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Q86X55 (CARM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CARM1
Synonyms:PRMT4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.12

Catalytic activity

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. Ref.12

Enzyme regulation

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.

Subunit structure

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. Ref.7 Ref.9 Ref.10

Subcellular location

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. Ref.6 Ref.13

Tissue specificity

Overexpressed in prostate adenocarcinomas and high-grade prostatic intraepithelial neoplasia. Ref.6

Post-translational modification

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. Ref.5 Ref.8 Ref.10

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.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.

Contains 1 SAM-dependent MTase PRMT-type domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

endochondral bone morphogenesis

Inferred from electronic annotation. Source: Ensembl

histone H3-R17 methylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3-R2 methylation

Inferred from mutant phenotype PubMed 17898714. Source: UniProtKB

histone methylation

Inferred from direct assay Ref.12. Source: UniProtKB

intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

pathogenesis

Inferred from electronic annotation. Source: InterPro

peptidyl-arginine methylation, to asymmetrical-dimethyl arginine

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of growth plate cartilage chondrocyte proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of intracellular estrogen receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

response to cAMP

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionbeta-catenin binding

Traceable author statement PubMed 16344550. Source: AgBase

histone methyltransferase activity

Inferred from direct assay Ref.12. Source: UniProtKB

histone methyltransferase activity (H3-R17 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

histone-arginine N-methyltransferase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

lysine-acetylated histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20111005PubMed 23455924PubMed 24434208. Source: IntAct

protein methyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein-arginine N-methyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein-arginine omega-N asymmetric methyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q86X55-3)

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.
Isoform 1 (identifier: Q86X55-1)

The sequence of this isoform differs from the canonical sequence as follows:
     539-561: Missing.
Isoform 2 (identifier: Q86X55-2)

The sequence of this isoform differs from the canonical sequence as follows:
     369-384: RIEIPFKFHMLHSGLV → SACLASPAATALCLPG
     385-608: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 608607Histone-arginine methyltransferase CARM1
PRO_0000212338

Regions

Domain146 – 453308SAM-dependent MTase PRMT-type
Region499 – 608110Transactivation domain By similarity

Sites

Binding site1591S-adenosyl-L-methionine
Binding site1681S-adenosyl-L-methionine
Binding site1921S-adenosyl-L-methionine; via carbonyl oxygen
Binding site2141S-adenosyl-L-methionine
Binding site2431S-adenosyl-L-methionine
Binding site2711S-adenosyl-L-methionine

Amino acid modifications

Modified residue21N-acetylalanine Ref.11 Ref.15
Modified residue2161Phosphoserine Ref.13
Modified residue5501Dimethylated arginine By similarity

Natural variations

Alternative sequence369 – 38416RIEIP…HSGLV → SACLASPAATALCLPG in isoform 2.
VSP_012506
Alternative sequence385 – 608224Missing in isoform 2.
VSP_012507
Alternative sequence539 – 56123Missing in isoform 1.
VSP_039876

Secondary structure

............................................................... 608
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: 094AC60D4A70B263

FASTA60865,854
        10         20         30         40         50         60 
MAAAAAAVGP GAGGAGSAVP GGAGPCATVS VFPGARLLTI GDANGEIQRH AEQQALRLEV 

        70         80         90        100        110        120 
RAGPDSAGIA LYSHEDVCVF KCSVSRETEC SRVGKQSFII TLGCNSVLIQ FATPNDFCSF 

       130        140        150        160        170        180 
YNILKTCRGH TLERSVFSER TEESSAVQYF QFYGYLSQQQ NMMQDYVRTG TYQRAILQNH 

       190        200        210        220        230        240 
TDFKDKIVLD VGCGSGILSF FAAQAGARKI YAVEASTMAQ HAEVLVKSNN LTDRIVVIPG 

       250        260        270        280        290        300 
KVEEVSLPEQ VDIIISEPMG YMLFNERMLE SYLHAKKYLK PSGNMFPTIG DVHLAPFTDE 

       310        320        330        340        350        360 
QLYMEQFTKA NFWYQPSFHG VDLSALRGAA VDEYFRQPVV DTFDIRILMA KSVKYTVNFL 

       370        380        390        400        410        420 
EAKEGDLHRI EIPFKFHMLH SGLVHGLAFW FDVAFIGSIM TVWLSTAPTE PLTHWYQVRC 

       430        440        450        460        470        480 
LFQSPLFAKA GDTLSGTCLL IANKRQSYDI SIVAQVDQTG SKSSNLLDLK NPFFRYTGTT 

       490        500        510        520        530        540 
PSPPPGSHYT SPSENMWNTG STYNLSSGMA VAGMPTAYDL SSVIASGSSV GHNNLIPLAN 

       550        560        570        580        590        600 
TGIVNHTHSR MGSIMSTGIV QGSSGAQGSG GGSTSAHYAV NSQFTMGGPA ISMASPMSIP 


TNTMHYGS 

« Hide

Isoform 1 [UniParc].

Checksum: 15C6720FBEB864FE
Show »

FASTA58563,460
Isoform 2 [UniParc].

Checksum: 722E8576DD6353D6
Show »

FASTA38441,885

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Structural basis for CARM1 inhibition by indole and pyrazole inhibitors."
Sack J.S., Thieffine S., Bandiera T., Fasolini M., Duke G.J., Jayaraman L., Kish K.F., Klei H.E., Purandare A.V., Rosettani P., Troiani S., Xie D., Bertrand J.A.
Biochem. J. 436:331-339(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 135-482 IN COMPLEX WITH SAM ANALOG AND INHIBITORS, SAM BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12250.1. [Q86X55-3]
RefSeqNP_954592.1. NM_199141.1. [Q86X55-3]
XP_005259765.1. XM_005259708.2. [Q86X55-1]
UniGeneHs.323213.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y1WX-ray2.10A/B/C/D135-482[»]
2Y1XX-ray2.40A/B/C/D135-482[»]
4IKPX-ray2.00A/B/C/D140-480[»]
ProteinModelPortalQ86X55.
SMRQ86X55. Positions 27-130, 143-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115760. 72 interactions.
IntActQ86X55. 21 interactions.
MINTMINT-3379851.
STRING9606.ENSP00000325690.

Chemistry

BindingDBQ86X55.
ChEMBLCHEMBL5406.

PTM databases

PhosphoSiteQ86X55.

Polymorphism databases

DMDM308153622.

Proteomic databases

MaxQBQ86X55.
PaxDbQ86X55.
PRIDEQ86X55.

Protocols and materials databases

DNASU10498.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327064; ENSP00000325690; ENSG00000142453. [Q86X55-3]
ENST00000344150; ENSP00000340934; ENSG00000142453. [Q86X55-1]
GeneID10498.
KEGGhsa:10498.
UCSCuc002mpz.3. human. [Q86X55-3]
uc002mqa.3. human. [Q86X55-1]

Organism-specific databases

CTD10498.
GeneCardsGC19P010982.
H-InvDBHIX0014757.
HGNCHGNC:23393. CARM1.
HPACAB032961.
MIM603934. gene.
neXtProtNX_Q86X55.
PharmGKBPA134959553.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0500.
HOGENOMHOG000198522.
HOVERGENHBG050797.
KOK05931.
OMAHAKKYLR.
OrthoDBEOG72NRPM.
PhylomeDBQ86X55.
TreeFamTF323332.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ86X55.
BgeeQ86X55.
CleanExHS_CARM1.
GenevestigatorQ86X55.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025799. Arg_MeTrfase.
IPR020989. Histone-Arg_MeTrfase_N.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR11006. PTHR11006. 1 hit.
PfamPF11531. CARM1. 1 hit.
PF05185. PRMT5. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCARM1. human.
GenomeRNAi10498.
NextBio39836.
PROQ86X55.
SOURCESearch...

Entry information

Entry nameCARM1_HUMAN
AccessionPrimary (citable) accession number: Q86X55
Secondary accession number(s): A6NN38
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM