RCOR1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RCOR1_MOUSE
• UniProt AC: Q8CFE3
• Protein Name: REST corepressor 1
• Gene Name: Rcor1
• Organism: Mus musculus (Mouse).
• Sequence Length: 480
• Subcellular Localization: Nucleus .
• Protein Description: Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation..
• Protein Sequence: MPAMVEKGPEVSGKRRGRNTAASAASAAASAASAAASAAASAGTASASAAAAASAAAAPNNGQNKSLAAAAPNGNSGSNSWEEGSSGSSSDEEHGGGGMRVGPQYQAAVPDFDPAKLARRSQERDNLGMLVWSPNQSLSEAKLDEYIAIAKEKHGYNMEQALGMLFWHKHNIEKSLADLPNFTPFPDEWTVEDKVLFEQAFSFHGKTFHRIQQMLPDKSIASLVKFYYSWKKTRTKTSVMDRHARKQKREREESEDELEETNGSNPVDIEIDPNKESKKEVPPTETVPQVKKEKHSTQAKNRAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSIKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAEHGKDETNGPANQKPVKSPESSIKIPEEEDEAASVLDVRYASAS

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
85	Phosphorylation	SNSWEEGSSGSSSDE CCCCCCCCCCCCCCC	28.72	19854140
86	Phosphorylation	NSWEEGSSGSSSDEE CCCCCCCCCCCCCCC	45.38	19854140
87	Phosphorylation	SWEEGSSGSSSDEEH CCCCCCCCCCCCCCC	51.22	25338131
88	Phosphorylation	WEEGSSGSSSDEEHG CCCCCCCCCCCCCCC	68.22	19854140
89	Phosphorylation	EEGSSGSSSDEEHGG CCCCCCCCCCCCCCC	54.57	19854140
90	Phosphorylation	EGSSGSSSDEEHGGG CCCCCCCCCCCCCCC	53.47	25338131
118	Phosphorylation	DFDPAKLARRSQERD CCCHHHHHHHHHHHC	30.73	21659605
121	Phosphorylation	PAKLARRSQERDNLG HHHHHHHHHHHCCCC	30.40	25168779
131	Phosphorylation	RDNLGMLVWSPNQSL HCCCCEEEECCCCCC	27.45	24719451
133	Phosphorylation	NLGMLVWSPNQSLSE CCCEEEECCCCCCCH	49.48	27600695
137	Phosphorylation	LVWSPNQSLSEAKLD EEECCCCCCCHHHHH	55.93	28066266
139	Phosphorylation	WSPNQSLSEAKLDEY ECCCCCCCHHHHHHH	53.04	28066266
148	Ubiquitination	AKLDEYIAIAKEKHG HHHHHHHHHHHHHHC	62.27	22790023
151	Ubiquitination	DEYIAIAKEKHGYNM HHHHHHHHHHHCCCH	45.09	-
156	Phosphorylation	IAKEKHGYNMEQALG HHHHHHCCCHHHHHH	29.12	24719451
229	Phosphorylation	SLVKFYYSWKKTRTK HHHHHHHHCCCCCCC	36.66	-
251	Phosphorylation	ARKQKREREESEDEL HHHHHHHHHHCHHHH	45.66	17203969
254	Phosphorylation	QKREREESEDELEET HHHHHHHCHHHHHHH	54.77	25521595
258	Phosphorylation	REESEDELEETNGSN HHHCHHHHHHHCCCC	35.19	22817900
261	Phosphorylation	SEDELEETNGSNPVD CHHHHHHHCCCCCCC	39.78	27087446
264	Phosphorylation	ELEETNGSNPVDIEI HHHHHCCCCCCCEEE	15.75	25619855
311	Phosphorylation	KRKPPKGMFLSQEDV HCCCCCCCCCCHHHH	21.91	-
314	Phosphorylation	PPKGMFLSQEDVEAV CCCCCCCCHHHHHHH	35.60	22802335
322	Phosphorylation	QEDVEAVSANATAAT HHHHHHHHCCHHHHH	9.80	22802335
326	Phosphorylation	EAVSANATAATTVLR HHHHCCHHHHHHHHH	18.25	-
327	Phosphorylation	AVSANATAATTVLRQ HHHCCHHHHHHHHHH	16.90	-
329	Phosphorylation	SANATAATTVLRQLD HCCHHHHHHHHHHHH	2.44	22802335
330	Phosphorylation	ANATAATTVLRQLDM CCHHHHHHHHHHHHH	30.58	22802335
338	Phosphorylation	VLRQLDMELVSIKRQ HHHHHHHHHHHHHHH	34.71	-
341	Phosphorylation	QLDMELVSIKRQIQN HHHHHHHHHHHHHHH	36.84	22802335
451	Phosphorylation	NGPANQKPVKSPESS CCCCCCCCCCCCHHH	33.85	25266776
454	Phosphorylation	ANQKPVKSPESSIKI CCCCCCCCCHHHCCC	40.52	25521595
457	Phosphorylation	KPVKSPESSIKIPEE CCCCCCHHHCCCCCC	54.90	25159016
458	Phosphorylation	PVKSPESSIKIPEEE CCCCCHHHCCCCCCH	5.04	25159016

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

Oops, there are no upstream regulatory protein records of RCOR1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RCOR1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RCOR1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RCOR1_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASSSPECTROMETRY.
PubMed: 19367708

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASSSPECTROMETRY.
PubMed: 17203969

"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 THR-258, AND MASSSPECTROMETRY.
PubMed: 17242355