EIFCL_HUMAN - dbPTM
EIFCL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIFCL_HUMAN
UniProt AC B5ME19
Protein Name Eukaryotic translation initiation factor 3 subunit C-like protein
Gene Name EIF3CL
Organism Homo sapiens (Human).
Sequence Length 914
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. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression..
Protein Sequence MSRFFTTGSDSESESSLSGEELVTKPVGGNYGKQPLLLSEDEEDTKRVVRSAKDKRFEELTNLIRTIRNAMKIRDVTKCLEEFELLGKAYGKAKSIVDKEGVPRFYIRILADLEDYLNELWEDKEGKKKMNKNNAKALSTLRQKIRKYNRDFESHITSYKQNPEQSADEDAEKNEEDSEGSSDEDEDEDGVSAATFLKKKSEAPSGESRKFLKKMDDEDEDSEDSEDDEDWDTGSTSSDSDSEEEEGKQTALASRFLKKAPTTDEDKKAAEKKREDKAKKKHDRKSKRLDEEEEEDNEGGEWERVRGGVPLVKEKPKMFAKGTEITHAVVIKKLNEILQARGKKGTDRAAQIELLQLLVQIAAENNLGEGVIVKIKFNIIASLYDYNPNLATYMKPEMWGKCLDCINELMDILFANPNIFVGENILEESENLHNADQPLRVRGCILTLVERMDEEFTKIMQNTDPHSQEYVEHLKDEAQVCAIIERVQRYLEEKGTTEEVCRIYLLRILHTYYKFDYKAHQRQLTPPEGSSKSEQDQAENEGEDSAVLMERLCKYIYAKDRTDRIRTCAILCHIYHHALHSRWYQARDLMLMSHLQDNIQHADPPVQILYNRTMVQLGICAFRQGLTKDAHNALLDIQSSGRAKELLGQGLLLRSLQERNQEQEKVERRRQVPFHLHINLELLECVYLVSAMLLEIPYMAAHESDARRRMISKQFHHQLRVGERQPLLGPPESMREHVVAASKAMKMGDWKTCHSFIINEKMNGKVWDLFPEADKVRTMLVRKIQEESLRTYLFTYSSVYDSISMETLSDMFELDLPTVHSIISKMIINEELMASLDQPTQTVVMHRTEPTAQQNLALQLAEKLGSLVENNERVFDHKQGTYGGYFRDQKDGYRKNEGYMRRGGYRQQQSQTAY
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
2Phosphorylation------MSRFFTTGS
------CCCCCCCCC
29514088
6Phosphorylation--MSRFFTTGSDSES
--CCCCCCCCCCCCC
23927012
7Phosphorylation-MSRFFTTGSDSESE
-CCCCCCCCCCCCCC
30278072
9PhosphorylationSRFFTTGSDSESESS
CCCCCCCCCCCCCCC
23927012
11PhosphorylationFFTTGSDSESESSLS
CCCCCCCCCCCCCCC
23927012
13PhosphorylationTTGSDSESESSLSGE
CCCCCCCCCCCCCCC
25159151
15PhosphorylationGSDSESESSLSGEEL
CCCCCCCCCCCCCCE
25159151
16PhosphorylationSDSESESSLSGEELV
CCCCCCCCCCCCCEE
23927012
18PhosphorylationSESESSLSGEELVTK
CCCCCCCCCCCEEEC
28355574
24PhosphorylationLSGEELVTKPVGGNY
CCCCCEEECCCCCCC
23927012
31PhosphorylationTKPVGGNYGKQPLLL
ECCCCCCCCCCCCCC
23927012
39PhosphorylationGKQPLLLSEDEEDTK
CCCCCCCCCCHHHHH
19664994
45PhosphorylationLSEDEEDTKRVVRSA
CCCCHHHHHHHHHHH
22167270
61PhosphorylationDKRFEELTNLIRTIR
HHHHHHHHHHHHHHH
-
66PhosphorylationELTNLIRTIRNAMKI
HHHHHHHHHHHHHHH
-
78UbiquitinationMKIRDVTKCLEEFEL
HHHHHHHHHHHHHHH
-
88UbiquitinationEEFELLGKAYGKAKS
HHHHHHHHHHCCHHH
-
92UbiquitinationLLGKAYGKAKSIVDK
HHHHHHCCHHHCCCC
-
942-HydroxyisobutyrylationGKAYGKAKSIVDKEG
HHHHCCHHHCCCCCC
-
94UbiquitinationGKAYGKAKSIVDKEG
HHHHCCHHHCCCCCC
-
95PhosphorylationKAYGKAKSIVDKEGV
HHHCCHHHCCCCCCC
22817900
99AcetylationKAKSIVDKEGVPRFY
CHHHCCCCCCCCHHH
-
99UbiquitinationKAKSIVDKEGVPRFY
CHHHCCCCCCCCHHH
-
104MethylationVDKEGVPRFYIRILA
CCCCCCCHHHHHHHH
-
127AcetylationLWEDKEGKKKMNKNN
HHCCHHHHHHCCHHH
24430999
128AcetylationWEDKEGKKKMNKNNA
HCCHHHHHHCCHHHH
24471041
136MalonylationKMNKNNAKALSTLRQ
HCCHHHHHHHHHHHH
26320211
136UbiquitinationKMNKNNAKALSTLRQ
HCCHHHHHHHHHHHH
-
140PhosphorylationNNAKALSTLRQKIRK
HHHHHHHHHHHHHHH
-
148PhosphorylationLRQKIRKYNRDFESH
HHHHHHHHHHHHHHH
21406692
154PhosphorylationKYNRDFESHITSYKQ
HHHHHHHHHHHHCCC
21406692
157PhosphorylationRDFESHITSYKQNPE
HHHHHHHHHCCCCCC
21406692
158PhosphorylationDFESHITSYKQNPEQ
HHHHHHHHCCCCCCC
21406692
159PhosphorylationFESHITSYKQNPEQS
HHHHHHHCCCCCCCC
21406692
160UbiquitinationESHITSYKQNPEQSA
HHHHHHCCCCCCCCC
-
166PhosphorylationYKQNPEQSADEDAEK
CCCCCCCCCCHHHHH
29255136
178PhosphorylationAEKNEEDSEGSSDED
HHHCHHCCCCCCCCC
26503892
181PhosphorylationNEEDSEGSSDEDEDE
CHHCCCCCCCCCCCC
26503892
182PhosphorylationEEDSEGSSDEDEDED
HHCCCCCCCCCCCCC
26503892
192PhosphorylationDEDEDGVSAATFLKK
CCCCCCCCHHHHHHH
25850435
195PhosphorylationEDGVSAATFLKKKSE
CCCCCHHHHHHHHCC
25850435
201PhosphorylationATFLKKKSEAPSGES
HHHHHHHCCCCCHHH
28674151
205PhosphorylationKKKSEAPSGESRKFL
HHHCCCCCHHHHHHH
30576142
208PhosphorylationSEAPSGESRKFLKKM
CCCCCHHHHHHHHHC
28102081
222PhosphorylationMDDEDEDSEDSEDDE
CCCCCCCCCCCCCCC
22210691
225PhosphorylationEDEDSEDSEDDEDWD
CCCCCCCCCCCCCCC
25137130
233PhosphorylationEDDEDWDTGSTSSDS
CCCCCCCCCCCCCCC
25137130
235PhosphorylationDEDWDTGSTSSDSDS
CCCCCCCCCCCCCCC
25137130
236PhosphorylationEDWDTGSTSSDSDSE
CCCCCCCCCCCCCCH
22210691
237PhosphorylationDWDTGSTSSDSDSEE
CCCCCCCCCCCCCHH
25137130
238PhosphorylationWDTGSTSSDSDSEEE
CCCCCCCCCCCCHHH
25137130
240PhosphorylationTGSTSSDSDSEEEEG
CCCCCCCCCCHHHHH
22210691
242PhosphorylationSTSSDSDSEEEEGKQ
CCCCCCCCHHHHHHH
26657352
250PhosphorylationEEEEGKQTALASRFL
HHHHHHHHHHHHHHH
24719451
262PhosphorylationRFLKKAPTTDEDKKA
HHHHHCCCCHHHHHH
30576142
263PhosphorylationFLKKAPTTDEDKKAA
HHHHCCCCHHHHHHH
26657352
306MethylationGGEWERVRGGVPLVK
CCCCEECCCCCCCCC
-
313UbiquitinationRGGVPLVKEKPKMFA
CCCCCCCCCCCCCCC
-
315UbiquitinationGVPLVKEKPKMFAKG
CCCCCCCCCCCCCCC
-
321MalonylationEKPKMFAKGTEITHA
CCCCCCCCCCCCCHH
32601280
321UbiquitinationEKPKMFAKGTEITHA
CCCCCCCCCCCCCHH
-
332UbiquitinationITHAVVIKKLNEILQ
CCHHHHHHHHHHHHH
21906983
3332-HydroxyisobutyrylationTHAVVIKKLNEILQA
CHHHHHHHHHHHHHH
-
333UbiquitinationTHAVVIKKLNEILQA
CHHHHHHHHHHHHHH
-
447PhosphorylationRVRGCILTLVERMDE
HHHHHHHHHHHHCHH
20068231
463PhosphorylationFTKIMQNTDPHSQEY
HHHHHHCCCCCCHHH
28851738
467PhosphorylationMQNTDPHSQEYVEHL
HHCCCCCCHHHHHHH
28851738
470PhosphorylationTDPHSQEYVEHLKDE
CCCCCHHHHHHHHHH
-
475UbiquitinationQEYVEHLKDEAQVCA
HHHHHHHHHHHHHHH
-
4942-HydroxyisobutyrylationVQRYLEEKGTTEEVC
HHHHHHHCCCHHHHH
-
494UbiquitinationVQRYLEEKGTTEEVC
HHHHHHHCCCHHHHH
-
514UbiquitinationRILHTYYKFDYKAHQ
HHHHHHHHCCHHHHH
-
518UbiquitinationTYYKFDYKAHQRQLT
HHHHCCHHHHHCCCC
-
525PhosphorylationKAHQRQLTPPEGSSK
HHHHCCCCCCCCCCH
25159151
530PhosphorylationQLTPPEGSSKSEQDQ
CCCCCCCCCHHHHHH
30266825
531PhosphorylationLTPPEGSSKSEQDQA
CCCCCCCCHHHHHHH
30266825
532UbiquitinationTPPEGSSKSEQDQAE
CCCCCCCHHHHHHHH
21890473
533PhosphorylationPPEGSSKSEQDQAEN
CCCCCCHHHHHHHHH
25159151
545PhosphorylationAENEGEDSAVLMERL
HHHCCCHHHHHHHHH
23322592
549SulfoxidationGEDSAVLMERLCKYI
CCHHHHHHHHHHHHH
28183972
551MethylationDSAVLMERLCKYIYA
HHHHHHHHHHHHHHH
-
554UbiquitinationVLMERLCKYIYAKDR
HHHHHHHHHHHHCCC
-
5592-HydroxyisobutyrylationLCKYIYAKDRTDRIR
HHHHHHHCCCCHHHH
-
559AcetylationLCKYIYAKDRTDRIR
HHHHHHHCCCCHHHH
-
559UbiquitinationLCKYIYAKDRTDRIR
HHHHHHHCCCCHHHH
-
613PhosphorylationVQILYNRTMVQLGIC
HHHEECCHHHHHHHH
-
628MalonylationAFRQGLTKDAHNALL
HHHCCCCCHHHHHHH
26320211
628UbiquitinationAFRQGLTKDAHNALL
HHHCCCCCHHHHHHH
21890473
639PhosphorylationNALLDIQSSGRAKEL
HHHHHHHCCCHHHHH
20873877
640PhosphorylationALLDIQSSGRAKELL
HHHHHHCCCHHHHHH
20873877
6442-HydroxyisobutyrylationIQSSGRAKELLGQGL
HHCCCHHHHHHHHHH
-
644AcetylationIQSSGRAKELLGQGL
HHCCCHHHHHHHHHH
-
644MalonylationIQSSGRAKELLGQGL
HHCCCHHHHHHHHHH
26320211
644UbiquitinationIQSSGRAKELLGQGL
HHCCCHHHHHHHHHH
21906983
654MethylationLGQGLLLRSLQERNQ
HHHHHHHHHHHHHHH
-
665AcetylationERNQEQEKVERRRQV
HHHHHHHHHHHHHHC
178226225
665UbiquitinationERNQEQEKVERRRQV
HHHHHHHHHHHHHHC
21906983
713AcetylationARRRMISKQFHHQLR
HHHHHHHHHHHHHCC
24695921
713UbiquitinationARRRMISKQFHHQLR
HHHHHHHHHHHHHCC
21890473
720MethylationKQFHHQLRVGERQPL
HHHHHHCCCCCCCCC
-
733PhosphorylationPLLGPPESMREHVVA
CCCCCCHHHHHHHHH
22985185
743UbiquitinationEHVVAASKAMKMGDW
HHHHHHHHHHHCCCC
-
746UbiquitinationVAASKAMKMGDWKTC
HHHHHHHHCCCCCCC
-
751UbiquitinationAMKMGDWKTCHSFII
HHHCCCCCCCEEEEE
-
752PhosphorylationMKMGDWKTCHSFIIN
HHCCCCCCCEEEEEE
21406692
755PhosphorylationGDWKTCHSFIINEKM
CCCCCCEEEEEEHHH
21406692
761UbiquitinationHSFIINEKMNGKVWD
EEEEEEHHHCCCHHH
-
765UbiquitinationINEKMNGKVWDLFPE
EEHHHCCCHHHCCCC
-
7752-HydroxyisobutyrylationDLFPEADKVRTMLVR
HCCCCHHHHHHHHHH
-
775UbiquitinationDLFPEADKVRTMLVR
HCCCCHHHHHHHHHH
-
7832-HydroxyisobutyrylationVRTMLVRKIQEESLR
HHHHHHHHHCHHHHH
-
783UbiquitinationVRTMLVRKIQEESLR
HHHHHHHHHCHHHHH
-
788PhosphorylationVRKIQEESLRTYLFT
HHHHCHHHHHHHHHC
21406692
821PhosphorylationLDLPTVHSIISKMII
CCHHHHHHHHHHHHC
24719451
840PhosphorylationMASLDQPTQTVVMHR
HHCCCCCCCEEEEEC
20860994
842PhosphorylationSLDQPTQTVVMHRTE
CCCCCCCEEEEECCC
21601212
848PhosphorylationQTVVMHRTEPTAQQN
CEEEEECCCCHHHHH
20860994
863UbiquitinationLALQLAEKLGSLVEN
HHHHHHHHHHHHHHC
21890473
866PhosphorylationQLAEKLGSLVENNER
HHHHHHHHHHHCCCC
21815630
878UbiquitinationNERVFDHKQGTYGGY
CCCEECCCCCCCCCC
21890473
881PhosphorylationVFDHKQGTYGGYFRD
EECCCCCCCCCCCCC
28152594
882PhosphorylationFDHKQGTYGGYFRDQ
ECCCCCCCCCCCCCC
28152594
885PhosphorylationKQGTYGGYFRDQKDG
CCCCCCCCCCCCCCC
28152594
890UbiquitinationGGYFRDQKDGYRKNE
CCCCCCCCCCCCCCC
890473
893PhosphorylationFRDQKDGYRKNEGYM
CCCCCCCCCCCCCCC
29759185
895UbiquitinationDQKDGYRKNEGYMRR
CCCCCCCCCCCCCCC
21890473
899PhosphorylationGYRKNEGYMRRGGYR
CCCCCCCCCCCCCCC
-
902MethylationKNEGYMRRGGYRQQQ
CCCCCCCCCCCCCCC
-
905PhosphorylationGYMRRGGYRQQQSQT
CCCCCCCCCCCCCCC
26074081
910PhosphorylationGGYRQQQSQTAY---
CCCCCCCCCCCC---
25159151
912PhosphorylationYRQQQSQTAY-----
CCCCCCCCCC-----
22617229
914PhosphorylationQQQSQTAY-------
CCCCCCCC-------
22199227

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 EIFCL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIFCL_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 EIFCL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3A_HUMANEIF3Aphysical
22863883
EIF3E_HUMANEIF3Ephysical
22863883
CPSF5_HUMANNUDT21physical
22863883
RS12_HUMANRPS12physical
22863883
RS18_HUMANRPS18physical
22863883
RS24_HUMANRPS24physical
22863883
RS2_HUMANRPS2physical
22863883
RS3_HUMANRPS3physical
22863883
EIF3B_HUMANEIF3Bphysical
26344197
EIF3D_HUMANEIF3Dphysical
26344197
EIF3G_HUMANEIF3Gphysical
26344197
CLCB_HUMANCLTBphysical
27173435
DP13A_HUMANAPPL1physical
27173435
CLCA_HUMANCLTAphysical
27173435

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EIFCL_HUMAN

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Related Literatures of Post-Translational Modification

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