dbPTM

ERF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERF1_HUMAN
UniProt AC	P62495
Protein Name	Eukaryotic peptide chain release factor subunit 1
Gene Name	ETF1
Organism	Homo sapiens (Human).
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	22814378
10	Methylation	DDPSAADRNVEIWKI CCCCHHHHCHHHHHH	44.35	-
23	Phosphorylation	KIKKLIKSLEAARGN HHHHHHHHHHHHHCC	25.17	24719451
32	Phosphorylation	EAARGNGTSMISLII HHHHCCCCEEEEEEE	21.08	24114839
33	Phosphorylation	AARGNGTSMISLIIP HHHCCCCEEEEEEEC	18.60	24114839
36	Phosphorylation	GNGTSMISLIIPPKD CCCCEEEEEEECCHH	12.60	24114839
63	Hydroxylation	FGTASNIKSRVNRLS HCCCHHHHHHHHHHH	36.14	24486019
70	Phosphorylation	KSRVNRLSVLGAITS HHHHHHHHHHHHHHC	16.44	28555341
87	Sumoylation	QRLKLYNKVPPNGLV HHHHHHCCCCCCCEE	42.43	28112733
106	Ubiquitination	TIVTEEGKEKKVNID EEECCCCCEEEEECC	70.42	-
109	Ubiquitination	TEEGKEKKVNIDFEP CCCCCEEEEECCCCC	41.42	-
109	2-Hydroxyisobutyrylation	TEEGKEKKVNIDFEP CCCCCEEEEECCCCC	41.42	-
118	Acetylation	NIDFEPFKPINTSLY ECCCCCCCCCCCEEE	56.56	26051181
123	Phosphorylation	PFKPINTSLYLCDNK CCCCCCCEEEEECCC	15.55	25627689
141	Phosphorylation	EALTALLSDDSKFGF HHHHHHHCCCCCEEE	39.98	-
171	Ubiquitination	NTREVLHKFTVDLPK CHHHHEEEEEEECCH	38.27	21890473
171	Acetylation	NTREVLHKFTVDLPK CHHHHEEEEEEECCH	38.27	25953088
171	Ubiquitination	NTREVLHKFTVDLPK CHHHHEEEEEEECCH	38.27	21890473
182	Dimethylation	DLPKKHGRGGQSALR ECCHHCCCCHHHHHH	45.87	-
182	Methylation	DLPKKHGRGGQSALR ECCHHCCCCHHHHHH	45.87	-
185	Methylation	KKHGRGGQSALRFAR HHCCCCHHHHHHHHH	28.49	20606008
189	Methylation	RGGQSALRFARLRME CCHHHHHHHHHHHHH	23.93	-
201	Phosphorylation	RMEKRHNYVRKVAET HHHHHHHHHHHHHHH	8.77	-
208	Phosphorylation	YVRKVAETAVQLFIS HHHHHHHHHHHHHHC	23.53	20068231
215	Phosphorylation	TAVQLFISGDKVNVA HHHHHHHCCCCEEEE	33.34	20068231
234	Phosphorylation	AGSADFKTELSQSDM EECCCCCCCCCCHHH	42.00	20068231
237	Phosphorylation	ADFKTELSQSDMFDQ CCCCCCCCCHHHHHH	22.77	20068231
239	Phosphorylation	FKTELSQSDMFDQRL CCCCCCCHHHHHHHH	27.89	29449344
241	Sulfoxidation	TELSQSDMFDQRLQS CCCCCHHHHHHHHHH	4.89	21406390
249	2-Hydroxyisobutyrylation	FDQRLQSKVLKLVDI HHHHHHHHHHHHHCC	38.33	-
249	Ubiquitination	FDQRLQSKVLKLVDI HHHHHHHHHHHHHCC	38.33	-
289	Methylation	QEKKLIGRYFDEISQ HHHHHHHHHHHHHHC	23.19	-
300	Acetylation	EISQDTGKYCFGVED HHHCCCCCEECCHHH	40.72	26051181
308	Phosphorylation	YCFGVEDTLKALEMG EECCHHHHHHHHHCC	19.36	28509920
331	Phosphorylation	ENLDIMRYVLHCQGT ECHHHHHHHHHCCCC	7.03	28152594
335	S-nitrosocysteine	IMRYVLHCQGTEEEK HHHHHHHCCCCCCEE	3.31	-
335	S-nitrosylation	IMRYVLHCQGTEEEK HHHHHHHCCCCCCEE	3.31	19483679
342	Acetylation	CQGTEEEKILYLTPE CCCCCCEEEEEECCC	41.09	25953088
345	Phosphorylation	TEEEKILYLTPEQEK CCCEEEEEECCCHHC	16.41	23898821
347	Phosphorylation	EEKILYLTPEQEKDK CEEEEEECCCHHCCC	15.95	28112733
352	Ubiquitination	YLTPEQEKDKSHFTD EECCCHHCCCCCCCC	70.87	-
352	2-Hydroxyisobutyrylation	YLTPEQEKDKSHFTD EECCCHHCCCCCCCC	70.87	-
352	Succinylation	YLTPEQEKDKSHFTD EECCCHHCCCCCCCC	70.87	23954790
352	Acetylation	YLTPEQEKDKSHFTD EECCCHHCCCCCCCC	70.87	23236377
354	2-Hydroxyisobutyrylation	TPEQEKDKSHFTDKE CCCHHCCCCCCCCCC	57.82	-
384	Ubiquitination	WFANNYKKFGATLEI HHHHCCHHHCCEEEE	38.37	21890473
384	Ubiquitination	WFANNYKKFGATLEI HHHHCCHHHCCEEEE	38.37	21890473
388	O-linked_Glycosylation	NYKKFGATLEIVTDK CCHHHCCEEEEEECC	25.88	30379171
395	Ubiquitination	TLEIVTDKSQEGSQF EEEEEECCCHHHCCC	44.68	21906983
395	Acetylation	TLEIVTDKSQEGSQF EEEEEECCCHHHCCC	44.68	26051181
396	Phosphorylation	LEIVTDKSQEGSQFV EEEEECCCHHHCCCC	35.95	22210691
400	Phosphorylation	TDKSQEGSQFVKGFG ECCCHHHCCCCCCCC	21.50	22210691
404	Methylation	QEGSQFVKGFGGIGG HHHCCCCCCCCCCCC	50.22	-
404	Ubiquitination	QEGSQFVKGFGGIGG HHHCCCCCCCCCCCC	50.22	21890473
404	Sumoylation	QEGSQFVKGFGGIGG HHHCCCCCCCCCCCC	50.22	28112733
404	Ubiquitination	QEGSQFVKGFGGIGG HHHCCCCCCCCCCCC	50.22	21890473
424	Phosphorylation	VDFQGMEYQGGDDEF EEECCCEEECCCCCC	11.99	27642862
437	Phosphorylation	EFFDLDDY------- CCCCCCCC-------	21.81	27642862

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_HUMAN !!

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	18539146
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KEAP1_HUMAN	KEAP1	physical	16189514
PABP1_HUMAN	PABPC1	physical	18056425
PP2AA_HUMAN	PPP2CA	physical	9003791
ERF3B_HUMAN	GSPT2	physical	9712840
ERF3A_HUMAN	GSPT1	physical	9712840
RENT1_HUMAN	UPF1	physical	18256688
ERF3A_HUMAN	GSPT1	physical	18256688
TSN_HUMAN	TSN	physical	22863883
KEAP1_HUMAN	KEAP1	physical	25416956
IF2A_HUMAN	EIF2S1	physical	26344197
IF2B_HUMAN	EIF2S2	physical	26344197
PSA1_HUMAN	PSMA1	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
SYAP1_HUMAN	SYAP1	physical	26344197
ZPR1_HUMAN	ZPR1	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.

Regulatory Network of ERF1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.	12665801 [Abstract]

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