PRMT2 protein arginine methyltransferase 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PRMT2provided by HGNC
Official Full Name: protein arginine methyltransferase 2provided by HGNC
Primary source: HGNC:HGNC:5186
See related: Ensembl:ENSG00000160310 MIM:601961; AllianceGenome:HGNC:5186
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: HRMT1L1
Summary: Enables several functions, including nuclear receptor binding activity; peroxisome proliferator activated receptor binding activity; and protein homodimerization activity. Involved in positive regulation of apoptotic process; regulation of DNA-templated transcription; and regulation of androgen receptor signaling pathway. Located in cytosol and nucleoplasm. [provided by Alliance of Genome Resources, Nov 2024]
Expression: Ubiquitous expression in ovary (RPKM 11.6), spleen (RPKM 8.9) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 21q22.3

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	21	NC_000021.9 (46635674..46665124)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	21	NC_060945.1 (45021936..45051495)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	21	NC_000021.8 (48055586..48085036)

Chromosome 21 - NC_000021.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

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

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Protein arginine methyltransferase 2 controls inflammatory signaling in acute myeloid leukemia.
Title: Protein arginine methyltransferase 2 controls inflammatory signaling in acute myeloid leukemia.
Human C15orf39 Inhibits Inflammatory Response via PRMT2 in Human Microglial HMC3 Cell Line.
Title: Human C15orf39 Inhibits Inflammatory Response via PRMT2 in Human Microglial HMC3 Cell Line.
Advances in Research on Protein Arginine Methyltransferase 2: Functions and Diseases.
Title: Advances in Research on Protein Arginine Methyltransferase 2: Functions and Diseases.
Protein arginine N-methyltransferase 2 plays a noncatalytic role in the histone methylation activity of PRMT1.
Title: Protein arginine N-methyltransferase 2 plays a noncatalytic role in the histone methylation activity of PRMT1.
PRMT2 promotes HIV-1 latency by preventing nucleolar exit and phase separation of Tat into the Super Elongation Complex.
Title: PRMT2 promotes HIV-1 latency by preventing nucleolar exit and phase separation of Tat into the Super Elongation Complex.
PRMT2 promotes RCC tumorigenesis and metastasis via enhancing WNT5A transcriptional expression.
Title: PRMT2 promotes RCC tumorigenesis and metastasis via enhancing WNT5A transcriptional expression.
Loss of PRMT2 in myeloid cells in normoglycemic mice phenocopies impaired regression of atherosclerosis in diabetic mice.
Title: Loss of PRMT2 in myeloid cells in normoglycemic mice phenocopies impaired regression of atherosclerosis in diabetic mice.
PRMT2 accelerates tumorigenesis of hepatocellular carcinoma by activating Bcl2 via histone H3R8 methylation.
Title: PRMT2 accelerates tumorigenesis of hepatocellular carcinoma by activating Bcl2 via histone H3R8 methylation.
PRMT2beta suppressed glycolytic pathway in MCF7 cells.
Title: PRMT2β suppresses autophagy and glycolysis pathway in human breast cancer MCF-7 cell lines.
PRMT2 acts as a transcriptional co-activator for oncogenic gene expression programs in glioblastoma pathogenesis.
Title: PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma.

Submit: New GeneRIF Correction See all GeneRIFs (24)

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Variation

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See Variation Viewer (GRCh37.p13)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH69334 (e-PCR)
- UniSTS:28165

SHGC-87734 (e-PCR)
- UniSTS:83207

G32442 (e-PCR)
- UniSTS:117028

RH92547 (e-PCR)
- UniSTS:90406

RH101971 (e-PCR)
- UniSTS:96306

A009D14 (e-PCR)
- UniSTS:20555

SHGC-34143 (e-PCR)
- UniSTS:20558

G32217 (e-PCR)
- UniSTS:116823

A005B33 (e-PCR)
- UniSTS:35449

SHGC-16482 (e-PCR)
- UniSTS:21670

A007B35 (e-PCR)
- UniSTS:60651

SHGC-87732 (e-PCR)
- UniSTS:41460

SHGC-33747 (e-PCR)
- UniSTS:67831

G19632 (e-PCR)
- UniSTS:43516

A001T33 (e-PCR)
- UniSTS:43517

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables histone H2AQ104 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3 methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables histone H3K37 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3K56 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3R17 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3R2 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3R26 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H3R8 methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables histone H4K12 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone H4R3 methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables histone methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables histone methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables nuclear androgen receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables nuclear estrogen receptor binding	IDA Inferred from Direct Assay more info	PubMed
enables nuclear estrogen receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables nuclear progesterone receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables nuclear retinoic acid receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables nuclear thyroid hormone receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables peroxisome proliferator activated receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	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 N-methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein-arginine omega-N asymmetric methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-containing complex binding	ISS Inferred from Sequence or Structural Similarity more info
enables transcription coactivator activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in chromatin remodeling	IBA Inferred from Biological aspect of Ancestor more info
involved_in developmental cell growth	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of DNA-templated transcription	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of G1/S transition of mitotic cell cycle	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of NF-kappaB transcription factor activity	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of DNA-templated transcription	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of apoptotic process	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein methylation	TAS Traceable Author Statement more info	PubMed
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of androgen receptor signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in signal transduction	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in nucleolus	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	IDA Inferred from Direct Assay more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: protein arginine N-methyltransferase 2

Names: HMT1 (hnRNP methyltransferase, S. cerevisiae)-like 1; HMT1 hnRNP methyltransferase-like 1; PRMT2 alpha; PRMT2 beta; PRMT2 gamma; histone-arginine N-methyltransferase PRMT2

NP_001229793.1

EC 2.1.1.319

NP_001229794.1

EC 2.1.1.319

NP_001229795.1

EC 2.1.1.319

NP_001273605.1

EC 2.1.1.319

NP_001273606.1

EC 2.1.1.319

NP_001273607.1

EC 2.1.1.319

NP_001526.2

EC 2.1.1.319

NP_996845.1

EC 2.1.1.319

XP_005261168.1

EC 2.1.1.319

XP_006724061.1

EC 2.1.1.319

XP_006724062.1

EC 2.1.1.319

XP_006724063.1

EC 2.1.1.319

XP_047296715.1

EC 2.1.1.319

XP_047296716.1

EC 2.1.1.319

XP_047296717.1

EC 2.1.1.319

XP_054180436.1

EC 2.1.1.319

XP_054180437.1

EC 2.1.1.319

XP_054180438.1

EC 2.1.1.319

XP_054180439.1

EC 2.1.1.319

XP_054180440.1

EC 2.1.1.319

XP_054180441.1

EC 2.1.1.319

XP_054180442.1

EC 2.1.1.319

NCBI Reference Sequences (RefSeq)

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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.

mRNA and Protein(s)

NM_001242864.3 → NP_001229793.1 protein arginine N-methyltransferase 2 isoform 2

See identical proteins and their annotated locations for NP_001229793.1

Status: VALIDATED

Description

Transcript Variant: This variant (3) differs in the 5' UTR and lacks 2 consecutive exons in the 3' coding region compared to variant 1. However, it maintains the reading frame and encodes a shorter isoform (2) lacking an internal protein segment compared to isoform 1.

Source sequence(s)

AK123650, BC100026, BQ267811, DA169949

Consensus CDS

CCDS56220.1

UniProtKB/Swiss-Prot

P55345

Related

ENSP00000397266.1, ENST00000440086.5

Conserved Domains (3) summary

cd02440
Location:141 → 221

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). ...

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:110 → 169

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). ...
NM_001242865.3 → NP_001229794.1 protein arginine N-methyltransferase 2 isoform 3

See identical proteins and their annotated locations for NP_001229794.1

Status: VALIDATED

Description

Transcript Variant: This variant (4) differs in the 5' UTR and has an alternate 3' terminal exon that causes a frame-shift compared to variant 1. The resulting shorter isoform (3) has a distinct C-terminus compared to isoform 1.

Source sequence(s)

AK123650, AP000339, DA169949, DA517312, DA708321, DB160043, U79286

Consensus CDS

CCDS56219.1

UniProtKB/Swiss-Prot

P55345

Related

ENSP00000335490.4, ENST00000334494.8

Conserved Domains (2) summary

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:138 → 210

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). ...
NM_001242866.3 → NP_001229795.1 protein arginine N-methyltransferase 2 isoform 4

See identical proteins and their annotated locations for NP_001229795.1

Status: VALIDATED

Description

Transcript Variant: This variant (5) differs in the 5' UTR and has an alternate 3' terminal exon compared to variant 1. The resulting isoform (4) has a shorter C-terminus compared to isoform 1.

Source sequence(s)

AY786414, BM976817, BY799824, CA427786, CB045875, DA169949

UniProtKB/TrEMBL

A0A0S2Z3W8

Conserved Domains (2) summary

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:112 → 242

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). ...
NM_001286676.2 → NP_001273605.1 protein arginine N-methyltransferase 2 isoform 5

See identical proteins and their annotated locations for NP_001273605.1

Status: VALIDATED

Description

Transcript Variant: This variant (6) differs in the 5' UTR and lacks 3 consecutive exons in the 3' coding region that causes a frame-shift compared to variant 1. The resulting shorter isoform (5) has a distinct C-terminus compared to isoform 1.

Source sequence(s)

AK123650, AY786414, BQ267811, DA169949, FJ436411

Consensus CDS

CCDS68231.1

UniProtKB/Swiss-Prot

P55345

Related

ENSP00000407463.2, ENST00000458387.6

Conserved Domains (2) summary

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:138 → 220

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). ...
NM_001286677.2 → NP_001273606.1 protein arginine N-methyltransferase 2 isoform 6

See identical proteins and their annotated locations for NP_001273606.1

Status: VALIDATED

Description

Transcript Variant: This variant (7) differs in the 5' UTR and lacks 3 consecutive exons in the 3' coding region that causes a frame-shift compared to variant 1. The resulting shorter isoform (6) has a distinct C-terminus compared to isoform 1.

Source sequence(s)

AK123650, AY786414, BQ267811, DA169949

Consensus CDS

CCDS68230.1

UniProtKB/TrEMBL

A0A0S2Z3W8

Related

ENSP00000411984.2, ENST00000451211.6

Conserved Domains (3) summary

cd02440
Location:141 → 241

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). ...

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:110 → 169

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). ...
NM_001286678.2 → NP_001273607.1 protein arginine N-methyltransferase 2 isoform 7

See identical proteins and their annotated locations for NP_001273607.1

Status: VALIDATED

Description

Transcript Variant: This variant (8) differs in the 5' UTR and lacks 4 consecutive exons in the 3' coding region compared to variant 1. However, it maintains the reading frame and encodes a shorter isoform (7) lacking an internal protein segment compared to isoform 1.

Source sequence(s)

AK123650, AY786414, BQ267811, DA169949

Consensus CDS

CCDS74806.1

UniProtKB/TrEMBL

A8MXR3

Related

ENSP00000291705.6, ENST00000291705.11

Conserved Domains (2) summary

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:112 → 223

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). ...
NM_001535.5 → NP_001526.2 protein arginine N-methyltransferase 2 isoform 1

See identical proteins and their annotated locations for NP_001526.2

Status: VALIDATED

Description

Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Variants 1 and 2 encode the same isoform (1).

Source sequence(s)

AK123650, BQ267811, DA169949, X99209

Consensus CDS

CCDS13737.1

UniProtKB/Swiss-Prot

B7U630, B7U631, B7U632, P55345, P78350, Q498Y5, Q5U7D4, Q6FHF0, Q99781, Q9BW15, Q9UMC2

UniProtKB/TrEMBL

A0A0S2Z3N3, Q53FX4

Related

ENSP00000380760.2, ENST00000397638.7

Conserved Domains (3) summary

cd02440
Location:141 → 241

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). ...

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:110 → 169

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). ...
NM_206962.4 → NP_996845.1 protein arginine N-methyltransferase 2 isoform 1

See identical proteins and their annotated locations for NP_996845.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) encodes the longest isoform (1). Variants 1 and 2 encode the same isoform.

Source sequence(s)

AK123650, BC000727, BQ267811, DA169949

Consensus CDS

CCDS13737.1

UniProtKB/Swiss-Prot

B7U630, B7U631, B7U632, P55345, P78350, Q498Y5, Q5U7D4, Q6FHF0, Q99781, Q9BW15, Q9UMC2

UniProtKB/TrEMBL

A0A0S2Z3N3, Q53FX4

Related

ENSP00000347906.3, ENST00000355680.8

Conserved Domains (3) summary

cd02440
Location:141 → 241

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). ...

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:110 → 169

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). ...

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

NC_000021.9 Reference GRCh38.p14 Primary Assembly

Range

46635674..46665124

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006723998.5 → XP_006724061.1 protein arginine N-methyltransferase 2 isoform X2

See identical proteins and their annotated locations for XP_006724061.1

UniProtKB/Swiss-Prot

P55345

Conserved Domains (2) summary

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:138 → 220

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). ...
XM_006724000.4 → XP_006724063.1 protein arginine N-methyltransferase 2 isoform X4

See identical proteins and their annotated locations for XP_006724063.1

UniProtKB/TrEMBL

A8MXR3

Conserved Domains (2) summary

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:112 → 223

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). ...
XM_005261111.5 → XP_005261168.1 protein arginine N-methyltransferase 2 isoform X1

See identical proteins and their annotated locations for XP_005261168.1

UniProtKB/Swiss-Prot

B7U630, B7U631, B7U632, P55345, P78350, Q498Y5, Q5U7D4, Q6FHF0, Q99781, Q9BW15, Q9UMC2

UniProtKB/TrEMBL

A0A0S2Z3N3, Q53FX4

Conserved Domains (3) summary

cd02440
Location:141 → 241

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). ...

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:110 → 169

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). ...
XM_047440759.1 → XP_047296715.1 protein arginine N-methyltransferase 2 isoform X2
XM_006723999.4 → XP_006724062.1 protein arginine N-methyltransferase 2 isoform X3

Conserved Domains (3) summary

cd02440
Location:141 → 222

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). ...

cd11806
Location:34 → 86

SH3_PRMT2; Src homology 3 domain of Protein arginine N-methyltransferase 2

cl17173
Location:110 → 169

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). ...
XM_047440761.1 → XP_047296717.1 protein arginine N-methyltransferase 2 isoform X3
XM_047440760.1 → XP_047296716.1 protein arginine N-methyltransferase 2 isoform X3

Alternate T2T-CHM13v2.0

Genomic

NC_060945.1 Alternate T2T-CHM13v2.0

Range

45021936..45051495

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054324462.1 → XP_054180437.1 protein arginine N-methyltransferase 2 isoform X2
XM_054324467.1 → XP_054180442.1 protein arginine N-methyltransferase 2 isoform X4
XM_054324461.1 → XP_054180436.1 protein arginine N-methyltransferase 2 isoform X1

UniProtKB/Swiss-Prot

B7U630, B7U631, B7U632, P55345, P78350, Q498Y5, Q5U7D4, Q6FHF0, Q99781, Q9BW15, Q9UMC2

UniProtKB/TrEMBL

A0A0S2Z3N3
XM_054324463.1 → XP_054180438.1 protein arginine N-methyltransferase 2 isoform X2
XM_054324464.1 → XP_054180439.1 protein arginine N-methyltransferase 2 isoform X3
XM_054324466.1 → XP_054180441.1 protein arginine N-methyltransferase 2 isoform X3
XM_054324465.1 → XP_054180440.1 protein arginine N-methyltransferase 2 isoform X3