IF2B_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF2B_ARATH
• UniProt AC: Q41969
• Protein Name: Eukaryotic translation initiation factor 2 subunit beta {ECO:0000305}
• Gene Name: EIF2B {ECO:0000305}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 268
• Protein Description: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 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 eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity)..
• Protein Sequence: MADEINEIREEQEQLAPFDPSKKKKKKKVVIQEPVEDLAESSQTEKSDSLPVNDGLESSFTGMKKKKKKPTESSLLNNESVDAGEDLDEIANDEQEGEEGIVLQQRYPWEGSERDYIYDELLGRVFNILRENNPELAGDRRRTVMRPPQVLREGTKKTVFVNFMDLCKTMHRQPDHVMQYLLAELGTSGSLDGQQRLVVKGRFAPKNFEGILRRYITDYVICLGCKSPDTILSKENRLFFLRCEKCGSQRSVAPIKTGFVARVSRRKT

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	------MADEINEIR ------CHHHHHHHH	24.12	22223895
40	Phosphorylation	EPVEDLAESSQTEKS CCHHHHHHCCCCCCC	59.21	22631563
41	Phosphorylation	PVEDLAESSQTEKSD CHHHHHHCCCCCCCC	23.34	23776212
42	Phosphorylation	VEDLAESSQTEKSDS HHHHHHCCCCCCCCC	32.40	23776212
43	Phosphorylation	EDLAESSQTEKSDSL HHHHHCCCCCCCCCC	64.06	19880383
44	Phosphorylation	DLAESSQTEKSDSLP HHHHCCCCCCCCCCC	47.53	23776212
58	Phosphorylation	PVNDGLESSFTGMKK CCCCCCHHCCCCCCC	35.48	27545962
59	Phosphorylation	VNDGLESSFTGMKKK CCCCCHHCCCCCCCC	19.90	27545962
61	Phosphorylation	DGLESSFTGMKKKKK CCCHHCCCCCCCCCC	38.01	27545962
63	Sulfoxidation	LESSFTGMKKKKKKP CHHCCCCCCCCCCCC	5.37	23289948
80	Phosphorylation	SSLLNNESVDAGEDL HHHCCCCCCCCCCCH	27.67	19509420
112	Phosphorylation	QRYPWEGSERDYIYD ECCCCCCCCCHHHHH	20.24	19509420
170	Sulfoxidation	FMDLCKTMHRQPDHV HHHHHHHHHHCCHHH	1.18	23289948
227	Phosphorylation	VICLGCKSPDTILSK EEECCCCCHHHCCCC	31.89	25561503

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
41	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
42	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
42	S	Phosphorylation	Kinase	CK2	-	Uniprot
44	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
80	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
80	S	Phosphorylation	Kinase	CK2	-	Uniprot
112	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
112	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
42	S	Phosphorylation	Phosphorylated at Ser-42, Ser-80 and Ser-112 by CK2.	19509420
80	S	Phosphorylation	Phosphorylated at Ser-42, Ser-80 and Ser-112 by CK2.	19509420
112	S	Phosphorylation	Phosphorylated at Ser-42, Ser-80 and Ser-112 by CK2.	19509420

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of IF2B_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

Drug and Disease Associations

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