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Protein

Histone-arginine methyltransferase CARM1

Gene

Carm1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.17 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.5 Publications

Enzyme regulationi

Methylation of H3R17 (H3R17me) by CARM1 is stimulated by preacetylation of H3 'Lys-18' (H3K18ac) H3 'Lys-23' (H3K23ac) by EP300 and blocked by citrullination of H3 'Arg-17' (H3R17ci) by PADI4.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei160 – 1601S-adenosyl-L-methionine
Binding sitei169 – 1691S-adenosyl-L-methionine
Binding sitei193 – 1931S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei215 – 2151S-adenosyl-L-methionine
Binding sitei244 – 2441S-adenosyl-L-methionine
Binding sitei272 – 2721S-adenosyl-L-methionine

GO - Molecular functioni

  • histone-arginine N-methyltransferase activity Source: MGI
  • histone methyltransferase activity Source: UniProtKB
  • histone methyltransferase activity (H3-R17 specific) Source: UniProtKB
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • lysine-acetylated histone binding Source: UniProtKB
  • protein-arginine N-methyltransferase activity Source: UniProtKB
  • protein-arginine omega-N asymmetric methyltransferase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein methyltransferase activity Source: MGI
  • transcription coactivator activity Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  • aging Source: Ensembl
  • endochondral bone morphogenesis Source: MGI
  • histone arginine methylation Source: UniProtKB
  • histone H3-R17 methylation Source: UniProtKB
  • histone H3-R2 methylation Source: MGI
  • histone methylation Source: MGI
  • intracellular estrogen receptor signaling pathway Source: MGI
  • intracellular steroid hormone receptor signaling pathway Source: HGNC
  • negative regulation of dendrite development Source: Ensembl
  • negative regulation of protein binding Source: MGI
  • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: GOC
  • peptidyl-arginine N-methylation Source: GOC
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of fat cell differentiation Source: UniProtKB
  • protein methylation Source: MGI
  • regulation of growth plate cartilage chondrocyte proliferation Source: MGI
  • regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
  • regulation of mRNA binding Source: Ensembl
  • regulation of transcription, DNA-templated Source: MGI
  • response to cAMP Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-MMU-3214858. RMTs methylate histone arginines.
R-MMU-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-arginine methyltransferase CARM1 (EC:2.1.1.3195 Publications)
Alternative name(s):
Coactivator-associated arginine methyltransferase 1
Protein arginine N-methyltransferase 4
Gene namesi
Name:Carm1
Synonyms:Prmt4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1913208. Carm1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Mainly nuclear during the G1, S and G2 phases of the cell cycle. Cytoplasmic during mitosis, after breakup of the nuclear membrane (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • RNA polymerase II transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Neonatal lethality. The lungs of neonates do not inflate and they do not breathe. The same neonate lethality is observed with mutants that produce CARM1 protein without enzyme activity. Embryos are distinctly smaller at 18.5 dpc. They show reduced lipid accumulation in brown adipose tissue and reduced amounts of brown adipose tissue. Thymocyte differentiation is blocked at an early stage. Mutants display complete loss of protein methylation of the CARM1 substrates PABPC1 and EP300/P300.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi154 – 1541Y → A, F or R: Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity. 1 Publication
Mutagenesisi169 – 1691R → A: Loss of protein methyltransferase activity. 1 Publication
Mutagenesisi173 – 1731Y → A: Reduces protein methyltransferase activity. 1 Publication
Mutagenesisi189 – 1913VLD → AAA: Abolishes histone methyltransferase activity and coactivator activity. 2 Publications
Mutagenesisi217 – 2171S → A: Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity. Localized in the nucleus. 1 Publication
Mutagenesisi217 – 2171S → C or T: Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity. 1 Publication
Mutagenesisi217 – 2171S → E: Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity. Localized in the cytosol. 1 Publication
Mutagenesisi229 – 2291S → E: Abolishes dimerization. 1 Publication
Mutagenesisi267 – 2671E → Q: Abolishes histone methyltransferase activity and reduces coactivator activity. 2 Publications
Mutagenesisi551 – 5511R → K: Abolishes dimethylation. Impairs transcription coactivator activity and regulation of alternative splicing. No effect on methyltransferase activity. 1 Publication

Chemistry

ChEMBLiCHEMBL5538.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 608608Histone-arginine methyltransferase CARM1PRO_0000212339Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei217 – 2171PhosphoserineBy similarity
Modified residuei551 – 5511Dimethylated arginine1 Publication

Post-translational modificationi

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). Phosphorylation at Ser-217 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity. Phosphorylation at Ser-217 may promote cytosolic location.By similarity1 Publication
Auto-methylated on Arg-551. Methylation enhances transcription coactivator activity. Methylation is required for its role in the regulation of pre-mRNA alternative splicing.11 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ9WVG6.
MaxQBiQ9WVG6.
PaxDbiQ9WVG6.
PRIDEiQ9WVG6.

PTM databases

iPTMnetiQ9WVG6.
PhosphoSiteiQ9WVG6.

Expressioni

Tissue specificityi

Ubiquitously expressed. Within the brain, present in proliferating cells from lateral ventricular zone and dentate gyrus (at protein level).2 Publications

Developmental stagei

At E9, expression is prominent in the neural tube and somites.1 Publication

Gene expression databases

BgeeiQ9WVG6.
ExpressionAtlasiQ9WVG6. baseline and differential.
GenevisibleiQ9WVG6. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with NR1H4. Interacts with SNRPC (By similarity). Interacts with the C-terminus of NCOA2/GRIP1, NCO3/ACTR and NCOA1/SRC1. Part of a complex consisting of CARM1, EP300/P300 and NCOA2/GRIP1. Interacts with FLII, TP53, myogenic factor MEF2, EP300/P300, TRIM24, CREBBP and CTNNB1. Interacts with RELA. Identified in a complex containing CARM1, TRIM24 and NCOA2/GRIP1. Interacts with NCOA3/SRC3.By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Hist1h3iP684334EBI-4414343,EBI-1179609From a different organism.

GO - Molecular functioni

  • lysine-acetylated histone binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi208501. 7 interactions.
DIPiDIP-44593N.
IntActiQ9WVG6. 5 interactions.
MINTiMINT-6166798.
STRINGi10090.ENSMUSP00000034703.

Chemistry

BindingDBiQ9WVG6.

Structurei

Secondary structure

1
608
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi148 – 1536Combined sources
Helixi157 – 1648Combined sources
Helixi167 – 17913Combined sources
Helixi180 – 1834Combined sources
Turni184 – 1863Combined sources
Beta strandi188 – 1936Combined sources
Helixi198 – 2069Combined sources
Beta strandi209 – 2157Combined sources
Helixi219 – 22911Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2416Combined sources
Turni243 – 2453Combined sources
Beta strandi252 – 2565Combined sources
Helixi266 – 2683Combined sources
Helixi269 – 2757Combined sources
Helixi276 – 2794Combined sources
Beta strandi280 – 2889Combined sources
Beta strandi290 – 2989Combined sources
Helixi301 – 31111Combined sources
Helixi312 – 3154Combined sources
Beta strandi319 – 3213Combined sources
Helixi325 – 3273Combined sources
Helixi328 – 3369Combined sources
Beta strandi340 – 3423Combined sources
Helixi346 – 3483Combined sources
Beta strandi354 – 3596Combined sources
Turni360 – 3623Combined sources
Helixi365 – 3695Combined sources
Beta strandi370 – 3789Combined sources
Beta strandi383 – 39513Combined sources
Beta strandi404 – 4063Combined sources
Beta strandi418 – 42912Combined sources
Beta strandi434 – 4429Combined sources
Turni445 – 4473Combined sources
Beta strandi450 – 4578Combined sources
Turni458 – 4614Combined sources
Beta strandi462 – 4698Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V74X-ray2.70B/D/F/H147-490[»]
2V7EX-ray2.70A/B147-490[»]
ProteinModelPortaliQ9WVG6.
SMRiQ9WVG6. Positions 28-131, 144-477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WVG6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 454308SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni500 – 608109Transactivation domainAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1500. Eukaryota.
ENOG410XPDD. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198522.
HOVERGENiHBG050797.
InParanoidiQ9WVG6.
KOiK05931.
OrthoDBiEOG72NRPM.
PhylomeDBiQ9WVG6.
TreeFamiTF323332.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR020989. Histone-Arg_MeTrfase_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF11531. CARM1. 1 hit.
PF05185. PRMT5. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WVG6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAATAVG PGAGSAGVAG PGGAGPCATV SVFPGARLLT IGDANGEIQR
60 70 80 90 100
HAEQQALRLE VRAGPDAAGI ALYSHEDVCV FKCSVSRETE CSRVGRQSFI
110 120 130 140 150
ITLGCNSVLI QFATPHDFCS FYNILKTCRG HTLERSVFSE RTEESSAVQY
160 170 180 190 200
FQFYGYLSQQ QNMMQDYVRT GTYQRAILQN HTDFKDKIVL DVGCGSGILS
210 220 230 240 250
FFAAQAGARK IYAVEASTMA QHAEVLVKSN NLTDRIVVIP GKVEEVSLPE
260 270 280 290 300
QVDIIISEPM GYMLFNERML ESYLHAKKYL KPSGNMFPTI GDVHLAPFTD
310 320 330 340 350
EQLYMEQFTK ANFWYQPSFH GVDLSALRGA AVDEYFRQPV VDTFDIRILM
360 370 380 390 400
AKSVKYTVNF LEAKEGDLHR IEIPFKFHML HSGLVHGLAF WFDVAFIGSI
410 420 430 440 450
MTVWLSTAPT EPLTHWYQVR CLFQSPLFAK AGDTLSGTCL LIANKRQSYD
460 470 480 490 500
ISIVAQVDQT GSKSSNLLDL KNPFFRYTGT TPSPPPGSHY TSPSENMWNT
510 520 530 540 550
GSTYNLSSGV AVAGMPTAYD LSSVIAGGSS VGHNNLIPLA NTGIVNHTHS
560 570 580 590 600
RMGSIMSTGI VQGSSGAQGG GGSSSAHYAV NNQFTMGGPA ISMASPMSIP

TNTMHYGS
Length:608
Mass (Da):65,854
Last modified:September 13, 2004 - v2
Checksum:iC621F2AA9FBA2DA3
GO
Isoform 2 (identifier: Q9WVG6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     540-562: Missing.

Note: No experimental confirmation available.
Show »
Length:585
Mass (Da):63,460
Checksum:iC419059E314B2D51
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti400 – 4001I → L in BAE34644 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei540 – 56223Missing in isoform 2. 1 PublicationVSP_012508Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117887 mRNA. Translation: AAD41265.2.
BC003964 mRNA. Translation: AAH03964.1.
BC008263 mRNA. Translation: AAH08263.1.
BC036974 mRNA. Translation: AAH36974.1.
AK158757 mRNA. Translation: BAE34644.1.
CCDSiCCDS22906.1. [Q9WVG6-1]
CCDS52736.1. [Q9WVG6-2]
RefSeqiNP_067506.2. NM_021531.6. [Q9WVG6-1]
NP_694781.1. NM_153141.1. [Q9WVG6-2]
UniGeneiMm.178115.

Genome annotation databases

EnsembliENSMUST00000034703; ENSMUSP00000034703; ENSMUSG00000032185. [Q9WVG6-1]
ENSMUST00000115395; ENSMUSP00000111053; ENSMUSG00000032185. [Q9WVG6-2]
GeneIDi59035.
KEGGimmu:59035.
UCSCiuc009olu.2. mouse. [Q9WVG6-1]
uc009olw.2. mouse. [Q9WVG6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117887 mRNA. Translation: AAD41265.2.
BC003964 mRNA. Translation: AAH03964.1.
BC008263 mRNA. Translation: AAH08263.1.
BC036974 mRNA. Translation: AAH36974.1.
AK158757 mRNA. Translation: BAE34644.1.
CCDSiCCDS22906.1. [Q9WVG6-1]
CCDS52736.1. [Q9WVG6-2]
RefSeqiNP_067506.2. NM_021531.6. [Q9WVG6-1]
NP_694781.1. NM_153141.1. [Q9WVG6-2]
UniGeneiMm.178115.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V74X-ray2.70B/D/F/H147-490[»]
2V7EX-ray2.70A/B147-490[»]
ProteinModelPortaliQ9WVG6.
SMRiQ9WVG6. Positions 28-131, 144-477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208501. 7 interactions.
DIPiDIP-44593N.
IntActiQ9WVG6. 5 interactions.
MINTiMINT-6166798.
STRINGi10090.ENSMUSP00000034703.

Chemistry

BindingDBiQ9WVG6.
ChEMBLiCHEMBL5538.

PTM databases

iPTMnetiQ9WVG6.
PhosphoSiteiQ9WVG6.

Proteomic databases

EPDiQ9WVG6.
MaxQBiQ9WVG6.
PaxDbiQ9WVG6.
PRIDEiQ9WVG6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034703; ENSMUSP00000034703; ENSMUSG00000032185. [Q9WVG6-1]
ENSMUST00000115395; ENSMUSP00000111053; ENSMUSG00000032185. [Q9WVG6-2]
GeneIDi59035.
KEGGimmu:59035.
UCSCiuc009olu.2. mouse. [Q9WVG6-1]
uc009olw.2. mouse. [Q9WVG6-2]

Organism-specific databases

CTDi10498.
MGIiMGI:1913208. Carm1.

Phylogenomic databases

eggNOGiKOG1500. Eukaryota.
ENOG410XPDD. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198522.
HOVERGENiHBG050797.
InParanoidiQ9WVG6.
KOiK05931.
OrthoDBiEOG72NRPM.
PhylomeDBiQ9WVG6.
TreeFamiTF323332.

Enzyme and pathway databases

ReactomeiR-MMU-3214858. RMTs methylate histone arginines.
R-MMU-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Miscellaneous databases

ChiTaRSiCarm1. mouse.
EvolutionaryTraceiQ9WVG6.
PROiQ9WVG6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVG6.
ExpressionAtlasiQ9WVG6. baseline and differential.
GenevisibleiQ9WVG6. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR020989. Histone-Arg_MeTrfase_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF11531. CARM1. 1 hit.
PF05185. PRMT5. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of transcription by a protein methyltransferase."
    Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T., Aswad D.W., Stallcup M.R.
    Science 284:2174-2177(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF 189-VAL--ASP-191, FUNCTION, TISSUE SPECIFICITY, METHYLATION OF HISTONE H3, INTERACTION WITH NCOA1; NCOA2 AND NCOA3.
    Tissue: Embryo.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-608 (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary gland and Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-608 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Visual cortex.
  4. "Methylation of histone H3 by coactivator-associated arginine methyltransferase 1."
    Schurter B.T., Koh S.S., Chen D., Bunick G.J., Harp J.M., Hanson B.L., Henschen-Edman A., Mackay D.R., Stallcup M.R., Aswad D.W.
    Biochemistry 40:5747-5756(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN METHYLATION OF HISTONE H3, CATALYTIC ACTIVITY.
  5. "Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter."
    Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A., Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R.
    Curr. Biol. 11:1981-1985(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION OF HISTONE H3.
  6. "A transcriptional switch mediated by cofactor methylation."
    Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M.
    Science 294:2507-2511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, METHYLATION OF EP300 AND CREBBP, MUTAGENESIS OF 189-VAL--ASP-191, INTERACTION WITH EP300 AND CREBBP.
  7. "Crosstalk between CARM1 methylation and CBP acetylation on histone H3."
    Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.
    Curr. Biol. 12:2090-2097(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION OF HISTONE H3.
  8. "Methylation at arginine 17 of histone H3 is linked to gene activation."
    Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.
    EMBO Rep. 3:39-44(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION OF HISTONE H3.
  9. "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays."
    Lee J., Bedford M.T.
    EMBO Rep. 3:268-273(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION OF PABPC1.
  10. "The coactivator-associated arginine methyltransferase is necessary for muscle differentiation: CARM1 coactivates myocyte enhancer factor-2."
    Chen S.L., Loffler K.A., Chen D., Stallcup M.R., Muscat G.E.
    J. Biol. Chem. 277:4324-4333(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH MEF2C.
  11. "Synergistic coactivator function by coactivator-associated arginine methyltransferase (CARM) 1 and beta-catenin with two different classes of DNA-binding transcriptional activators."
    Koh S.S., Li H., Lee Y.-H., Widelitz R.B., Chuong C.-M., Stallcup M.R.
    J. Biol. Chem. 277:26031-26035(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-267, INTERACTION WITH CTNNB1.
  12. "Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase."
    Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W., Stallcup M.R., Laird-Offringa I.A.
    J. Biol. Chem. 277:44623-44630(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION OF ELAVL1.
  13. "Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function."
    Teyssier C., Chen D., Stallcup M.R.
    J. Biol. Chem. 277:46066-46072(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, HOMOOLIGOMERIZATION.
  14. "Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities."
    Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R.
    Mol. Cell. Biol. 22:3621-3632(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH EP300 AND NCOA2, MUTAGENESIS OF GLU-267.
  15. "Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice."
    Yadav N., Lee J., Kim J., Shen J., Hu M.C.-T., Aldaz C.M., Bedford M.T.
    Proc. Natl. Acad. Sci. U.S.A. 100:6464-6468(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, METHYLATION OF PABPC1.
  16. "Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53."
    An W., Kim J., Roeder R.G.
    Cell 117:735-748(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53.
  17. Cited for: METHYLATION OF HISTONE H3.
  18. "Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activity."
    Lee Y.-H., Campbell H.D., Stallcup M.R.
    Mol. Cell. Biol. 24:2103-2117(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FLII.
  19. "Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression."
    Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C., Imhof R., Bedford M.T., Natoli G., Hottiger M.O.
    EMBO J. 24:85-96(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION OF HISTONE H3, FUNCTION, INTERACTION WITH RELA.
  20. Cited for: TISSUE SPECIFICITY.
  21. "Transcriptional intermediary factor 1alpha mediates physical interaction and functional synergy between the coactivator-associated arginine methyltransferase 1 and glucocorticoid receptor-interacting protein 1 nuclear receptor coactivators."
    Teyssier C., Ou C.Y., Khetchoumian K., Losson R., Stallcup M.R.
    Mol. Endocrinol. 20:1276-1286(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRIM24, IDENTIFICATION IN A COMPLEX WITH TRIM24 AND NCOA2.
  22. "The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing."
    Cheng D., Cote J., Shaaban S., Bedford M.T.
    Mol. Cell 25:71-83(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "CARM1 promotes adipocyte differentiation by coactivating PPARgamma."
    Yadav N., Cheng D., Richard S., Morel M., Iyer V.R., Aldaz C.M., Bedford M.T.
    EMBO Rep. 9:193-198(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  24. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH EP300 AND NCOA3, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-154; SER-217 AND SER-229, PHOSPHORYLATION AT SER-217.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Spleen and Testis.
  26. "Enzymatic activity is required for the in vivo functions of CARM1."
    Kim D., Lee J., Cheng D., Li J., Carter C., Richie E., Bedford M.T.
    J. Biol. Chem. 285:1147-1152(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBUNIT, MUTAGENESIS OF ARG-169 AND TYR-173.
  27. "Automethylation of CARM1 allows coupling of transcription and mRNA splicing."
    Kuhn P., Chumanov R., Wang Y., Ge Y., Burgess R.R., Xu W.
    Nucleic Acids Res. 39:2717-2726(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-551, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-551, IDENTIFICATION BY MASS SPECTROMETRY.
  28. "Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase."
    Yue W.W., Hassler M., Roe S.M., Thompson-Vale V., Pearl L.H.
    EMBO J. 26:4402-4412(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 147-490 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH NCOA2/GRIP1, ENZYME REGULATION, SUBUNIT.

Entry informationi

Entry nameiCARM1_MOUSE
AccessioniPrimary (citable) accession number: Q9WVG6
Secondary accession number(s): Q3TYB9
, Q8K1Y5, Q91W24, Q99KX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: September 13, 2004
Last modified: June 8, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.