Q922H1 (ANM3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein arginine N-methyltransferase 3
EC=2.1.1.-

Alternative name(s):
Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3

Gene names

Name:	Prmt3
Synonyms:	Hrmt1l3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	532 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins By similarity.
Enzyme regulation	Inhibited by N-ethylmaleimide and high concentrations of zinc chloride By similarity.
Subunit structure	May exist as a monomer or homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	The zinc-finger is responsible for substrate specificity By similarity.
Sequence similarities	Belongs to the protein arginine N-methyltransferase family. Contains 1 C2H2-type zinc finger.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein methylation Inferred from mutant phenotype PubMed 15473865. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay PubMed 15473865. Source: UniProtKB
Molecular_function	protein-arginine omega-N asymmetric methyltransferase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q922H1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform 2 (identifier: Q922H1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     417-420: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 532

532

Protein arginine N-methyltransferase 3

PRO_0000212327

Regions

Zinc finger

46 – 69

24

C2H2-type

Sites

Active site

326

1

By similarity

Active site

335

1

By similarity

Binding site

227

1

S-adenosyl-L-methionine By similarity

Binding site

236

1

S-adenosyl-L-methionine By similarity

Binding site

260

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Binding site

282

1

S-adenosyl-L-methionine By similarity

Binding site

311

1

S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue

22

1

Phosphoserine By similarity

Modified residue

24

1

Phosphoserine By similarity

Natural variations

Alternative sequence

417 – 420

4

Missing in isoform 2.

VSP_010498

Secondary structure

1

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532

Helix Strand Turn

Details...

Beta strand

49 – 51

3

Beta strand

54 – 57

4

Helix

58 – 67

10

Helix

73 – 79

7

Helix

84 – 96

13

Helix

101 – 105

5

Helix

116 – 119

4

Beta strand

122 – 125

4

Helix

127 – 130

4

Helix

133 – 136

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: 878ADDCCF4054F17	FASTA	532	59,902
	10 20 30 40 50 60 MCSLAAGNGR GAELGPEPLE LSDSGDDAGW EDEDADTEPA HGRQHTPCLF CDRLFASAEE 70 80 90 100 110 120 TFSHCKLEHQ FNIDSMVHKH GLEFYGYIKL INFIRLKNPT VEYMNSIYNP VPWEKDEYLK 130 140 150 160 170 180 PVLEDDLLLQ FDVEDLYEPV STPFSYPNGL SESASVVEKL KHMEARALSA EAALARARED 190 200 210 220 230 240 LQKMKQFAQD FVMNVDVRTC SSTTTIADLQ EDEDGVYFSS YGHYGIHEEM LKDKVRTESY 250 260 270 280 290 300 RDFIYQNPHI FKDKVVLDVG CGTGILSMFA AKVGAKKVIA VDQSEILYQA MDIIRLNKLE 310 320 330 340 350 360 DTIVLIKGKI EEVSLPVEKV DVIISEWMGY FLLFESMLDS VLYAKSKYLA KGGSVYPDIC 370 380 390 400 410 420 TISLVAVSDV SKHADRIAFW DDVYGFNMSC MKKAVIPEAV VEVVDHKTLI SDPCDIKMDG 430 440 450 460 470 480 KHIDCHTTSI SDLEFSSDFT LRTTKTAMCT AVAGYFDIYF EKNCHNRVVF STGPQSTKTH 490 500 510 520 530 WKQTVFLLEK PFPVKAGEAL KGKITVHKNK KDPRSLIVTL TLNSSTQTYS LQ
	Isoform 2 [UniParc]. Checksum: E8DF5B88AB6B92FF	FASTA	528	59,471
	10 20 30 40 50 60 MCSLAAGNGR GAELGPEPLE LSDSGDDAGW EDEDADTEPA HGRQHTPCLF CDRLFASAEE 70 80 90 100 110 120 TFSHCKLEHQ FNIDSMVHKH GLEFYGYIKL INFIRLKNPT VEYMNSIYNP VPWEKDEYLK 130 140 150 160 170 180 PVLEDDLLLQ FDVEDLYEPV STPFSYPNGL SESASVVEKL KHMEARALSA EAALARARED 190 200 210 220 230 240 LQKMKQFAQD FVMNVDVRTC SSTTTIADLQ EDEDGVYFSS YGHYGIHEEM LKDKVRTESY 250 260 270 280 290 300 RDFIYQNPHI FKDKVVLDVG CGTGILSMFA AKVGAKKVIA VDQSEILYQA MDIIRLNKLE 310 320 330 340 350 360 DTIVLIKGKI EEVSLPVEKV DVIISEWMGY FLLFESMLDS VLYAKSKYLA KGGSVYPDIC 370 380 390 400 410 420 TISLVAVSDV SKHADRIAFW DDVYGFNMSC MKKAVIPEAV VEVVDHKTLI SDPCDIKHID 430 440 450 460 470 480 CHTTSISDLE FSSDFTLRTT KTAMCTAVAG YFDIYFEKNC HNRVVFSTGP QSTKTHWKQT 490 500 510 520 VFLLEKPFPV KAGEALKGKI TVHKNKKDPR SLIVTLTLNS STQTYSLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization, chromosomal mapping, and expression analysis of the murine Prmt3 and Htatip2 genes." Hauser L.J., Webb L.S., Dhar M.S., Mural R.M., Larimer F.W., Johnson D.K. Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2). Strain: 129/SvJ.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Head and Thymus.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-532 (ISOFORM 2). Strain: FVB/N. Tissue: Brain and Mammary gland.
[4]	"Solution structure of the C2H2 zinc finger domain of the protein arginine N-methyltransferase 3 from Mus musculus." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 38-145.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY151050 Genomic DNA. Translation: AAN84530.1.
AK031738 mRNA. Translation: BAC27531.1.
AK086646 mRNA. Translation: BAC39708.1.
BC008128 mRNA. Translation: AAH08128.1.
BC050775 mRNA. Translation: AAH50775.1.

IPI

IPI00262117.
IPI00417140.

RefSeq

NP_598501.1. NM_133740.2.

UniGene

Mm.33202.
Mm.349442.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WIR	NMR	-	A	38-145	[»]

ProteinModelPortal

Q922H1.

SMR

Q922H1. Positions 38-145, 208-532.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q922H1. 1 interaction.

STRING

10090.ENSMUSP00000082373.

PTM databases

PhosphoSite

Q922H1.

Proteomic databases

PaxDb

Q922H1.

PRIDE

Q922H1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000032715; ENSMUSP00000032715; ENSMUSG00000030505.

GeneID

71974.

KEGG

mmu:71974.

UCSC

uc009hbt.1. mouse.

Organism-specific databases

CTD

10196.

MGI

MGI:1919224. Prmt3.

Phylogenomic databases

eggNOG

COG0500.

GeneTree

ENSGT00550000074406.

HOGENOM

HOG000198521.

HOVERGEN

HBG001793.

InParanoid

Q922H1.

KO

K11436.

OMA

ITKTSMC.

OrthoDB

EOG40S0FT.

Gene expression databases

ArrayExpress

Q922H1.

Bgee

Q922H1.

CleanEx

MM_PRMT3.

Genevestigator

Q922H1.

GermOnline

ENSMUSG00000030505. Mus musculus.

Family and domain databases

InterPro

IPR025799. Arg_MeTrfase.
IPR010456. Ribosomal-L11_MeTrfase_PrmA.
IPR015880. Znf_C2H2-like.
[Graphical view]

PANTHER

PTHR11006. PTHR11006. 1 hit.

Pfam

PF06325. PrmA. 1 hit.
[Graphical view]

SMART

SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q922H1.

NextBio

335102.

SOURCE

Search...

Entry information

Entry name

ANM3_MOUSE

Accession

Primary (citable) accession number: Q922H1
Secondary accession number(s): Q80VU9, Q8BFV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	June 7, 2004
Last modified:	April 3, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program