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Protein

Protein arginine N-methyltransferase 2

Gene

PRMT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-dependent manner). May be involved in growth regulation.4 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.1 Publication

Kineticsi

  1. KM=2.6 µM for AdoMet1 Publication
  2. KM=3.3 µM for H41 Publication
  1. Vmax=1.4 nmol/min/mg enzyme toward AdoMet1 Publication
  2. Vmax=1.5 nmol/min/mg enzyme toward H41 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121S-adenosyl-L-methionineBy similarity
Binding sitei121 – 1211S-adenosyl-L-methionineBy similarity
Binding sitei145 – 1451S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei168 – 1681S-adenosyl-L-methionineBy similarity
Binding sitei197 – 1971S-adenosyl-L-methionineBy similarity
Active sitei211 – 2111By similarity
Active sitei220 – 2201By similarity

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • estrogen receptor binding Source: UniProtKB
  • histone-arginine N-methyltransferase activity Source: UniProtKB
  • histone methyltransferase activity Source: UniProtKB
  • peroxisome proliferator activated receptor binding Source: UniProtKB
  • progesterone receptor binding Source: UniProtKB
  • protein-arginine N-methyltransferase activity Source: UniProtKB
  • protein-arginine omega-N asymmetric methyltransferase activity Source: GO_Central
  • protein homodimerization activity Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB
  • signal transducer activity Source: ProtInc
  • thyroid hormone receptor binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • developmental cell growth Source: UniProtKB
  • histone arginine methylation Source: GOC
  • histone methylation Source: UniProtKB
  • negative regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: GOC
  • peptidyl-arginine N-methylation Source: GOC
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein methylation Source: ProtInc
  • regulation of androgen receptor signaling pathway Source: UniProtKB
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.125. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 2 (EC:2.1.1.3191 Publication)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT2
Gene namesi
Name:PRMT2
Synonyms:HMT1, HRMT1L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:5186. PRMT2.

Subcellular locationi

Isoform 1 :
  • Cytoplasm
  • Nucleus

  • Note: Translocates from the cytoplasm to the nucleus, after hormone exposure. Excluded from nucleolus.
Isoform PRMT2Alpha :
  • Nucleus

  • Note: Excluded from nucleolus.
Isoform PRMT2Gamma :
  • Nucleus

  • Note: Excluded from nucleolus.
Isoform PRMT2L2 :
  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Predominantly cytoplasmic.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29460.

Polymorphism and mutation databases

DMDMi2499805.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433Protein arginine N-methyltransferase 2PRO_0000212324Add
BLAST

Proteomic databases

PaxDbiP55345.
PRIDEiP55345.

PTM databases

iPTMnetiP55345.
PhosphoSiteiP55345.
SwissPalmiP55345.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in androgen target organs such as heart, prostate, skeletal muscle, ovary and spinal cord.1 Publication

Gene expression databases

BgeeiP55345.
CleanExiHS_PRMT2.
ExpressionAtlasiP55345. baseline and differential.
GenevisibleiP55345. HS.

Organism-specific databases

HPAiHPA018976.
HPA029591.

Interactioni

Subunit structurei

Self-associates. Interacts with RB1 and E2F1 (By similarity). Interacts with NCOA6 coactivator. Interacts (via SH3 domain) with PRMT8. Interacts with AR. Interacts with NFKBIA. Interacts with ESR1, ESR2, PGR, PPARG, RARA, RXRA and THRB. Interacts with HNRNPUL1.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033729EBI-78458,EBI-78473
RB1P064003EBI-78458,EBI-491274
SF1Q156375EBI-78458,EBI-744603

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • estrogen receptor binding Source: UniProtKB
  • peroxisome proliferator activated receptor binding Source: UniProtKB
  • progesterone receptor binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB
  • thyroid hormone receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109511. 50 interactions.
IntActiP55345. 23 interactions.
MINTiMINT-1437993.
STRINGi9606.ENSP00000347906.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 396Combined sources
Beta strandi56 – 616Combined sources
Beta strandi64 – 718Combined sources
Beta strandi77 – 859Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X2PNMR-A33-87[»]
ProteinModelPortaliP55345.
SMRiP55345. Positions 29-420.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55345.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 8960SH3PROSITE-ProRule annotationAdd
BLAST
Domaini99 – 432334SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 277277Interaction with ESR1Add
BLAST
Regioni83 – 207125Interaction with RB1By similarityAdd
BLAST
Regioni133 – 275143Interaction with ESR1Add
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG105734.
InParanoidiP55345.
KOiK11435.
OMAiYEFNLSA.
OrthoDBiEOG7Q8CN7.
PhylomeDBiP55345.
TreeFamiTF332196.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF05185. PRMT5. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55345-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATSGDCPRS ESQGEEPAEC SEAGLLQEGV QPEEFVAIAD YAATDETQLS
60 70 80 90 100
FLRGEKILIL RQTTADWWWG ERAGCCGYIP ANHVGKHVDE YDPEDTWQDE
110 120 130 140 150
EYFGSYGTLK LHLEMLADQP RTTKYHSVIL QNKESLTDKV ILDVGCGTGI
160 170 180 190 200
ISLFCAHYAR PRAVYAVEAS EMAQHTGQLV LQNGFADIIT VYQQKVEDVV
210 220 230 240 250
LPEKVDVLVS EWMGTCLLFE FMIESILYAR DAWLKEDGVI WPTMAALHLV
260 270 280 290 300
PCSADKDYRS KVLFWDNAYE FNLSALKSLA VKEFFSKPKY NHILKPEDCL
310 320 330 340 350
SEPCTILQLD MRTVQISDLE TLRGELRFDI RKAGTLHGFT AWFSVHFQSL
360 370 380 390 400
QEGQPPQVLS TGPFHPTTHW KQTLFMMDDP VPVHTGDVVT GSVVLQRNPV
410 420 430
WRRHMSVALS WAVTSRQDPT SQKVGEKVFP IWR
Length:433
Mass (Da):49,042
Last modified:November 1, 1997 - v1
Checksum:i6DEE0350C15ECD4F
GO
Isoform 2 (identifier: P55345-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-433: FEFMIESILY...VGEKVFPIWR → AAPLLSCRIL...LHLSWPIFLL

Note: No experimental confirmation available.
Show »
Length:284
Mass (Da):31,162
Checksum:i83703F72DDFA885B
GO
Isoform 3 (identifier: P55345-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-320: Missing.

Note: No experimental confirmation available.
Show »
Length:331
Mass (Da):37,167
Checksum:iB3FDADFE7F9133E9
GO
Isoform PRMT2Alpha (identifier: P55345-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-289: SLAVKEFFSKPK → LEKKSSPSGDDS
     290-433: Missing.

Note: Higher expression in breast cancer tissues.
Show »
Length:289
Mass (Da):32,424
Checksum:i49DEAA4267BF98ED
GO
Isoform PRMT2Beta (identifier: P55345-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-301: FEFMIESILY...HILKPEDCLS → HHTLEADAVH...FGKQCAYLEG
     302-433: Missing.

Note: Higher expression in breast cancer tissues. Doesn't interact with ESR1.
Show »
Length:301
Mass (Da):33,543
Checksum:iFBEC6C51A1CE8B64
GO
Isoform PRMT2Gamma (identifier: P55345-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-423: Missing.

Note: Higher expression in breast cancer tissues.
Show »
Length:228
Mass (Da):25,494
Checksum:iC02A5A20FB63338C
GO
Isoform PRMT2L2 (identifier: P55345-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-433: Missing.

Show »
Length:277
Mass (Da):31,193
Checksum:i970E9AD5A09EB8CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2605KDYRS → RIIVA in AAB48437 (PubMed:9196002).Curated
Sequence conflicti402 – 4021R → I in AAH00727 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei219 – 433215FEFMI…FPIWR → AAPLLSCRILPCTCASGPLH VLLACCLPLPCTCASVPLHV LLACCLPVLRAPQPSGLHLS WPIFLL in isoform 2. 1 PublicationVSP_042680Add
BLAST
Alternative sequencei219 – 423205Missing in isoform PRMT2Gamma. 1 PublicationVSP_054927Add
BLAST
Alternative sequencei219 – 320102Missing in isoform 3. 1 PublicationVSP_043381Add
BLAST
Alternative sequencei219 – 30183FEFMI…EDCLS → HHTLEADAVHDGRPSPCPYR RRGHGFSCVAEKPSVEKAHV CGSELGCHFQTRPHISKSWR KSLPHLEMTVDALFGKQCAY LEG in isoform PRMT2Beta. 1 PublicationVSP_054928Add
BLAST
Alternative sequencei278 – 433156Missing in isoform PRMT2L2. 1 PublicationVSP_054929Add
BLAST
Alternative sequencei278 – 28912SLAVK…FSKPK → LEKKSSPSGDDS in isoform PRMT2Alpha. 1 PublicationVSP_054930Add
BLAST
Alternative sequencei290 – 433144Missing in isoform PRMT2Alpha. 1 PublicationVSP_054931Add
BLAST
Alternative sequencei302 – 433132Missing in isoform PRMT2Beta. 1 PublicationVSP_054932Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99209 mRNA. Translation: CAA67599.1.
U80213 mRNA. Translation: AAB48437.1.
AY786414 mRNA. Translation: AAV48568.2.
FJ436410 mRNA. Translation: ACJ66866.1.
FJ436411 mRNA. Translation: ACJ66867.1.
FJ436412 mRNA. Translation: ACJ66868.1.
U79286 mRNA. Translation: AAB50221.1.
CR541804 mRNA. Translation: CAG46603.1.
AK123650 mRNA. Translation: BAG53931.1.
AP000339 Genomic DNA. No translation available.
AP000340 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09259.1.
CH471079 Genomic DNA. Translation: EAX09265.1.
BC000727 mRNA. Translation: AAH00727.1.
BC100026 mRNA. Translation: AAI00027.1.
AL109794 mRNA. Translation: CAB52454.1.
CCDSiCCDS13737.1. [P55345-1]
CCDS56219.1. [P55345-2]
CCDS56220.1. [P55345-3]
CCDS68230.1. [P55345-4]
CCDS68231.1. [P55345-5]
CCDS74806.1. [P55345-6]
RefSeqiNP_001229793.1. NM_001242864.2. [P55345-3]
NP_001229794.1. NM_001242865.2. [P55345-2]
NP_001229795.1. NM_001242866.2. [P55345-7]
NP_001273605.1. NM_001286676.1. [P55345-5]
NP_001273606.1. NM_001286677.1. [P55345-4]
NP_001273607.1. NM_001286678.1. [P55345-6]
NP_001526.2. NM_001535.4. [P55345-1]
NP_996845.1. NM_206962.3. [P55345-1]
XP_005261168.1. XM_005261111.2. [P55345-1]
XP_006724061.1. XM_006723998.2. [P55345-5]
XP_006724063.1. XM_006724000.2. [P55345-6]
UniGeneiHs.154163.
Hs.661229.

Genome annotation databases

EnsembliENST00000291705; ENSP00000291705; ENSG00000160310. [P55345-6]
ENST00000334494; ENSP00000335490; ENSG00000160310. [P55345-2]
ENST00000355680; ENSP00000347906; ENSG00000160310. [P55345-1]
ENST00000397637; ENSP00000380759; ENSG00000160310. [P55345-1]
ENST00000397638; ENSP00000380760; ENSG00000160310. [P55345-1]
ENST00000440086; ENSP00000397266; ENSG00000160310. [P55345-3]
ENST00000451211; ENSP00000411984; ENSG00000160310. [P55345-4]
ENST00000458387; ENSP00000407463; ENSG00000160310. [P55345-5]
GeneIDi3275.
KEGGihsa:3275.
UCSCiuc002zjx.5. human. [P55345-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99209 mRNA. Translation: CAA67599.1.
U80213 mRNA. Translation: AAB48437.1.
AY786414 mRNA. Translation: AAV48568.2.
FJ436410 mRNA. Translation: ACJ66866.1.
FJ436411 mRNA. Translation: ACJ66867.1.
FJ436412 mRNA. Translation: ACJ66868.1.
U79286 mRNA. Translation: AAB50221.1.
CR541804 mRNA. Translation: CAG46603.1.
AK123650 mRNA. Translation: BAG53931.1.
AP000339 Genomic DNA. No translation available.
AP000340 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09259.1.
CH471079 Genomic DNA. Translation: EAX09265.1.
BC000727 mRNA. Translation: AAH00727.1.
BC100026 mRNA. Translation: AAI00027.1.
AL109794 mRNA. Translation: CAB52454.1.
CCDSiCCDS13737.1. [P55345-1]
CCDS56219.1. [P55345-2]
CCDS56220.1. [P55345-3]
CCDS68230.1. [P55345-4]
CCDS68231.1. [P55345-5]
CCDS74806.1. [P55345-6]
RefSeqiNP_001229793.1. NM_001242864.2. [P55345-3]
NP_001229794.1. NM_001242865.2. [P55345-2]
NP_001229795.1. NM_001242866.2. [P55345-7]
NP_001273605.1. NM_001286676.1. [P55345-5]
NP_001273606.1. NM_001286677.1. [P55345-4]
NP_001273607.1. NM_001286678.1. [P55345-6]
NP_001526.2. NM_001535.4. [P55345-1]
NP_996845.1. NM_206962.3. [P55345-1]
XP_005261168.1. XM_005261111.2. [P55345-1]
XP_006724061.1. XM_006723998.2. [P55345-5]
XP_006724063.1. XM_006724000.2. [P55345-6]
UniGeneiHs.154163.
Hs.661229.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X2PNMR-A33-87[»]
ProteinModelPortaliP55345.
SMRiP55345. Positions 29-420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109511. 50 interactions.
IntActiP55345. 23 interactions.
MINTiMINT-1437993.
STRINGi9606.ENSP00000347906.

PTM databases

iPTMnetiP55345.
PhosphoSiteiP55345.
SwissPalmiP55345.

Polymorphism and mutation databases

DMDMi2499805.

Proteomic databases

PaxDbiP55345.
PRIDEiP55345.

Protocols and materials databases

DNASUi3275.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291705; ENSP00000291705; ENSG00000160310. [P55345-6]
ENST00000334494; ENSP00000335490; ENSG00000160310. [P55345-2]
ENST00000355680; ENSP00000347906; ENSG00000160310. [P55345-1]
ENST00000397637; ENSP00000380759; ENSG00000160310. [P55345-1]
ENST00000397638; ENSP00000380760; ENSG00000160310. [P55345-1]
ENST00000440086; ENSP00000397266; ENSG00000160310. [P55345-3]
ENST00000451211; ENSP00000411984; ENSG00000160310. [P55345-4]
ENST00000458387; ENSP00000407463; ENSG00000160310. [P55345-5]
GeneIDi3275.
KEGGihsa:3275.
UCSCiuc002zjx.5. human. [P55345-1]

Organism-specific databases

CTDi3275.
GeneCardsiPRMT2.
HGNCiHGNC:5186. PRMT2.
HPAiHPA018976.
HPA029591.
MIMi601961. gene.
neXtProtiNX_P55345.
PharmGKBiPA29460.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG105734.
InParanoidiP55345.
KOiK11435.
OMAiYEFNLSA.
OrthoDBiEOG7Q8CN7.
PhylomeDBiP55345.
TreeFamiTF332196.

Enzyme and pathway databases

BRENDAi2.1.1.125. 2681.

Miscellaneous databases

ChiTaRSiPRMT2. human.
EvolutionaryTraceiP55345.
GeneWikiiPRMT2.
GenomeRNAii3275.
PROiP55345.
SOURCEiSearch...

Gene expression databases

BgeeiP55345.
CleanExiHS_PRMT2.
ExpressionAtlasiP55345. baseline and differential.
GenevisibleiP55345. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF05185. PRMT5. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)."
    Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A., Henry M.F.
    Genomics 48:330-340(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene."
    Katsanis N., Yaspo M.-L., Fisher E.M.C.
    Mamm. Genome 8:526-529(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Identification and expression analysis of a novel transcript of the human PRMT2 gene resulted from alternative polyadenylation in breast cancer."
    Zhong J., Cao R.X., Hong T., Yang J., Zu X.Y., Xiao X.H., Liu J.H., Wen G.B.
    Gene 487:1-9(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PRMT2L2), SUBCELLULAR LOCATION (ISOFORM PRMT2L2).
  4. "Identification and characterization of novel spliced variants of PRMT2 in breast carcinoma."
    Zhong J., Cao R.X., Zu X.Y., Hong T., Yang J., Liu L., Xiao X.H., Ding W.J., Zhao Q., Liu J.H., Wen G.B.
    FEBS J. 279:316-335(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PRMT2ALPHA; PRMT2BETA AND PRMT2GAMMA), SUBCELLULAR LOCATION, INTERACTION WITH AR AND ESR1.
  5. "Large-scale concatenation cDNA sequencing."
    Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
    Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  8. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Chondrosarcoma and Kidney.
  11. The European IMAGE consortium
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-277 (ISOFORM 1).
  12. "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1."
    Kzhyshkowska J., Schuett H., Liss M., Kremmer E., Stauber R., Wolf H., Dobner T.
    Biochem. J. 358:305-314(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRNPUL1, SUBCELLULAR LOCATION.
  13. "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
    Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.
    J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ESR1; ESR2; NCOA1; NCOA6; PGR; PPARG; RARA; RXRA AND THRB.
  14. "Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis."
    Ganesh L., Yoshimoto T., Moorthy N.C., Akahata W., Boehm M., Nabel E.G., Nabel G.J.
    Mol. Cell. Biol. 26:3864-3874(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NFKBIA.
  15. "Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain."
    Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G.
    J. Biol. Chem. 282:36444-36453(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRMT8.
  16. "PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor."
    Meyer R., Wolf S.S., Obendorf M.
    J. Steroid Biochem. Mol. Biol. 107:1-14(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AR AND ESR1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  17. "Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4."
    Lakowski T.M., Frankel A.
    Biochem. J. 421:253-261(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  18. "Solution structure of the SH3 domain of the protein arginine N-methyltransferase 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 33-87.

Entry informationi

Entry nameiANM2_HUMAN
AccessioniPrimary (citable) accession number: P55345
Secondary accession number(s): B7U630
, B7U631, B7U632, P78350, Q498Y5, Q5U7D4, Q6FHF0, Q99781, Q9BW15, Q9UMC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.