CCAR2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CCAR2_MOUSE
• UniProt AC: Q8VDP4
• Protein Name: Cell cycle and apoptosis regulator protein 2
• Gene Name: Ccar2
• Organism: Mus musculus (Mouse).
• Sequence Length: 922
• Subcellular Localization: Nucleus . Cytoplasm . Recruited to chromatin, post-UV irradiation. Sequestered to the cytoplasm in the presence of MCC. Translocated to the cytoplasm during UV-induced apoptosis.
• Protein Description: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (By similarity). As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Inhibits SUV39H1 methyltransferase activity. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (By similarity) Regulates the circadian expression of the core clock components NR1D1 and ARNTL/BMAL1. Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation. Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1. [PubMed: 24415752 Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization]
• Protein Sequence: MSQFKRQRINPLPGGRNFSGAASTSLLGPPPGLLTPPVATDLSQNARHLQSGEKQRVFTGIVTSLHDYFGVVDEEVFFQLSVVKGRLPQLGEKVLVKAAYNPGQAVPWNAVKVQTLSNQPLLKSPAPPLLHVAALGQKQGILGAQPQLIFQPHRIPPLFPQKPLSLFQTSHTLHLSHLNRFPARGPHGRLDQGRSDDYDSKKRKQRAGGEPWGAKKPRHDLSPYRVHLTPYTVDSPTCDFLELQRRYRSLLVPSDFLSVHLSWLSAFPLGQPFSLHHPSRIQVSSEKEAAPDTGAEPSPEDSDPTYSSKVLLLSSPGLEEFYRCCMLFVDDMAEPRETPEHPLKQLKFLLGRKEEEAVLVGGEWSPSLDGLDPQADPQVLVRTAIRCAQAQTGIDLSTCTKWWRFAEFQYLQPGPPRQLHTVVVYLPDVWTIMPTLEEWEALCQQKATEAAPQPHEASGEAEATEQAPDVSEQADTSKQNTETMEATTQQDVDTDLPEAPPPPLEPAVMARPRCVNLSLYGIVEDRRPKERISFEVVVLAELFVEMLQRDFGYRIYKTLLSLPEKVVSPPEPEKEEAAKEDAVKEEEAVKEEAVKVSKDEVQNEGTAAESDSPLKEDGLLPKRPSSGGEEEEKARGEAAEDLCEMALDPDLLLLRDDGEDEFAGAKLEETEVRSVASNQSEMEYSSLQDMPKELDPSTVLPLDCLLAFVFFDANWCGYLHRRDLERVLLTLGIRLSAEQAKQLVSRVVAQNICQYRSLQYSRAEVLDDGLPEDVLFGNLDLLPPSGKSTKPGAAPTEHKGLVPHNGSLINVGSLLQRAEQQDSGRLYLENKIHTLELKLEESHNRFSATEVTNKTLAAEMQELRARLAEAEETARTAERQKNQLQRQMQDFRRRLTPLHLEMQRIVEKADSWVEKEEPTPSN

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
35	Phosphorylation	GPPPGLLTPPVATDL CCCCCCCCCCCCCCC		26745281
40	Phosphorylation	LLTPPVATDLSQNAR CCCCCCCCCCCHHHH		26745281
43	Phosphorylation	PPVATDLSQNARHLQ CCCCCCCCHHHHHCC		26745281
112	Acetylation	AVPWNAVKVQTLSNQ CCCCCCEEEEECCCC		-
115	Phosphorylation	WNAVKVQTLSNQPLL CCCEEEEECCCCCCC		23984901
117	Phosphorylation	AVKVQTLSNQPLLKS CEEEEECCCCCCCCC		23984901
123	Methylation	LSNQPLLKSPAPPLL CCCCCCCCCCCCCEE		-
124	Phosphorylation	SNQPLLKSPAPPLLH CCCCCCCCCCCCEEE		26824392
180	Methylation	LHLSHLNRFPARGPH EEHHHHHCCCCCCCC		-
195	Phosphorylation	GRLDQGRSDDYDSKK CCCCCCCCCCCCHHH		27149854
215	Acetylation	GGEPWGAKKPRHDLS CCCCCCCCCCCCCCC		-
222	Phosphorylation	KKPRHDLSPYRVHLT CCCCCCCCCCEEECC		25521595
224	Phosphorylation	PRHDLSPYRVHLTPY CCCCCCCCEEECCCC		25159016
229	Phosphorylation	SPYRVHLTPYTVDSP CCCEEECCCCCCCCC		25266776
231	Phosphorylation	YRVHLTPYTVDSPTC CEEECCCCCCCCCCC		26643407
232	Phosphorylation	RVHLTPYTVDSPTCD EEECCCCCCCCCCCC		23984901
293	Phosphorylation	EKEAAPDTGAEPSPE CCCCCCCCCCCCCCC		28833060
298	Phosphorylation	PDTGAEPSPEDSDPT CCCCCCCCCCCCCCC		25521595
302	Phosphorylation	AEPSPEDSDPTYSSK CCCCCCCCCCCCCCE		28833060
305	Phosphorylation	SPEDSDPTYSSKVLL CCCCCCCCCCCEEEE		26160508
306	Phosphorylation	PEDSDPTYSSKVLLL CCCCCCCCCCEEEEE		26160508
307	Phosphorylation	EDSDPTYSSKVLLLS CCCCCCCCCEEEEEC		26160508
308	Phosphorylation	DSDPTYSSKVLLLSS CCCCCCCCEEEEECC		26160508
347	Ubiquitination	EHPLKQLKFLLGRKE CCHHHHHHHHHCCCC		22790023
448	Phosphorylation	ALCQQKATEAAPQPH HHHHHHHHHCCCCCC		25293948
458	Phosphorylation	APQPHEASGEAEATE CCCCCCCCCCCCHHC		22802335
464	Phosphorylation	ASGEAEATEQAPDVS CCCCCCHHCCCCCHH		25293948
483	Phosphorylation	TSKQNTETMEATTQQ CHHHCHHHHHHHCCC		-
520	Phosphorylation	RCVNLSLYGIVEDRR CEEEEEEEEEECCCC		-
568	Phosphorylation	SLPEKVVSPPEPEKE CCCCCCCCCCCHHHH		27180971
597	Phosphorylation	KEEAVKVSKDEVQNE HHHHHHCCHHHHHCC		25619855
606	Phosphorylation	DEVQNEGTAAESDSP HHHHCCCCCCCCCCC		24925903
610	Phosphorylation	NEGTAAESDSPLKED CCCCCCCCCCCCCCC		25521595
612	Phosphorylation	GTAAESDSPLKEDGL CCCCCCCCCCCCCCC		24925903
625	Phosphorylation	GLLPKRPSSGGEEEE CCCCCCCCCCCHHHH		25521595
626	Phosphorylation	LLPKRPSSGGEEEEK CCCCCCCCCCHHHHH		25521595
670	Phosphorylation	AGAKLEETEVRSVAS CCCCCCHHHHHHHHC		24925903
674	Phosphorylation	LEETEVRSVASNQSE CCHHHHHHHHCCCCH		25521595
677	Phosphorylation	TEVRSVASNQSEMEY HHHHHHHCCCCHHCH		18388127
680	Phosphorylation	RSVASNQSEMEYSSL HHHHCCCCHHCHHHH		25521595
684	Phosphorylation	SNQSEMEYSSLQDMP CCCCHHCHHHHHCCC		24925903
685	Phosphorylation	NQSEMEYSSLQDMPK CCCHHCHHHHHCCCC		24925903
686	Phosphorylation	QSEMEYSSLQDMPKE CCHHCHHHHHCCCCC		24925903
807	Phosphorylation	GLVPHNGSLINVGSL CCCCCCCCEEEHHHH		23984901
896	Phosphorylation	QDFRRRLTPLHLEMQ HHHHHHHHHHHHHHH		27600695
908	Acetylation	EMQRIVEKADSWVEK HHHHHHHHHHHHHHC		23236377
921	Phosphorylation	EKEEPTPSN------ HCCCCCCCC------		21183079

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

Oops, there are no upstream regulatory protein records of CCAR2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
112	K	Acetylation	Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory binding to SIRT1 and increases its deacetylase activity.	-
215	K	Acetylation	Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory binding to SIRT1 and increases its deacetylase activity.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CCAR2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CCAR2_MOUSE !!

Drug and Disease Associations

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