CARM1_HUMAN - dbPTM
CARM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CARM1_HUMAN
UniProt AC Q86X55
Protein Name Histone-arginine methyltransferase CARM1
Gene Name CARM1
Organism Homo sapiens (Human).
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.
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 activate 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 MAAAAAAVGPGAGGAGSAVPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDSAGIALYSHEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSFYNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPSPPPGSHYTSPSENMWNTGSTYNLSSGMAVAGMPTAYDLSSVIASGSSVGHNNLIPLANTGIVNHTHSRMGSIMSTGIVQGSSGAQGSGGGSTSAHYAVNSQFTMGGPAISMASPMSIPTNTMHYGS
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 Orthologous
Protein Cluster
2Acetylation------MAAAAAAVG
------CCCCCHHCC		13.0522223895
39PhosphorylationFPGARLLTIGDANGE
ECCCEEEEEECCCHH		27.7527174698
49DimethylationDANGEIQRHAEQQAL
CCCHHHHHHHHHHCH		36.32-
49MethylationDANGEIQRHAEQQAL
CCCHHHHHHHHHHCH		36.32-
66UbiquitinationEVRAGPDSAGIALYS
EEECCCCCCCEEEEE		31.3721890473
81UbiquitinationHEDVCVFKCSVSRET
CCCEEEEEEEECCCC		12.7622053931
81 (in isoform 1)Ubiquitination-12.7621890473
131PhosphorylationLKTCRGHTLERSVFS
HHHHCCCCCCCHHCC		32.8922210691
135PhosphorylationRGHTLERSVFSERTE
CCCCCCCHHCCCCCC		20.3822210691
149PhosphorylationEESSAVQYFQFYGYL
CCCHHHHHHHHHHHH		7.8622210691
153PhosphorylationAVQYFQFYGYLSQQQ
HHHHHHHHHHHHHHH		8.2822210691
166PhosphorylationQQNMMQDYVRTGTYQ
HHHHHHHHHHHHHHH		3.7922210691
169PhosphorylationMMQDYVRTGTYQRAI
HHHHHHHHHHHHHHH		24.6722210691
171PhosphorylationQDYVRTGTYQRAILQ
HHHHHHHHHHHHHHH		18.8322210691
172PhosphorylationDYVRTGTYQRAILQN
HHHHHHHHHHHHHHC		9.4222210691
184AcetylationLQNHTDFKDKIVLDV
HHCCCCCCCCEEEEE		62.0025953088
192UbiquitinationDKIVLDVGCGSGILS
CCEEEEECCCHHHHH		15.1032015554
202UbiquitinationSGILSFFAAQAGARK
HHHHHHHHHHCCCCE		9.1723000965
216PhosphorylationKIYAVEASTMAQHAE
EEEEEEHHHHHHHHE		12.7619060867
227 (in isoform 1)Ubiquitination-43.2221890473
227UbiquitinationQHAEVLVKSNNLTDR
HHHEEEEECCCCCCE		43.2221890473
227 (in isoform 2)Ubiquitination-43.2221890473
227UbiquitinationQHAEVLVKSNNLTDR
HHHEEEEECCCCCCE		43.2222817900
228PhosphorylationHAEVLVKSNNLTDRI
HHEEEEECCCCCCEE		24.3817640894
234MethylationKSNNLTDRIVVIPGK
ECCCCCCEEEEECCC		20.54-
276MethylationLESYLHAKKYLKPSG
HHHHHHHHHHCCCCC		31.07-
276AcetylationLESYLHAKKYLKPSG
HHHHHHHHHHCCCCC		31.077977051
309UbiquitinationLYMEQFTKANFWYQP
HHHHHHHHCCCCCCC		42.4921963094
328UbiquitinationVDLSALRGAAVDEYF
CCHHHHCCCHHHHHH		20.8133845483
355PhosphorylationLMAKSVKYTVNFLEA
EEECCCEEEEEEEEC		17.4824260401
356PhosphorylationMAKSVKYTVNFLEAK
EECCCEEEEEEEECC		11.8524260401
3632-HydroxyisobutyrylationTVNFLEAKEGDLHRI
EEEEEECCCCCCEEE		53.51-
363UbiquitinationTVNFLEAKEGDLHRI
EEEEEECCCCCCEEE		53.5123000965
435UbiquitinationAKAGDTLSGTCLLIA
HHCCCCCCCEEEEEE		33.8632015554
444UbiquitinationTCLLIANKRQSYDIS
EEEEEEECCCCEEEE		42.67-
444AcetylationTCLLIANKRQSYDIS
EEEEEEECCCCEEEE		42.6725953088
447PhosphorylationLIANKRQSYDISIVA
EEEECCCCEEEEEEE		28.89-
459PhosphorylationIVAQVDQTGSKSSNL
EEEEECCCCCCCCCC		38.6727251275
461PhosphorylationAQVDQTGSKSSNLLD
EEECCCCCCCCCCCC		32.5227251275
462UbiquitinationQVDQTGSKSSNLLDL
EECCCCCCCCCCCCC		60.28-
470 (in isoform 1)Ubiquitination-63.3421890473
470UbiquitinationSSNLLDLKNPFFRYT
CCCCCCCCCCCEEEE		63.3421890473
470UbiquitinationSSNLLDLKNPFFRYT
CCCCCCCCCCCEEEE		63.3421963094
550MethylationIVNHTHSRMGSIMST
CCCCCCCCCCCEEEE		26.36-
582O-linked_GlycosylationSAHYAVNSQFTMGGP
CCEEEECCCCCCCCC		21.77OGP
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
447SPhosphorylationKinasePKACAP17612
PSP
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:27309807:27867975
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
216SPhosphorylation

19843527
216SPhosphorylation

19843527
216SPhosphorylation

19843527
550RMethylation

-
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 CARM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PABP2_HUMANPABPN1physical
11850402
MEF2D_HUMANMEF2Dphysical
19188441
MYOD1_HUMANMYOD1physical
19188441
MYOG_HUMANMYOGphysical
19188441
NCOA3_HUMANNCOA3physical
17043108
CBP_HUMANCREBBPphysical
17043108
H31_HUMANHIST1H3Aphysical
17043108
EP300_HUMANEP300physical
16923966
NCOA2_HUMANNCOA2physical
16923966
NCOA3_HUMANNCOA3physical
16923966
SRCAP_HUMANSRCAPphysical
14500758
NCOA3_HUMANNCOA3physical
18511550
NCOA2_HUMANNCOA2physical
18511550
NCOA1_HUMANNCOA1physical
18511550
H31_HUMANHIST1H3Aphysical
12498683
CBP_HUMANCREBBPphysical
12374746
H33_BOVINH3F3Aphysical
11747826
CBP_HUMANCREBBPphysical
11701890
EP300_HUMANEP300physical
11701890
EP300_HUMANEP300physical
15731352
CBP_HUMANCREBBPphysical
15731352
TF65_HUMANRELAphysical
15616592
STA5A_HUMANSTAT5Aphysical
18413343
TF65_HUMANRELAphysical
18280497
EP300_HUMANEP300physical
18280497
H31_HUMANHIST1H3Aphysical
15471871
NR1H4_HUMANNR1H4physical
15471871
ARI1A_HUMANARID1Aphysical
14729568
SMCA4_HUMANSMARCA4physical
14729568
SMRC2_HUMANSMARCC2physical
14729568
SMRC1_HUMANSMARCC1physical
14729568
NFKB1_HUMANNFKB1physical
14729568
SMCE1_HUMANSMARCE1physical
14729568
SNF5_HUMANSMARCB1physical
14729568
ACTB_HUMANACTBphysical
14729568
SMRD1_HUMANSMARCD1physical
14729568
CEBPB_HUMANCEBPBphysical
20111005
WDR5_HUMANWDR5physical
19660582
AXIN1_HUMANAXIN1physical
21242974
AFF1_HUMANAFF1physical
21030982
NCOA3_HUMANNCOA3physical
15383283
H31_HUMANHIST1H3Aphysical
22451921
ORF73_HHV8PHHV8GK18_gp81physical
22179613
RBGP1_HUMANRABGAP1genetic
17124247
EP300_HUMANEP300physical
21988832
HS105_HUMANHSPH1physical
22863883
ILK_HUMANILKphysical
22863883
PARVA_HUMANPARVAphysical
22863883
PUR1_HUMANPPATphysical
22863883
UGPA_HUMANUGP2physical
22863883
XPO7_HUMANXPO7physical
22863883
KAT2B_HUMANKAT2Bphysical
20213728
CTBP1_HUMANCTBP1physical
26344197
NCOA1_HUMANNCOA1physical
16923966
DZIP3_MOUSEDzip3physical
26505218
DZIP3_HUMANDZIP3physical
26505218
EP300_HUMANEP300physical
28844863
ESR1_HUMANESR1physical
28844863
H31_HUMANHIST1H3Aphysical
28844863
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 CARM1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Biochemical control of CARM1 enzymatic activity by phosphorylation.";
Feng Q., He B., Jung S.Y., Song Y., Qin J., Tsai S.Y., Tsai M.J.,O'Malley B.W.;
J. Biol. Chem. 284:36167-36174(2009).
Cited for: PHOSPHORYLATION AT SER-216, SUBCELLULAR LOCATION, AND MASSSPECTROMETRY.

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