dbPTM

ERF1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERF1_MOUSE
UniProt AC	Q8BWY3
Protein Name	Eukaryotic peptide chain release factor subunit 1
Gene Name	Etf1
Organism	Mus musculus (Mouse).
Sequence Length	437
Subcellular Localization	Cytoplasm.
Protein Description	Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons..
Protein Sequence	MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQGTEEEKILYLTPEQEKDKSHFTDKETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRVDFQGMEYQGGDDEFFDLDDY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADDPSAAD ------CCCCCCHHH	29.88	-
16	Acetylation	DRNVEIWKIKKLIKS HHCHHHHHHHHHHHH	50.76	22826441
23	Phosphorylation	KIKKLIKSLEAARGN HHHHHHHHHHHHHCC	25.17	24719451
42	Ubiquitination	ISLIIPPKDQISRVA EEEEECCHHHHHHHH	57.84	-
63	Hydroxylation	FGTASNIKSRVNRLS HCCCHHHHHHHHHHH	36.14	24486019
70	Phosphorylation	KSRVNRLSVLGAITS HHHHHHHHHHHHHHC	16.44	24719451
109	Ubiquitination	TEEGKEKKVNIDFEP CCCCCEEEEECCCCC	41.42	-
127	S-nitrosylation	INTSLYLCDNKFHTE CCCEEEEECCCHHHH	3.24	20925432
127	S-nitrosocysteine	INTSLYLCDNKFHTE CCCEEEEECCCHHHH	3.24	-
185	Methylation	KKHGRGGQSALRFAR HHCCCCHHHHHHHHH	28.49	20606008
342	Acetylation	CQGTEEEKILYLTPE CCCCCCEEEEEECCC	41.09	22826441
347	Phosphorylation	EEKILYLTPEQEKDK CEEEEEECCCHHCCC	15.95	-
352	Acetylation	YLTPEQEKDKSHFTD EECCCHHCCCCCCCC	70.87	23954790
395	Ubiquitination	TLEIVTDKSQEGSQF EEEEEECCCHHHCCC	44.68	-
404	Ubiquitination	QEGSQFVKGFGGIGG HHHCCCCCCCCCCCC	50.22	-
424	Phosphorylation	VDFQGMEYQGGDDEF EEECCCEEECCCCCC	11.99	24224561
437	Phosphorylation	EFFDLDDY------- CCCCCCCC-------	21.81	24224561

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 ERF1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
63	K	Hydroxylation	24486019
Hydroxylation at Lys-63 by JMJD4 promotes its translational termination efficiency.
185	Q	Methylation	20606008
Methylated at Gln-185 by N6AMT1.

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 ERF1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ERF1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of ERF1_MOUSE

Related Literatures of Post-Translational Modification