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Protein

Protein arginine N-methyltransferase 5

Gene

prmt5

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins; such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates the arginine in the motif G-R-G-X-G in its substrates histone H2A, H2AFX and H4, producing both monomethylated and symmetrically dimethylated 'Arg-3'. Methylates nucleoplasmin at 'Arg-192', producing both monomethylated and symmetrically dimethylated 'Arg-192'. Involved in the DNA replication checkpoint. Promotes entry into mitosis by promoting the proteasomal degradation of wee2-a. May act as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1.3 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei300 – 3001Peptide substrateBy similarity
Binding sitei303 – 3031Peptide substrateBy similarity
Binding sitei320 – 3201S-adenosyl-L-methionine
Binding sitei388 – 3881S-adenosyl-L-methionine
Active sitei431 – 4311Proton donor/acceptorBy similarity
Active sitei440 – 4401Proton donor/acceptorBy similarity
Binding sitei440 – 4401S-adenosyl-L-methionine

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • circadian regulation of gene expression Source: UniProtKB
  • Golgi ribbon formation Source: UniProtKB
  • histone arginine methylation Source: UniProtKB
  • histone H4-R3 methylation Source: UniProtKB
  • mitotic DNA replication checkpoint Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of nucleic acid-templated transcription Source: GOC
  • positive regulation of proteasomal protein catabolic process Source: UniProtKB
  • regulation of mitotic nuclear division Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 5 (EC:2.1.1.3201 Publication)
Alternative name(s):
Histone synthetic lethal 7 protein
Short name:
Hsl7
Histone-arginine N-methyltransferase PRMT5
Gene namesi
Name:prmt5
Synonyms:hsl7
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • methylosome Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Protein arginine N-methyltransferase 5PRO_0000422972Add
BLAST

Proteomic databases

PRIDEiQ6NUA1.

Expressioni

Tissue specificityi

Detected in egg (at protein level).2 Publications

Interactioni

Subunit structurei

Heterotetramer; dimer of heterodimer with wdr77. Interacts with wee2-a; this interaction is disrupted upon activation of the DNA replication checkpoint.3 Publications

Structurei

Secondary structure

1
633
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 144Combined sources
Helixi21 – 299Combined sources
Turni30 – 323Combined sources
Beta strandi34 – 418Combined sources
Beta strandi49 – 513Combined sources
Helixi54 – 563Combined sources
Helixi70 – 756Combined sources
Beta strandi77 – 804Combined sources
Helixi92 – 11120Combined sources
Beta strandi115 – 1206Combined sources
Helixi127 – 13812Combined sources
Beta strandi145 – 1539Combined sources
Helixi155 – 1584Combined sources
Helixi180 – 19112Combined sources
Turni192 – 1943Combined sources
Beta strandi198 – 2036Combined sources
Helixi211 – 2177Combined sources
Beta strandi222 – 2287Combined sources
Beta strandi231 – 2344Combined sources
Helixi244 – 25411Combined sources
Turni255 – 2573Combined sources
Beta strandi259 – 2646Combined sources
Beta strandi269 – 2713Combined sources
Helixi274 – 28411Combined sources
Beta strandi292 – 2965Combined sources
Turni297 – 2993Combined sources
Turni310 – 3123Combined sources
Helixi317 – 3237Combined sources
Helixi327 – 34418Combined sources
Turni348 – 3525Combined sources
Beta strandi354 – 3618Combined sources
Turni363 – 3653Combined sources
Helixi366 – 37712Combined sources
Beta strandi381 – 3899Combined sources
Helixi391 – 40111Combined sources
Turni402 – 4054Combined sources
Beta strandi409 – 4146Combined sources
Turni416 – 4183Combined sources
Beta strandi425 – 4306Combined sources
Helixi442 – 4476Combined sources
Beta strandi453 – 4619Combined sources
Beta strandi463 – 47210Combined sources
Helixi474 – 4818Combined sources
Beta strandi486 – 4883Combined sources
Helixi492 – 4954Combined sources
Helixi502 – 5043Combined sources
Beta strandi505 – 5073Combined sources
Beta strandi512 – 5209Combined sources
Beta strandi530 – 5378Combined sources
Beta strandi542 – 55615Combined sources
Beta strandi559 – 5624Combined sources
Beta strandi578 – 58811Combined sources
Beta strandi593 – 60210Combined sources
Beta strandi604 – 61310Combined sources
Beta strandi615 – 6173Combined sources
Helixi624 – 6263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G56X-ray2.95A/C2-633[»]
ProteinModelPortaliQ6NUA1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini304 – 611308SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni329 – 3302S-adenosyl-L-methionine binding
Regioni414 – 4163S-adenosyl-L-methionine binding

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

Phylogenomic databases

HOVERGENiHBG057083.
KOiK02516.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10738. PTHR10738. 1 hit.
PfamiPF05185. PRMT5. 1 hit.
[Graphical view]
PIRSFiPIRSF015894. Skb1_MeTrfase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6NUA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGDGGRVS SGRDVACVTE VADTLGAMAN QGFDFLCMPI FHPRFKREFY
60 70 80 90 100
KEPAKSRPGP QTRSDLLLSG RDWNTLIVGK LSDWIKTDSE VSRIRKTSEA
110 120 130 140 150
AMQQELNFSA YLGLPAFLIP LKQEDNSNLS RLLINHIHVG HHSTMFWMRV
160 170 180 190 200
PLMAPNDLRD DLIENEPISL SEEDNSGEER TWIWWHNFRS LCDYNKKIAL
210 220 230 240 250
AIEIGADLPS GHVIDRWLGE PIKAAFLPTS IFLTNKKGFP VLTKVHQRLI
260 270 280 290 300
FKLFKLEVQF VISGSHHHSE KDLCSYLQYL EYLSQNSPPP NAYEMFAKGY
310 320 330 340 350
EDYLQSPLQP LMDNLESQTY EVFEKDPVKY SQYQQAVYKC LLDRVPEEEK
360 370 380 390 400
ETNIQILMVL GAGRGPLVNA SLRAAKQAER KIKVYAVEKN PNAVITLEGW
410 420 430 440 450
RYEEWGSQVT VVSGDMREWK APEKADIIVS ELLGSFGDNE LSPECLDGAQ
460 470 480 490 500
HFLKDDGVSI PGEYTSYLAP ISSSKLYNEV RACREKDRDP EAQFEMPYVV
510 520 530 540 550
RLHNFHQLSD PLPCFTFHHP NKDDVIDNNR YCCLQYRVDL NTVLHGFAGY
560 570 580 590 600
FNTVLYKDVT LSICPESHSP GMFSWFPILF PIKQPIPMRE GDTVCVRFWR
610 620 630
CNNGKKVWYE WAVTSPVCSA IHNPTGRSYT IGL
Length:633
Mass (Da):72,285
Last modified:July 5, 2004 - v1
Checksum:iF3A61499DF6623CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY535008 mRNA. Translation: AAS98802.1.
BC068696 mRNA. Translation: AAH68696.1.
RefSeqiNP_001084480.1. NM_001091011.1.
UniGeneiXl.46791.

Genome annotation databases

GeneIDi407754.
KEGGixla:407754.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY535008 mRNA. Translation: AAS98802.1.
BC068696 mRNA. Translation: AAH68696.1.
RefSeqiNP_001084480.1. NM_001091011.1.
UniGeneiXl.46791.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G56X-ray2.95A/C2-633[»]
ProteinModelPortaliQ6NUA1.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ6NUA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi407754.
KEGGixla:407754.

Organism-specific databases

CTDi407754.

Phylogenomic databases

HOVERGENiHBG057083.
KOiK02516.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10738. PTHR10738. 1 hit.
PfamiPF05185. PRMT5. 1 hit.
[Graphical view]
PIRSFiPIRSF015894. Skb1_MeTrfase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA replication checkpoint control of Wee1 stability by vertebrate Hsl7."
    Yamada A., Duffy B., Perry J.A., Kornbluth S.
    J. Cell Biol. 167:841-849(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH WEE2-A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  3. "Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs."
    Wilczek C., Chitta R., Woo E., Shabanowitz J., Chait B.T., Hunt D.F., Shechter D.
    J. Biol. Chem. 286:42221-42231(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH WDR77, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  4. "Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity."
    Ho M.C., Wilczek C., Bonanno J.B., Xing L., Seznec J., Matsui T., Carter L.G., Onikubo T., Kumar P.R., Chan M.K., Brenowitz M., Cheng R.H., Reimer U., Almo S.C., Shechter D.
    PLoS ONE 8:E57008-E57008(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH WDR77 AND S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, SUBUNIT, INTERACTION WITH WDR77.

Entry informationi

Entry nameiANM5_XENLA
AccessioniPrimary (citable) accession number: Q6NUA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2013
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.