ERR1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ERR1_MOUSE
• UniProt AC: O08580
• Protein Name: Steroid hormone receptor ERR1
• Gene Name: Esrra
• Organism: Mus musculus (Mouse).
• Sequence Length: 422
• 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 (By similarity)..
• Protein Sequence: MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVTLASGPAPARCLPGHKEEEDGEGAGSGEQGSGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAPVNALVSHLLVVEPEKLYAMPDPASPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGDLGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD

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
14	Sumoylation	GIEPLYIKAEPASPD CEEEEEEEEEECCCC	32.89	-
19	Phosphorylation	YIKAEPASPDSPKGS EEEEEECCCCCCCCC	39.70	25521595
22	Phosphorylation	AEPASPDSPKGSSET EEECCCCCCCCCCCC	31.71	25521595
26	Phosphorylation	SPDSPKGSSETETEP CCCCCCCCCCCCCCC	31.00	21082442
27	Phosphorylation	PDSPKGSSETETEPP CCCCCCCCCCCCCCC	58.15	25521595
29	Phosphorylation	SPKGSSETETEPPVT CCCCCCCCCCCCCEE	50.59	25521595
31	Phosphorylation	KGSSETETEPPVTLA CCCCCCCCCCCEEEC	62.30	21149613
36	Phosphorylation	TETEPPVTLASGPAP CCCCCCEEECCCCCC	23.52	21149613
39	Phosphorylation	EPPVTLASGPAPARC CCCEEECCCCCCCCC	48.71	30635358
61	Phosphorylation	EDGEGAGSGEQGSGK CCCCCCCCCCCCCCE	38.33	27681418
66	Phosphorylation	AGSGEQGSGKLVLSS CCCCCCCCCEEEECC	32.23	27681418
129	Acetylation	EITKRRRKACQACRF CHHHHHHHHHHHCHH	52.26	-
138	Acetylation	CQACRFTKCLRVGML HHHCHHHHHHCCCCC	28.67	-
146	Ubiquitination	CLRVGMLKEGVRLDR HHCCCCCCCCCCHHH	43.46	-
160	Acetylation	RVRGGRQKYKRRPEV HCCCCHHHCCCCCCC	51.91	-
162	Acetylation	RGGRQKYKRRPEVDP CCCHHHCCCCCCCCC	49.30	-
244	Phosphorylation	VTISWAKSIPGFSSL EEEEEHHHCCCCCCC	26.69	25777480
249	Phosphorylation	AKSIPGFSSLSLSDQ HHHCCCCCCCCHHHH	35.96	25777480
250	Phosphorylation	KSIPGFSSLSLSDQM HHCCCCCCCCHHHHH	21.51	25777480
252	Phosphorylation	IPGFSSLSLSDQMSV CCCCCCCCHHHHHHH	27.98	25777480
254	Phosphorylation	GFSSLSLSDQMSVLQ CCCCCCHHHHHHHHH	23.56	25777480
258	Phosphorylation	LSLSDQMSVLQSVWM CCHHHHHHHHHHHHH	17.65	25777480
262	Phosphorylation	DQMSVLQSVWMEVLV HHHHHHHHHHHHHHH	17.37	25777480
402	Sumoylation	LAHFYGVKLEGKVPM HHHHHCCCCCCCCCH	36.14	-

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

Oops, there are no upstream regulatory protein records of ERR1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
14	K	Phosphorylation	Main site is Lys-14 which is enhanced by phosphorylation on Ser-19, cofactor activation, and by interaction with PIAS4.	-
14	K	Phosphorylation	Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.	-
14	K	Sumoylation	Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.	-
19	S	Phosphorylation	Main site is Lys-14 which is enhanced by phosphorylation on Ser-19, cofactor activation, and by interaction with PIAS4.	17242355
19	S	Phosphorylation	Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.	17242355
19	S	Sumoylation	Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.	17242355
129	K	Acetylation	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 (By similarity).	-
138	K	Acetylation	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 (By similarity).	-
160	K	Acetylation	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 (By similarity).	-
162	K	Acetylation	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 (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ERR1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAT2B_MOUSE	Kat2b	physical	20484414

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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, AND PHOSPHORYLATION AT SER-19.
PubMed: 18063693

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
PubMed: 17242355