ERH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ERH_HUMAN
• UniProt AC: P84090
• Protein Name: Enhancer of rudimentary homolog
• Gene Name: ERH
• Organism: Homo sapiens (Human).
• Sequence Length: 104
• Protein Description: May have a role in the cell cycle..
• Protein Sequence: MSHTILLVQPTKRPEGRTYADYESVNECMEGVCKMYEEHLKRMNPNSPSITYDISQLFDFIDDLADLSCLVYRADTQTYQPYNKDWIKEKIYVLLRRQAQQAGK

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
2	Phosphorylation	------MSHTILLVQ ------CCCEEEEEC	29.36	25159151
2	Acetylation	------MSHTILLVQ ------CCCEEEEEC	29.36	20068231
4	Phosphorylation	----MSHTILLVQPT ----CCCEEEEECCC	13.15	22199227
11	Phosphorylation	TILLVQPTKRPEGRT EEEEECCCCCCCCCC	23.69	28112733
12	Malonylation	ILLVQPTKRPEGRTY EEEECCCCCCCCCCC	73.05	26320211
12	2-Hydroxyisobutyrylation	ILLVQPTKRPEGRTY EEEECCCCCCCCCCC	73.05	-
12	Sumoylation	ILLVQPTKRPEGRTY EEEECCCCCCCCCCC	73.05	28112733
12	Ubiquitination	ILLVQPTKRPEGRTY EEEECCCCCCCCCCC	73.05	21890473
12	Acetylation	ILLVQPTKRPEGRTY EEEECCCCCCCCCCC	73.05	23954790
12	Ubiquitination	ILLVQPTKRPEGRTY EEEECCCCCCCCCCC	73.05	21890473
17	Methylation	PTKRPEGRTYADYES CCCCCCCCCCCCHHH	23.93	-
18	Phosphorylation	TKRPEGRTYADYESV CCCCCCCCCCCHHHH	33.64	30108239
19	Phosphorylation	KRPEGRTYADYESVN CCCCCCCCCCHHHHH	8.98	27251275
22	Phosphorylation	EGRTYADYESVNECM CCCCCCCHHHHHHHH	11.26	30108239
24	Phosphorylation	RTYADYESVNECMEG CCCCCHHHHHHHHHH	24.82	25159151
28	Glutathionylation	DYESVNECMEGVCKM CHHHHHHHHHHHHHH	2.25	22555962
34	Acetylation	ECMEGVCKMYEEHLK HHHHHHHHHHHHHHH	41.95	25953088
34	Ubiquitination	ECMEGVCKMYEEHLK HHHHHHHHHHHHHHH	41.95	-
36	Phosphorylation	MEGVCKMYEEHLKRM HHHHHHHHHHHHHHC	12.03	28152594
41	Ubiquitination	KMYEEHLKRMNPNSP HHHHHHHHHCCCCCC	52.05	21890473
41	Succinylation	KMYEEHLKRMNPNSP HHHHHHHHHCCCCCC	52.05	23954790
41	Acetylation	KMYEEHLKRMNPNSP HHHHHHHHHCCCCCC	52.05	25953088
41	Ubiquitination	KMYEEHLKRMNPNSP HHHHHHHHHCCCCCC	52.05	21890473
41	2-Hydroxyisobutyrylation	KMYEEHLKRMNPNSP HHHHHHHHHCCCCCC	52.05	-
76	Phosphorylation	CLVYRADTQTYQPYN HEEEECCCCCCCCCC	23.09	28152594
78	Phosphorylation	VYRADTQTYQPYNKD EEECCCCCCCCCCHH	26.64	28152594
79	Phosphorylation	YRADTQTYQPYNKDW EECCCCCCCCCCHHH	9.55	28152594
82	Phosphorylation	DTQTYQPYNKDWIKE CCCCCCCCCHHHHHH	21.22	28152594
84	Ubiquitination	QTYQPYNKDWIKEKI CCCCCCCHHHHHHHH	48.90	21890473
84	2-Hydroxyisobutyrylation	QTYQPYNKDWIKEKI CCCCCCCHHHHHHHH	48.90	-
84	Ubiquitination	QTYQPYNKDWIKEKI CCCCCCCHHHHHHHH	48.90	21906983
84	Acetylation	QTYQPYNKDWIKEKI CCCCCCCHHHHHHHH	48.90	25825284
88	Acetylation	PYNKDWIKEKIYVLL CCCHHHHHHHHHHHH	49.02	26051181
88	Ubiquitination	PYNKDWIKEKIYVLL CCCHHHHHHHHHHHH	49.02	-
90	Malonylation	NKDWIKEKIYVLLRR CHHHHHHHHHHHHHH	34.04	26320211
90	2-Hydroxyisobutyrylation	NKDWIKEKIYVLLRR CHHHHHHHHHHHHHH	34.04	-
90	Ubiquitination	NKDWIKEKIYVLLRR CHHHHHHHHHHHHHH	34.04	-
90	Acetylation	NKDWIKEKIYVLLRR CHHHHHHHHHHHHHH	34.04	23749302
92	Phosphorylation	DWIKEKIYVLLRRQA HHHHHHHHHHHHHHH	8.98	28152594

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ERH_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 ERH_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSN6_HUMAN	COPS6	physical	16169070
IGS21_HUMAN	IGSF21	physical	16169070
SH3G2_HUMAN	SH3GL2	physical	16169070
MED31_HUMAN	MED31	physical	16169070
RBM48_HUMAN	RBM48	physical	16169070
SETB1_HUMAN	SETDB1	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
P53_HUMAN	TP53	physical	16169070
CTDP1_HUMAN	CTDP1	physical	15670829
PDIP3_HUMAN	POLDIP3	physical	23145069
CIZ1_HUMAN	CIZ1	physical	23145069
A4_HUMAN	APP	physical	21832049
DGCR8_HUMAN	DGCR8	physical	24778252
CHTOP_HUMAN	CHTOP	physical	25416956
F208B_HUMAN	FAM208B	physical	25416956
F208B_HUMAN	FAM208B	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-12, AND MASS SPECTROMETRY.
PubMed: 19608861