.00-
160AcetylationDWNLTTEKKHTLLRL
CCCCCHHHHHHHHHH		48.0026051181
160UbiquitinationDWNLTTEKKHTLLRL
CCCCCHHHHHHHHHH		48.0021906983
161UbiquitinationWNLTTEKKHTLLRLL
CCCCHHHHHHHHHHH		35.2722817900
164UbiquitinationTTEKKHTLLRLLYEA
CHHHHHHHHHHHHHH		2.3421963094
167UbiquitinationKKHTLLRLLYEALVD
HHHHHHHHHHHHHHH		6.3522817900
169PhosphorylationHTLLRLLYEALVDCK
HHHHHHHHHHHHHCC		12.0728152594
175GlutathionylationLYEALVDCKKSDAAS
HHHHHHHCCCCCHHH		4.6922555962
1762-HydroxyisobutyrylationYEALVDCKKSDAASK
HHHHHHCCCCCHHHH		51.34-
176AcetylationYEALVDCKKSDAASK
HHHHHHCCCCCHHHH		51.3426822725
176UbiquitinationYEALVDCKKSDAASK
HHHHHHCCCCCHHHH		51.3421963094
177UbiquitinationEALVDCKKSDAASKV
HHHHHCCCCCHHHHH		60.9622817900
183UbiquitinationKKSDAASKVMVELLG
CCCCHHHHHHHHHHC		29.6221906983
185UbiquitinationSDAASKVMVELLGSY
CCHHHHHHHHHHCCC		1.9223000965
187UbiquitinationAASKVMVELLGSYTE
HHHHHHHHHHCCCCC		21.85-
187UbiquitinationAASKVMVELLGSYTE
HHHHHHHHHHCCCCC		21.8523000965
191PhosphorylationVMVELLGSYTEDNAS
HHHHHHCCCCCCCHH		28.9327251275
191UbiquitinationVMVELLGSYTEDNAS
HHHHHHCCCCCCCHH		28.9321890473
192UbiquitinationMVELLGSYTEDNASQ
HHHHHCCCCCCCHHH		16.61-
192UbiquitinationMVELLGSYTEDNASQ
HHHHHCCCCCCCHHH		16.6123000965
193PhosphorylationVELLGSYTEDNASQA
HHHHCCCCCCCHHHH		38.2627251275
197UbiquitinationGSYTEDNASQARVDA
CCCCCCCHHHHHHHH		18.4923000965
198PhosphorylationSYTEDNASQARVDAH
CCCCCCHHHHHHHHH		30.5427251275
199UbiquitinationYTEDNASQARVDAHR
CCCCCHHHHHHHHHH		30.6729967540
212UbiquitinationHRCIVRALKDPNAFL
HHHHHHHHHCCCCCH		4.53-
212UbiquitinationHRCIVRALKDPNAFL
HHHHHHHHHCCCCCH		4.5323000965
213UbiquitinationRCIVRALKDPNAFLF
HHHHHHHHCCCCCHH		70.8821890473
213AcetylationRCIVRALKDPNAFLF
HHHHHHHHCCCCCHH		70.8823954790
213UbiquitinationRCIVRALKDPNAFLF
HHHHHHHHCCCCCHH		70.8821963094
226UbiquitinationLFDHLLTLKPVKFLE
HHHCCCCCCCHHHHC		6.27-
226UbiquitinationLFDHLLTLKPVKFLE
HHHCCCCCCCHHHHC		6.2721963094
227UbiquitinationFDHLLTLKPVKFLEG
HHCCCCCCCHHHHCC		42.3921890473
227AcetylationFDHLLTLKPVKFLEG
HHCCCCCCCHHHHCC		42.3925953088
227UbiquitinationFDHLLTLKPVKFLEG
HHCCCCCCCHHHHCC		42.3921906983
227UbiquitinationFDHLLTLKPVKFLEG
HHCCCCCCCHHHHCC		42.3922053931
230UbiquitinationLLTLKPVKFLEGELI
CCCCCCHHHHCCCHH		53.4022817900
231UbiquitinationLTLKPVKFLEGELIH
CCCCCHHHHCCCHHH		8.37-
231UbiquitinationLTLKPVKFLEGELIH
CCCCCHHHHCCCHHH		8.3723000965
233UbiquitinationLKPVKFLEGELIHDL
CCCHHHHCCCHHHHH		54.47-
233UbiquitinationLKPVKFLEGELIHDL
CCCHHHHCCCHHHHH		54.4723000965
248UbiquitinationLTIFVSAKLASYVKF
HHHHHHHHHHHHHHH		36.7623000965
254UbiquitinationAKLASYVKFYQNNKD
HHHHHHHHHHHCCHH		30.0721890473
254AcetylationAKLASYVKFYQNNKD
HHHHHHHHHHHCCHH		30.0719608861
254UbiquitinationAKLASYVKFYQNNKD
HHHHHHHHHHHCCHH		30.0723000965
256UbiquitinationLASYVKFYQNNKDFI
HHHHHHHHHCCHHHH		12.4723000965
260AcetylationVKFYQNNKDFIDSLG
HHHHHCCHHHHHHHH		62.6626051181
260UbiquitinationVKFYQNNKDFIDSLG
HHHHHCCHHHHHHHH		62.6623000965
261UbiquitinationKFYQNNKDFIDSLGL
HHHHCCHHHHHHHHH		48.1023000965
2762-HydroxyisobutyrylationLHEQNMAKMRLLTFM
HHHHHHHHHHHHHHH		17.49-
276UbiquitinationLHEQNMAKMRLLTFM
HHHHHHHHHHHHHHH		17.4929967540
281PhosphorylationMAKMRLLTFMGMAVE
HHHHHHHHHHHHHHC		19.0319664994
281UbiquitinationMAKMRLLTFMGMAVE
HHHHHHHHHHHHHHC		19.0323000965
283SulfoxidationKMRLLTFMGMAVENK
HHHHHHHHHHHHCCC		2.7821406390
295UbiquitinationENKEISFDTMQQELQ
CCCCCCHHHHHHHHC		34.1821963094
300UbiquitinationSFDTMQQELQIGADD
CHHHHHHHHCCCCCC		26.2523000965
302UbiquitinationDTMQQELQIGADDVE
HHHHHHHCCCCCCHH		31.1723000965
319AcetylationVIDAVRTKMVYCKID
HHHHHHCCEEEEECC		18.7925953088
319MalonylationVIDAVRTKMVYCKID
HHHHHHCCEEEEECC		18.7932601280
319UbiquitinationVIDAVRTKMVYCKID
HHHHHHCCEEEEECC		18.7923000965
3242-HydroxyisobutyrylationRTKMVYCKIDQTQRK
HCCEEEEECCCCCCE		31.46-
324AcetylationRTKMVYCKIDQTQRK
HCCEEEEECCCCCCE		31.4625953088
324UbiquitinationRTKMVYCKIDQTQRK
HCCEEEEECCCCCCE		31.4623000965
328PhosphorylationVYCKIDQTQRKVVVS
EEEECCCCCCEEEEE		26.96-
331UbiquitinationKIDQTQRKVVVSHST
ECCCCCCEEEEECCH		29.5729967540
335PhosphorylationTQRKVVVSHSTHRTF
CCCEEEEECCHHHCC		10.5026657352
337PhosphorylationRKVVVSHSTHRTFGK
CEEEEECCHHHCCCH		20.5725159151
338PhosphorylationKVVVSHSTHRTFGKQ
EEEEECCHHHCCCHH		15.2326074081
341PhosphorylationVSHSTHRTFGKQQWQ
EECCHHHCCCHHHHH		29.1828555341
344UbiquitinationSTHRTFGKQQWQQLY
CHHHCCCHHHHHHHH		34.8221890473
344AcetylationSTHRTFGKQQWQQLY
CHHHCCCHHHHHHHH		34.8226051181
344MethylationSTHRTFGKQQWQQLY
CHHHCCCHHHHHHHH		34.82-
344SumoylationSTHRTFGKQQWQQLY
CHHHCCCHHHHHHHH		34.82-
344UbiquitinationSTHRTFGKQQWQQLY
CHHHCCCHHHHHHHH		34.8223000965
344UbiquitinationSTHRTFGKQQWQQLY
CHHHCCCHHHHHHHH		34.8222053931
351PhosphorylationKQQWQQLYDTLNAWK
HHHHHHHHHHHHHHH		11.5321945579
353PhosphorylationQWQQLYDTLNAWKQN
HHHHHHHHHHHHHHH		14.3521945579
358AcetylationYDTLNAWKQNLNKVK
HHHHHHHHHHHHHHH		27.2226051181
358UbiquitinationYDTLNAWKQNLNKVK
HHHHHHHHHHHHHHH		27.2221963094
363UbiquitinationAWKQNLNKVKNSLLS
HHHHHHHHHHHHHHH		58.7221890473
363UbiquitinationAWKQNLNKVKNSLLS
HHHHHHHHHHHHHHH		58.7223000965
365UbiquitinationKQNLNKVKNSLLSLS
HHHHHHHHHHHHHCC		42.2921890473
365UbiquitinationKQNLNKVKNSLLSLS
HHHHHHHHHHHHHCC		42.2923000965
367PhosphorylationNLNKVKNSLLSLSDT
HHHHHHHHHHHCCCC		25.6020873877
370PhosphorylationKVKNSLLSLSDT---
HHHHHHHHCCCC---		30.9930108239
372PhosphorylationKNSLLSLSDT-----
HHHHHHCCCC-----		35.5130108239
374PhosphorylationSLLSLSDT-------
HHHHCCCC-------		36.8130108239
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 EIF3M_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3M_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 EIF3M_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3B_HUMANEIF3Bphysical
18599441
A4_HUMANAPPphysical
21832049
EIF3K_HUMANEIF3Kphysical
26186194
EIF3B_HUMANEIF3Bphysical
26186194
EIF3A_HUMANEIF3Aphysical
26186194
EIFCL_HUMANEIF3CLphysical
26186194
EIF3C_HUMANEIF3Cphysical
26186194
EIF3L_HUMANEIF3Lphysical
26186194
EIF3D_HUMANEIF3Dphysical
26186194
EIF3E_HUMANEIF3Ephysical
26186194
UBP34_HUMANUSP34physical
26186194
SAHH2_HUMANAHCYL1physical
26344197
EIF3B_HUMANEIF3Bphysical
26344197
EIF3C_HUMANEIF3Cphysical
26344197
EIFCL_HUMANEIF3CLphysical
26344197
EIF3D_HUMANEIF3Dphysical
26344197
EIF3K_HUMANEIF3Kphysical
26344197
RPN1_HUMANRPN1physical
26344197
EIF3A_HUMANEIF3Aphysical
17403899
EIF3B_HUMANEIF3Bphysical
17403899
EIF3C_HUMANEIF3Cphysical
17403899
EIF3D_HUMANEIF3Dphysical
17403899
EIF3E_HUMANEIF3Ephysical
17403899
EIF3F_HUMANEIF3Fphysical
17403899
EIF3G_HUMANEIF3Gphysical
17403899
EIF3H_HUMANEIF3Hphysical
17403899
EIF3I_HUMANEIF3Iphysical
17403899
EIF3J_HUMANEIF3Jphysical
17403899
EIF3K_HUMANEIF3Kphysical
17403899
EIF3L_HUMANEIF3Lphysical
17403899
EIF3E_HUMANEIF3Ephysical
28514442
EIFCL_HUMANEIF3CLphysical
28514442
EIF3L_HUMANEIF3Lphysical
28514442
EIF3A_HUMANEIF3Aphysical
28514442
EIF3C_HUMANEIF3Cphysical
28514442
EIF3D_HUMANEIF3Dphysical
28514442
EIF3B_HUMANEIF3Bphysical
28514442
EIF3K_HUMANEIF3Kphysical
28514442
PSD12_HUMANPSMD12physical
28514442
UBP34_HUMANUSP34physical
28514442
UBE2N_HUMANUBE2Nphysical
27173435
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 EIF3M_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 SER-2, ANDMASS 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-213 AND LYS-254, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-337, AND MASSSPECTROMETRY.
"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-351, AND MASSSPECTROMETRY.

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