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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)DescriptionActionsGraphical viewLength
Binding sitei300Peptide substrateBy similarity1
Binding sitei303Peptide substrateBy similarity1
Binding sitei320S-adenosyl-L-methionine1
Binding sitei388S-adenosyl-L-methionine1
Active sitei431Proton donor/acceptorBy similarity1
Active sitei440Proton donor/acceptorBy similarity1
Binding sitei440S-adenosyl-L-methionine1

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
  • 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)DescriptionActionsGraphical viewLength
ChainiPRO_00004229721 – 633Protein arginine N-methyltransferase 5Add BLAST633

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

1633
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 14Combined sources4
Helixi21 – 29Combined sources9
Turni30 – 32Combined sources3
Beta strandi34 – 41Combined sources8
Beta strandi49 – 51Combined sources3
Helixi54 – 56Combined sources3
Helixi70 – 75Combined sources6
Beta strandi77 – 80Combined sources4
Helixi92 – 111Combined sources20
Beta strandi115 – 120Combined sources6
Helixi127 – 138Combined sources12
Beta strandi145 – 153Combined sources9
Helixi155 – 158Combined sources4
Helixi180 – 191Combined sources12
Turni192 – 194Combined sources3
Beta strandi198 – 203Combined sources6
Helixi211 – 217Combined sources7
Beta strandi222 – 228Combined sources7
Beta strandi231 – 234Combined sources4
Helixi244 – 254Combined sources11
Turni255 – 257Combined sources3
Beta strandi259 – 264Combined sources6
Beta strandi269 – 271Combined sources3
Helixi274 – 284Combined sources11
Beta strandi292 – 296Combined sources5
Turni297 – 299Combined sources3
Turni310 – 312Combined sources3
Helixi317 – 323Combined sources7
Helixi327 – 344Combined sources18
Turni348 – 352Combined sources5
Beta strandi354 – 361Combined sources8
Turni363 – 365Combined sources3
Helixi366 – 377Combined sources12
Beta strandi381 – 389Combined sources9
Helixi391 – 401Combined sources11
Turni402 – 405Combined sources4
Beta strandi409 – 414Combined sources6
Turni416 – 418Combined sources3
Beta strandi425 – 430Combined sources6
Helixi442 – 447Combined sources6
Beta strandi453 – 461Combined sources9
Beta strandi463 – 472Combined sources10
Helixi474 – 481Combined sources8
Beta strandi486 – 488Combined sources3
Helixi492 – 495Combined sources4
Helixi502 – 504Combined sources3
Beta strandi505 – 507Combined sources3
Beta strandi512 – 520Combined sources9
Beta strandi530 – 537Combined sources8
Beta strandi542 – 556Combined sources15
Beta strandi559 – 562Combined sources4
Beta strandi578 – 588Combined sources11
Beta strandi593 – 602Combined sources10
Beta strandi604 – 613Combined sources10
Beta strandi615 – 617Combined sources3
Helixi624 – 626Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G56X-ray2.95A/C2-633[»]
ProteinModelPortaliQ6NUA1.
SMRiQ6NUA1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini304 – 611SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST308

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni329 – 330S-adenosyl-L-methionine binding2
Regioni414 – 416S-adenosyl-L-methionine binding3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G56X-ray2.95A/C2-633[»]
ProteinModelPortaliQ6NUA1.
SMRiQ6NUA1.
ModBaseiSearch...
MobiDBiSearch...

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...

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: November 2, 2016
This is version 64 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.