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Q86X55

- CARM1_HUMAN

UniProt

Q86X55 - CARM1_HUMAN

Protein

Histone-arginine methyltransferase CARM1

Gene

CARM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    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-arginine N-methyltransferase activity Source: RefGenome
    3. histone methyltransferase activity Source: UniProtKB
    4. histone methyltransferase activity (H3-R17 specific) Source: UniProtKB
    5. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    6. lysine-acetylated histone binding Source: UniProtKB
    7. protein-arginine N-methyltransferase activity Source: UniProtKB
    8. protein-arginine omega-N asymmetric methyltransferase activity Source: UniProtKB
    9. protein binding Source: IntAct
    10. protein 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

    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.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134959553.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 608607Histone-arginine methyltransferase CARM1PRO_0000212338Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei216 – 2161Phosphoserine1 Publication
    Modified residuei550 – 5501Dimethylated arginineBy 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.By similarity
    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.By similarity1 Publication

    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 Probable. 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.By similarity4 PublicationsCurated

    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. 23 interactions.
    MINTiMINT-3379851.
    STRINGi9606.ENSP00000325690.

    Structurei

    Secondary structure

    1
    608
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini146 – 453308SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni499 – 608110Transactivation domainBy similarityAdd
    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

    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. 1 PublicationVSP_012506Add
    BLAST
    Alternative sequencei385 – 608224Missing in isoform 2. 1 PublicationVSP_012507Add
    BLAST
    Alternative sequencei539 – 56123Missing in isoform 1. 1 PublicationVSP_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. 23 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

    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: October 1, 2014
    This is version 113 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