dbPTM

ERR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERR1_HUMAN
UniProt AC	P11474
Protein Name	Steroid hormone receptor ERR1
Gene Name	ESRRA
Organism	Homo sapiens (Human).
Sequence Length	423
Subcellular Localization	Nucleus . Cytoplasm . Co-localizes to the cytoplasm only in presence of MAPK15.
Protein Description	Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces the expression of PERM1 in the skeletal muscle..
Protein Sequence	MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSQVVGIE ------CCCCCCCEE	29.49	23663014
3	Phosphorylation	-----MSSQVVGIEP -----CCCCCCCEEE	26.20	23663014
14	Sumoylation	GIEPLYIKAEPASPD CEEEEEEEEEECCCC	32.89	-
14	Sumoylation	GIEPLYIKAEPASPD CEEEEEEEEEECCCC	32.89	17676930
19	Phosphorylation	YIKAEPASPDSPKGS EEEEEECCCCCCCCC	39.70	29255136
22	Phosphorylation	AEPASPDSPKGSSET EEECCCCCCCCCCCC	31.71	29255136
26	Phosphorylation	SPDSPKGSSETETEP CCCCCCCCCCCCCCC	31.00	30278072
27	Phosphorylation	PDSPKGSSETETEPP CCCCCCCCCCCCCCC	58.15	30278072
29	Phosphorylation	SPKGSSETETEPPVA CCCCCCCCCCCCCCE	50.59	30278072
31	Phosphorylation	KGSSETETEPPVALA CCCCCCCCCCCCEEC	62.30	30278072
44	Phosphorylation	LAPGPAPTRCLPGHK ECCCCCCCCCCCCCC	35.80	20068231
51	Acetylation	TRCLPGHKEEEDGEG CCCCCCCCCCCCCCC	73.13	26051181
68	Acetylation	PGEQGGGKLVLSSLP CCCCCCCEEEECCCC	38.40	26051181
73	Phosphorylation	GGKLVLSSLPKRLCL CCEEEECCCCCEEEE	44.52	28555341
76	Ubiquitination	LVLSSLPKRLCLVCG EEECCCCCEEEEEEC	64.39	-
95	Phosphorylation	GYHYGVASCEACKAF CCHHCHHCHHHHHHH	15.30	24275569
116	Phosphorylation	GSIEYSCPASNECEI CCEEEECCCCCCCCH	32.55	17676930
119	Phosphorylation	EYSCPASNECEITKR EEECCCCCCCCHHHH	61.11	17676930
124	Phosphorylation	ASNECEITKRRRKAC CCCCCCHHHHHHHHH	9.01	15302935
129	Acetylation	EITKRRRKACQACRF CHHHHHHHHHHHCHH	52.26	20484414
137	Phosphorylation	ACQACRFTKCLRVGM HHHHCHHHHHHCCCC	11.07	26074081
138	Acetylation	CQACRFTKCLRVGML HHHCHHHHHHCCCCC	28.67	20484414
146	Ubiquitination	CLRVGMLKEGVRLDR HHCCCCCCCCCCHHH	43.46	-
160	Acetylation	RVRGGRQKYKRRPEV HCCCCHHHCCCCCCC	51.91	20484414
162	Acetylation	RGGRQKYKRRPEVDP CCCHHHCCCCCCCCC	49.30	20484414
189	Sumoylation	AVAGGPRKTAAPVNA EECCCCCCCCHHHHH	45.72	28112733
189	Sumoylation	AVAGGPRKTAAPVNA EECCCCCCCCHHHHH	45.72	-
190 (in isoform 2)	Phosphorylation	-	29.36	20068231
362	Phosphorylation	LHEALLEYEAGRAGP HHHHHHHHHHHCCCC	15.85	-
403	Sumoylation	LAHFYGVKLEGKVPM HHHHHCCCCCCCCCH	36.14	17676930
403	Ubiquitination	LAHFYGVKLEGKVPM HHHHHCCCCCCCCCH	36.14	-
403	Sumoylation	LAHFYGVKLEGKVPM HHHHHCCCCCCCCCH	36.14	-

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 ERR1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
14	K	Phosphorylation	17676930
Main site is Lys-14 which is enhanced by phosphorylation on Ser-19, cofactor activation, and by interaction with PIAS4.
14	K	Phosphorylation	17676930
Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.
14	K	Sumoylation	17676930
Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.
19	S	Phosphorylation	17676930
Main site is Lys-14 which is enhanced by phosphorylation on Ser-19, cofactor activation, and by interaction with PIAS4.
19	S	Phosphorylation	17676930
Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.
19	S	Sumoylation	17676930
Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.
129	K	Acetylation	20484414
Acetylation by PCAF/KAT2 at Lys-129, Lys-138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional activity probably by inhibiting DNA-binding activity; deacetylation involves SIRT1 and HDAC8 and increases DNA-binding.
138	K	Acetylation	20484414
Acetylation by PCAF/KAT2 at Lys-129, Lys-138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional activity probably by inhibiting DNA-binding activity; deacetylation involves SIRT1 and HDAC8 and increases DNA-binding.
160	K	Acetylation	20484414
Acetylation by PCAF/KAT2 at Lys-129, Lys-138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional activity probably by inhibiting DNA-binding activity; deacetylation involves SIRT1 and HDAC8 and increases DNA-binding.
162	K	Acetylation	20484414
Acetylation by PCAF/KAT2 at Lys-129, Lys-138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional activity probably by inhibiting DNA-binding activity; deacetylation involves SIRT1 and HDAC8 and increases DNA-binding.

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 ERR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ERR3_HUMAN	ESRRG	physical	17157980
NRIP1_HUMAN	NRIP1	physical	16439465
PRGC1_HUMAN	PPARGC1A	physical	15337744
ERR3_HUMAN	ESRRG	physical	17488637
KAT2B_HUMAN	KAT2B	physical	20484414
SIR1_HUMAN	SIRT1	physical	20484414
HDAC8_HUMAN	HDAC8	physical	20484414
PRKN_HUMAN	PARK2	physical	21177257
ERR3_HUMAN	ESRRG	physical	15604093
DUT_HUMAN	DUT	physical	15604093
PROX1_HUMAN	PROX1	physical	15604093
TNNI2_HUMAN	TNNI2	physical	15604093
NR0B2_HUMAN	NR0B2	physical	15604093
MACF1_HUMAN	MACF1	physical	15604093
ERR3_HUMAN	ESRRG	physical	18673300
WDR36_HUMAN	WDR36	physical	22939629
ZN606_HUMAN	ZNF606	physical	22939629
IPO13_HUMAN	IPO13	physical	22939629
C2CD5_HUMAN	C2CD5	physical	22939629
ESR1_HUMAN	ESR1	physical	9395481
FUS_HUMAN	FUS	physical	21988832
MP2K5_HUMAN	MAP2K5	physical	21988832
NXF1_HUMAN	NXF1	physical	21988832
PIAS4_HUMAN	PIAS4	physical	21988832
NCOA1_HUMAN	NCOA1	physical	23975195
NCOA1_HUMAN	NCOA1	physical	15604093
PRS8_HUMAN	PSMC5	physical	15604093

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 ERR1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-22 AND SER-26,AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-22, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphorylation-dependent sumoylation regulates estrogen-relatedreceptor-alpha and -gamma transcriptional activity through a synergycontrol motif."; Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.; Mol. Endocrinol. 22:570-584(2008). Cited for: SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 ANDSER-22, INTERACTION WITH PIAS4, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF LYS-14; SER-19; SER-22 AND LYS-403.	18063693 [Abstract]
"Phosphorylation-dependent sumoylation of estrogen-related receptoralpha1."; Vu E.H., Kraus R.J., Mertz J.E.; Biochemistry 46:9795-9804(2007). Cited for: SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 ANDSER-22, FUNCTION, AND MUTAGENESIS OF LYS-14; SER-19; SER-22; LYS-403;LEU-413 AND LEU-418.	17676930 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-27, AND MASSSPECTROMETRY.	15302935 [Abstract]
Sumoylation
Reference	PubMed
"Phosphorylation-dependent sumoylation regulates estrogen-relatedreceptor-alpha and -gamma transcriptional activity through a synergycontrol motif."; Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.; Mol. Endocrinol. 22:570-584(2008). Cited for: SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 ANDSER-22, INTERACTION WITH PIAS4, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF LYS-14; SER-19; SER-22 AND LYS-403.	18063693 [Abstract]
"Phosphorylation-dependent sumoylation of estrogen-related receptoralpha1."; Vu E.H., Kraus R.J., Mertz J.E.; Biochemistry 46:9795-9804(2007). Cited for: SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 ANDSER-22, FUNCTION, AND MUTAGENESIS OF LYS-14; SER-19; SER-22; LYS-403;LEU-413 AND LEU-418.	17676930 [Abstract]

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