Reviewed, UniProtKB/Swiss-Prot Q8CIG8 (ANM5_MOUSE)

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
    Jak-binding protein 1

Gene names

Name:	Prmt5
Synonyms:	Jbp1, Skb1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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 protein 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. Ref.4 Ref.6
Catalytic activity	S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].
Subunit structure	Forms, at least, homodimers and homotetramers. Component of the methylosome, a 20S complex containing at least pICLn, PRMT5/SKB1 and MEP50. 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 COPR5; promoting its recruitment on histone H4 By similarity. Interacts with PRDM1. Ref.5
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Post-translational modification	Disulfide bonds and non-covalent association mediate homooligomers 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 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 direct assay. Source: UniProtKB
Molecular function	histone-arginine N-methyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from sequence or structural similarity. Source: UniProtKB 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_0000212344
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	200	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	169	1	A → E in BAE21155. Ref.1
	Sequence conflict	169	1	A → E in BAE38057. Ref.1
	Sequence conflict	376	1	L → F in AAF04503. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8CIG8-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E8014CA172B30543	FASTA	637	72,680
	10 20 30 40 50 60 MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFIQEPAK 70 80 90 100 110 120 NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI HPDSKVEKIR RNSEAAMLQE LNFGAYLGLP 130 140 150 160 170 180 AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDVIAN APTTHTEEYS 190 200 210 220 230 240 GEEKTWMWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK 250 260 270 280 290 300 KGFPVLSKVQ QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF 310 320 330 340 350 360 AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP EEEKETNVQV 370 380 390 400 410 420 LMVLGAGRGP LVNASLRAAK QAERRIRLYA VEKNPNAVVT LENWQFEEWG SQVTVVSSDM 430 440 450 460 470 480 REWVAPEKAD IIVSELLGSF ADNELSPECL DGAQHFLKDD GVSIPGEYTS FLAPISSSKL 490 500 510 520 530 540 YNEVRACREK DRDPEAQFEM PYVVRLHNFH QLSAPKPCFT FSHPNRDPMI DNNRYCTLEF 550 560 570 580 590 600 PVEVNTVLHG FAGYFETVLY RDITLSIRPE THSPGMFSWF PIFFPIKQPI TVHEGQNICV 610 620 630 RFWRCSNSKK VWYEWAVTAP VCSSIHNPTG RSYTIGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Skin.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[3]	"The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity." Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S. J. Biol. Chem. 274:31531-31542(1999) [PubMed: 10531356] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-637.
[4]	"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes." Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S. Mol. Cell. Biol. 24:9630-9645(2004) [PubMed: 15485929] [Abstract] Cited for: FUNCTION IN METHYLATION OF HISTONE H3.
[5]	"Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells." Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., Kouzarides T., Surani M.A. Nat. Cell Biol. 8:623-630(2006) [PubMed: 16699504] [Abstract] Cited for: INTERACTION WITH PRDM1.
[6]	"Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members." Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S., Girard A., Sachidanandam R., Hannon G.J., Aravin A.A. Genes Dev. 23:1749-1762(2009) [PubMed: 19584108] [Abstract] Cited for: FUNCTION IN METHYLATION OF PIWI PROTEINS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK132414 mRNA. Translation: BAE21155.1. AK165165 mRNA. Translation: BAE38057.1. BC023905 mRNA. Translation: AAH23905.1. AF167573 mRNA. Translation: AAF04503.1.
IPI	IPI00229845.
RefSeq	NP_038796.2.
UniGene	Mm.196585
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8CIG8.
PTM databases
PhosphoSite	Q8CIG8.
Proteomic databases
PRIDE	Q8CIG8.
Genome annotation databases
Ensembl	ENSMUST00000023873; ENSMUSP00000023873; ENSMUSG00000023110; Mus musculus. [Genome view]
GeneID	27374.
KEGG	mmu:27374.
UCSC	uc007twf.1. mouse.
Organism-specific databases
CTD	27374.
MGI	MGI:1351645. Prmt5.
Phylogenomic databases
eggNOG	roNOG13428.
HOGENOM	HBG628479.
HOVERGEN	Q8CIG8.
InParanoid	Q8CIG8.
PhylomeDB	Q8CIG8.
Enzyme and pathway databases
BRENDA	2.1.1.125. 244.
Gene expression databases
ArrayExpress	Q8CIG8.
Bgee	Q8CIG8.
CleanEx	MM_PRMT5.
Genevestigator	Q8CIG8.
GermOnline	ENSMUSG00000023110. Mus musculus.
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...
Other Resources
SOURCE	Search...

Entry information

Entry name

ANM5_MOUSE

Accession

Primary (citable) accession number: Q8CIG8
Secondary accession number(s): Q3TNN1, Q9QZS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 62 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)