Q86X55 (CARM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CARM1
Synonyms:	PRMT4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	608 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
Catalytic activity	S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. Ref.11
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.12
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 protein arginine N-methyltransferase family.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular lipid metabolic process Traceable author statement. Source: Reactome endochondral bone morphogenesis Inferred from electronic annotation. Source: Compara histone H3-R2 methylation Inferred from mutant phenotype PubMed 17898714. Source: UniProtKB intracellular estrogen receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of protein binding Inferred from electronic annotation. Source: Compara pathogenesis Inferred from electronic annotation. Source: InterPro positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara 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: Compara regulation of intracellular estrogen receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB response to cAMP Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	beta-catenin binding Traceable author statement PubMed 16344550. Source: AgBase histone acetyl-lysine binding Inferred from sequence or structural similarity. Source: UniProtKB histone methyltransferase activity (H3-R17 specific) Inferred from sequence or structural similarity. Source: UniProtKB ligand-dependent nuclear receptor transcription coactivator 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 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 608

608

Histone-arginine methyltransferase CARM1

PRO_0000212338

Regions

Region

499 – 608

110

Transactivation domain By similarity

Sites

Binding site

159

1

S-adenosyl-L-methionine

Binding site

168

1

S-adenosyl-L-methionine

Binding site

192

1

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

214

1

S-adenosyl-L-methionine

Binding site

243

1

S-adenosyl-L-methionine

Binding site

271

1

S-adenosyl-L-methionine

Amino acid modifications

Modified residue

216

1

Phosphoserine Ref.12

Modified residue

550

1

Dimethylated arginine By similarity

Natural variations

Alternative sequence

369 – 384

16

RIEIP…HSGLV → SACLASPAATALCLPG in isoform 2.

VSP_012506

Alternative sequence

385 – 608

224

Missing in isoform 2.

VSP_012507

Alternative sequence

539 – 561

23

Missing in isoform 1.

VSP_039876

Secondary structure

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608

Helix Strand Turn

Details...

Helix

136 – 140

5

Helix

145 – 152

8

Helix

156 – 163

8

Helix

166 – 177

12

Helix

178 – 182

5

Turn

183 – 185

3

Beta strand

187 – 192

6

Helix

197 – 204

8

Beta strand

208 – 214

7

Helix

218 – 228

11

Turn

232 – 234

3

Beta strand

235 – 240

6

Turn

242 – 244

3

Beta strand

251 – 256

6

Turn

264 – 266

3

Helix

268 – 274

7

Helix

275 – 278

4

Beta strand

279 – 287

9

Beta strand

289 – 297

9

Helix

300 – 310

11

Helix

311 – 314

4

Helix

324 – 326

3

Helix

327 – 335

9

Beta strand

339 – 341

3

Helix

345 – 347

3

Beta strand

353 – 358

6

Turn

359 – 361

3

Helix

364 – 368

5

Beta strand

369 – 377

9

Beta strand

382 – 396

15

Beta strand

401 – 405

5

Beta strand

417 – 428

12

Beta strand

433 – 442

10

Beta strand

446 – 456

11

Turn

457 – 459

3

Beta strand

462 – 468

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: 094AC60D4A70B263	FASTA	608	65,854
	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
	Isoform 1 [UniParc]. Checksum: 15C6720FBEB864FE	FASTA	585	63,460
	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 GHNNLIPLGS 550 560 570 580 SGAQGSGGGS TSAHYAVNSQ FTMGGPAISM ASPMSIPTNT MHYGS
	Isoform 2 [UniParc]. Checksum: 722E8576DD6353D6	FASTA	384	41,885
	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 EAKEGDLHSA CLASPAATAL CLPG

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[12]	"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, MASS SPECTROMETRY.
[13]	"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].
[14]	"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.

IPI

IPI00412880.
IPI00514607.
IPI00639957.

RefSeq

NP_954592.1. NM_199141.1.

UniGene

Hs.323213.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q86X55.

SMR

Q86X55. Positions 27-130, 135-477.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q86X55. 8 interactions.

MINT

MINT-3379851.

STRING

9606.ENSP00000325690.

PTM databases

PhosphoSite

Q86X55.

Polymorphism databases

DMDM

308153622.

Proteomic databases

PaxDb

Q86X55.

PRIDE

Q86X55.

Protocols and materials databases

DNASU

10498.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327064; ENSP00000325690; ENSG00000142453.
ENST00000344150; ENSP00000340934; ENSG00000142453.

GeneID

10498.

KEGG

hsa:10498.

UCSC

uc002mpz.3. human.
uc002mqa.3. human.

Organism-specific databases

CTD

10498.

GeneCards

GC19P010982.

H-InvDB

HIX0014757.

HGNC

HGNC:23393. CARM1.

HPA

CAB032961.

MIM

603934. gene.

neXtProt

NX_Q86X55.

PharmGKB

PA134959553.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0500.

HOGENOM

HOG000198522.

HOVERGEN

HBG050797.

KO

K05931.

OMA

MPAAYDL.

OrthoDB

EOG4XKV6M.

PhylomeDB

Q86X55.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.
ar_tf_pathway. Regulation of Androgen receptor activity.

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

Q86X55.

CleanEx

HS_CARM1.

Genevestigator

Q86X55.

GermOnline

ENSG00000142453. Homo sapiens.

Family and domain databases

InterPro

IPR025799. Arg_MeTrfase.
IPR025797. Arg_MeTrfase_CARM1.
IPR020989. Histone-Arg_MeTrfase_N.
[Graphical view]

PANTHER

PTHR11006. PTHR11006. 1 hit.

Pfam

PF11531. CARM1. 1 hit.
PF05185. PRMT5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q86X55.

ChEMBL

CHEMBL5406.

ChiTaRS

CARM1. human.

GenomeRNAi

10498.

NextBio

39836.

SOURCE

Search...

Entry information

Entry name

CARM1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 99 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.