IF4A2_HUMAN - dbPTM
IF4A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF4A2_HUMAN
UniProt AC Q14240
Protein Name Eukaryotic initiation factor 4A-II
Gene Name EIF4A2
Organism Homo sapiens (Human).
Sequence Length 407
Subcellular Localization
Protein Description ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon..
Protein Sequence MSGGSADYNREHGGPEGMDPDGVIESNWNEIVDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEWKLDTLCDLYETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETFYNTTVEEMPMNVADLI
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
2 (in isoform 2)Phosphorylation-52.4326852163
2Phosphorylation------MSGGSADYN
------CCCCCCCCC		52.4323663014
5Phosphorylation---MSGGSADYNREH
---CCCCCCCCCHHC		22.8423663014
5 (in isoform 2)Phosphorylation-22.8426852163
8PhosphorylationMSGGSADYNREHGGP
CCCCCCCCCHHCCCC		18.8124043423
49PhosphorylationESLLRGIYAYGFEKP
HHHHHHHHHCCCCCC		9.1528152594
51PhosphorylationLLRGIYAYGFEKPSA
HHHHHHHCCCCCCCH		12.8428152594
55SumoylationIYAYGFEKPSAIQQR
HHHCCCCCCCHHHHH		41.85-
55 (in isoform 1)Ubiquitination-41.8521890473
55MethylationIYAYGFEKPSAIQQR
HHHCCCCCCCHHHHH		41.85-
55SumoylationIYAYGFEKPSAIQQR
HHHCCCCCCCHHHHH		41.85-
55UbiquitinationIYAYGFEKPSAIQQR
HHHCCCCCCCHHHHH		41.8527667366
55AcetylationIYAYGFEKPSAIQQR
HHHCCCCCCCHHHHH		41.8516209465
56 (in isoform 2)Ubiquitination-23.0721890473
57PhosphorylationAYGFEKPSAIQQRAI
HCCCCCCCHHHHHCH		49.4228152594
67S-nitrosylationQQRAIIPCIKGYDVI
HHHCHHCCCCCCEEE		3.3724105792
69MethylationRAIIPCIKGYDVIAQ
HCHHCCCCCCEEEEE		59.12-
69 (in isoform 1)Ubiquitination-59.1221890473
69UbiquitinationRAIIPCIKGYDVIAQ
HCHHCCCCCCEEEEE		59.126983
69AcetylationRAIIPCIKGYDVIAQ
HCHHCCCCCCEEEEE		59.1226051181
70 (in isoform 2)Ubiquitination-12.1721890473
71PhosphorylationIIPCIKGYDVIAQAQ
HHCCCCCCEEEEEEC		11.3120090780
79PhosphorylationDVIAQAQSGTGKTAT
EEEEEECCCCCHHHH		41.1420873877
81PhosphorylationIAQAQSGTGKTATFA
EEEECCCCCHHHHHH		40.5320873877
83UbiquitinationQAQSGTGKTATFAIS
EECCCCCHHHHHHHH		34.5216196087
119UbiquitinationELAQQIQKVILALGD
HHHHHHHHHHHHHHH		32.6416196087
131PhosphorylationLGDYMGATCHACIGG
HHHCCCCCHHHHHCC		10.09-
139PhosphorylationCHACIGGTNVRNEMQ
HHHHHCCCHHHHHHH		25.9020068231
147UbiquitinationNVRNEMQKLQAEAPH
HHHHHHHHHHHCCCE		41.0521906983
147 (in isoform 1)Ubiquitination-41.0521890473
147AcetylationNVRNEMQKLQAEAPH
HHHHHHHHHHHCCCE		41.0526051181
148 (in isoform 2)Ubiquitination-3.0821890473
159PhosphorylationAPHIVVGTPGRVFDM
CCEEEECCCHHHHHH		15.8030266825
169MethylationRVFDMLNRRYLSPKW
HHHHHHCCCCCCHHH		25.34-
173PhosphorylationMLNRRYLSPKWIKMF
HHCCCCCCHHHHHEE		18.5924719451
175 (in isoform 1)Ubiquitination-59.1721890473
175UbiquitinationNRRYLSPKWIKMFVL
CCCCCCHHHHHEEEC		59.1721890473
175AcetylationNRRYLSPKWIKMFVL
CCCCCCHHHHHEEEC		59.1725953088
176 (in isoform 2)Ubiquitination-9.9821890473
178UbiquitinationYLSPKWIKMFVLDEA
CCCHHHHHEEECHHH		25.7723503661
179SulfoxidationLSPKWIKMFVLDEAD
CCHHHHHEEECHHHH		1.7528183972
190PhosphorylationDEADEMLSRGFKDQI
HHHHHHHHCCCHHHH		29.1023911959
194UbiquitinationEMLSRGFKDQIYEIF
HHHHCCCHHHHHHHH		52.1021906983
194 (in isoform 1)Ubiquitination-52.1021890473
195 (in isoform 2)Ubiquitination-37.5421890473
198PhosphorylationRGFKDQIYEIFQKLN
CCCHHHHHHHHHHHC		9.42-
199 (in isoform 2)Phosphorylation-38.6725147952
219PhosphorylationLLSATMPTDVLEVTK
EEECCCCCCHHHHHH		28.1120068231
225PhosphorylationPTDVLEVTKKFMRDP
CCCHHHHHHHHHCCC		21.0920068231
226UbiquitinationTDVLEVTKKFMRDPI
CCHHHHHHHHHCCCE		49.5422817900
226SumoylationTDVLEVTKKFMRDPI
CCHHHHHHHHHCCCE		49.54-
226SumoylationTDVLEVTKKFMRDPI
CCHHHHHHHHHCCCE		49.54-
227UbiquitinationDVLEVTKKFMRDPIR
CHHHHHHHHHCCCEE		34.7222817900
228 (in isoform 2)Ubiquitination-5.31-
238UbiquitinationDPIRILVKKEELTLE
CCEEEEEECCEECHH		51.5323000965
239UbiquitinationPIRILVKKEELTLEG
CEEEEEECCEECHHH		49.2823000965
243PhosphorylationLVKKEELTLEGIKQF
EEECCEECHHHHHHE		26.5029255136
248UbiquitinationELTLEGIKQFYINVE
EECHHHHHHEEEEEC		45.2529967540
251PhosphorylationLEGIKQFYINVEREE
HHHHHHEEEEECCCC		6.7828152594
256MethylationQFYINVEREEWKLDT
HEEEEECCCCCCHHH		42.74-
263PhosphorylationREEWKLDTLCDLYET
CCCCCHHHHHHHHHH		39.46-
268PhosphorylationLDTLCDLYETLTITQ
HHHHHHHHHHHCCEE		8.13-
285UbiquitinationIFLNTRRKVDWLTEK
HHHCCCCCCHHHHHH		41.0521890473
285 (in isoform 1)Ubiquitination-41.0521890473
286 (in isoform 2)Ubiquitination-6.3921890473
292SumoylationKVDWLTEKMHARDFT
CCHHHHHHHHHCCCC		30.65-
292AcetylationKVDWLTEKMHARDFT
CCHHHHHHHHHCCCC		30.6521690213
292SumoylationKVDWLTEKMHARDFT
CCHHHHHHHHHCCCC		30.65-
292 (in isoform 1)Ubiquitination-30.6521890473
292UbiquitinationKVDWLTEKMHARDFT
CCHHHHHHHHHCCCC		30.6527667366
293 (in isoform 2)Ubiquitination-2.1321890473
299PhosphorylationKMHARDFTVSALHGD
HHHHCCCCHHHHCCC		20.1729978859
301PhosphorylationHARDFTVSALHGDMD
HHCCCCHHHHCCCCC		23.2729978859
307SulfoxidationVSALHGDMDQKERDV
HHHHCCCCCHHHHHH		7.5221406390
310 (in isoform 1)Ubiquitination-50.9121890473
310UbiquitinationLHGDMDQKERDVIMR
HCCCCCHHHHHHHHH		50.9127667366
310AcetylationLHGDMDQKERDVIMR
HCCCCCHHHHHHHHH		50.9123749302
310MalonylationLHGDMDQKERDVIMR
HCCCCCHHHHHHHHH		50.9126320211
311 (in isoform 2)Malonylation-48.7826320211
311 (in isoform 2)Ubiquitination-48.7821890473
317MethylationKERDVIMREFRSGSS
HHHHHHHHHHHCCCC		28.86-
329PhosphorylationGSSRVLITTDLLARG
CCCCEEEEHHHHHCC		15.3121712546
330PhosphorylationSSRVLITTDLLARGI
CCCEEEEHHHHHCCC		20.0421712546
354MethylationNYDLPTNRENYIHRI
ECCCCCCCHHHCHHC		35.70-
370UbiquitinationRGGRFGRKGVAINFV
CCCCCCCCCEEEEEE		59.1022817900
371 (in isoform 2)Ubiquitination-16.84-
378PhosphorylationGVAINFVTEEDKRIL
CEEEEEECHHHHHHH		29.5328509920
382UbiquitinationNFVTEEDKRILRDIE
EEECHHHHHHHHHHH		44.6222505724
383 (in isoform 2)Ubiquitination-45.56-
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 IF4A2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF4A2_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 IF4A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4G1_HUMANEIF4G1physical
17353931
EIF3A_HUMANEIF3Aphysical
17353931
PDCD4_HUMANPDCD4physical
17353931
PDIA1_HUMANP4HBphysical
17353931
EIF3L_HUMANEIF3Lphysical
17353931
EIF3D_HUMANEIF3Dphysical
17353931
EIF3H_HUMANEIF3Hphysical
17353931
MYO1B_HUMANMYO1Bphysical
17353931
EIF3M_HUMANEIF3Mphysical
17353931
PABP1_HUMANPABPC1physical
17353931
EIF3K_HUMANEIF3Kphysical
17353931
IF4G3_HUMANEIF4G3physical
17353931
DDX3X_HUMANDDX3Xphysical
17353931
IF4G2_HUMANEIF4G2physical
17353931
IF4E_HUMANEIF4Ephysical
17353931
CD2B2_HUMANCD2BP2physical
17353931
JIP4_HUMANSPAG9physical
17353931
AK17A_HUMANAKAP17Aphysical
17353931
ATRX_HUMANATRXphysical
17353931
VAC14_HUMANVAC14physical
17353931
PPBI_HUMANALPIphysical
17353931
PTPRS_HUMANPTPRSphysical
17353931
RS29_HUMANRPS29physical
17353931
TPM3_HUMANTPM3physical
17353931
CMBL_HUMANCMBLphysical
17353931
IF4G3_HUMANEIF4G3physical
22939629
DX39B_HUMANDDX39Bphysical
22939629
IF4A2_HUMANEIF4A2physical
25416956
MDFI_HUMANMDFIphysical
25416956
PDCD4_HUMANPDCD4physical
25416956
IPO11_HUMANIPO11physical
25416956
DPPA4_HUMANDPPA4physical
25416956
TRI36_HUMANTRIM36physical
25416956
TRI39_HUMANTRIM39physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
PIHD2_HUMANPIH1D2physical
25416956
MOT9_HUMANSLC16A9physical
25416956
AIMP1_HUMANAIMP1physical
26344197
CETN2_HUMANCETN2physical
26344197
IF4A1_HUMANEIF4A1physical
26344197
IF4A3_HUMANEIF4A3physical
26344197
LAGE3_HUMANLAGE3physical
26344197
GOGA2_HUMANGOLGA2physical
21516116
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 IF4A2_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-292, AND MASS SPECTROMETRY.

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