dbPTM

EIF1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF1B_HUMAN
UniProt AC	O60739
Protein Name	Eukaryotic translation initiation factor 1b
Gene Name	EIF1B
Organism	Homo sapiens (Human).
Sequence Length	113
Subcellular Localization
Protein Description	Probably involved in translation..
Protein Sequence	MSTIQNLQSFDPFADATKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLLEVGIVKEEQLKVHGF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSTIQNLQS ------CCCCCCHHH	33.93	23186163
2	Acetylation	------MSTIQNLQS ------CCCCCCHHH	33.93	21406692
3	Phosphorylation	-----MSTIQNLQSF -----CCCCCCHHHC	25.86	27251275
9	Phosphorylation	STIQNLQSFDPFADA CCCCCHHHCCCCCCC	34.48	23663014
17	Phosphorylation	FDPFADATKGDDLLP CCCCCCCCCCCCCCC	35.79	26270265
18	Ubiquitination	DPFADATKGDDLLPA CCCCCCCCCCCCCCC	63.16	-
27	Phosphorylation	DDLLPAGTEDYIHIR CCCCCCCCCCEEEEE	27.99	27732954
30	Phosphorylation	LPAGTEDYIHIRIQQ CCCCCCCEEEEEEEE	6.54	25159151
42	Ubiquitination	IQQRNGRKTLTTVQG EEECCCCEEEEEEEC	49.65	-
42	Malonylation	IQQRNGRKTLTTVQG EEECCCCEEEEEEEC	49.65	26320211
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	Acetylation	GIADDYDKKKLVKAF CCCCCCCHHHHHHHH	45.65	25953088
58	Acetylation	ADDYDKKKLVKAFKK CCCCCHHHHHHHHHH	65.34	19608861
61	Acetylation	YDKKKLVKAFKKKFA CCHHHHHHHHHHHHC	59.55	26051181
65	Acetylation	KLVKAFKKKFACNGT HHHHHHHHHHCCCCE	46.82	25953088
66	Ubiquitination	LVKAFKKKFACNGTV HHHHHHHHHCCCCEE	38.49	-
66	Acetylation	LVKAFKKKFACNGTV HHHHHHHHHCCCCEE	38.49	25953088
72	Phosphorylation	KKFACNGTVIEHPEY HHHCCCCEEEECCCC	12.34	27307780
79	Phosphorylation	TVIEHPEYGEVIQLQ EEEECCCCCCEEEEC	24.04	27307780
91	Ubiquitination	QLQGDQRKNICQFLL EECCHHHHCHHHHHH	45.06	21890473
104	Sumoylation	LLEVGIVKEEQLKVH HHHCCCCCHHHCCCC	54.32	-
104	Sumoylation	LLEVGIVKEEQLKVH HHHCCCCCHHHCCCC	54.32	-
109	Ubiquitination	IVKEEQLKVHGF--- CCCHHHCCCCCC---	31.70	-

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 EIF1B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF1B_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 EIF1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF3A_HUMAN	EIF3A	physical	17353931
EIF3L_HUMAN	EIF3L	physical	17353931
EIF3M_HUMAN	EIF3M	physical	17353931
EIF3F_HUMAN	EIF3F	physical	17353931
EIF3D_HUMAN	EIF3D	physical	17353931
EIF3E_HUMAN	EIF3E	physical	17353931
ARP3_HUMAN	ACTR3	physical	17353931
RS11_HUMAN	RPS11	physical	17353931
IF2G_HUMAN	EIF2S3	physical	17353931
RS3A_HUMAN	RPS3A	physical	17353931
EIF3H_HUMAN	EIF3H	physical	17353931
RS9_HUMAN	RPS9	physical	17353931
EIF3I_HUMAN	EIF3I	physical	17353931
RFA3_HUMAN	RPA3	physical	17353931
HPRT_HUMAN	HPRT1	physical	17353931
RS29_HUMAN	RPS29	physical	17353931
SYYC_HUMAN	YARS	physical	17353931
GLYM_HUMAN	SHMT2	physical	17353931
TAGL2_HUMAN	TAGLN2	physical	17353931
EIF3K_HUMAN	EIF3K	physical	17353931
ERH_HUMAN	ERH	physical	17353931
PIMT_HUMAN	PCMT1	physical	17353931
ELOC_HUMAN	TCEB1	physical	17353931
EIF3G_HUMAN	EIF3G	physical	17353931
IF2A_HUMAN	EIF2S1	physical	17353931
TSR1_HUMAN	TSR1	physical	17353931
ML12A_HUMAN	MYL12A	physical	17353931
THIL_HUMAN	ACAT1	physical	17353931
RAB7A_HUMAN	RAB7A	physical	17353931
EIF2D_HUMAN	EIF2D	physical	22939629
PEX19_HUMAN	PEX19	physical	21988832
TRI38_HUMAN	TRIM38	physical	25416956
EIF2D_HUMAN	EIF2D	physical	26344197
EIF3G_HUMAN	EIF3G	physical	26344197
ZO2_HUMAN	TJP2	physical	26344197
DVL2_HUMAN	DVL2	physical	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 EIF1B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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.	19608861 [Abstract]