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Protein

Protein arginine N-methyltransferase 5

Gene

Prmt5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:15485929, PubMed:19584108, PubMed:19858291, PubMed:21917714, PubMed:23133559). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation (By similarity). Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription (PubMed:15485929). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed:19584108). Methylates RPS10 (By similarity). Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (PubMed:23133559). Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (By similarity). Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression (By similarity). Symmetrically methylates NCL (By similarity).By similarity5 Publications

Catalytic activityi

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

Enzyme regulationi

Activity is increased by EGF, HGF, FGF1 or FGF2 treatments, and slightly decreased by NGF treatment.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei304Peptide substrateBy similarity1
Binding sitei307Peptide substrateBy similarity1
Binding sitei324S-adenosyl-L-methionineBy similarity1
Sitei327Critical for specifying symmetric addition of methyl groupsBy similarity1
Binding sitei392S-adenosyl-L-methionineBy similarity1
Active sitei435Proton donor/acceptorBy similarity1
Active sitei444Proton donor/acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, Methyltransferase, Repressor, Transferase
Biological processBiological rhythms, Transcription, Transcription regulation
LigandS-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 5 (EC:2.1.1.320By similarity)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT5
Jak-binding protein 1
Shk1 kinase-binding protein 1 homolog
Short name:
SKB1 homolog
Gene namesi
Name:Prmt5
Synonyms:Jbp1, Skb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1351645 Prmt5

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, Golgi apparatus, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002123442 – 637Protein arginine N-methyltransferase 5Add BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8CIG8
MaxQBiQ8CIG8
PaxDbiQ8CIG8
PeptideAtlasiQ8CIG8
PRIDEiQ8CIG8

PTM databases

iPTMnetiQ8CIG8
PhosphoSitePlusiQ8CIG8
SwissPalmiQ8CIG8

Expressioni

Gene expression databases

CleanExiMM_PRMT5

Interactioni

Subunit structurei

Forms, at least, homodimers and homotetramers. Component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A (By similarity). Found in a complex composed of PRMT5, WDR77 and RIOK1 (By similarity). RIOK1 and CLNS1A associate with PRMT5 in a mutually exclusive fashion, which allows the recruitment of distinct methylation substrates, such as nucleolin/NCL and Sm proteins, respectively (By similarity). Interacts with PRDM1 (PubMed:16699504). Identified in a complex composed of methylosome and PRMT1 and ERH. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Also interacts with Sm proteins, JAK2 and SSTR1. Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with LSM11, PRMT7 and SNRPD3. Interacts with COPRS; promoting its recruitment on histone H4 (By similarity). Interacts with PRDM1. Interacts with RPS10. Interacts with EGFR; methylates EGFR and stimulates EGFR-mediated ERK activation (By similarity). Interacts with BRAF and with active RAF1 (By similarity). Interacts with HOXA9 (By similarity). Interacts with SRGAP2. Interacts with EPB41L3; this modulates methylation of target proteins (By similarity). Found in a complex with COPRS, RUNX1 and CBFB (PubMed:22193545). Interacts with CHTOP; the interaction symmetrically methylates CHTOP, but seems to require the presence of PRMT1 (PubMed:19858291, PubMed:22872859). Interacts with IWS1 (By similarity). Interacts with CRY1 (PubMed:23133559). Interacts with POLR2A (By similarity). Interacts with SMN1/SMN2 (By similarity). Interacts with LYAR; this interaction is direct (By similarity).By similarity5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi205181, 22 interactors
IntActiQ8CIG8, 15 interactors
STRINGi10090.ENSMUSP00000023873

Structurei

3D structure databases

ProteinModelPortaliQ8CIG8
SMRiQ8CIG8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini308 – 615SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST308

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 292TIM barrelBy similarityAdd BLAST280
Regioni333 – 334S-adenosyl-L-methionine bindingBy similarity2
Regioni419 – 420S-adenosyl-L-methionine bindingBy similarity2
Regioni465 – 637Beta barrelBy similarityAdd BLAST173
Regioni488 – 494DimerizationBy similarity7

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0822 Eukaryota
ENOG410XNZM LUCA
HOGENOMiHOG000175933
HOVERGENiHBG057083
InParanoidiQ8CIG8
KOiK02516
PhylomeDBiQ8CIG8
TreeFamiTF300626

Family and domain databases

InterProiView protein in InterPro
IPR025799 Arg_MeTrfase
IPR007857 Arg_MeTrfase_PRMT5
IPR035075 PRMT5
IPR035248 PRMT5_C
IPR035247 PRMT5_TIM
IPR029063 SAM-dependent_MTases
PANTHERiPTHR10738 PTHR10738, 1 hit
PfamiView protein in Pfam
PF05185 PRMT5, 1 hit
PF17286 PRMT5_C, 1 hit
PF17285 PRMT5_TIM, 1 hit
PIRSFiPIRSF015894 Skb1_MeTrfase, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51678 SAM_MT_PRMT, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q8CIG8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF
60 70 80 90 100
KREFIQEPAK NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI HPDSKVEKIR
110 120 130 140 150
RNSEAAMLQE LNFGAYLGLP AFLLPLNQED NTNLARVLTN HIHTGHHSSM
160 170 180 190 200
FWMRVPLVAP EDLRDDVIAN APTTHTEEYS GEEKTWMWWH NFRTLCDYSK
210 220 230 240 250
RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK KGFPVLSKVQ
260 270 280 290 300
QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF
310 320 330 340 350
AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP
360 370 380 390 400
EEEKETNVQV LMVLGAGRGP LVNASLRAAK QAERRIRLYA VEKNPNAVVT
410 420 430 440 450
LENWQFEEWG SQVTVVSSDM REWVAPEKAD IIVSELLGSF ADNELSPECL
460 470 480 490 500
DGAQHFLKDD GVSIPGEYTS FLAPISSSKL YNEVRACREK DRDPEAQFEM
510 520 530 540 550
PYVVRLHNFH QLSAPKPCFT FSHPNRDPMI DNNRYCTLEF PVEVNTVLHG
560 570 580 590 600
FAGYFETVLY RDITLSIRPE THSPGMFSWF PIFFPIKQPI TVHEGQNICV
610 620 630
RFWRCSNSKK VWYEWAVTAP VCSSIHNPTG RSYTIGL
Length:637
Mass (Da):72,680
Last modified:January 23, 2007 - v3
Checksum:iE8014CA172B30543
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti169A → E in BAE21155 (PubMed:16141072).Curated1
Sequence conflicti169A → E in BAE38057 (PubMed:16141072).Curated1
Sequence conflicti376L → F in AAF04503 (PubMed:10531356).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK132414 mRNA Translation: BAE21155.1
AK165165 mRNA Translation: BAE38057.1
BC023905 mRNA Translation: AAH23905.1
AF167573 mRNA Translation: AAF04503.1
CCDSiCCDS27091.1
RefSeqiNP_001300835.1, NM_001313906.1
NP_001300836.1, NM_001313907.1
NP_038796.2, NM_013768.3
UniGeneiMm.196585

Genome annotation databases

GeneIDi27374
KEGGimmu:27374
UCSCiuc007twf.2 mouse

Similar proteinsi

Entry informationi

Entry nameiANM5_MOUSE
AccessioniPrimary (citable) accession number: Q8CIG8
Secondary accession number(s): Q3TNN1, Q9QZS9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 135 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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