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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.HMP:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei230S-adenosyl-L-methionineHMP:1
Binding sitei239S-adenosyl-L-methionine1
Binding sitei263S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei285S-adenosyl-L-methionine1
Binding sitei314S-adenosyl-L-methionine1
Active sitei329HMP:1
Active sitei338HMP:1

Regions

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMethyltransferase, Transferase
LigandMetal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3214858. RMTs methylate histone arginines.
R-HSA-8876725. Protein methylation.
SABIO-RKiO60678.

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

EuPathDBiHostDB:ENSG00000185238.12.
HGNCiHGNC:30163. PRMT3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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.
DrugBankiDB01752. S-Adenosyl-L-Homocysteine.
GuidetoPHARMACOLOGYi1254.

Polymorphism and mutation databases

BioMutaiPRMT3.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylcysteineND:1
Modified residuei25PhosphoserineND:1 Publication1
Modified residuei27PhosphoserineND:1 Publication1
Modified residuei171PhosphoserineND:1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei87Not phosphorylated1 Publication1

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.HMP:3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi115491. 46 interactors.
IntActiO60678. 16 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 – 225ND:3
Helixi227 – 234ND:8
Helixi237 – 249ND:13
Helixi251 – 253ND:3
Turni254 – 256ND:3
Beta strandi258 – 263ND:6
Helixi268 – 275ND:8
Beta strandi279 – 287ND:9
Helixi289 – 299ND:11
Turni303 – 305ND:3
Beta strandi306 – 311ND:6
Turni313 – 315ND:3
Beta strandi319 – 321ND:3
Beta strandi323 – 328ND:6
Turni336 – 338ND:3
Helixi340 – 351ND:12
Beta strandi352 – 360ND:9
Beta strandi362 – 370ND:9
Helixi373 – 379ND:7
Helixi381 – 384ND:4
Helixi392 – 394ND:3
Helixi395 – 398ND:4
Beta strandi403 – 405ND:3
Helixi409 – 411ND:3
Beta strandi417 – 423ND:7
Turni424 – 426ND:3
Helixi429 – 432ND:4
Beta strandi433 – 442ND:10
Beta strandi446 – 459ND:14
Beta strandi467 – 470ND:4
Beta strandi482 – 493ND:12
Beta strandi498 – 507ND:10
Beta strandi514 – 521ND:8
Beta strandi524 – 530ND:7

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-typeIEP:Add BLAST315

Domaini

The zinc-finger is responsible for substrate specificity.HMP:

Sequence similaritiesi

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

InterProiView protein in InterPro
IPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
IPR036236. Znf_C2H2_sf.
IPR013087. Znf_C2H2_type.
SUPFAMiSSF53335. SSF53335. 1 hit.
SSF57667. SSF57667. 1 hit.
PROSITEiView protein in PROSITE
PS51678. SAM_MT_PRMT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.

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).IKR:1
Sequence conflicti103V → F in BAG62289 (PubMed:14702039).IKR:1
Sequence conflicti510K → R in BAG62289 (PubMed:14702039).IKR:1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_024584440L → V. Corresponds to variant dbSNP:rs3758805Ensembl.1
Natural variantiVAR_030943470S → C. Corresponds to variant dbSNP:rs11025585Ensembl.1
Natural variantiVAR_024585508S → N3 PublicationsCorresponds to variant dbSNP:rs6483700Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04033011 – 99GRGAV…FIRLK → YSHLLKKHFHTVSLSISLIL TAWFINM in isoform 2. IBD:Add 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

Similar proteinsi

Entry informationi

Entry nameiANM3_HUMAN
AccessioniPrimary (citable) accession number: O60678
Secondary accession number(s): B4DUC7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2011
Last modified: October 25, 2017
This is version 160 of the entry and version 3 of the sequence. See 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