EIF3A_HUMAN - dbPTM
EIF3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3A_HUMAN
UniProt AC Q14152
Protein Name Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000}
Gene Name EIF3A {ECO:0000255|HAMAP-Rule:MF_03000}
Organism Homo sapiens (Human).
Sequence Length 1382
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: 17581632]
Protein Sequence MPAYFQRPENALKRANEFLEVGKKQPALDVLYDVMKSKKHRTWQKIHEPIMLKYLELCVDLRKSHLAKEGLYQYKNICQQVNIKSLEDVVRAYLKMAEEKTEAAKEESQQMVLDIEDLDNIQTPESVLLSAVSGEDTQDRTDRLLLTPWVKFLWESYRQCLDLLRNNSRVERLYHDIAQQAFKFCLQYTRKAEFRKLCDNLRMHLSQIQRHHNQSTAINLNNPESQSMHLETRLVQLDSAISMELWQEAFKAVEDIHGLFSLSKKPPKPQLMANYYNKVSTVFWKSGNALFHASTLHRLYHLSREMRKNLTQDEMQRMSTRVLLATLSIPITPERTDIARLLDMDGIIVEKQRRLATLLGLQAPPTRIGLINDMVRFNVLQYVVPEVKDLYNWLEVEFNPLKLCERVTKVLNWVREQPEKEPELQQYVPQLQNNTILRLLQQVSQIYQSIEFSRLTSLVPFVDAFQLERAIVDAARHCDLQVRIDHTSRTLSFGSDLNYATREDAPIGPHLQSMPSEQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHNRLEERKRQRKEERRITYYREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVERKKRQRELEIEERERRREEERRLGDSSLSRKDSRWGDRDSEGTWRKGPEADSEWRRGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVPRRGMDDDRGPRRGPEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSWRTADEDRGPRRGMDDDRGPRRGGADDERSSWRNADDDRGPRRGLDDDRGPRRGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRGPWRNADDDRIPRRGAEDDRGPWRNMDDDRLSRRADDDRFPRRGDDSRPGPWRPLVKPGGWREKEKAREESWGPPRESRPSEEREWDREKERDRDNQDREENDKDPERERDRERDVDREDRFRRPRDEGGWRRGPAEESSSWRDSSRRDDRDRDDRRRERDDRRDLRERRDLRDDRDRRGPPLRSEREEVSSWRRADDRKDDRVEERDPPRRVPPPALSRDRERDRDREREGEKEKASWRAEKDRESLRRTKNETDEDGWTTVRR
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
4Phosphorylation----MPAYFQRPENA
----CCCCCCCHHHH
15.8028152594
11UbiquitinationYFQRPENALKRANEF
CCCCHHHHHHHHHHH
16.88-
13UbiquitinationQRPENALKRANEFLE
CCHHHHHHHHHHHHH
47.2421890473
13MethylationQRPENALKRANEFLE
CCHHHHHHHHHHHHH
47.24-
13UbiquitinationQRPENALKRANEFLE
CCHHHHHHHHHHHHH
47.2422817900
232-HydroxyisobutyrylationNEFLEVGKKQPALDV
HHHHHHCCCCCHHHH
54.10-
23AcetylationNEFLEVGKKQPALDV
HHHHHHCCCCCHHHH
54.1025953088
23MalonylationNEFLEVGKKQPALDV
HHHHHHCCCCCHHHH
54.1030639696
23UbiquitinationNEFLEVGKKQPALDV
HHHHHHCCCCCHHHH
54.1021906983
24UbiquitinationEFLEVGKKQPALDVL
HHHHHCCCCCHHHHH
56.4329967540
32PhosphorylationQPALDVLYDVMKSKK
CCHHHHHHHHHHHCC
13.3127259358
34AcetylationALDVLYDVMKSKKHR
HHHHHHHHHHHCCCC
3.08-
34UbiquitinationALDVLYDVMKSKKHR
HHHHHHHHHHHCCCC
3.08-
36AcetylationDVLYDVMKSKKHRTW
HHHHHHHHHCCCCCH
60.0025953088
36UbiquitinationDVLYDVMKSKKHRTW
HHHHHHHHHCCCCCH
60.0032015554
39UbiquitinationYDVMKSKKHRTWQKI
HHHHHHCCCCCHHHC
45.4723000965
41UbiquitinationVMKSKKHRTWQKIHE
HHHHCCCCCHHHCCH
46.68-
45UbiquitinationKKHRTWQKIHEPIML
CCCCCHHHCCHHHHH
37.2821890473
45AcetylationKKHRTWQKIHEPIML
CCCCCHHHCCHHHHH
37.2826051181
45UbiquitinationKKHRTWQKIHEPIML
CCCCCHHHCCHHHHH
37.2823000965
50UbiquitinationWQKIHEPIMLKYLEL
HHHCCHHHHHHHHHH
4.62-
51SulfoxidationQKIHEPIMLKYLELC
HHCCHHHHHHHHHHH
3.7530846556
54AcetylationHEPIMLKYLELCVDL
CHHHHHHHHHHHHHH
11.0519413330
682-HydroxyisobutyrylationLRKSHLAKEGLYQYK
HHHHHHHHHHHHHHH
59.69-
68AcetylationLRKSHLAKEGLYQYK
HHHHHHHHHHHHHHH
59.6919608861
68MalonylationLRKSHLAKEGLYQYK
HHHHHHHHHHHHHHH
59.6926320211
68UbiquitinationLRKSHLAKEGLYQYK
HHHHHHHHHHHHHHH
59.6933845483
71UbiquitinationSHLAKEGLYQYKNIC
HHHHHHHHHHHHHHH
2.24-
72PhosphorylationHLAKEGLYQYKNICQ
HHHHHHHHHHHHHHH
22.2128152594
74PhosphorylationAKEGLYQYKNICQQV
HHHHHHHHHHHHHHC
7.7628152594
75AcetylationKEGLYQYKNICQQVN
HHHHHHHHHHHHHCC
25.0625953088
75UbiquitinationKEGLYQYKNICQQVN
HHHHHHHHHHHHHCC
25.0621906983
78GlutathionylationLYQYKNICQQVNIKS
HHHHHHHHHHCCCCC
3.0222555962
84AcetylationICQQVNIKSLEDVVR
HHHHCCCCCHHHHHH
43.7326051181
84UbiquitinationICQQVNIKSLEDVVR
HHHHCCCCCHHHHHH
43.7329967540
95AcetylationDVVRAYLKMAEEKTE
HHHHHHHHHHHHHHH
24.3225953088
95UbiquitinationDVVRAYLKMAEEKTE
HHHHHHHHHHHHHHH
24.3232015554
100UbiquitinationYLKMAEEKTEAAKEE
HHHHHHHHHHHHHHH
43.0723503661
101PhosphorylationLKMAEEKTEAAKEES
HHHHHHHHHHHHHHH
33.8524043423
105UbiquitinationEEKTEAAKEESQQMV
HHHHHHHHHHHHHHC
69.8933845483
108PhosphorylationTEAAKEESQQMVLDI
HHHHHHHHHHHCCCH
27.1424043423
123PhosphorylationEDLDNIQTPESVLLS
HHHCCCCCCHHHHHH
25.8124043423
126PhosphorylationDNIQTPESVLLSAVS
CCCCCCHHHHHHHHC
21.1924043423
130PhosphorylationTPESVLLSAVSGEDT
CCHHHHHHHHCCCCC
23.5924043423
133PhosphorylationSVLLSAVSGEDTQDR
HHHHHHHCCCCCCCC
35.8624043423
147PhosphorylationRTDRLLLTPWVKFLW
CHHHHHHHHHHHHHH
18.31-
162AcetylationESYRQCLDLLRNNSR
HHHHHHHHHHHCCHH
51.81-
162UbiquitinationESYRQCLDLLRNNSR
HHHHHHHHHHHCCHH
51.81-
174PhosphorylationNSRVERLYHDIAQQA
CHHHHHHHHHHHHHH
12.0328152594
196AcetylationTRKAEFRKLCDNLRM
HHHHHHHHHHHHHHH
59.8123749302
196MalonylationTRKAEFRKLCDNLRM
HHHHHHHHHHHHHHH
59.8126320211
196UbiquitinationTRKAEFRKLCDNLRM
HHHHHHHHHHHHHHH
59.8129967540
203SulfoxidationKLCDNLRMHLSQIQR
HHHHHHHHHHHHHHH
4.1430846556
206PhosphorylationDNLRMHLSQIQRHHN
HHHHHHHHHHHHHHC
15.5720873877
243SulfoxidationQLDSAISMELWQEAF
HHHHHHHHHHHHHHH
3.9228183972
251UbiquitinationELWQEAFKAVEDIHG
HHHHHHHHHHHHHHH
59.58-
261PhosphorylationEDIHGLFSLSKKPPK
HHHHHHHHCCCCCCC
36.4521406692
263PhosphorylationIHGLFSLSKKPPKPQ
HHHHHHCCCCCCCCC
37.1221406692
265UbiquitinationGLFSLSKKPPKPQLM
HHHHCCCCCCCCCCC
64.2829967540
268UbiquitinationSLSKKPPKPQLMANY
HCCCCCCCCCCCHHH
54.6532015554
274UbiquitinationPKPQLMANYYNKVST
CCCCCCHHHHHHCEE
26.34-
278UbiquitinationLMANYYNKVSTVFWK
CCHHHHHHCEEEEEE
22.8032015554
285UbiquitinationKVSTVFWKSGNALFH
HCEEEEEECCCHHHH
36.7023000965
294PhosphorylationGNALFHASTLHRLYH
CCHHHHHHHHHHHHH
23.9620873877
295PhosphorylationNALFHASTLHRLYHL
CHHHHHHHHHHHHHH
27.6320873877
300PhosphorylationASTLHRLYHLSREMR
HHHHHHHHHHCHHHH
10.7324719451
303PhosphorylationLHRLYHLSREMRKNL
HHHHHHHCHHHHHCC
16.9424719451
308MalonylationHLSREMRKNLTQDEM
HHCHHHHHCCCHHHH
55.8126320211
308UbiquitinationHLSREMRKNLTQDEM
HHCHHHHHCCCHHHH
55.8123000965
311PhosphorylationREMRKNLTQDEMQRM
HHHHHCCCHHHHHHH
43.2821406692
315SulfoxidationKNLTQDEMQRMSTRV
HCCCHHHHHHHHHHH
4.0530846556
317UbiquitinationLTQDEMQRMSTRVLL
CCHHHHHHHHHHHHH
21.51-
319PhosphorylationQDEMQRMSTRVLLAT
HHHHHHHHHHHHHHH
18.4328176443
320PhosphorylationDEMQRMSTRVLLATL
HHHHHHHHHHHHHHH
18.5628176443
326PhosphorylationSTRVLLATLSIPITP
HHHHHHHHHCCCCCC
22.4728176443
328PhosphorylationRVLLATLSIPITPER
HHHHHHHCCCCCCCC
23.2028176443
332PhosphorylationATLSIPITPERTDIA
HHHCCCCCCCCCCHH
17.4728176443
336PhosphorylationIPITPERTDIARLLD
CCCCCCCCCHHHHHC
30.0526270265
344SulfoxidationDIARLLDMDGIIVEK
CHHHHHCCCCCHHHH
5.2621406390
3512-HydroxyisobutyrylationMDGIIVEKQRRLATL
CCCCHHHHHHHHHHH
37.91-
351AcetylationMDGIIVEKQRRLATL
CCCCHHHHHHHHHHH
37.9126051181
351UbiquitinationMDGIIVEKQRRLATL
CCCCHHHHHHHHHHH
37.9121906983
368UbiquitinationLQAPPTRIGLINDMV
CCCCCCHHHHHHHHH
6.07-
374SulfoxidationRIGLINDMVRFNVLQ
HHHHHHHHHHHCHHH
1.6930846556
375UbiquitinationIGLINDMVRFNVLQY
HHHHHHHHHHCHHHH
7.63-
382PhosphorylationVRFNVLQYVVPEVKD
HHHCHHHHHCHHHHH
10.1527259358
386UbiquitinationVLQYVVPEVKDLYNW
HHHHHCHHHHHHHCH
51.06-
402UbiquitinationEVEFNPLKLCERVTK
CCCCCHHHHHHHHHH
52.9621906983
409UbiquitinationKLCERVTKVLNWVRE
HHHHHHHHHHHHHHH
41.7021890473
409AcetylationKLCERVTKVLNWVRE
HHHHHHHHHHHHHHH
41.7026051181
409UbiquitinationKLCERVTKVLNWVRE
HHHHHHHHHHHHHHH
41.7022817900
420UbiquitinationWVREQPEKEPELQQY
HHHHCCCCCHHHHHH
82.3921890473
420AcetylationWVREQPEKEPELQQY
HHHHCCCCCHHHHHH
82.3926051181
420UbiquitinationWVREQPEKEPELQQY
HHHHCCCCCHHHHHH
82.3923000965
435PhosphorylationVPQLQNNTILRLLQQ
HHHHHHHHHHHHHHH
29.0124719451
478S-nitrosocysteineIVDAARHCDLQVRID
HHHHHHHCCEEEEEE
4.68-
478S-nitrosylationIVDAARHCDLQVRID
HHHHHHHCCEEEEEE
4.6819483679
490PhosphorylationRIDHTSRTLSFGSDL
EEECCCCCEECCCCC
26.9030266825
492PhosphorylationDHTSRTLSFGSDLNY
ECCCCCEECCCCCCC
27.2730266825
495PhosphorylationSRTLSFGSDLNYATR
CCCEECCCCCCCCCC
36.5930266825
498UbiquitinationLSFGSDLNYATREDA
EECCCCCCCCCCCCC
29.41-
499PhosphorylationSFGSDLNYATREDAP
ECCCCCCCCCCCCCC
19.3530266825
501PhosphorylationGSDLNYATREDAPIG
CCCCCCCCCCCCCCC
25.0030266825
504AcetylationLNYATREDAPIGPHL
CCCCCCCCCCCCHHH
55.12-
514SulfoxidationIGPHLQSMPSEQIRN
CCHHHHCCCHHHHHH
2.4630846556
524PhosphorylationEQIRNQLTAMSSVLA
HHHHHHHHHHHHHHH
15.5620068231
525UbiquitinationQIRNQLTAMSSVLAK
HHHHHHHHHHHHHHH
12.40-
528PhosphorylationNQLTAMSSVLAKALE
HHHHHHHHHHHHHHH
14.2021712546
532UbiquitinationAMSSVLAKALEVIKP
HHHHHHHHHHHHHCH
49.7133845483
5382-HydroxyisobutyrylationAKALEVIKPAHILQE
HHHHHHHCHHHHHHH
41.13-
538AcetylationAKALEVIKPAHILQE
HHHHHHHCHHHHHHH
41.1323236377
538UbiquitinationAKALEVIKPAHILQE
HHHHHHHCHHHHHHH
41.1333845483
546AcetylationPAHILQEKEEQHQLA
HHHHHHHHHHHHHHH
54.3025953088
546UbiquitinationPAHILQEKEEQHQLA
HHHHHHHHHHHHHHH
54.3033845483
557UbiquitinationHQLAVTAYLKNSRKE
HHHHHHHHHHHCHHH
14.62-
559AcetylationLAVTAYLKNSRKEHQ
HHHHHHHHHCHHHHH
39.9525953088
559MalonylationLAVTAYLKNSRKEHQ
HHHHHHHHHCHHHHH
39.9526320211
559MethylationLAVTAYLKNSRKEHQ
HHHHHHHHHCHHHHH
39.95-
559UbiquitinationLAVTAYLKNSRKEHQ
HHHHHHHHHCHHHHH
39.9533845483
563UbiquitinationAYLKNSRKEHQRILA
HHHHHCHHHHHHHHH
60.4123503661
569UbiquitinationRKEHQRILARRQTIE
HHHHHHHHHHHHHHH
3.10-
574PhosphorylationRILARRQTIEERKER
HHHHHHHHHHHHHHH
28.6627273156
584PhosphorylationERKERLESLNIQREK
HHHHHHHHCCHHHHH
31.1619664994
591UbiquitinationSLNIQREKEELEQRE
HCCHHHHHHHHHHHH
59.6933845483
598MethylationKEELEQREAELQKVR
HHHHHHHHHHHHHHH
46.30-
598UbiquitinationKEELEQREAELQKVR
HHHHHHHHHHHHHHH
46.30-
599MethylationEELEQREAELQKVRK
HHHHHHHHHHHHHHH
25.62-
599UbiquitinationEELEQREAELQKVRK
HHHHHHHHHHHHHHH
25.62-
600MethylationELEQREAELQKVRKA
HHHHHHHHHHHHHHH
47.16-
600UbiquitinationELEQREAELQKVRKA
HHHHHHHHHHHHHHH
47.16-
603AcetylationQREAELQKVRKAEEE
HHHHHHHHHHHHHHH
57.5425953088
603UbiquitinationQREAELQKVRKAEEE
HHHHHHHHHHHHHHH
57.5427667366
617UbiquitinationERLRQEAKEREKERI
HHHHHHHHHHHHHHH
57.46-
617UbiquitinationERLRQEAKEREKERI
HHHHHHHHHHHHHHH
57.4629967540
620UbiquitinationRQEAKEREKERILQE
HHHHHHHHHHHHHHH
61.43-
621UbiquitinationQEAKEREKERILQEH
HHHHHHHHHHHHHHH
59.5229967540
6322-HydroxyisobutyrylationLQEHEQIKKKTVRER
HHHHHHHHHHHHHHH
48.16-
632AcetylationLQEHEQIKKKTVRER
HHHHHHHHHHHHHHH
48.1625953088
632MethylationLQEHEQIKKKTVRER
HHHHHHHHHHHHHHH
48.1623644510
632UbiquitinationLQEHEQIKKKTVRER
HHHHHHHHHHHHHHH
48.1621906983
633MethylationQEHEQIKKKTVRERL
HHHHHHHHHHHHHHH
56.1323644510
633UbiquitinationQEHEQIKKKTVRERL
HHHHHHHHHHHHHHH
56.1322817900
634MethylationEHEQIKKKTVRERLE
HHHHHHHHHHHHHHH
47.4523644510
634UbiquitinationEHEQIKKKTVRERLE
HHHHHHHHHHHHHHH
47.4522817900
635PhosphorylationHEQIKKKTVRERLEQ
HHHHHHHHHHHHHHH
33.40-
638UbiquitinationIKKKTVRERLEQIKK
HHHHHHHHHHHHHHH
58.23-
644UbiquitinationRERLEQIKKTELGAK
HHHHHHHHHCHHHHH
54.0227667366
645UbiquitinationERLEQIKKTELGAKA
HHHHHHHHCHHHHHH
49.1932015554
646PhosphorylationRLEQIKKTELGAKAF
HHHHHHHCHHHHHHC
31.2930576142
6512-HydroxyisobutyrylationKKTELGAKAFKDIDI
HHCHHHHHHCCCCCH
53.19-
651UbiquitinationKKTELGAKAFKDIDI
HHCHHHHHHCCCCCH
53.1921906983
654UbiquitinationELGAKAFKDIDIEDL
HHHHHHCCCCCHHHH
59.6421906983
660UbiquitinationFKDIDIEDLEELDPD
CCCCCHHHHHHHCHH
60.77-
670SulfoxidationELDPDFIMAKQVEQL
HHCHHHHHHHHHHHH
3.7330846556
672UbiquitinationDPDFIMAKQVEQLEK
CHHHHHHHHHHHHHH
37.1821906983
677UbiquitinationMAKQVEQLEKEKKEL
HHHHHHHHHHHHHHH
6.85-
679UbiquitinationKQVEQLEKEKKELQE
HHHHHHHHHHHHHHH
81.2233845483
681UbiquitinationVEQLEKEKKELQERL
HHHHHHHHHHHHHHH
63.7229967540
682UbiquitinationEQLEKEKKELQERLK
HHHHHHHHHHHHHHH
65.8229967540
686UbiquitinationKEKKELQERLKNQEK
HHHHHHHHHHHHHHH
73.02-
689UbiquitinationKELQERLKNQEKKID
HHHHHHHHHHHHHHH
63.9122817900
693AcetylationERLKNQEKKIDYFER
HHHHHHHHHHHHHHH
45.317978581
693UbiquitinationERLKNQEKKIDYFER
HHHHHHHHHHHHHHH
45.3122817900
694AcetylationRLKNQEKKIDYFERA
HHHHHHHHHHHHHHH
39.8026051181
694MalonylationRLKNQEKKIDYFERA
HHHHHHHHHHHHHHH
39.8026320211
694UbiquitinationRLKNQEKKIDYFERA
HHHHHHHHHHHHHHH
39.8022817900
697PhosphorylationNQEKKIDYFERAKRL
HHHHHHHHHHHHHHH
15.7128152594
700MethylationKKIDYFERAKRLEEI
HHHHHHHHHHHHHHC
35.19-
711UbiquitinationLEEIPLIKSAYEEQR
HHHCCCCHHHHHHHC
36.3921890473
7112-HydroxyisobutyrylationLEEIPLIKSAYEEQR
HHHCCCCHHHHHHHC
36.39-
711AcetylationLEEIPLIKSAYEEQR
HHHCCCCHHHHHHHC
36.3925953088
711UbiquitinationLEEIPLIKSAYEEQR
HHHCCCCHHHHHHHC
36.3923000965
7202-HydroxyisobutyrylationAYEEQRIKDMDLWEQ
HHHHHCCCCCCHHHH
49.54-
720UbiquitinationAYEEQRIKDMDLWEQ
HHHHHCCCCCCHHHH
49.5421906983
722SulfoxidationEEQRIKDMDLWEQQE
HHHCCCCCCHHHHHH
3.7630846556
736SulfoxidationEEERITTMQLEREKA
HHHHHHHHHHHHHHH
2.9921406390
741UbiquitinationTTMQLEREKALEHKN
HHHHHHHHHHHHHHH
33.05-
7422-HydroxyisobutyrylationTMQLEREKALEHKNR
HHHHHHHHHHHHHHH
65.57-
742UbiquitinationTMQLEREKALEHKNR
HHHHHHHHHHHHHHH
65.5724816145
743UbiquitinationMQLEREKALEHKNRM
HHHHHHHHHHHHHHH
17.27-
7472-HydroxyisobutyrylationREKALEHKNRMSRML
HHHHHHHHHHHHHHH
36.55-
757MethylationMSRMLEDRDLFVMRL
HHHHHCHHCHHHHHH
32.91-
770PhosphorylationRLKAARQSVYEEKLK
HHHHHHHHHHHHHHH
22.5523401153
772PhosphorylationKAARQSVYEEKLKQF
HHHHHHHHHHHHHHH
24.5028152594
775UbiquitinationRQSVYEEKLKQFEER
HHHHHHHHHHHHHHH
49.3921890473
7752-HydroxyisobutyrylationRQSVYEEKLKQFEER
HHHHHHHHHHHHHHH
49.39-
775AcetylationRQSVYEEKLKQFEER
HHHHHHHHHHHHHHH
49.3927452117
775NeddylationRQSVYEEKLKQFEER
HHHHHHHHHHHHHHH
49.3932015554
775UbiquitinationRQSVYEEKLKQFEER
HHHHHHHHHHHHHHH
49.3921906983
777UbiquitinationSVYEEKLKQFEERLA
HHHHHHHHHHHHHHH
65.1021890473
777UbiquitinationSVYEEKLKQFEERLA
HHHHHHHHHHHHHHH
65.1023000965
782MethylationKLKQFEERLAEERHN
HHHHHHHHHHHHHHH
31.81-
790UbiquitinationLAEERHNRLEERKRQ
HHHHHHHHHHHHHHH
37.03-
822SulfoxidationQRRAEEQMLKEREER
HHHHHHHHHHHHHHH
6.9830846556
824UbiquitinationRAEEQMLKEREERER
HHHHHHHHHHHHHHH
49.7521906983
842MethylationAKREEELREYQERVK
HHHHHHHHHHHHHHH
43.80-
844PhosphorylationREEELREYQERVKKL
HHHHHHHHHHHHHHH
14.83-
850UbiquitinationEYQERVKKLEEVERK
HHHHHHHHHHHHHHH
59.2724816145
881PhosphorylationEERRLGDSSLSRKDS
HHHHHCCCCCCCCCC
31.2329255136
882PhosphorylationERRLGDSSLSRKDSR
HHHHCCCCCCCCCCC
34.7929255136
884PhosphorylationRLGDSSLSRKDSRWG
HHCCCCCCCCCCCCC
38.9530266825
888PhosphorylationSSLSRKDSRWGDRDS
CCCCCCCCCCCCCCC
32.7326074081
895PhosphorylationSRWGDRDSEGTWRKG
CCCCCCCCCCCCCCC
38.5325159151
898PhosphorylationGDRDSEGTWRKGPEA
CCCCCCCCCCCCCCC
20.3222115753
916AcetylationWRRGPPEKEWRRGEG
CCCCCCHHHCCCCCC
69.2426051181
949PhosphorylationDDEDREPSLRPDDDR
CCCCCCCCCCCCCCC
32.0526657352
956MethylationSLRPDDDRVPRRGMD
CCCCCCCCCCCCCCC
47.54-
960MethylationDDDRVPRRGMDDDRG
CCCCCCCCCCCCCCC
38.42-
966MethylationRRGMDDDRGPRRGPE
CCCCCCCCCCCCCCH
65.10-
976MethylationRRGPEEDRFSRRGAD
CCCCHHHCCCCCCCC
34.42-
978PhosphorylationGPEEDRFSRRGADDD
CCHHHCCCCCCCCCC
23.2029255136
986MethylationRRGADDDRPSWRNTD
CCCCCCCCCCCCCCC
33.86-
988PhosphorylationGADDDRPSWRNTDDD
CCCCCCCCCCCCCCC
39.2926091039
992PhosphorylationDRPSWRNTDDDRPPR
CCCCCCCCCCCCCCC
32.0328555341
1006MethylationRRIADEDRGNWRHAD
CCCCCCCCCCCCCCC
37.99-
1026MethylationRRGLDEDRGSWRTAD
CCCCCCCCCCCCCCC
38.71-
1028PhosphorylationGLDEDRGSWRTADED
CCCCCCCCCCCCCCC
17.8023401153
1031PhosphorylationEDRGSWRTADEDRGP
CCCCCCCCCCCCCCC
32.0030576142
1040MethylationDEDRGPRRGMDDDRG
CCCCCCCCCCCCCCC
48.17-
1046MethylationRRGMDDDRGPRRGGA
CCCCCCCCCCCCCCC
65.10-
1057MethylationRGGADDERSSWRNAD
CCCCCCCCHHCCCCC
42.88-
1058PhosphorylationGGADDERSSWRNADD
CCCCCCCHHCCCCCC
32.0027251275
1059PhosphorylationGADDERSSWRNADDD
CCCCCCHHCCCCCCC
35.9520068231
1071MethylationDDDRGPRRGLDDDRG
CCCCCCCCCCCCCCC
53.83-
1081MethylationDDDRGPRRGMDDDRG
CCCCCCCCCCCCCCC
48.17-
1087MethylationRRGMDDDRGPRRGMD
CCCCCCCCCCCCCCC
65.10-
1091MethylationDDDRGPRRGMDDDRG
CCCCCCCCCCCCCCC
48.17-
1097MethylationRRGMDDDRGPRRGMD
CCCCCCCCCCCCCCC
65.10-
1101MethylationDDDRGPRRGMDDDRG
CCCCCCCCCCCCCCC
48.17-
1107MethylationRRGMDDDRGPRRGLD
CCCCCCCCCCCCCCC
65.10-
1111MethylationDDDRGPRRGLDDDRG
CCCCCCCCCCCCCCC
53.83-
1117MethylationRRGLDDDRGPWRNAD
CCCCCCCCCCCCCCC
61.13-
1127MethylationWRNADDDRIPRRGAE
CCCCCCCCCCCCCCC
48.05-
1137MethylationRRGAEDDRGPWRNMD
CCCCCCCCCCCCCCC
66.45-
1149PhosphorylationNMDDDRLSRRADDDR
CCCCHHHHHHCCCCC
22.1825850435
1156MethylationSRRADDDRFPRRGDD
HHHCCCCCCCCCCCC
50.92-
1174AcetylationGPWRPLVKPGGWREK
CCCCCCCCCCCHHHH
45.7012433583
1188PhosphorylationKEKAREESWGPPRES
HHHHHHHHCCCCCCC
32.3623401153
1195PhosphorylationSWGPPRESRPSEERE
HCCCCCCCCCCHHHH
51.2623403867
1198PhosphorylationPPRESRPSEEREWDR
CCCCCCCCHHHHHHH
51.4825159151
1238MethylationRDVDREDRFRRPRDE
CCCCHHHHCCCCCCC
23.40-
1256PhosphorylationRRGPAEESSSWRDSS
CCCCCCCCCCCCCCC
22.6028857561
1257PhosphorylationRGPAEESSSWRDSSR
CCCCCCCCCCCCCCC
36.8826434776
1258PhosphorylationGPAEESSSWRDSSRR
CCCCCCCCCCCCCCC
35.1028985074
1262PhosphorylationESSSWRDSSRRDDRD
CCCCCCCCCCCCCCC
19.7126434776
1263PhosphorylationSSSWRDSSRRDDRDR
CCCCCCCCCCCCCCH
35.3122617229
1302PhosphorylationRRGPPLRSEREEVSS
CCCCCCHHHHHHHHH
49.0028555341
1309PhosphorylationSEREEVSSWRRADDR
HHHHHHHHHCCCCCC
29.76-
1336PhosphorylationRVPPPALSRDRERDR
CCCCCCCCCHHHHHH
33.9523401153
1351AcetylationDREREGEKEKASWRA
HHHHHHHHHHHHHHH
75.3120167786
1355PhosphorylationEGEKEKASWRAEKDR
HHHHHHHHHHHHHHH
28.32-
1364PhosphorylationRAEKDRESLRRTKNE
HHHHHHHHHHHHCCC
28.2428355574
1368PhosphorylationDRESLRRTKNETDED
HHHHHHHHCCCCCCC
31.6126074081
1372PhosphorylationLRRTKNETDEDGWTT
HHHHCCCCCCCCCCC
54.8321815630
1378PhosphorylationETDEDGWTTVRR---
CCCCCCCCCCCC---
22.4226074081
1379PhosphorylationTDEDGWTTVRR----
CCCCCCCCCCC----
12.9026074081

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
1364SPhosphorylationKinasePKCB ISO2P05771-2
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3A_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 EIF3A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3L_HUMANEIF3Lphysical
17353931
EIF3E_HUMANEIF3Ephysical
17353931
EIF3H_HUMANEIF3Hphysical
17353931
EIF3I_HUMANEIF3Iphysical
17353931
EIF3F_HUMANEIF3Fphysical
17353931
EIF3K_HUMANEIF3Kphysical
17353931
EIF3M_HUMANEIF3Mphysical
17353931
EIF3D_HUMANEIF3Dphysical
17353931
EIF3K_HUMANEIF3Kphysical
14519125
EIF3B_HUMANEIF3Bphysical
14519125
EIF3E_HUMANEIF3Ephysical
14519125
EIF3G_HUMANEIF3Gphysical
14519125
EIF3I_HUMANEIF3Iphysical
14519125
EIF3J_HUMANEIF3Jphysical
14519125
EIF3C_HUMANEIF3Cphysical
14519125
EIF3D_HUMANEIF3Dphysical
14519125
EIF3F_HUMANEIF3Fphysical
14519125
EIF3H_HUMANEIF3Hphysical
14519125
EIF3I_HUMANEIF3Iphysical
8995409
EIF3L_HUMANEIF3Lphysical
11590142
EIF3B_HUMANEIF3Bphysical
9822659
EIF3C_HUMANEIF3Cphysical
9822659
EIF3D_HUMANEIF3Dphysical
9822659
EIF3F_HUMANEIF3Fphysical
9822659
EIF3G_HUMANEIF3Gphysical
9822659
EIF3H_HUMANEIF3Hphysical
9822659
EIF3J_HUMANEIF3Jphysical
9822659
EIF3B_HUMANEIF3Bphysical
8995410
EIF3D_HUMANEIF3Dphysical
9341143
EIF3F_HUMANEIF3Fphysical
9341143
EIF3G_HUMANEIF3Gphysical
9341143
EIF3F_HUMANEIF3Fphysical
19245811
EIF3B_HUMANEIF3Bphysical
19245811
EIF3B_HUMANEIF3Bphysical
22939629
EIF3I_HUMANEIF3Iphysical
22939629
EIF3E_HUMANEIF3Ephysical
22939629
EIF3F_HUMANEIF3Fphysical
22939629
EIF3D_HUMANEIF3Dphysical
22939629
EIF3K_HUMANEIF3Kphysical
22939629
EIF3C_HUMANEIF3Cphysical
22939629
EIF3G_HUMANEIF3Gphysical
22939629
EIF3H_HUMANEIF3Hphysical
22939629
EIF3L_HUMANEIF3Lphysical
22939629
EIF3M_HUMANEIF3Mphysical
22939629
IF4H_HUMANEIF4Hphysical
22939629
RLA1_HUMANRPLP1physical
22939629
NUCL_HUMANNCLphysical
22939629
NP1L4_HUMANNAP1L4physical
22939629
HNRPF_HUMANHNRNPFphysical
22939629
MSMO1_HUMANMSMO1physical
22939629
MYH9_HUMANMYH9physical
22939629
RM46_HUMANMRPL46physical
22939629
MYH11_HUMANMYH11physical
22939629
TOM40_HUMANTOMM40physical
22939629
TBB6_HUMANTUBB6physical
22939629
RENT1_HUMANUPF1physical
18423202
EIF3E_HUMANEIF3Ephysical
22863883
EIF3K_HUMANEIF3Kphysical
22863883
LARP1_HUMANLARP1physical
22863883
CPSF5_HUMANNUDT21physical
22863883
RS25_HUMANRPS25physical
22863883
RS9_HUMANRPS9physical
22863883
YTHD2_HUMANYTHDF2physical
22863883
TFP11_HUMANTFIP11physical
25416956
ABCF2_HUMANABCF2physical
26344197
EIF3B_HUMANEIF3Bphysical
26344197
EIF3C_HUMANEIF3Cphysical
26344197
EIFCL_HUMANEIF3CLphysical
26344197
EIF3D_HUMANEIF3Dphysical
26344197
EIF3F_HUMANEIF3Fphysical
26344197
EIF3G_HUMANEIF3Gphysical
26344197
EIF3H_HUMANEIF3Hphysical
26344197
EIF3I_HUMANEIF3Iphysical
26344197
EIF3K_HUMANEIF3Kphysical
26344197
UBIM_HUMANFAUphysical
27082860

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 EIF3A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-68, 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-492, AND MASSSPECTROMETRY.
"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-584 AND SER-1336, ANDMASS 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, PHOSPHORYLATION AT SER-881;SER-1198; SER-1336 AND SER-1364, AND MASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-382, AND MASSSPECTROMETRY.

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