Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 151 (13 Feb 2019)
Sequence version 1 (01 Nov 1997)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Protein arginine N-methyltransferase 1

Gene

Prmt1

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

Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4 and SERBP1 (PubMed:12737817, PubMed:15837430, PubMed:18492485). Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation (By similarity). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway (By similarity). Methylates RBM15, promoting ubiquitination and degradation of RBM15 (By similarity). Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (By similarity).By similarity3 Publications

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei45S-adenosyl-L-methionine1 Publication1
Binding sitei54S-adenosyl-L-methionine1 Publication1
Binding sitei78S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
Binding sitei100S-adenosyl-L-methionine1 Publication1
Binding sitei129S-adenosyl-L-methionine1 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1441 Publication1
Active sitei1531 Publication1

<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 functionMethyltransferase, Transferase
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-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
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:
Protein arginine N-methyltransferase 1 (EC:2.1.1.319By similarity)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT1
<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:Prmt1
Synonyms:Hrmt1l2
<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 1

Organism-specific databases

Rat genome database

More...
RGDi
62020 Prmt1

<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi144E → D: Reduces catalytic activity 10-fold, and causes higher order oligomers of the protein. 1 Publication1
Mutagenesisi144E → Q: Reduces catalytic activity 3000-fold, and causes higher order oligomers of the protein. 1 Publication1
Mutagenesisi153E → D: Reduces catalytic activity to 0.03%, but does not affect oligomerization. 1 Publication1
Mutagenesisi153E → Q: Completely abolishes catalytic activity, but does not affect oligomerization. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1275220

<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_00002123231 – 353Protein arginine N-methyltransferase 1Add BLAST353

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 residuei116N6-succinyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki127Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei210N6-acetyllysineBy similarity1
Modified residuei215N6-acetyllysineBy similarity1
Modified residuei286PhosphoserineBy similarity1
Modified residuei289PhosphoserineBy 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

Polyubiquitinated at Lys-127 by the SCF(FBXL17) complex, leading to its subsequent degradation. Ubiquitination is regulated by acetylation at Lys-210 and Lys-215.By similarity
Acetylation at Lys-210 and Lys-215 regulates ubiquitination by the SCF(FBXL17) complex. Acetylated at Lys-215 by p300/EP300. Deacetylated at Lys-210 and Lys-215 by SIRT1.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q63009

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q63009

PRoteomics IDEntifications database

More...
PRIDEi
Q63009

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q63009

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

More...
PhosphoSitePlusi
Q63009

<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

Ubiquitous.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000026109 Expressed in 9 organ(s), highest expression level in heart

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q63009 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 and heterodimer with PRMT8. Homooctamer; individual homodimers associates to form a homooctamer. Interacts with NFATC2IP. Interacts with ILF3 and SUPT5H. Individual homodimers can associate to form a homohexamer. Interacts with FOXO1; the interaction methylates FOXO1, retaining it in the nucleus and increasing its transcriptional activity. Methylation of FOXO1 is increased with oxidative stress. Interacts with CHTOP; the interaction methylates CHTOP, enabling its interaction with the 5FMC complex (By similarity). Interacts with BTG1, BTG2 and IFNAR1. Interacts with and probably methylates ATXN2L (By similarity). Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH (By similarity). Interacts with DHX9 (via RGG region) (By similarity). Interacts (via N-terminus) with HABP4 (By similarity).By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
248825, 1 interactor

Protein interaction database and analysis system

More...
IntActi
Q63009, 6 interactors

Molecular INTeraction database

More...
MINTi
Q63009

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000063624

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q63009

<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

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OR8X-ray2.35A14-353[»]
1ORHX-ray2.64A1-353[»]
1ORIX-ray2.50A11-353[»]
3Q7EX-ray2.20A14-353[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q63009

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

More...
SMRi
Q63009

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q63009

<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>Domaini32 – 353SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST322

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1499 Eukaryota
ENOG410XQYH LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154700

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000198521

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG001793

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q63009

KEGG Orthology (KO)

More...
KOi
K11434

Identification of Orthologs from Complete Genome Data

More...
OMAi
RCHKRIG

Database of Orthologous Groups

More...
OrthoDBi
840669at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025799 Arg_MeTrfase
IPR029063 SAM-dependent_MTases

Superfamily database of structural and functional annotation

More...
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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

Q63009-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK
60 70 80 90 100
DEVRTLTYRN SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE
110 120 130 140 150
CSSISDYAVK IVKANKLDHV VTIIKGKVEE VELPVEKVDI IISEWMGYCL
160 170 180 190 200
FYESMLNTVL HARDKWLAPD GLIFPDRATL YVTAIEDRQY KDYKIHWWEN
210 220 230 240 250
VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY TVKVEDLTFT
260 270 280 290 300
SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY
310 320 330 340 350
MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY

RMR
Length:353
Mass (Da):40,522
Last modified:November 1, 1997 - 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:iEDBB0587784C527E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U60882 mRNA Translation: AAC52622.1
BC078815 mRNA Translation: AAH78815.1

NCBI Reference Sequences

More...
RefSeqi
NP_077339.1, NM_024363.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.5870

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000064272; ENSRNOP00000063624; ENSRNOG00000026109

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
60421

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:60421

UCSC genome browser

More...
UCSCi
RGD:62020 rat

<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
U60882 mRNA Translation: AAC52622.1
BC078815 mRNA Translation: AAH78815.1
RefSeqiNP_077339.1, NM_024363.1
UniGeneiRn.5870

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OR8X-ray2.35A14-353[»]
1ORHX-ray2.64A1-353[»]
1ORIX-ray2.50A11-353[»]
3Q7EX-ray2.20A14-353[»]
ProteinModelPortaliQ63009
SMRiQ63009
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248825, 1 interactor
IntActiQ63009, 6 interactors
MINTiQ63009
STRINGi10116.ENSRNOP00000063624

Chemistry databases

BindingDBiQ63009
ChEMBLiCHEMBL1275220

PTM databases

iPTMnetiQ63009
PhosphoSitePlusiQ63009

Proteomic databases

jPOSTiQ63009
PaxDbiQ63009
PRIDEiQ63009

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000064272; ENSRNOP00000063624; ENSRNOG00000026109
GeneIDi60421
KEGGirno:60421
UCSCiRGD:62020 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3276
RGDi62020 Prmt1

Phylogenomic databases

eggNOGiKOG1499 Eukaryota
ENOG410XQYH LUCA
GeneTreeiENSGT00940000154700
HOGENOMiHOG000198521
HOVERGENiHBG001793
InParanoidiQ63009
KOiK11434
OMAiRCHKRIG
OrthoDBi840669at2759

Enzyme and pathway databases

BRENDAi2.1.1.125 5301
ReactomeiR-RNO-3214858 RMTs methylate histone arginines
R-RNO-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-RNO-9018519 Estrogen-dependent gene expression

Miscellaneous databases

EvolutionaryTraceiQ63009

Protein Ontology

More...
PROi
PR:Q63009

Gene expression databases

BgeeiENSRNOG00000026109 Expressed in 9 organ(s), highest expression level in heart
GenevisibleiQ63009 RN

Family and domain databases

InterProiView protein in InterPro
IPR025799 Arg_MeTrfase
IPR029063 SAM-dependent_MTases
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51678 SAM_MT_PRMT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 nameiANM1_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: Q63009
<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: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 13, 2019
This is version 151 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again