EIF3L_HUMAN - dbPTM
EIF3L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3L_HUMAN
UniProt AC Q9Y262
Protein Name Eukaryotic translation initiation factor 3 subunit L {ECO:0000255|HAMAP-Rule:MF_03011}
Gene Name EIF3L {ECO:0000255|HAMAP-Rule:MF_03011}
Organism Homo sapiens (Human).
Sequence Length 564
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: 17581632]
Protein Sequence MSYPADDYESEAAYDPYAYPSDYDMHTGDPKQDLAYERQYEQQTYQVIPEVIKNFIQYFHKTVSDLIDQKVYELQASRVSSDVIDQKVYEIQDIYENSWTKLTERFFKNTPWPEAEAIAPQVGNDAVFLILYKELYYRHIYAKVSGGPSLEQRFESYYNYCNLFNYILNADGPAPLELPNQWLWDIIDEFIYQFQSFSQYRCKTAKKSEEEIDFLRSNPKIWNVHSVLNVLHSLVDKSNINRQLEVYTSGGDPESVAGEYGRHSLYKMLGYFSLVGLLRLHSLLGDYYQAIKVLENIELNKKSMYSRVPECQVTTYYYVGFAYLMMRRYQDAIRVFANILLYIQRTKSMFQRTTYKYEMINKQNEQMHALLAIALTMYPMRIDESIHLQLREKYGDKMLRMQKGDPQVYEELFSYSCPKFLSPVVPNYDNVHPNYHKEPFLQQLKVFSDEVQQQAQLSTIRSFLKLYTTMPVAKLAGFLDLTEQEFRIQLLVFKHKMKNLVWTSGISALDGEFQSASEVDFYIDKDMIHIADTKVARRYGDFFIRQIHKFEELNRTLKKMGQRP
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------MSYPADDYE
------CCCCCCCCC
39.5617322308
2Phosphorylation------MSYPADDYE
------CCCCCCCCC
39.5623663014
3Phosphorylation-----MSYPADDYES
-----CCCCCCCCCC
10.9223663014
8PhosphorylationMSYPADDYESEAAYD
CCCCCCCCCCCCCCC
23.1523663014
10PhosphorylationYPADDYESEAAYDPY
CCCCCCCCCCCCCCC
26.7223663014
14PhosphorylationDYESEAAYDPYAYPS
CCCCCCCCCCCCCCC
25.2126074081
17PhosphorylationSEAAYDPYAYPSDYD
CCCCCCCCCCCCCCC
18.8328450419
19PhosphorylationAAYDPYAYPSDYDMH
CCCCCCCCCCCCCCC
9.4526074081
21PhosphorylationYDPYAYPSDYDMHTG
CCCCCCCCCCCCCCC
35.8126074081
23PhosphorylationPYAYPSDYDMHTGDP
CCCCCCCCCCCCCCC
21.3626074081
27PhosphorylationPSDYDMHTGDPKQDL
CCCCCCCCCCCHHHH
36.3226074081
36PhosphorylationDPKQDLAYERQYEQQ
CCHHHHHHHHHHHHH
20.9521945579
40PhosphorylationDLAYERQYEQQTYQV
HHHHHHHHHHHHHHH
23.1721945579
44PhosphorylationERQYEQQTYQVIPEV
HHHHHHHHHHHHHHH
18.6721945579
45PhosphorylationRQYEQQTYQVIPEVI
HHHHHHHHHHHHHHH
9.1021945579
45UbiquitinationRQYEQQTYQVIPEVI
HHHHHHHHHHHHHHH
9.1021963094
58PhosphorylationVIKNFIQYFHKTVSD
HHHHHHHHHHHHHHH
11.6628152594
61UbiquitinationNFIQYFHKTVSDLID
HHHHHHHHHHHHHHH
40.50-
62PhosphorylationFIQYFHKTVSDLIDQ
HHHHHHHHHHHHHHH
19.3730622161
64PhosphorylationQYFHKTVSDLIDQKV
HHHHHHHHHHHHHHH
31.7521712546
70AcetylationVSDLIDQKVYELQAS
HHHHHHHHHHHHHHH
42.9326051181
70UbiquitinationVSDLIDQKVYELQAS
HHHHHHHHHHHHHHH
42.9321906983
72PhosphorylationDLIDQKVYELQASRV
HHHHHHHHHHHHHCC
20.2528152594
77PhosphorylationKVYELQASRVSSDVI
HHHHHHHHCCCCHHH
21.9128152594
80PhosphorylationELQASRVSSDVIDQK
HHHHHCCCCHHHCCH
21.5128985074
81PhosphorylationLQASRVSSDVIDQKV
HHHHCCCCHHHCCHH
32.8021712546
87UbiquitinationSSDVIDQKVYEIQDI
CCHHHCCHHEEHHHH
42.9321906983
89PhosphorylationDVIDQKVYEIQDIYE
HHHCCHHEEHHHHHH
17.8527273156
95PhosphorylationVYEIQDIYENSWTKL
HEEHHHHHHCCHHHH
19.8329496907
98PhosphorylationIQDIYENSWTKLTER
HHHHHHCCHHHHHHH
24.9630622161
100PhosphorylationDIYENSWTKLTERFF
HHHHCCHHHHHHHHH
18.9230622161
101UbiquitinationIYENSWTKLTERFFK
HHHCCHHHHHHHHHH
47.3421890473
101AcetylationIYENSWTKLTERFFK
HHHCCHHHHHHHHHH
47.3426051181
101UbiquitinationIYENSWTKLTERFFK
HHHCCHHHHHHHHHH
47.3421906983
109UbiquitinationLTERFFKNTPWPEAE
HHHHHHHCCCCHHHH
46.3324816145
110PhosphorylationTERFFKNTPWPEAEA
HHHHHHCCCCHHHHH
27.5928674151
113UbiquitinationFFKNTPWPEAEAIAP
HHHCCCCHHHHHHCC
31.9321963094
122UbiquitinationAEAIAPQVGNDAVFL
HHHHCCCCCCHHHHH
8.2321963094
130UbiquitinationGNDAVFLILYKELYY
CCHHHHHHHHHHHHH
2.4121963094
139UbiquitinationYKELYYRHIYAKVSG
HHHHHHHHHHHHCCC
10.9921963094
143AcetylationYYRHIYAKVSGGPSL
HHHHHHHHCCCCCCH
21.6926051181
143UbiquitinationYYRHIYAKVSGGPSL
HHHHHHHHCCCCCCH
21.6921906983
144UbiquitinationYRHIYAKVSGGPSLE
HHHHHHHCCCCCCHH
4.9721963094
145PhosphorylationRHIYAKVSGGPSLEQ
HHHHHHCCCCCCHHH
37.0123403867
159UbiquitinationQRFESYYNYCNLFNY
HHHHHHHHHHHHHHH
27.0124816145
172UbiquitinationNYILNADGPAPLELP
HHHHCCCCCCCCCCC
20.1921963094
186UbiquitinationPNQWLWDIIDEFIYQ
CCHHHHHHHHHHHHH
2.6421963094
189UbiquitinationWLWDIIDEFIYQFQS
HHHHHHHHHHHHHHC
24.4421963094
203UbiquitinationSFSQYRCKTAKKSEE
CCCCCCCCCCCCCHH
42.3822817900
204UbiquitinationFSQYRCKTAKKSEEE
CCCCCCCCCCCCHHH
47.5422817900
206UbiquitinationQYRCKTAKKSEEEID
CCCCCCCCCCHHHHH
63.16-
2072-HydroxyisobutyrylationYRCKTAKKSEEEIDF
CCCCCCCCCHHHHHH
61.71-
207UbiquitinationYRCKTAKKSEEEIDF
CCCCCCCCCHHHHHH
61.7124816145
208PhosphorylationRCKTAKKSEEEIDFL
CCCCCCCCHHHHHHH
49.9230622161
220UbiquitinationDFLRSNPKIWNVHSV
HHHHCCCCHHHHHHH
65.6821963094
226PhosphorylationPKIWNVHSVLNVLHS
CCHHHHHHHHHHHHH
24.8228450419
237UbiquitinationVLHSLVDKSNINRQL
HHHHHHCCCCCCCEE
37.6121963094
247PhosphorylationINRQLEVYTSGGDPE
CCCEEEEEECCCCHH
5.9420068231
249UbiquitinationRQLEVYTSGGDPESV
CEEEEEECCCCHHHH
24.0824816145
250UbiquitinationQLEVYTSGGDPESVA
EEEEEECCCCHHHHH
36.4024816145
253UbiquitinationVYTSGGDPESVAGEY
EEECCCCHHHHHCCC
38.7522817900
254UbiquitinationYTSGGDPESVAGEYG
EECCCCHHHHHCCCH
63.6922817900
255PhosphorylationTSGGDPESVAGEYGR
ECCCCHHHHHCCCHH
23.7428152594
258UbiquitinationGDPESVAGEYGRHSL
CCHHHHHCCCHHHHH
26.8821963094
260PhosphorylationPESVAGEYGRHSLYK
HHHHHCCCHHHHHHH
20.6728152594
263UbiquitinationVAGEYGRHSLYKMLG
HHCCCHHHHHHHHHH
20.1421963094
264UbiquitinationAGEYGRHSLYKMLGY
HCCCHHHHHHHHHHH
31.8423503661
268SulfoxidationGRHSLYKMLGYFSLV
HHHHHHHHHHHHHHH
1.9128183972
280UbiquitinationSLVGLLRLHSLLGDY
HHHHHHHHHHHHCHH
3.0321963094
287PhosphorylationLHSLLGDYYQAIKVL
HHHHHCHHHHHHHHH
8.8320090780
288PhosphorylationHSLLGDYYQAIKVLE
HHHHCHHHHHHHHHH
9.0120090780
299UbiquitinationKVLENIELNKKSMYS
HHHHHCCCCCCCHHH
11.4524816145
3012-HydroxyisobutyrylationLENIELNKKSMYSRV
HHHCCCCCCCHHHCC
59.87-
301AcetylationLENIELNKKSMYSRV
HHHCCCCCCCHHHCC
59.8723954790
301MalonylationLENIELNKKSMYSRV
HHHCCCCCCCHHHCC
59.8726320211
301UbiquitinationLENIELNKKSMYSRV
HHHCCCCCCCHHHCC
59.8727667366
302UbiquitinationENIELNKKSMYSRVP
HHCCCCCCCHHHCCC
39.1122817900
305UbiquitinationELNKKSMYSRVPECQ
CCCCCCHHHCCCCCE
10.6230230243
308UbiquitinationKKSMYSRVPECQVTT
CCCHHHCCCCCEEEE
3.7321963094
314UbiquitinationRVPECQVTTYYYVGF
CCCCCEEEEHHHHHH
5.3423503661
321UbiquitinationTTYYYVGFAYLMMRR
EEHHHHHHHHHHHHH
2.6321890473
339UbiquitinationAIRVFANILLYIQRT
HHHHHHHHHHHHHHH
2.2222817900
342PhosphorylationVFANILLYIQRTKSM
HHHHHHHHHHHHHHH
7.49-
344UbiquitinationANILLYIQRTKSMFQ
HHHHHHHHHHHHHHH
33.1722817900
345UbiquitinationNILLYIQRTKSMFQR
HHHHHHHHHHHHHHH
34.2622817900
3472-HydroxyisobutyrylationLLYIQRTKSMFQRTT
HHHHHHHHHHHHHHH
41.95-
347AcetylationLLYIQRTKSMFQRTT
HHHHHHHHHHHHHHH
41.9527452117
347UbiquitinationLLYIQRTKSMFQRTT
HHHHHHHHHHHHHHH
41.9524816145
349UbiquitinationYIQRTKSMFQRTTYK
HHHHHHHHHHHHHHH
3.3724816145
355PhosphorylationSMFQRTTYKYEMINK
HHHHHHHHHHHHCCC
15.8029496907
355UbiquitinationSMFQRTTYKYEMINK
HHHHHHHHHHHHCCC
15.8032015554
3562-HydroxyisobutyrylationMFQRTTYKYEMINKQ
HHHHHHHHHHHCCCH
32.42-
356AcetylationMFQRTTYKYEMINKQ
HHHHHHHHHHHCCCH
32.4226051181
356UbiquitinationMFQRTTYKYEMINKQ
HHHHHHHHHHHCCCH
32.4221906983
357PhosphorylationFQRTTYKYEMINKQN
HHHHHHHHHHCCCHH
10.5820090780
362UbiquitinationYKYEMINKQNEQMHA
HHHHHCCCHHHHHHH
43.5023503661
367UbiquitinationINKQNEQMHALLAIA
CCCHHHHHHHHHHHH
1.3021963094
371UbiquitinationNEQMHALLAIALTMY
HHHHHHHHHHHHHHC
3.1721890473
376PhosphorylationALLAIALTMYPMRID
HHHHHHHHHCCCCCC
12.9727251275
385PhosphorylationYPMRIDESIHLQLRE
CCCCCCCHHHHHHHH
16.1527251275
386UbiquitinationPMRIDESIHLQLREK
CCCCCCHHHHHHHHH
3.3721890473
389AcetylationIDESIHLQLREKYGD
CCCHHHHHHHHHHHH
25.0619608861
389UbiquitinationIDESIHLQLREKYGD
CCCHHHHHHHHHHHH
25.0622817900
390UbiquitinationDESIHLQLREKYGDK
CCHHHHHHHHHHHHH
10.8524816145
393UbiquitinationIHLQLREKYGDKMLR
HHHHHHHHHHHHHHH
48.37-
394PhosphorylationHLQLREKYGDKMLRM
HHHHHHHHHHHHHHH
26.29-
396UbiquitinationQLREKYGDKMLRMQK
HHHHHHHHHHHHHCC
30.0621890473
3972-HydroxyisobutyrylationLREKYGDKMLRMQKG
HHHHHHHHHHHHCCC
35.16-
397AcetylationLREKYGDKMLRMQKG
HHHHHHHHHHHHCCC
35.1625953088
397MalonylationLREKYGDKMLRMQKG
HHHHHHHHHHHHCCC
35.1626320211
397UbiquitinationLREKYGDKMLRMQKG
HHHHHHHHHHHHCCC
35.1624816145
398UbiquitinationREKYGDKMLRMQKGD
HHHHHHHHHHHCCCC
3.2323503661
399UbiquitinationEKYGDKMLRMQKGDP
HHHHHHHHHHCCCCH
5.2021963094
400UbiquitinationKYGDKMLRMQKGDPQ
HHHHHHHHHCCCCHH
23.2223503661
403AcetylationDKMLRMQKGDPQVYE
HHHHHHCCCCHHHHH
56.8126051181
403MalonylationDKMLRMQKGDPQVYE
HHHHHHCCCCHHHHH
56.8126320211
403UbiquitinationDKMLRMQKGDPQVYE
HHHHHHCCCCHHHHH
56.8132015554
404UbiquitinationKMLRMQKGDPQVYEE
HHHHHCCCCHHHHHH
34.6321890473
405UbiquitinationMLRMQKGDPQVYEEL
HHHHCCCCHHHHHHH
37.1823503661
409PhosphorylationQKGDPQVYEELFSYS
CCCCHHHHHHHHCCC
9.8429759185
414PhosphorylationQVYEELFSYSCPKFL
HHHHHHHCCCCHHHH
28.8528152594
415PhosphorylationVYEELFSYSCPKFLS
HHHHHHCCCCHHHHC
13.6320090780
416PhosphorylationYEELFSYSCPKFLSP
HHHHHCCCCHHHHCC
23.8128152594
417AcetylationEELFSYSCPKFLSPV
HHHHCCCCHHHHCCC
3.0119608861
417GlutathionylationEELFSYSCPKFLSPV
HHHHCCCCHHHHCCC
3.0122555962
417S-palmitoylationEELFSYSCPKFLSPV
HHHHCCCCHHHHCCC
3.0129575903
417UbiquitinationEELFSYSCPKFLSPV
HHHHCCCCHHHHCCC
3.0127667366
419AcetylationLFSYSCPKFLSPVVP
HHCCCCHHHHCCCCC
64.3625953088
419UbiquitinationLFSYSCPKFLSPVVP
HHCCCCHHHHCCCCC
64.3621906983
422PhosphorylationYSCPKFLSPVVPNYD
CCCHHHHCCCCCCCC
20.8425159151
428PhosphorylationLSPVVPNYDNVHPNY
HCCCCCCCCCCCCCC
11.6529496907
434UbiquitinationNYDNVHPNYHKEPFL
CCCCCCCCCCCCHHH
36.3424816145
435PhosphorylationYDNVHPNYHKEPFLQ
CCCCCCCCCCCHHHH
20.7929496907
436UbiquitinationDNVHPNYHKEPFLQQ
CCCCCCCCCCHHHHH
34.3427667366
437AcetylationNVHPNYHKEPFLQQL
CCCCCCCCCHHHHHH
57.6423954790
437MalonylationNVHPNYHKEPFLQQL
CCCCCCCCCHHHHHH
57.6426320211
437UbiquitinationNVHPNYHKEPFLQQL
CCCCCCCCCHHHHHH
57.6422817900
440UbiquitinationPNYHKEPFLQQLKVF
CCCCCCHHHHHHHHC
11.4524816145
445AcetylationEPFLQQLKVFSDEVQ
CHHHHHHHHCCHHHH
36.578273333
445UbiquitinationEPFLQQLKVFSDEVQ
CHHHHHHHHCCHHHH
36.57-
446UbiquitinationPFLQQLKVFSDEVQQ
HHHHHHHHCCHHHHH
8.2621890473
448UbiquitinationLQQLKVFSDEVQQQA
HHHHHHCCHHHHHHH
35.5323503661
450UbiquitinationQLKVFSDEVQQQAQL
HHHHCCHHHHHHHHH
40.8223503661
451UbiquitinationLKVFSDEVQQQAQLS
HHHCCHHHHHHHHHH
8.1633845483
458PhosphorylationVQQQAQLSTIRSFLK
HHHHHHHHHHHHHHH
15.0930622161
459PhosphorylationQQQAQLSTIRSFLKL
HHHHHHHHHHHHHHH
29.0630622161
461UbiquitinationQAQLSTIRSFLKLYT
HHHHHHHHHHHHHHH
22.8021890473
461UbiquitinationQAQLSTIRSFLKLYT
HHHHHHHHHHHHHHH
22.8024816145
462PhosphorylationAQLSTIRSFLKLYTT
HHHHHHHHHHHHHHH
30.9524719451
462UbiquitinationAQLSTIRSFLKLYTT
HHHHHHHHHHHHHHH
30.9521890473
465AcetylationSTIRSFLKLYTTMPV
HHHHHHHHHHHHHCH
37.1219608861
465UbiquitinationSTIRSFLKLYTTMPV
HHHHHHHHHHHHHCH
37.1221906983
470SulfoxidationFLKLYTTMPVAKLAG
HHHHHHHHCHHHHHC
1.6130846556
474UbiquitinationYTTMPVAKLAGFLDL
HHHHCHHHHHCCCCC
38.82-
480UbiquitinationAKLAGFLDLTEQEFR
HHHHCCCCCCCCHHH
49.6521890473
486UbiquitinationLDLTEQEFRIQLLVF
CCCCCCHHHHHHHHH
9.2427667366
494AcetylationRIQLLVFKHKMKNLV
HHHHHHHHHHCCCCC
34.5326051181
494UbiquitinationRIQLLVFKHKMKNLV
HHHHHHHHHHCCCCC
34.5321890473
496UbiquitinationQLLVFKHKMKNLVWT
HHHHHHHHCCCCCCC
52.7623503661
498UbiquitinationLVFKHKMKNLVWTSG
HHHHHHCCCCCCCCC
52.5123503661
501AcetylationKHKMKNLVWTSGISA
HHHCCCCCCCCCHHH
7.9719608861
501UbiquitinationKHKMKNLVWTSGISA
HHHCCCCCCCCCHHH
7.9733845483
508UbiquitinationVWTSGISALDGEFQS
CCCCCHHHCCCCCCC
14.0421963094
511UbiquitinationSGISALDGEFQSASE
CCHHHCCCCCCCHHE
38.1724816145
5342-HydroxyisobutyrylationMIHIADTKVARRYGD
HEEECCHHHHHHHHH
34.15-
534UbiquitinationMIHIADTKVARRYGD
HEEECCHHHHHHHHH
34.1521906983
537UbiquitinationIADTKVARRYGDFFI
ECCHHHHHHHHHHHH
35.0321890473
539PhosphorylationDTKVARRYGDFFIRQ
CHHHHHHHHHHHHHH
18.5928152594
539UbiquitinationDTKVARRYGDFFIRQ
CHHHHHHHHHHHHHH
18.5923503661
541UbiquitinationKVARRYGDFFIRQIH
HHHHHHHHHHHHHHH
26.7523503661
549AcetylationFFIRQIHKFEELNRT
HHHHHHHHHHHHHHH
56.9819608861
549MalonylationFFIRQIHKFEELNRT
HHHHHHHHHHHHHHH
56.9826320211
549UbiquitinationFFIRQIHKFEELNRT
HHHHHHHHHHHHHHH
56.9833845483
556PhosphorylationKFEELNRTLKKMGQR
HHHHHHHHHHHHCCC
41.6823186163
558MethylationEELNRTLKKMGQRP-
HHHHHHHHHHCCCC-
39.85-
559UbiquitinationELNRTLKKMGQRP--
HHHHHHHHHCCCC--
51.9124816145
575Ubiquitination------------------
------------------
24816145

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 EIF3L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3L_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 EIF3L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3D_HUMANEIF3Dphysical
11590142
EIF3A_HUMANEIF3Aphysical
11590142
EIF3E_HUMANEIF3Ephysical
11590142
EIF3B_HUMANEIF3Bphysical
18599441
EIF3M_HUMANEIF3Mphysical
22939629
NUCL_HUMANNCLphysical
22939629
RRN3_HUMANRRN3physical
12393749
DDX3X_HUMANDDX3Xphysical
22863883
EIF3A_HUMANEIF3Aphysical
22863883
EIF3C_HUMANEIF3Cphysical
22863883
EIF3D_HUMANEIF3Dphysical
22863883
EIF3E_HUMANEIF3Ephysical
22863883
EIF3K_HUMANEIF3Kphysical
22863883
EIF3H_HUMANEIF3Hphysical
22863883
LARP1_HUMANLARP1physical
22863883
RS13_HUMANRPS13physical
22863883
RS16_HUMANRPS16physical
22863883
RS18_HUMANRPS18physical
22863883
RS20_HUMANRPS20physical
22863883
RS25_HUMANRPS25physical
22863883
RS28_HUMANRPS28physical
22863883
RS4X_HUMANRPS4Xphysical
22863883
RS5_HUMANRPS5physical
22863883
RS8_HUMANRPS8physical
22863883
RS9_HUMANRPS9physical
22863883
EIF3A_HUMANEIF3Aphysical
26344197
EIF3B_HUMANEIF3Bphysical
26344197
EIF3C_HUMANEIF3Cphysical
26344197
EIFCL_HUMANEIF3CLphysical
26344197
EIF3D_HUMANEIF3Dphysical
26344197
EIF3F_HUMANEIF3Fphysical
26344197
EIF3G_HUMANEIF3Gphysical
26344197
EIF3H_HUMANEIF3Hphysical
26344197
EIF3K_HUMANEIF3Kphysical
26344197
EIF3M_HUMANEIF3Mphysical
26344197
NUCL_HUMANNCLphysical
26344197
NUMA1_HUMANNUMA1physical
26344197
EIFCL_HUMANEIF3CLphysical
28514442
PRC2B_HUMANPRRC2Bphysical
28514442
EIF3A_HUMANEIF3Aphysical
28514442
EIF3C_HUMANEIF3Cphysical
28514442
EIF3K_HUMANEIF3Kphysical
28514442
EIF3D_HUMANEIF3Dphysical
28514442
EIF3B_HUMANEIF3Bphysical
28514442
ZN746_HUMANZNF746physical
28514442
GBB2_HUMANGNB2physical
28514442
TT21B_HUMANTTC21Bphysical
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 EIF3L_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-437; LYS-465 AND LYS-549,AND MASS SPECTROMETRY.

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