IF1AY_HUMAN - dbPTM
IF1AY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF1AY_HUMAN
UniProt AC O14602
Protein Name Eukaryotic translation initiation factor 1A, Y-chromosomal
Gene Name EIF1AY
Organism Homo sapiens (Human).
Sequence Length 144
Subcellular Localization
Protein Description Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity)..
Protein Sequence MPKNKGKGGKNRRRGKNENESEKRELVFKEDGQEYAQVIKMLGNGRLEALCFDGVKRLCHIRGKLRKKVWINTSDIILVGLRDYQDNKADVILKYNADEARSLKAYGELPEHAKINETDTFGPGDDDEIQFDDIGDDDEDIDDI
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
3Acetylation-----MPKNKGKGGK
-----CCCCCCCCCC
70.7318435499
5Acetylation---MPKNKGKGGKNR
---CCCCCCCCCCCC
69.0318435509
7Acetylation-MPKNKGKGGKNRRR
-CCCCCCCCCCCCCC
67.1318435519
23UbiquitinationKNENESEKRELVFKE
CCCCHHHHHEEEEEC
61.52-
29UbiquitinationEKRELVFKEDGQEYA
HHHEEEEECCHHHHH
47.63-
29AcetylationEKRELVFKEDGQEYA
HHHEEEEECCHHHHH
47.6326051181
292-HydroxyisobutyrylationEKRELVFKEDGQEYA
HHHEEEEECCHHHHH
47.63-
35PhosphorylationFKEDGQEYAQVIKML
EECCHHHHHHHHHHH
8.4127642862
40UbiquitinationQEYAQVIKMLGNGRL
HHHHHHHHHHCCCCE
29.2621906983
56UbiquitinationALCFDGVKRLCHIRG
EEEEHHHHHHHHHHH
45.22-
56AcetylationALCFDGVKRLCHIRG
EEEEHHHHHHHHHHH
45.2223749302
67UbiquitinationHIRGKLRKKVWINTS
HHHHHHCCCEEEECC
63.21-
68UbiquitinationIRGKLRKKVWINTSD
HHHHHCCCEEEECCC
36.05-
73PhosphorylationRKKVWINTSDIILVG
CCCEEEECCCEEEEE
20.7421815630
74PhosphorylationKKVWINTSDIILVGL
CCEEEECCCEEEEEC
23.4821815630
82MethylationDIILVGLRDYQDNKA
CEEEEECCCCCCCCC
34.36-
84PhosphorylationILVGLRDYQDNKADV
EEEECCCCCCCCCCE
16.0128152594
88MalonylationLRDYQDNKADVILKY
CCCCCCCCCCEEEEE
55.0126320211
88UbiquitinationLRDYQDNKADVILKY
CCCCCCCCCCEEEEE
55.01-
88AcetylationLRDYQDNKADVILKY
CCCCCCCCCCEEEEE
55.0123954790
94SumoylationNKADVILKYNADEAR
CCCCEEEEECHHHHH
25.90-
94AcetylationNKADVILKYNADEAR
CCCCEEEEECHHHHH
25.9026051181
94UbiquitinationNKADVILKYNADEAR
CCCCEEEEECHHHHH
25.9021890473
942-HydroxyisobutyrylationNKADVILKYNADEAR
CCCCEEEEECHHHHH
25.90-
95PhosphorylationKADVILKYNADEARS
CCCEEEEECHHHHHH
16.49-
102PhosphorylationYNADEARSLKAYGEL
ECHHHHHHHHHHCCC
41.0725849741
104AcetylationADEARSLKAYGELPE
HHHHHHHHHHCCCCC
40.5925953088
104MalonylationADEARSLKAYGELPE
HHHHHHHHHHCCCCC
40.5926320211
1042-HydroxyisobutyrylationADEARSLKAYGELPE
HHHHHHHHHHCCCCC
40.59-
104UbiquitinationADEARSLKAYGELPE
HHHHHHHHHHCCCCC
40.592190698
106PhosphorylationEARSLKAYGELPEHA
HHHHHHHHCCCCCCC
15.0028152594

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 IF1AY_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF1AY_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 IF1AY_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF1AX_HUMANEIF1AXphysical
28514442
KLH36_HUMANKLHL36physical
28514442

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 IF1AY_HUMAN

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-88, AND MASSSPECTROMETRY.

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