U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    PRMT7 protein arginine methyltransferase 7 [ Homo sapiens (human) ]

    Gene ID: 54496, updated on 3-Nov-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    PRMT7provided by HGNC
    Official Full Name
    protein arginine methyltransferase 7provided by HGNC
    Primary source
    HGNC:HGNC:25557
    See related
    Ensembl:ENSG00000132600 MIM:610087; AllianceGenome:HGNC:25557
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    SBIDDS
    Summary
    This gene encodes a member of the protein arginine N-methyltransferase family of proteins. The encoded enzyme transfers single methyl groups to arginine residues to generate monomethylarginines on histone proteins as well as other protein substrates. This enzyme plays a role in a wide range of biological processes, including neuronal differentiation, male germ line imprinting, small nuclear ribonucleoprotein biogenesis, and regulation of the Wnt signaling pathway. Mutations in this gene underlie multiple related syndromes in human patients characterized by intellectual disability, short stature and other features. The encoded protein may promote breast cancer cell invasion and metastasis in human patients. [provided by RefSeq, May 2017]
    Expression
    Ubiquitous expression in small intestine (RPKM 5.3), testis (RPKM 5.1) and 25 other tissues See more
    Orthologs
    mouse all
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    See PRMT7 in Genome Data Viewer
    Location:
    16q22.1
    Exon count:
    22
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 16 NC_000016.10 (68311019..68360870)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 16 NC_060940.1 (74106797..74156712)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 16 NC_000016.9 (68344922..68392487)

    Chromosome 16 - NC_000016.10Genomic Context describing neighboring genes Neighboring gene solute carrier family 7 member 6 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11010 Neighboring gene Sharpr-MPRA regulatory region 6227 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11011 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11012 Neighboring gene RNA, U6 small nuclear 1262, pseudogene Neighboring gene Sharpr-MPRA regulatory region 7703 Neighboring gene solute carrier family 7 member 6 opposite strand Neighboring gene H3K27ac hESC enhancer GRCh37_chr16:68343854-68344818 Neighboring gene small nucleolar RNA U13 Neighboring gene RNA, U4 small nuclear 30, pseudogene Neighboring gene H3K27ac hESC enhancer GRCh37_chr16:68382607-68383107 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11013 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68396471-68397283 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68397284-68398095 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68400892-68401445 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68401446-68401998 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11014 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11015 Neighboring gene sphingomyelin phosphodiesterase 3 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68413436-68413938 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68413939-68414439 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68415806-68416642 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68416643-68417477 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68422765-68423592 Neighboring gene Sharpr-MPRA regulatory region 9240 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68431713-68432213 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr16:68432795-68433424 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr16:68433425-68434052 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr16:68442570-68443549 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr16:68444678-68445630 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr16:68445631-68446581 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 7646 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11016 Neighboring gene uncharacterized LOC124903705 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr16:68504627-68505126 Neighboring gene ribosomal protein L35a pseudogene 33

    Genomic regions, transcripts, and products

    Go to the top of the page Help

    Go to nucleotide: Graphics FASTA GenBank

    Expression

    Go to the top of the page Help
    • Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
    • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
    • BioProject: PRJEB4337
    • Publication: PMID 24309898
    • Analysis date: Wed Apr 4 07:08:55 2018

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Discovery of a Dual PRMT5-PRMT7 Inhibitor. Smil D, et al. ACS Med Chem Lett, 2015 Apr 9. PMID 25893041, Free PMC Article
    2. Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response. Szewczyk MM, et al. Nat Commun, 2020 May 14. PMID 32409666, Free PMC Article
    3. Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues. Zurita-Lopez CI, et al. J Biol Chem, 2012 Mar 9. PMID 22241471, Free PMC Article
    4. PRMT7 promotes the growth of renal cell carcinoma through modulating the β-catenin/C-MYC axis. Liu F, et al. Int J Biochem Cell Biol, 2020 Mar. PMID 31926310
    5. Prenatal and postnatal presentation of PRMT7 related syndrome: Expanding the phenotypic manifestations. Birnbaum R, et al. Am J Med Genet A, 2019 Jan. PMID 30513135

    See all (63) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites.
      Title: The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites.
    2. Short stature in PRMT7 Mutations: first evidence of response to growth hormone treatment.
      Title: Short stature in PRMT7 Mutations: first evidence of response to growth hormone treatment.
    3. Biallelic PRMT7 pathogenic variants are associated with a recognizable syndromic neurodevelopmental disorder with short stature, obesity, and craniofacial and digital abnormalities.
      Title: Biallelic PRMT7 pathogenic variants are associated with a recognizable syndromic neurodevelopmental disorder with short stature, obesity, and craniofacial and digital abnormalities.
    4. An enhancer variant at 16q22.1 predisposes to hepatocellular carcinoma via regulating PRMT7 expression.
      Title: An enhancer variant at 16q22.1 predisposes to hepatocellular carcinoma via regulating PRMT7 expression.
    5. The arginine methyltransferase PRMT7 promotes extravasation of monocytes resulting in tissue injury in COPD.
      Title: The arginine methyltransferase PRMT7 promotes extravasation of monocytes resulting in tissue injury in COPD.
    6. Arginine monomethylation by PRMT7 controls MAVS-mediated antiviral innate immunity.
      Title: Arginine monomethylation by PRMT7 controls MAVS-mediated antiviral innate immunity.
    7. The role of protein arginine methyltransferase 7 in human developmentally arrested embryos cultured in vitro.
      Title: The role of protein arginine methyltransferase 7 in human developmentally arrested embryos cultured in vitro.
    8. Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth.
      Title: Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth.
    9. PRMT7 promotes the growth of renal cell carcinoma through modulating the beta-catenin/C-MYC axis.
      Title: PRMT7 promotes the growth of renal cell carcinoma through modulating the β-catenin/C-MYC axis.
    10. Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response.
      Title: Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response.
    Submit: New GeneRIF Correction See all GeneRIFs (24)

    Phenotypes

    Go to the top of the page Help

    Review eQTL and phenotype association data in this region using PheGenI

    Associated conditions

    Description Tests
    Short stature-brachydactyly-obesity-global developmental delay syndrome
    MedGen: C4310689 OMIM: 617157 GeneReviews: Not available
    		Compare labs

    EBI GWAS Catalog

    Description
    Genome-wide association studies of serum magnesium, potassium, and sodium concentrations identify six Loci influencing serum magnesium levels.
    EBI GWAS Catalog

    Variation

    Go to the top of the page Help

    See variants in ClinVar

    See studies and variants in dbVar

    See Variation Viewer (GRCh37.p13)

    See Variation Viewer (GRCh38)

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Markers

    Homology

    Clone Names

    • FLJ10640, KIAA1933

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    enables S-adenosylmethionine-dependent methyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables histone H4 methyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables histone H4R3 methyltransferase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    enables histone binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables histone methyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein-arginine N-methyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein-arginine omega-N monomethyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein-arginine omega-N symmetric methyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein-arginine omega-N symmetric methyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ribonucleoprotein complex binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in chromatin remodeling IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in genomic imprinting ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in peptidyl-arginine methylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in peptidyl-arginine methylation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in regulation of DNA-templated transcription IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in regulation of protein binding IC
    Inferred by Curator
    more info
    		 PubMed 
    involved_in spliceosomal snRNP assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in fibrillar center IDA
    Inferred from Direct Assay
    more info
    		  
    located_in nucleoplasm IDA
    Inferred from Direct Assay
    more info
    		  
    located_in nucleoplasm TAS
    Traceable Author Statement
    more info
    		  
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    protein arginine N-methyltransferase 7
    Names
    [Myelin basic protein]-arginine N-methyltransferase PRMT7
    histone-arginine N-methyltransferase PRMT7
    NP_001171753.1
    NP_001276947.1
    NP_001338072.1
    NP_001338073.1
    NP_001364947.1
    NP_001364949.1
    NP_001364950.1
    NP_001364951.1
    NP_001364952.1
    NP_061896.1
    XP_011521414.1
    XP_011521415.1
    XP_011521417.1
    XP_011521418.1
    XP_011521423.1
    XP_016878781.1
    XP_016878785.1
    XP_016878786.1
    XP_016878787.1
    XP_016878788.1
    XP_016878789.1
    XP_016878790.1
    XP_016878793.1
    XP_047290173.1
    XP_047290174.1
    XP_047290175.1
    XP_047290176.1
    XP_047290177.1
    XP_047290178.1
    XP_047290179.1
    XP_047290180.1
    XP_047290181.1
    XP_047290182.1
    XP_047290183.1
    XP_047290184.1
    XP_047290185.1
    XP_047290186.1
    XP_047290187.1
    XP_047290188.1
    XP_047290189.1
    XP_047290190.1
    XP_047290191.1
    XP_047290192.1
    XP_047290193.1
    XP_047290194.1
    XP_047290195.1
    XP_054236454.1
    XP_054236455.1
    XP_054236456.1
    XP_054236457.1
    XP_054236458.1
    XP_054236459.1
    XP_054236460.1
    XP_054236461.1
    XP_054236462.1
    XP_054236463.1
    XP_054236464.1
    XP_054236465.1
    XP_054236466.1
    XP_054236467.1
    XP_054236468.1
    XP_054236469.1
    XP_054236470.1
    XP_054236471.1
    XP_054236472.1
    XP_054236473.1
    XP_054236474.1
    XP_054236475.1
    XP_054236476.1
    XP_054236477.1
    XP_054236478.1
    XP_054236479.1
    XP_054236480.1
    XP_054236481.1
    XP_054236482.1
    XP_054236483.1
    XP_054236484.1
    XP_054236485.1
    XP_054236486.1

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    Genomic

    1. NG_054896.2 RefSeqGene

      Range
      5002..52567
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001184824.4 → NP_001171753.1  protein arginine N-methyltransferase 7 isoform 2

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) differs in the 5' UTR, lacks an exon in the 5' coding region, and its 3' terminal exon extends past a splice site that is used in variant 4, which results in a novel 3' coding region and 3' UTR compared to variant 4. The encoded isoform (2) is shorter and has a distinct C-terminus compared to isoform 4.
      Source sequence(s)
      AC099521, AK304605, CB140365, DA648148
      Consensus CDS
      CCDS54033.1
      UniProtKB/TrEMBL
      A0A8I5QKZ3
      Related
      ENSP00000414716.3, ENST00000449359.7

    2. NM_001290018.2 → NP_001276947.1  protein arginine N-methyltransferase 7 isoform 1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (3) differs in the 5' UTR and its 3' terminal exon extends past a splice site that is used in variant 4, which results in a novel 3' coding region and 3' UTR compared to variant 4. The encoded isoform (1) is shorter and has a distinct C-terminus compared to isoform 4. Both variants 1 and 3 encode the same isoform (1).
      Source sequence(s)
      AC020978, AC099521, AK056647, AK304605, CB140365
      Consensus CDS
      CCDS10866.1
      UniProtKB/Swiss-Prot
      B3KPR0, B3KUG9, B4E379, Q96PV5, Q9H9L0, Q9NVM4
      UniProtKB/TrEMBL
      H3BRD3
      Related
      ENSP00000343103.5, ENST00000339507.9
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    3. NM_001351143.3 → NP_001338072.1  protein arginine N-methyltransferase 7 isoform 4

      Status: REVIEWED

      Description
      Transcript Variant: This variant (4) encodes the longest isoform (4).
      Source sequence(s)
      AC020978, AC099521
      Consensus CDS
      CCDS92187.1
      UniProtKB/TrEMBL
      A0A8I5KYD6, H3BRD3
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    4. NM_001351144.3 → NP_001338073.1  protein arginine N-methyltransferase 7 isoform 5

      Status: REVIEWED

      Description
      Transcript Variant: This variant (5) uses two alternate in-frame splice sites and its 3' terminal exon extends past a splice site that is used in variant 4, which results in a novel 3' coding region and 3' UTR compared to variant 4. The encoded isoform (5) is shorter and has a distinct C-terminus compared to isoform 4.
      Source sequence(s)
      AC020978, AC099521, CB140365
      Consensus CDS
      CCDS92184.1
      UniProtKB/TrEMBL
      A0A8I5KZ92, H3BRD3
      Related
      ENSP00000510669.1, ENST00000692632.1
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    5. NM_001378018.1 → NP_001364947.1  protein arginine N-methyltransferase 7 isoform 1

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521
      Consensus CDS
      CCDS10866.1
      UniProtKB/Swiss-Prot
      B3KPR0, B3KUG9, B4E379, Q96PV5, Q9H9L0, Q9NVM4
      UniProtKB/TrEMBL
      H3BRD3
      Related
      ENSP00000510748.1, ENST00000692760.1
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    6. NM_001378020.1 → NP_001364949.1  protein arginine N-methyltransferase 7 isoform 10

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521
      UniProtKB/TrEMBL
      A0A8I5QKZ3

    7. NM_001378021.1 → NP_001364950.1  protein arginine N-methyltransferase 7 isoform 11

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521
      UniProtKB/TrEMBL
      A0A8I5QKZ3
      Related
      ENSP00000510167.1, ENST00000691663.1

    8. NM_001378022.1 → NP_001364951.1  protein arginine N-methyltransferase 7 isoform 11

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521
      UniProtKB/TrEMBL
      A0A8I5QKZ3

    9. NM_001378023.1 → NP_001364952.1  protein arginine N-methyltransferase 7 isoform 11

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521
      UniProtKB/TrEMBL
      A0A8I5QKZ3

    10. NM_019023.5 → NP_061896.1  protein arginine N-methyltransferase 7 isoform 1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) includes a 3' terminal exon that extends past a splice site that is used in variant 4, which results in a novel 3' coding region and 3' UTR compared to variant 4. The encoded isoform (1) is shorter and has a distinct C-terminus compared to isoform 4. Both variants 1 and 3 encode the same isoform (1).
      Source sequence(s)
      AC020978, AC099521, AK001502, AK022739, DB150163
      Consensus CDS
      CCDS10866.1
      UniProtKB/Swiss-Prot
      B3KPR0, B3KUG9, B4E379, Q96PV5, Q9H9L0, Q9NVM4
      UniProtKB/TrEMBL
      H3BRD3
      Related
      ENSP00000409324.2, ENST00000441236.3
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    RNA

    1. NR_147056.3 RNA Sequence

      Status: REVIEWED

      Description
      Transcript Variant: This variant (6) lacks two exons and uses two alternate splice sites compared to variant 4. This variant is represented as non-coding because the use of the 5'-most expected translational start codon renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).
      Source sequence(s)
      AC020978, AC099521, CB140365

    2. NR_147057.3 RNA Sequence

      Status: REVIEWED

      Description
      Transcript Variant: This variant (7) contains an alternate exon, lacks an exon, and uses two alternate splice sites compared to variant 4. This variant is represented as non-coding because the use of the 5'-most expected translational start codon renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).
      Source sequence(s)
      AC020978, AC099521, CB140365

    3. NR_147058.3 RNA Sequence

      Status: REVIEWED

      Description
      Transcript Variant: This variant (8) lacks an exon and uses two alternate splice sites compared to variant 4. This variant is represented as non-coding because the use of the 5'-most expected translational start codon renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).
      Source sequence(s)
      AC020978, AC099521, CB140365
      Related
      ENST00000688969.1

    4. NR_165365.1 RNA Sequence

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521

    5. NR_165366.1 RNA Sequence

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521
      Related
      ENST00000688470.1

    6. NR_165367.1 RNA Sequence

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521

    7. NR_165368.1 RNA Sequence

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521

    8. NR_165369.1 RNA Sequence

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521

    9. NR_165370.1 RNA Sequence

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521

    10. NR_165371.1 RNA Sequence

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521

    11. NR_165372.1 RNA Sequence

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521
      Related
      ENST00000675132.1

    12. NR_165373.1 RNA Sequence

      Status: REVIEWED

      Source sequence(s)
      AC020978, AC099521

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000016.10 Reference GRCh38.p14 Primary Assembly

      Range
      68311019..68360870
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_047434220.1 → XP_047290176.1  protein arginine N-methyltransferase 7 isoform X5

      UniProtKB/TrEMBL
      A0A8I5KXS9

    2. XM_047434222.1 → XP_047290178.1  protein arginine N-methyltransferase 7 isoform X5

      UniProtKB/TrEMBL
      A0A8I5KXS9

    3. XM_017023297.3 → XP_016878786.1  protein arginine N-methyltransferase 7 isoform X5

      UniProtKB/TrEMBL
      A0A8I5KXS9, H3BRD3
      Related
      ENSP00000510630.1, ENST00000686904.1

    4. XM_017023296.3 → XP_016878785.1  protein arginine N-methyltransferase 7 isoform X4

      UniProtKB/TrEMBL
      H3BRD3
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    5. XM_047434221.1 → XP_047290177.1  protein arginine N-methyltransferase 7 isoform X5

      UniProtKB/TrEMBL
      A0A8I5KXS9

    6. XM_047434218.1 → XP_047290174.1  protein arginine N-methyltransferase 7 isoform X2

      UniProtKB/TrEMBL
      A0A8I5KYD6
      Related
      ENSP00000509677.1, ENST00000687654.1

    7. XM_047434217.1 → XP_047290173.1  protein arginine N-methyltransferase 7 isoform X1

    8. XM_017023292.3 → XP_016878781.1  protein arginine N-methyltransferase 7 isoform X2

      UniProtKB/TrEMBL
      A0A8I5KYD6, H3BRD3
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    9. XM_011523115.4 → XP_011521417.1  protein arginine N-methyltransferase 7 isoform X1

      UniProtKB/TrEMBL
      H3BRD3
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    10. XM_047434224.1 → XP_047290180.1  protein arginine N-methyltransferase 7 isoform X8

    11. XM_047434229.1 → XP_047290185.1  protein arginine N-methyltransferase 7 isoform X12

    12. XM_047434226.1 → XP_047290182.1  protein arginine N-methyltransferase 7 isoform X9

    13. XM_011523113.4 → XP_011521415.1  protein arginine N-methyltransferase 7 isoform X1

      UniProtKB/TrEMBL
      H3BRD3
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    14. XM_017023299.3 → XP_016878788.1  protein arginine N-methyltransferase 7 isoform X8

      UniProtKB/TrEMBL
      A0A8I5KPT4
      Related
      ENSP00000510574.1, ENST00000691961.1

    15. XM_017023298.3 → XP_016878787.1  protein arginine N-methyltransferase 7 isoform X6

      UniProtKB/TrEMBL
      A0A8I5KPT4
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    16. XM_017023301.3 → XP_016878790.1  protein arginine N-methyltransferase 7 isoform X12

      UniProtKB/TrEMBL
      A0A8I5KPT4
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    17. XM_017023300.3 → XP_016878789.1  protein arginine N-methyltransferase 7 isoform X11

      UniProtKB/TrEMBL
      A0A8I5KPT4
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    18. XM_047434227.1 → XP_047290183.1  protein arginine N-methyltransferase 7 isoform X10

    19. XM_047434225.1 → XP_047290181.1  protein arginine N-methyltransferase 7 isoform X9

    20. XM_047434234.1 → XP_047290190.1  protein arginine N-methyltransferase 7 isoform X17

    21. XM_011523116.4 → XP_011521418.1  protein arginine N-methyltransferase 7 isoform X2

      UniProtKB/TrEMBL
      A0A8I5KYD6, H3BRD3
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    22. XM_047434219.1 → XP_047290175.1  protein arginine N-methyltransferase 7 isoform X3

      UniProtKB/TrEMBL
      A0A8I5KZ92

    23. XM_011523112.4 → XP_011521414.1  protein arginine N-methyltransferase 7 isoform X1

      UniProtKB/TrEMBL
      H3BRD3
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    24. XM_047434223.1 → XP_047290179.1  protein arginine N-methyltransferase 7 isoform X7

    25. XM_047434228.1 → XP_047290184.1  protein arginine N-methyltransferase 7 isoform X12

    26. XM_011523121.4 → XP_011521423.1  protein arginine N-methyltransferase 7 isoform X9

      UniProtKB/TrEMBL
      A0A8I5QKZ3

    27. XM_047434235.1 → XP_047290191.1  protein arginine N-methyltransferase 7 isoform X17

    28. XM_017023304.3 → XP_016878793.1  protein arginine N-methyltransferase 7 isoform X14

      UniProtKB/TrEMBL
      A0A6Q8PFP4
      Conserved Domains (1) summary
      cl17173
      Location:37 → 186
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    29. XM_047434231.1 → XP_047290187.1  protein arginine N-methyltransferase 7 isoform X15

      UniProtKB/TrEMBL
      H3BNC0, H3BTY1
      Related
      ENSP00000510428.1, ENST00000692966.1

    30. XM_047434232.1 → XP_047290188.1  protein arginine N-methyltransferase 7 isoform X15

      UniProtKB/TrEMBL
      H3BNC0, H3BTY1
      Related
      ENSP00000454776.1, ENST00000568975.5

    31. XM_047434238.1 → XP_047290194.1  protein arginine N-methyltransferase 7 isoform X20

    32. XM_047434236.1 → XP_047290192.1  protein arginine N-methyltransferase 7 isoform X18

    33. XM_047434237.1 → XP_047290193.1  protein arginine N-methyltransferase 7 isoform X19

      UniProtKB/TrEMBL
      A0A8I5KPP4
      Related
      ENSP00000509231.1, ENST00000692621.1

    34. XM_047434233.1 → XP_047290189.1  protein arginine N-methyltransferase 7 isoform X16

    35. XM_047434230.1 → XP_047290186.1  protein arginine N-methyltransferase 7 isoform X13

    36. XM_047434239.1 → XP_047290195.1  protein arginine N-methyltransferase 7 isoform X21

    RNA

    1. XR_007064885.1 RNA Sequence

    2. XR_001751915.3 RNA Sequence

    3. XR_007064887.1 RNA Sequence

    4. XR_002957814.2 RNA Sequence

    5. XR_007064888.1 RNA Sequence

    6. XR_007064886.1 RNA Sequence

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060940.1 Alternate T2T-CHM13v2.0

      Range
      74106797..74156712
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_054380487.1 → XP_054236462.1  protein arginine N-methyltransferase 7 isoform X5

      UniProtKB/TrEMBL
      A0A8I5KXS9

    2. XM_054380489.1 → XP_054236464.1  protein arginine N-methyltransferase 7 isoform X5

      UniProtKB/TrEMBL
      A0A8I5KXS9

    3. XM_054380486.1 → XP_054236461.1  protein arginine N-methyltransferase 7 isoform X5

      UniProtKB/TrEMBL
      A0A8I5KXS9

    4. XM_054380485.1 → XP_054236460.1  protein arginine N-methyltransferase 7 isoform X4

    5. XM_054380488.1 → XP_054236463.1  protein arginine N-methyltransferase 7 isoform X5

      UniProtKB/TrEMBL
      A0A8I5KXS9

    6. XM_054380492.1 → XP_054236467.1  protein arginine N-methyltransferase 7 isoform X8

    7. XM_054380496.1 → XP_054236471.1  protein arginine N-methyltransferase 7 isoform X12

    8. XM_054380499.1 → XP_054236474.1  protein arginine N-methyltransferase 7 isoform X23

    9. XM_054380480.1 → XP_054236455.1  protein arginine N-methyltransferase 7 isoform X2

      UniProtKB/TrEMBL
      A0A8I5KYD6

    10. XM_054380494.1 → XP_054236469.1  protein arginine N-methyltransferase 7 isoform X8

    11. XM_054380498.1 → XP_054236473.1  protein arginine N-methyltransferase 7 isoform X12

    12. XM_054380491.1 → XP_054236466.1  protein arginine N-methyltransferase 7 isoform X8

    13. XM_054380495.1 → XP_054236470.1  protein arginine N-methyltransferase 7 isoform X12

    14. XM_054380500.1 → XP_054236475.1  protein arginine N-methyltransferase 7 isoform X24

    15. XM_054380506.1 → XP_054236481.1  protein arginine N-methyltransferase 7 isoform X17

    16. XM_054380483.1 → XP_054236458.1  protein arginine N-methyltransferase 7 isoform X3

      UniProtKB/TrEMBL
      A0A8I5KZ92

    17. XM_054380479.1 → XP_054236454.1  protein arginine N-methyltransferase 7 isoform X1

    18. XM_054380490.1 → XP_054236465.1  protein arginine N-methyltransferase 7 isoform X7

    19. XM_054380497.1 → XP_054236472.1  protein arginine N-methyltransferase 7 isoform X12

    20. XM_054380507.1 → XP_054236482.1  protein arginine N-methyltransferase 7 isoform X17

    21. XM_054380503.1 → XP_054236478.1  protein arginine N-methyltransferase 7 isoform X15

    22. XM_054380504.1 → XP_054236479.1  protein arginine N-methyltransferase 7 isoform X15

    23. XM_054380505.1 → XP_054236480.1  protein arginine N-methyltransferase 7 isoform X15

    24. XM_054380502.1 → XP_054236477.1  protein arginine N-methyltransferase 7 isoform X26

    25. XM_054380511.1 → XP_054236486.1  protein arginine N-methyltransferase 7 isoform X20

    26. XM_054380508.1 → XP_054236483.1  protein arginine N-methyltransferase 7 isoform X18

    27. XM_054380509.1 → XP_054236484.1  protein arginine N-methyltransferase 7 isoform X19

      UniProtKB/TrEMBL
      A0A8I5KPP4

    28. XM_054380510.1 → XP_054236485.1  protein arginine N-methyltransferase 7 isoform X19

      UniProtKB/TrEMBL
      A0A8I5KPP4

    29. XM_054380481.1 → XP_054236456.1  protein arginine N-methyltransferase 7 isoform X2

      UniProtKB/TrEMBL
      A0A8I5KYD6

    30. XM_054380482.1 → XP_054236457.1  protein arginine N-methyltransferase 7 isoform X3

      UniProtKB/TrEMBL
      A0A8I5KZ92

    31. XM_054380493.1 → XP_054236468.1  protein arginine N-methyltransferase 7 isoform X8

    32. XM_054380501.1 → XP_054236476.1  protein arginine N-methyltransferase 7 isoform X25

      UniProtKB/TrEMBL
      A0A8I5KZ05

    33. XM_054380484.1 → XP_054236459.1  protein arginine N-methyltransferase 7 isoform X22

      UniProtKB/Swiss-Prot
      B3KPR0, B3KUG9, B4E379, Q96PV5, Q9H9L0, Q9NVM4

    RNA

    1. XR_008489096.1 RNA Sequence

    2. XR_008489095.1 RNA Sequence

    3. XR_008489098.1 RNA Sequence

    4. XR_008489094.1 RNA Sequence

    5. XR_008489099.1 RNA Sequence

    6. XR_008489097.1 RNA Sequence

    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q9NVM4.1 GenPept UniProtKB/Swiss-Prot:Q9NVM4

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Chemical Information
    Molecular Biology Databases
    Research Materials
    Tools
    Miscellaneous