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Protein

Protein arginine N-methyltransferase 3

Gene

PRMT3

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

Functioni

Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.

Enzyme regulationi

Inhibited by N-ethylmaleimide and high concentrations of zinc chloride.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei230S-adenosyl-L-methionineBy similarity1
Binding sitei239S-adenosyl-L-methionine1
Binding sitei263S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei285S-adenosyl-L-methionine1
Binding sitei314S-adenosyl-L-methionine1
Active sitei329By similarity1
Active sitei338By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri48 – 71C2H2-typeAdd BLAST24

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

SABIO-RKO60678.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 3 (EC:2.1.1.-)
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3
Gene namesi
Name:PRMT3
Synonyms:HRMT1L3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:30163. PRMT3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: GO_Central
  • ribosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi87Y → C: Markedly reduced affinity for RPS2. 1 Publication1
Mutagenesisi87Y → E: Markedly reduced affinity for RPS2. 1 Publication1
Mutagenesisi87Y → F: No effect on interaction with RPS2. 1 Publication1

Organism-specific databases

DisGeNETi10196.
PharmGKBiPA29462.

Chemistry databases

ChEMBLiCHEMBL5891.
GuidetoPHARMACOLOGYi1254.

Polymorphism and mutation databases

BioMutaiPRMT3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002123262 – 531Protein arginine N-methyltransferase 3Add BLAST530

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylcysteineCombined sources1
Modified residuei25PhosphoserineCombined sources1 Publication1
Modified residuei27PhosphoserineCombined sources1 Publication1
Modified residuei171PhosphoserineCombined sources1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei87Not phosphorylated1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO60678.
MaxQBiO60678.
PaxDbiO60678.
PeptideAtlasiO60678.
PRIDEiO60678.

PTM databases

iPTMnetiO60678.
PhosphoSitePlusiO60678.

Expressioni

Gene expression databases

BgeeiENSG00000185238.
CleanExiHS_PRMT3.
ExpressionAtlasiO60678. baseline and differential.
GenevisibleiO60678. HS.

Organism-specific databases

HPAiCAB022083.
HPA007832.

Interactioni

Subunit structurei

Monomer or homodimer (By similarity). Interacts with EPB41L3; this inhibits methylation of target proteins. Interacts with the 40S ribosomal protein RPS2.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SCN5AQ145242EBI-2809009,EBI-726858

Protein-protein interaction databases

BioGridi115491. 43 interactors.
IntActiO60678. 11 interactors.
MINTiMINT-6803908.
STRINGi9606.ENSP00000331879.

Chemistry databases

BindingDBiO60678.

Structurei

Secondary structure

1531
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi223 – 225Combined sources3
Helixi227 – 234Combined sources8
Helixi237 – 249Combined sources13
Helixi251 – 253Combined sources3
Turni254 – 256Combined sources3
Beta strandi258 – 263Combined sources6
Helixi268 – 275Combined sources8
Beta strandi279 – 287Combined sources9
Helixi289 – 299Combined sources11
Turni303 – 305Combined sources3
Beta strandi306 – 311Combined sources6
Turni313 – 315Combined sources3
Beta strandi319 – 321Combined sources3
Beta strandi323 – 328Combined sources6
Turni336 – 338Combined sources3
Helixi340 – 351Combined sources12
Beta strandi352 – 360Combined sources9
Beta strandi362 – 370Combined sources9
Helixi373 – 379Combined sources7
Helixi381 – 384Combined sources4
Helixi392 – 394Combined sources3
Helixi395 – 398Combined sources4
Beta strandi403 – 405Combined sources3
Helixi409 – 411Combined sources3
Beta strandi417 – 423Combined sources7
Turni424 – 426Combined sources3
Helixi429 – 432Combined sources4
Beta strandi433 – 442Combined sources10
Beta strandi446 – 459Combined sources14
Beta strandi467 – 470Combined sources4
Beta strandi482 – 493Combined sources12
Beta strandi498 – 507Combined sources10
Beta strandi514 – 521Combined sources8
Beta strandi524 – 530Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FYTX-ray2.00A211-531[»]
3SMQX-ray2.00A211-531[»]
4HSGX-ray2.30A211-531[»]
4QQNX-ray2.08A211-531[»]
4RYLX-ray2.10A211-531[»]
ProteinModelPortaliO60678.
SMRiO60678.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60678.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini217 – 531SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST315

Domaini

The zinc-finger is responsible for substrate specificity.By similarity

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
Contains 1 C2H2-type zinc finger.Curated
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri48 – 71C2H2-typeAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiO60678.
KOiK11436.
OrthoDBiEOG091G0ADC.
PhylomeDBiO60678.
TreeFamiTF323587.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
IPR007087. Znf_C2H2.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 2 hits.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60678-1) [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
MCSLASGATG GRGAVENEED LPELSDSGDE AAWEDEDDAD LPHGKQQTPC
60 70 80 90 100
LFCNRLFTSA EETFSHCKSE HQFNIDSMVH KHGLEFYGYI KLINFIRLKN
110 120 130 140 150
PTVEYMNSIY NPVPWEKEEY LKPVLEDDLL LQFDVEDLYE PVSVPFSYPN
160 170 180 190 200
GLSENTSVVE KLKHMEARAL SAEAALARAR EDLQKMKQFA QDFVMHTDVR
210 220 230 240 250
TCSSSTSVIA DLQEDEDGVY FSSYGHYGIH EEMLKDKIRT ESYRDFIYQN
260 270 280 290 300
PHIFKDKVVL DVGCGTGILS MFAAKAGAKK VLGVDQSEIL YQAMDIIRLN
310 320 330 340 350
KLEDTITLIK GKIEEVHLPV EKVDVIISEW MGYFLLFESM LDSVLYAKNK
360 370 380 390 400
YLAKGGSVYP DICTISLVAV SDVNKHADRI AFWDDVYGFK MSCMKKAVIP
410 420 430 440 450
EAVVEVLDPK TLISEPCGIK HIDCHTTSIS DLEFSSDFTL KITRTSMCTA
460 470 480 490 500
IAGYFDIYFE KNCHNRVVFS TGPQSTKTHW KQTVFLLEKP FSVKAGEALK
510 520 530
GKVTVHKSKK DPRSLTVTLT LNNSTQTYGL Q
Length:531
Mass (Da):59,876
Last modified:January 11, 2011 - v3
Checksum:iD02159E2BEDBE7B9
GO
Isoform 2 (identifier: O60678-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     11-99: GRGAVENEED...IKLINFIRLK → YSHLLKKHFHTVSLSISLILTAWFINM

Note: No experimental confirmation available.
Show »
Length:469
Mass (Da):52,875
Checksum:i4A67AC40A78A7B01
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21L → E in AAC39837 (PubMed:9642256).Curated1
Sequence conflicti103V → F in BAG62289 (PubMed:14702039).Curated1
Sequence conflicti510K → R in BAG62289 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_024584440L → V.Corresponds to variant rs3758805dbSNPEnsembl.1
Natural variantiVAR_030943470S → C.Corresponds to variant rs11025585dbSNPEnsembl.1
Natural variantiVAR_024585508S → N.3 PublicationsCorresponds to variant rs6483700dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04033011 – 99GRGAV…FIRLK → YSHLLKKHFHTVSLSISLIL TAWFINM in isoform 2. 1 PublicationAdd BLAST89

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK300591 mRNA. Translation: BAG62289.1.
AC025972 Genomic DNA. No translation available.
AC108005 Genomic DNA. No translation available.
BC037544 mRNA. Translation: AAH37544.1.
BC064831 mRNA. Translation: AAH64831.1.
AF059531 mRNA. Translation: AAC39837.1.
CCDSiCCDS44554.1. [O60678-2]
CCDS7853.1. [O60678-1]
RefSeqiNP_005779.1. NM_005788.3.
UniGeneiHs.152337.

Genome annotation databases

EnsembliENST00000331079; ENSP00000331879; ENSG00000185238.
GeneIDi10196.
KEGGihsa:10196.
UCSCiuc001mqb.4. human. [O60678-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK300591 mRNA. Translation: BAG62289.1.
AC025972 Genomic DNA. No translation available.
AC108005 Genomic DNA. No translation available.
BC037544 mRNA. Translation: AAH37544.1.
BC064831 mRNA. Translation: AAH64831.1.
AF059531 mRNA. Translation: AAC39837.1.
CCDSiCCDS44554.1. [O60678-2]
CCDS7853.1. [O60678-1]
RefSeqiNP_005779.1. NM_005788.3.
UniGeneiHs.152337.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FYTX-ray2.00A211-531[»]
3SMQX-ray2.00A211-531[»]
4HSGX-ray2.30A211-531[»]
4QQNX-ray2.08A211-531[»]
4RYLX-ray2.10A211-531[»]
ProteinModelPortaliO60678.
SMRiO60678.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115491. 43 interactors.
IntActiO60678. 11 interactors.
MINTiMINT-6803908.
STRINGi9606.ENSP00000331879.

Chemistry databases

BindingDBiO60678.
ChEMBLiCHEMBL5891.
GuidetoPHARMACOLOGYi1254.

PTM databases

iPTMnetiO60678.
PhosphoSitePlusiO60678.

Polymorphism and mutation databases

BioMutaiPRMT3.

Proteomic databases

EPDiO60678.
MaxQBiO60678.
PaxDbiO60678.
PeptideAtlasiO60678.
PRIDEiO60678.

Protocols and materials databases

DNASUi10196.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331079; ENSP00000331879; ENSG00000185238.
GeneIDi10196.
KEGGihsa:10196.
UCSCiuc001mqb.4. human. [O60678-1]

Organism-specific databases

CTDi10196.
DisGeNETi10196.
GeneCardsiPRMT3.
HGNCiHGNC:30163. PRMT3.
HPAiCAB022083.
HPA007832.
MIMi603190. gene.
neXtProtiNX_O60678.
PharmGKBiPA29462.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiO60678.
KOiK11436.
OrthoDBiEOG091G0ADC.
PhylomeDBiO60678.
TreeFamiTF323587.

Enzyme and pathway databases

SABIO-RKO60678.

Miscellaneous databases

ChiTaRSiPRMT3. human.
EvolutionaryTraceiO60678.
GeneWikiiPRMT3.
GenomeRNAii10196.
PROiO60678.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185238.
CleanExiHS_PRMT3.
ExpressionAtlasiO60678. baseline and differential.
GenevisibleiO60678. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
IPR007087. Znf_C2H2.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 2 hits.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANM3_HUMAN
AccessioniPrimary (citable) accession number: O60678
Secondary accession number(s): B4DUC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 151 of the entry and version 3 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.