Reviewed, UniProtKB/Swiss-Prot Q5R698 (ANM5_PONAB)

Names and origin

Protein names

Recommended name:
    Protein arginine N-methyltransferase 5
    EC=2.1.1.-
Alternative name(s):
    Histone-arginine N-methyltransferase PRMT5
    EC=2.1.1.125
    Shk1 kinase-binding protein 1 homolog
      Short name=SKB1 homolog

Gene names

Name:	PRMT5
Synonyms:	SKB1

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	637 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	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 Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. 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 By similarity.
Catalytic activity	S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine.
Subunit structure	Forms, at least, homodimers and homotetramers. Interacts with PRDM1 By similarity. Component of the methylosome, a 20S complex containing at least pICLn, PRMT1/SKB1 and MEP50. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Also interacts with Sm proteins, JAK2, SSTR1 and SUPT5H. Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with PRMT7 and SNRPD3. Interacts with COPR5; promoting its recruitment on histone H4 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Post-translational modification	Disulfide bonds and non-covalent association mediate homooligomer formation By similarity.
Sequence similarities	Belongs to the protein arginine N-methyltransferase family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Acetylation Disulfide bond
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-arginine methylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW spliceosomal snRNP assembly Inferred from sequence or structural similarity. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone-arginine N-methyltransferase activity Inferred from electronic annotation. Source: EC protein-arginine omega-N symmetric methyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 637	636	Protein arginine N-methyltransferase 5		PRO_0000212345
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	200	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R698-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2195B04C72EF47D2	FASTA	637	72,666
	10 20 30 40 50 60 MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFIQEPAK 70 80 90 100 110 120 NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI RPDSEVEKIR RNSEAAMLQE LNFGAYLGLP 130 140 150 160 170 180 AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDIIEN APTTHTQEYS 190 200 210 220 230 240 GEEKTWIWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK 250 260 270 280 290 300 KGFPVLSKMH QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF 310 320 330 340 350 360 AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP EEEKDTNVQV 370 380 390 400 410 420 LMVLGAGRGP LVNASLRAAK QADRRIKLYA VEKNPNAVVT LENWQFEEWG SQVTVVSSDM 430 440 450 460 470 480 REWVAPEKAD IIVSELLGSF ADNELSPECL DGAQHFLKDD GVSIPGEYTS FLAPISSSKL 490 500 510 520 530 540 YNEVRACREK DRDPEAQFEM PYVVRLHNFH QLSAPQPCFT FSHPNRDPMI DNNRYCTLEF 550 560 570 580 590 600 PVEVNTVLHG FAGYFETVLY QDITLSIRPE THSPGMFSWF PILFPIKQPI TVREGQTICV 610 620 630 RFWRCSNSKK VWYEWAVTAP VCSAIHNPTG RSYTIGL

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR860596 mRNA. Translation: CAH92718.1.
RefSeq	NP_001126589.1.
UniGene	Pab.18711
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100173581.
Organism-specific databases
CTD	100173581.
Phylogenomic databases
HOVERGEN	Q5R698.
Enzyme and pathway databases
BRENDA	2.1.1.125. 269192.
Family and domain databases
InterPro	IPR007857. Skb1_MeTrfase. [Graphical view]
PANTHER	PTHR10738. Skb1_mtfrase. 1 hit.
Pfam	PF05185. PRMT5. 1 hit. [Graphical view]
PIRSF	PIRSF015894. Skb1_MeTrfase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ANM5_PONAB

Accession

Primary (citable) accession number: Q5R698

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 35 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)