IF2G_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF2G_RAT
• UniProt AC: P81795
• Protein Name: Eukaryotic translation initiation factor 2 subunit 3, X-linked
• Gene Name: Eif2s3
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 472
• Protein Description: As a subunit of eukaryotic initiation factor 2 (eIF2), involved in the early steps of protein synthesis. In the presence of GTP, eIF2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex, a step that determines the rate of protein translation. This step is followed by mRNA binding to form the 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). Along with its paralog on chromosome X, may contribute to spermatogenesis up to the round spermatid stage (By similarity)..
• Protein Sequence: MAGGEAGVTLGQPHLSRQDLATLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD

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
2	Acetylation	------MAGGEAGVT ------CCCCCCCCC	34.40	-
9	Phosphorylation	AGGEAGVTLGQPHLS CCCCCCCCCCCCCCC	25.01	23984901
16	Phosphorylation	TLGQPHLSRQDLATL CCCCCCCCHHHHEEC	25.51	23984901
22	Phosphorylation	LSRQDLATLDVTKLT CCHHHHEECCCCCCC	30.68	23984901
26	Phosphorylation	DLATLDVTKLTPLSH HHEECCCCCCCCCCH	21.72	23984901
303	Acetylation	VRPGIVSKDSEGKLM ECCCCCCCCCCCCEE	55.14	22902405
421	Acetylation	GGRVSAVKADLGKIV CCCCEEEECCCCCEE	35.58	22902405
449	Acetylation	ALSRRVEKHWRLIGW HHHHHHHHHHEECCC	45.68	22902405

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of IF2G_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IF2G_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of IF2G_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of IF2G_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.