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Entry version 130 (16 Oct 2019)
Sequence version 1 (13 Sep 2005)
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Protein

Histone-arginine methyltransferase CARM1

Gene

Carm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.1 Publication
Isoform 3 specifically affects pre-mRNA splicing. This activity is independent from methyltransferase activity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei160S-adenosyl-L-methionine1
Binding sitei169S-adenosyl-L-methionine1
Binding sitei193S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei215S-adenosyl-L-methionine1
Binding sitei244S-adenosyl-L-methionine1
Binding sitei272S-adenosyl-L-methionine1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, Methyltransferase, Transferase
Biological processmRNA processing, mRNA splicing, Transcription, Transcription regulation
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.1.1.125 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-3214858 RMTs methylate histone arginines
R-RNO-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)
R-RNO-9018519 Estrogen-dependent gene expression

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone-arginine methyltransferase CARM1 (EC:2.1.1.319By similarity)
Alternative name(s):
Coactivator-associated arginine methyltransferase 1
Protein arginine N-methyltransferase 4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Carm1
Synonyms:Prmt4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Rat genome database

More...
RGDi
1305879 Carm1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002492501 – 651Histone-arginine methyltransferase CARM1Add BLAST651

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei217PhosphoserineBy similarity1
Modified residuei551Dimethylated arginineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Auto-methylated on Arg-551. 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-217 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity. Phosphorylation at Ser-217 is strongly increased during mitosis, and decreases rapidly to a very low, basal level after entry into the G1 phase of the cell cycle. Phosphorylation at Ser-217 may promote location in the cytosol (By similarity).By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q4AE70

PRoteomics IDEntifications database

More...
PRIDEi
Q4AE70

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
Q4AE70

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q4AE70

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform 1 is expressed at low levels in brain, liver and testis. Isoform 2 is highly expressed in brain, liver, skeletal muscle and testis. Isoform 3 is highly expressed in spleen, liver and kidney. Isoform 4 is expressed in spleen, liver and kidney.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Isoforms 2 and 3 are expressed in fetal brain.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000031129 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q4AE70 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (Probable).

Interacts with NR1H4.

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 RELA (By similarity).

Interacts with SNRPC.

By similarityCurated2 Publications

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q4AE70, 1 interactor

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1651
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q4AE70

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q4AE70

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini147 – 454SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST308

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni500 – 651Transactivation domainBy similarityAdd BLAST152

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00940000160377

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000198522

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q4AE70

KEGG Orthology (KO)

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KOi
K05931

Identification of Orthologs from Complete Genome Data

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OMAi
FHILQTG

Database of Orthologous Groups

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OrthoDBi
840669at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q4AE70

TreeFam database of animal gene trees

More...
TreeFami
TF323332

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025799 Arg_MeTrfase
IPR020989 Histone-Arg_MeTrfase_N
IPR011993 PH-like_dom_sf
IPR029063 SAM-dependent_MTases

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF11531 CARM1, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53335 SSF53335, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51678 SAM_MT_PRMT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Named isoforms=2.
Isoform 1 (identifier: Q4AE70-1) [UniParc]FASTAAdd to basket
Also known as: CARM1-v2

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAAAAATAVG PGAGSAGVAG PGGAGPCATV SVFPGARLLT IGDANGEIQR
60 70 80 90 100
HAEQQALRLE VRAGPDAAGI ALYSHEDVCV FKCSVSRETE CSRVGRQSFI
110 120 130 140 150
ITLGCNSVLI QFATPHDFCS FYNILKTCRG HTLERSVFSE RTEESSAVQY
160 170 180 190 200
FQFYGYLSQQ QNMMQDYVRT GTYQRAILQN HTDFKDKIVL DVGCGSGILS
210 220 230 240 250
FFAAQAGARK IYAVEASTMA QHAEVLVKSN NLTDRIVVIP GKVEEVSLPE
260 270 280 290 300
QVDIIISEPM GYMLFNERML ESYLHAKKYL KPSGNMFPTI GDVHLAPFTD
310 320 330 340 350
EQLYMEQFTK ANFWYQPSFH GVDLSALRGA AVDEYFRQPV VDTFDIRILM
360 370 380 390 400
AKSVKYTVNF LEAKEGDLHR IEIPFKFHML HSGLVHGLAF WFDVAFIGSI
410 420 430 440 450
MTVWLSTAPT EPLTHWYQVR CLFQSPLFAK AGDTLSGTCL LIANKRQSYD
460 470 480 490 500
ISIVAQVDQT GSKSSNLLDL KNPFFRYTGT TPSPPPGSHY TSPSENMWNT
510 520 530 540 550
GSTYNLSSGV AVAGMPTAYD LSSVIAGGSS VGHNNLIPLA NTGIVNHTHS
560 570 580 590 600
RMGSIMSTGI VQGNRVAGPW AGDLPPGLRT RSSYQWGPGR LRGHAGSSVP
610 620 630 640 650
MTCPTGSSGA QGGGGSSSAH YAVNNQFTMG GPAISMASPM SIPTNTMHYG

S
Length:651
Mass (Da):70,341
Last modified:September 13, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2C71ED2D8E1BE12F
GO
Isoform 2 (identifier: Q4AE70-2) [UniParc]FASTAAdd to basket
Also known as: CARM1-v1

The sequence of this isoform differs from the canonical sequence as follows:
     564-606: Missing.

Show »
Length:608
Mass (Da):65,854
Checksum:iC621F2AA9FBA2DA3
GO
Isoform 3 (identifier: Q4AE70-3) [UniParc]FASTAAdd to basket
Also known as: CARM1-v3

The sequence of this isoform differs from the canonical sequence as follows:
     540-643: ANTGIVNHTH...ISMASPMSIP → GECPLGSMACQGRTGICQWPAKPVLGSLPPLSLS
     644-651: Missing.

Show »
Length:573
Mass (Da):62,453
Checksum:i19E82DC42316B317
GO
Isoform 4 (identifier: Q4AE70-4) [UniParc]FASTAAdd to basket
Also known as: CARM1-v4

The sequence of this isoform differs from the canonical sequence as follows:
     540-605: Missing.

Show »
Length:585
Mass (Da):63,460
Checksum:iC419059E314B2D51
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_020382540 – 643ANTGI…PMSIP → GECPLGSMACQGRTGICQWP AKPVLGSLPPLSLS in isoform 3. 1 PublicationAdd BLAST104
Alternative sequenceiVSP_020383540 – 605Missing in isoform 4. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_020384564 – 606Missing in isoform 2. 1 PublicationAdd BLAST43
Alternative sequenceiVSP_020385644 – 651Missing in isoform 3. 1 Publication8

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB201114 mRNA Translation: BAE16333.1
AB201115 mRNA Translation: BAE16334.1
AB201116 mRNA Translation: BAE16335.1
AB201117 mRNA Translation: BAE16336.1

NCBI Reference Sequences

More...
RefSeqi
NP_001025212.1, NM_001030041.3 [Q4AE70-2]
NP_001029260.1, NM_001034088.2 [Q4AE70-4]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000041577; ENSRNOP00000049428; ENSRNOG00000031129 [Q4AE70-4]
ENSRNOT00000048245; ENSRNOP00000042739; ENSRNOG00000031129 [Q4AE70-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
363026

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:363026

UCSC genome browser

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UCSCi
RGD:1305879 rat [Q4AE70-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB201114 mRNA Translation: BAE16333.1
AB201115 mRNA Translation: BAE16334.1
AB201116 mRNA Translation: BAE16335.1
AB201117 mRNA Translation: BAE16336.1
RefSeqiNP_001025212.1, NM_001030041.3 [Q4AE70-2]
NP_001029260.1, NM_001034088.2 [Q4AE70-4]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OQBX-ray1.69A/B28-140[»]
3B3FX-ray2.20A/B/C/D140-480[»]
3B3GX-ray2.40A/B140-480[»]
3B3JX-ray2.55A28-507[»]
SMRiQ4AE70
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiQ4AE70, 1 interactor

PTM databases

CarbonylDBiQ4AE70
PhosphoSitePlusiQ4AE70

Proteomic databases

jPOSTiQ4AE70
PRIDEiQ4AE70

Genome annotation databases

EnsembliENSRNOT00000041577; ENSRNOP00000049428; ENSRNOG00000031129 [Q4AE70-4]
ENSRNOT00000048245; ENSRNOP00000042739; ENSRNOG00000031129 [Q4AE70-2]
GeneIDi363026
KEGGirno:363026
UCSCiRGD:1305879 rat [Q4AE70-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
10498
RGDi1305879 Carm1

Phylogenomic databases

GeneTreeiENSGT00940000160377
HOGENOMiHOG000198522
InParanoidiQ4AE70
KOiK05931
OMAiFHILQTG
OrthoDBi840669at2759
PhylomeDBiQ4AE70
TreeFamiTF323332

Enzyme and pathway databases

BRENDAi2.1.1.125 5301
ReactomeiR-RNO-3214858 RMTs methylate histone arginines
R-RNO-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)
R-RNO-9018519 Estrogen-dependent gene expression

Miscellaneous databases

EvolutionaryTraceiQ4AE70

Protein Ontology

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PROi
PR:Q4AE70

Gene expression databases

BgeeiENSRNOG00000031129 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
GenevisibleiQ4AE70 RN

Family and domain databases

Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR025799 Arg_MeTrfase
IPR020989 Histone-Arg_MeTrfase_N
IPR011993 PH-like_dom_sf
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF11531 CARM1, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51678 SAM_MT_PRMT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCARM1_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q4AE70
Secondary accession number(s): Q4AE68, Q4AE69, Q4AE71
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 13, 2005
Last modified: October 16, 2019
This is version 130 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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