dbPTM

IEX1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IEX1_HUMAN
UniProt AC	P46695
Protein Name	Radiation-inducible immediate-early gene IEX-1
Gene Name	IER3
Organism	Homo sapiens (Human).
Sequence Length	156
Subcellular Localization	Membrane Single-pass type II membrane protein .
Protein Description	May play a role in the ERK signaling pathway by inhibiting the dephosphorylation of ERK by phosphatase PP2A-PPP2R5C holoenzyme. Acts also as an ERK downstream effector mediating survival. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment..
Protein Sequence	MCHSRSCHPTMTILQAPTPAPSTIPGPRRGSGPEIFTFDPLPEPAAAPAGRPSASRGHRKRSRRVLYPRVVRRQLPVEEPNPAKRLLFLLLTIVFCQILMAEEGVPAPLPPEDAPNAASLAPTPVSAVLEPFNLTSEPSDYALDLSTFLQQHPAAF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	MTILQAPTPAPSTIP EEEEECCCCCCCCCC	34.79	22817900
31	Phosphorylation	IPGPRRGSGPEIFTF CCCCCCCCCCCCEEE	49.73	30266825
37	Phosphorylation	GSGPEIFTFDPLPEP CCCCCCEEECCCCCC	32.56	30266825
53	Phosphorylation	AAPAGRPSASRGHRK CCCCCCCCCCCCCHH	37.20	18669648
55	Phosphorylation	PAGRPSASRGHRKRS CCCCCCCCCCCHHHH	43.03	18669648
84	Ubiquitination	VEEPNPAKRLLFLLL CCCCCHHHHHHHHHH	44.85	21906983
123	Phosphorylation	NAASLAPTPVSAVLE CCHHCCCCCCHHHCC	30.62	12356731
126	Phosphorylation	SLAPTPVSAVLEPFN HCCCCCCHHHCCCCC	17.54	9196025
133	N-linked_Glycosylation	SAVLEPFNLTSEPSD HHHCCCCCCCCCCCC	53.80	UniProtKB CARBOHYD

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
18	T	Phosphorylation	Kinase	ERK2	P28482	PSP
18	T	Phosphorylation	Kinase	MAPK6	Q16659	GPS
123	T	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
126	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:26973248

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
18	T	Phosphorylation	12356731
Phosphorylated at Thr-18, Thr-123 and Ser-126 by MAPK1/ERK2 and probably MAPK3/ERK1.
123	T	Phosphorylation	12356731
Phosphorylated at Thr-18, Thr-123 and Ser-126 by MAPK1/ERK2 and probably MAPK3/ERK1.
126	S	Phosphorylation	12356731
Phosphorylated at Thr-18, Thr-123 and Ser-126 by MAPK1/ERK2 and probably MAPK3/ERK1.

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 IEX1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
2A5B_HUMAN	PPP2R5B	physical	16456541
2A5G_HUMAN	PPP2R5C	physical	16456541
FHL2_HUMAN	FHL2	physical	26973248
MDM2_HUMAN	MDM2	physical	26973248

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 IEX1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"IEX-1: a new ERK substrate involved in both ERK survival activity andERK activation."; Garcia J., Ye Y., Arranz V., Letourneux C., Pezeron G., Porteu F.; EMBO J. 21:5151-5163(2002). Cited for: PHOSPHORYLATION AT THR-18; THR-123 AND SER-126, INTERACTION WITHMAPK1/ERK2, SUBCELLLAR LOCATION, AND FUNCTION.	12356731 [Abstract]