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Q86X55

- CARM1_HUMAN

UniProt

Q86X55 - CARM1_HUMAN

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Protein
Histone-arginine methyltransferase CARM1
Gene
CARM1, PRMT4
Organism
Homo sapiens (Human)
Status
Reviewed - 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 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.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].1 Publication

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei159 – 1591S-adenosyl-L-methionine
Binding sitei168 – 1681S-adenosyl-L-methionine
Binding sitei192 – 1921S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei214 – 2141S-adenosyl-L-methionine
Binding sitei243 – 2431S-adenosyl-L-methionine
Binding sitei271 – 2711S-adenosyl-L-methionine

GO - Molecular functioni

  1. beta-catenin binding Source: AgBase
  2. histone methyltransferase activity Source: UniProtKB
  3. histone methyltransferase activity (H3-R17 specific) Source: UniProtKB
  4. histone-arginine N-methyltransferase activity Source: RefGenome
  5. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  6. lysine-acetylated histone binding Source: UniProtKB
  7. protein binding Source: IntAct
  8. protein methyltransferase activity Source: UniProtKB
  9. protein-arginine N-methyltransferase activity Source: UniProtKB
  10. protein-arginine omega-N asymmetric methyltransferase activity Source: UniProtKB
  11. transcription coactivator activity Source: UniProtKB
  12. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. endochondral bone morphogenesis Source: Ensembl
  3. histone H3-R17 methylation Source: UniProtKB
  4. histone H3-R2 methylation Source: UniProtKB
  5. histone methylation Source: UniProtKB
  6. intracellular estrogen receptor signaling pathway Source: Ensembl
  7. negative regulation of protein binding Source: Ensembl
  8. pathogenesis Source: InterPro
  9. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: RefGenome
  10. positive regulation of cell proliferation Source: Ensembl
  11. positive regulation of fat cell differentiation Source: UniProtKB
  12. regulation of growth plate cartilage chondrocyte proliferation Source: Ensembl
  13. regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
  14. regulation of transcription, DNA-templated Source: UniProtKB
  15. response to cAMP Source: Ensembl
  16. small molecule metabolic process Source: Reactome
  17. transcription, DNA-templated Source: UniProtKB-KW
  18. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118789. REV-ERBA represses gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-arginine methyltransferase CARM1 (EC:2.1.1.-, EC:2.1.1.125)
Alternative name(s):
Coactivator-associated arginine methyltransferase 1
Protein arginine N-methyltransferase 4
Gene namesi
Name:CARM1
Synonyms:PRMT4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:23393. 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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134959553.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 608607Histone-arginine methyltransferase CARM1
PRO_0000212338Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei216 – 2161Phosphoserine1 Publication
Modified residuei550 – 5501Dimethylated arginine By similarity

Post-translational modificationi

Auto-methylated on Arg-550. Methylation enhances transcription coactivator activity. Methylation is required for its role in the regulation of pre-mRNA alternative splicing By similarity.3 Publications
Phosphorylation at Ser-216 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity By similarity. Phosphorylation at Ser-216 is strongly increased during mitosis, and decreases rapidly to a very low, basal level after entry into the G1 phase of the cell cycle. Phosphorylation at Ser-216 may promote location in the cytosol.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ86X55.
PaxDbiQ86X55.
PRIDEiQ86X55.

PTM databases

PhosphoSiteiQ86X55.

Expressioni

Tissue specificityi

Overexpressed in prostate adenocarcinomas and high-grade prostatic intraepithelial neoplasia.1 Publication

Gene expression databases

ArrayExpressiQ86X55.
BgeeiQ86X55.
CleanExiHS_CARM1.
GenevestigatoriQ86X55.

Organism-specific databases

HPAiCAB032961.

Interactioni

Subunit structurei

Homodimer Inferred. 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. Identified in a complex containing CARM1, TRIM24 and NCOA2/GRIP1. Interacts with NCOA3/SRC3. Interacts with SNRPC By similarity. Interacts with NR1H4. Interacts with RELA. Interacts with HTLV-1 Tax-1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEBPBP176762EBI-2339854,EBI-969696
CEBPBQ058263EBI-2339854,EBI-7774198From a different organism.
DNAJA3Q96EY12EBI-2339854,EBI-356767
NUDT21O438092EBI-2339854,EBI-355720
QKIQ96PU82EBI-2339854,EBI-945792
SMARCC1Q929224EBI-2339854,EBI-355653

Protein-protein interaction databases

BioGridi115760. 74 interactions.
IntActiQ86X55. 21 interactions.
MINTiMINT-3379851.
STRINGi9606.ENSP00000325690.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi136 – 1405
Helixi145 – 1528
Helixi156 – 1638
Helixi166 – 17712
Helixi178 – 1825
Turni183 – 1853
Beta strandi187 – 1926
Helixi197 – 2048
Beta strandi208 – 2147
Helixi218 – 22811
Turni232 – 2343
Beta strandi235 – 2406
Turni242 – 2443
Beta strandi251 – 2566
Turni264 – 2663
Helixi268 – 2747
Helixi275 – 2784
Beta strandi279 – 2879
Beta strandi289 – 2979
Helixi300 – 31011
Helixi311 – 3144
Helixi324 – 3263
Helixi327 – 3359
Beta strandi339 – 3413
Helixi345 – 3473
Beta strandi353 – 3586
Turni359 – 3613
Helixi364 – 3685
Beta strandi369 – 3779
Beta strandi382 – 39615
Beta strandi401 – 4055
Beta strandi417 – 42812
Beta strandi433 – 44210
Beta strandi446 – 45611
Turni457 – 4593
Beta strandi462 – 4687

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y1WX-ray2.10A/B/C/D135-482[»]
2Y1XX-ray2.40A/B/C/D135-482[»]
4IKPX-ray2.00A/B/C/D140-480[»]
ProteinModelPortaliQ86X55.
SMRiQ86X55. Positions 27-130, 143-476.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini146 – 453308SAM-dependent MTase PRMT-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni499 – 608110Transactivation domain By similarity
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0500.
HOGENOMiHOG000198522.
HOVERGENiHBG050797.
KOiK05931.
OMAiHAKKYLR.
OrthoDBiEOG72NRPM.
PhylomeDBiQ86X55.
TreeFamiTF323332.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR020989. Histone-Arg_MeTrfase_N.
IPR029063. SAM-dependent_MTases-like.
[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 (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 3 (identifier: Q86X55-3) [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

MAAAAAAVGP GAGGAGSAVP GGAGPCATVS VFPGARLLTI GDANGEIQRH    50
AEQQALRLEV RAGPDSAGIA LYSHEDVCVF KCSVSRETEC SRVGKQSFII 100
TLGCNSVLIQ FATPNDFCSF YNILKTCRGH TLERSVFSER TEESSAVQYF 150
QFYGYLSQQQ NMMQDYVRTG TYQRAILQNH TDFKDKIVLD VGCGSGILSF 200
FAAQAGARKI YAVEASTMAQ HAEVLVKSNN LTDRIVVIPG KVEEVSLPEQ 250
VDIIISEPMG YMLFNERMLE SYLHAKKYLK PSGNMFPTIG DVHLAPFTDE 300
QLYMEQFTKA NFWYQPSFHG VDLSALRGAA VDEYFRQPVV DTFDIRILMA 350
KSVKYTVNFL EAKEGDLHRI EIPFKFHMLH SGLVHGLAFW FDVAFIGSIM 400
TVWLSTAPTE PLTHWYQVRC LFQSPLFAKA GDTLSGTCLL IANKRQSYDI 450
SIVAQVDQTG SKSSNLLDLK NPFFRYTGTT PSPPPGSHYT SPSENMWNTG 500
STYNLSSGMA VAGMPTAYDL SSVIASGSSV GHNNLIPLAN TGIVNHTHSR 550
MGSIMSTGIV QGSSGAQGSG GGSTSAHYAV NSQFTMGGPA ISMASPMSIP 600
TNTMHYGS 608
Length:608
Mass (Da):65,854
Last modified:October 5, 2010 - v3
Checksum:i094AC60D4A70B263
GO
Isoform 1 (identifier: Q86X55-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-561: Missing.

Show »
Length:585
Mass (Da):63,460
Checksum:i15C6720FBEB864FE
GO
Isoform 2 (identifier: Q86X55-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     369-384: RIEIPFKFHMLHSGLV → SACLASPAATALCLPG
     385-608: Missing.

Note: No experimental confirmation available.

Show »
Length:384
Mass (Da):41,885
Checksum:i722E8576DD6353D6
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei369 – 38416RIEIP…HSGLV → SACLASPAATALCLPG in isoform 2.
VSP_012506Add
BLAST
Alternative sequencei385 – 608224Missing in isoform 2.
VSP_012507Add
BLAST
Alternative sequencei539 – 56123Missing in isoform 1.
VSP_039876Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC007565 Genomic DNA. No translation available.
AC011442 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84156.1.
BC046240 mRNA. Translation: AAH46240.1.
BC172490 mRNA. No translation available.
AL833242 mRNA. No translation available.
CCDSiCCDS12250.1. [Q86X55-3]
RefSeqiNP_954592.1. NM_199141.1. [Q86X55-3]
XP_005259765.1. XM_005259708.2. [Q86X55-1]
UniGeneiHs.323213.

Genome annotation databases

EnsembliENST00000327064; ENSP00000325690; ENSG00000142453. [Q86X55-3]
ENST00000344150; ENSP00000340934; ENSG00000142453. [Q86X55-1]
GeneIDi10498.
KEGGihsa:10498.
UCSCiuc002mpz.3. human. [Q86X55-3]
uc002mqa.3. human. [Q86X55-1]

Polymorphism databases

DMDMi308153622.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC007565 Genomic DNA. No translation available.
AC011442 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84156.1 .
BC046240 mRNA. Translation: AAH46240.1 .
BC172490 mRNA. No translation available.
AL833242 mRNA. No translation available.
CCDSi CCDS12250.1. [Q86X55-3 ]
RefSeqi NP_954592.1. NM_199141.1. [Q86X55-3 ]
XP_005259765.1. XM_005259708.2. [Q86X55-1 ]
UniGenei Hs.323213.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y1W X-ray 2.10 A/B/C/D 135-482 [» ]
2Y1X X-ray 2.40 A/B/C/D 135-482 [» ]
4IKP X-ray 2.00 A/B/C/D 140-480 [» ]
ProteinModelPortali Q86X55.
SMRi Q86X55. Positions 27-130, 143-476.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115760. 74 interactions.
IntActi Q86X55. 21 interactions.
MINTi MINT-3379851.
STRINGi 9606.ENSP00000325690.

Chemistry

BindingDBi Q86X55.
ChEMBLi CHEMBL5406.
GuidetoPHARMACOLOGYi 1255.

PTM databases

PhosphoSitei Q86X55.

Polymorphism databases

DMDMi 308153622.

Proteomic databases

MaxQBi Q86X55.
PaxDbi Q86X55.
PRIDEi Q86X55.

Protocols and materials databases

DNASUi 10498.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327064 ; ENSP00000325690 ; ENSG00000142453 . [Q86X55-3 ]
ENST00000344150 ; ENSP00000340934 ; ENSG00000142453 . [Q86X55-1 ]
GeneIDi 10498.
KEGGi hsa:10498.
UCSCi uc002mpz.3. human. [Q86X55-3 ]
uc002mqa.3. human. [Q86X55-1 ]

Organism-specific databases

CTDi 10498.
GeneCardsi GC19P010982.
H-InvDB HIX0014757.
HGNCi HGNC:23393. CARM1.
HPAi CAB032961.
MIMi 603934. gene.
neXtProti NX_Q86X55.
PharmGKBi PA134959553.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0500.
HOGENOMi HOG000198522.
HOVERGENi HBG050797.
KOi K05931.
OMAi HAKKYLR.
OrthoDBi EOG72NRPM.
PhylomeDBi Q86X55.
TreeFami TF323332.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118789. REV-ERBA represses gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

ChiTaRSi CARM1. human.
GenomeRNAii 10498.
NextBioi 39836.
PROi Q86X55.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q86X55.
Bgeei Q86X55.
CleanExi HS_CARM1.
Genevestigatori Q86X55.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025799. Arg_MeTrfase.
IPR020989. Histone-Arg_MeTrfase_N.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR11006. PTHR11006. 1 hit.
Pfami PF11531. CARM1. 1 hit.
PF05185. PRMT5. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 194-608 (ISOFORM 1).
    Tissue: Skin.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-608 (ISOFORM 2).
    Tissue: Amygdala.
  5. "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.
  6. "Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status."
    Hong H., Kao C., Jeng M.-H., Eble J.N., Koch M.O., Gardner T.A., Zhang S., Li L., Pan C.-X., Hu Z., MacLennan G.T., Cheng L.
    Cancer 101:83-89(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. "Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1."
    Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J.
    J. Biol. Chem. 279:54348-54357(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR1H4.
  8. "Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination."
    Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R.
    Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION OF EP300.
  9. "Coactivator-associated arginine methyltransferase 1 enhances transcriptional activity of the human T-cell lymphotropic virus type 1 long terminal repeat through direct interaction with Tax."
    Jeong S.J., Lu H., Cho W.K., Park H.U., Pise-Masison C., Brady J.N.
    J. Virol. 80:10036-10044(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX-1.
  10. "Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17."
    Miao F., Li S., Chavez V., Lanting L., Natarajan R.
    Mol. Endocrinol. 20:1562-1573(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION OF HISTONE H3, INTERACTION WITH RELA, FUNCTION.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4."
    Lakowski T.M., Frankel A.
    Biochem. J. 421:253-261(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  13. "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: PHOSPHORYLATION AT SER-216, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 135-482 IN COMPLEX WITH SAM ANALOG AND INHIBITORS, SAM BINDING SITES.

Entry informationi

Entry nameiCARM1_HUMAN
AccessioniPrimary (citable) accession number: Q86X55
Secondary accession number(s): A6NN38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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