EIF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF1_HUMAN
• UniProt AC: P41567
• Protein Name: Eukaryotic translation initiation factor 1
• Gene Name: EIF1
• Organism: Homo sapiens (Human).
• Sequence Length: 113
• Protein Description: Necessary for scanning and involved in initiation site selection. Promotes the assembly of 48S ribosomal complexes at the authentic initiation codon of a conventional capped mRNA..
• Protein Sequence: MSAIQNLHSFDPFADASKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLVEIGLAKDDQLKVHGF

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
1	Acetylation	-------MSAIQNLH -------CCHHCCHH	5.72	-
2	Acetylation	------MSAIQNLHS ------CCHHCCHHH	33.79	20068231
2	Phosphorylation	------MSAIQNLHS ------CCHHCCHHH	33.79	29255136
9	Phosphorylation	SAIQNLHSFDPFADA CHHCCHHHCCCCCCC	34.21	25159151
17	Phosphorylation	FDPFADASKGDDLLP CCCCCCCCCCCCCCC	37.41	28464451
18	Ubiquitination	DPFADASKGDDLLPA CCCCCCCCCCCCCCC	68.99	-
27	Phosphorylation	DDLLPAGTEDYIHIR CCCCCCCCCCEEEEE	27.99	28450419
30	Phosphorylation	LPAGTEDYIHIRIQQ CCCCCCCEEEEEEEE	6.54	25159151
42	Ubiquitination	IQQRNGRKTLTTVQG EEECCCCEEEEEEEC	49.65	21906983
43	Phosphorylation	QQRNGRKTLTTVQGI EECCCCEEEEEEECC	28.16	22199227
45	Phosphorylation	RNGRKTLTTVQGIAD CCCCEEEEEEECCCC	30.10	20068231
46	Phosphorylation	NGRKTLTTVQGIADD CCCEEEEEEECCCCC	17.59	28555341
54	Phosphorylation	VQGIADDYDKKKLVK EECCCCCCCHHHHHH	30.15	20068231
56	2-Hydroxyisobutyrylation	GIADDYDKKKLVKAF CCCCCCCHHHHHHHH	45.65	-
58	Acetylation	ADDYDKKKLVKAFKK CCCCCHHHHHHHHHH	65.34	19608861
61	Acetylation	YDKKKLVKAFKKKFA CCHHHHHHHHHHHHC	59.55	19608861
66	Ubiquitination	LVKAFKKKFACNGTV HHHHHHHHHCCCCEE	38.49	-
69	S-nitrosocysteine	AFKKKFACNGTVIEH HHHHHHCCCCEEEEC	5.63	-
69	S-nitrosylation	AFKKKFACNGTVIEH HHHHHHCCCCEEEEC	5.63	22178444
72	Phosphorylation	KKFACNGTVIEHPEY HHHCCCCEEEECCCC	12.34	27307780
79	Phosphorylation	TVIEHPEYGEVIQLQ EEEECCCCCCEEEEE	24.04	27307780
91	Ubiquitination	QLQGDQRKNICQFLV EEECHHHHCHHHHHH	45.06	21890473
109	Acetylation	LAKDDQLKVHGF--- CCCCCCCEECCC---	26.93	25953088
109	Ubiquitination	LAKDDQLKVHGF--- CCCCCCCEECCC---	26.93	21906983
109	2-Hydroxyisobutyrylation	LAKDDQLKVHGF--- CCCCCCCEECCC---	26.93	-

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

Oops, there are no upstream regulatory protein records of EIF1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EIF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
EIF2D_HUMAN	EIF2D	physical	22939629
EIF3G_HUMAN	EIF3G	physical	26344197

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-58 AND LYS-61, AND MASSSPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND MASSSPECTROMETRY.
PubMed: 15592455