CARM1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CARM1_MOUSE
• UniProt AC: Q9WVG6
• Protein Name: Histone-arginine methyltransferase CARM1
• Gene Name: Carm1
• Organism: Mus musculus (Mouse).
• Sequence Length: 608
• Subcellular Localization: Nucleus. Cytoplasm. Mainly nuclear during the G1, S and G2 phases of the cell cycle. Cytoplasmic during mitosis, after breakup of the nuclear membrane (By similarity)..
• Protein Description: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs..
• Protein Sequence: MAAAAATAVGPGAGSAGVAGPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDAAGIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLIQFATPHDFCSFYNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPSPPPGSHYTSPSENMWNTGSTYNLSSGVAVAGMPTAYDLSSVIAGGSSVGHNNLIPLANTGIVNHTHSRMGSIMSTGIVQGSSGAQGGGGSSSAHYAVNNQFTMGGPAISMASPMSIPTNTMHYGS

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
132	Phosphorylation	LKTCRGHTLERSVFS HHHHCCCCCCCHHCC	32.89	-
217	Phosphorylation	KIYAVEASTMAQHAE EEEEEEHHHHHHHHE	12.76	19843527
229	Phosphorylation	HAEVLVKSNNLTDRI HHEEEEECCCCCCEE	24.38	17640894
414	Phosphorylation	TAPTEPLTHWYQVRC CCCCCCCCCCHHHHH	22.52	-
463	Ubiquitination	QVDQTGSKSSNLLDL EECCCCCCCCCCCCC	60.28	-
471	Ubiquitination	SSNLLDLKNPFFRYT CCCCCCCCCCCEEEE	63.34	-
551	Methylation	IVNHTHSRMGSIMST CCCCCCCCCCCEEEC	26.36	21138967

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
132	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
217	S	Phosphorylation	Phosphorylation at Ser-217 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity.	19843527
217	S	Phosphorylation	Phosphorylation at Ser-217 is strongly increased during mitosis, and decreases rapidly to a very low, basal level after entry into the G1 phase of the cell cycle (By similarity).	19843527
217	S	Phosphorylation	Phosphorylation at Ser-217 may promote cytosolic location.	19843527
551	R	Methylation	Auto-methylated on Arg-551.	21138967

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CARM1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MEF2C_MOUSE	Mef2c	physical	11713257
NCOA2_MOUSE	Ncoa2	physical	11713257
NCOA1_MOUSE	Ncoa1	physical	10381882
RBGP1_HUMAN	RABGAP1	physical	17124247
H31_MOUSE	Hist1h3a	physical	10381882
NCOA2_MOUSE	Ncoa2	physical	10381882

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Methylation

"Automethylation of CARM1 allows coupling of transcription and mRNAsplicing.";
Kuhn P., Chumanov R., Wang Y., Ge Y., Burgess R.R., Xu W.;
Nucleic Acids Res. 39:2717-2726(2011).
Cited for: METHYLATION AT ARG-551, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OFARG-551, AND MASS SPECTROMETRY.
PubMed: 21138967