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O60678 (ANM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.

Enzyme regulation

Inhibited by N-ethylmaleimide and high concentrations of zinc chloride By similarity.

Subunit structure

Monomer or homodimer By similarity. Interacts with EPB41L3; this inhibits methylation of target proteins. Interacts with the 40S ribosomal protein RPS2. Ref.5 Ref.11

Subcellular location

Cytoplasm.

Domain

The zinc-finger is responsible for substrate specificity By similarity.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.

Contains 1 C2H2-type zinc finger.

Contains 1 SAM-dependent MTase PRMT-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionMethyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone arginine methylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of protein ubiquitination

Inferred from direct assay PubMed 18573314. Source: UniProtKB

peptidyl-arginine methylation, to asymmetrical-dimethyl arginine

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of transcription, DNA-templated

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytoplasm

Non-traceable author statement Ref.4. Source: UniProtKB

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

ribosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionhistone-arginine N-methyltransferase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methyltransferase activity

Inferred from direct assay PubMed 18573314. Source: UniProtKB

modified amino acid binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 18573314. Source: UniProtKB

protein-arginine N-methyltransferase activity

Non-traceable author statement Ref.4. Source: UniProtKB

protein-arginine omega-N asymmetric methyltransferase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SCN5AQ145242EBI-2809009,EBI-726858

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60678-1)

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.
Isoform 2 (identifier: O60678-2)

The sequence of this isoform differs from the canonical sequence as follows:
     11-99: GRGAVENEED...IKLINFIRLK → YSHLLKKHFHTVSLSISLILTAWFINM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 531530Protein arginine N-methyltransferase 3
PRO_0000212326

Regions

Domain217 – 531315SAM-dependent MTase PRMT-type
Zinc finger48 – 7124C2H2-type

Sites

Active site3291 By similarity
Active site3381 By similarity
Binding site2301S-adenosyl-L-methionine By similarity
Binding site2391S-adenosyl-L-methionine
Binding site2631S-adenosyl-L-methionine; via carbonyl oxygen
Binding site2851S-adenosyl-L-methionine
Binding site3141S-adenosyl-L-methionine
Site871Not phosphorylated

Amino acid modifications

Modified residue21N-acetylcysteine Ref.7 Ref.13 Ref.14
Modified residue251Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12
Modified residue271Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12

Natural variations

Alternative sequence11 – 9989GRGAV…FIRLK → YSHLLKKHFHTVSLSISLIL TAWFINM in isoform 2.
VSP_040330
Natural variant4401L → V.
Corresponds to variant rs3758805 [ dbSNP | Ensembl ].
VAR_024584
Natural variant4701S → C.
Corresponds to variant rs11025585 [ dbSNP | Ensembl ].
VAR_030943
Natural variant5081S → N. Ref.1 Ref.3 Ref.4
Corresponds to variant rs6483700 [ dbSNP | Ensembl ].
VAR_024585

Experimental info

Mutagenesis871Y → C: Markedly reduced affinity for RPS2. Ref.11
Mutagenesis871Y → E: Markedly reduced affinity for RPS2. Ref.11
Mutagenesis871Y → F: No effect on interaction with RPS2. Ref.11
Sequence conflict211L → E in AAC39837. Ref.4
Sequence conflict1031V → F in BAG62289. Ref.1
Sequence conflict5101K → R in BAG62289. Ref.1

Secondary structure

............................................................... 531
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: D02159E2BEDBE7B9

FASTA53159,876
        10         20         30         40         50         60 
MCSLASGATG GRGAVENEED LPELSDSGDE AAWEDEDDAD LPHGKQQTPC LFCNRLFTSA 

        70         80         90        100        110        120 
EETFSHCKSE HQFNIDSMVH KHGLEFYGYI KLINFIRLKN PTVEYMNSIY NPVPWEKEEY 

       130        140        150        160        170        180 
LKPVLEDDLL LQFDVEDLYE PVSVPFSYPN GLSENTSVVE KLKHMEARAL SAEAALARAR 

       190        200        210        220        230        240 
EDLQKMKQFA QDFVMHTDVR TCSSSTSVIA DLQEDEDGVY FSSYGHYGIH EEMLKDKIRT 

       250        260        270        280        290        300 
ESYRDFIYQN PHIFKDKVVL DVGCGTGILS MFAAKAGAKK VLGVDQSEIL YQAMDIIRLN 

       310        320        330        340        350        360 
KLEDTITLIK GKIEEVHLPV EKVDVIISEW MGYFLLFESM LDSVLYAKNK YLAKGGSVYP 

       370        380        390        400        410        420 
DICTISLVAV SDVNKHADRI AFWDDVYGFK MSCMKKAVIP EAVVEVLDPK TLISEPCGIK 

       430        440        450        460        470        480 
HIDCHTTSIS DLEFSSDFTL KITRTSMCTA IAGYFDIYFE KNCHNRVVFS TGPQSTKTHW 

       490        500        510        520        530 
KQTVFLLEKP FSVKAGEALK GKVTVHKSKK DPRSLTVTLT LNNSTQTYGL Q 

« Hide

Isoform 2 [UniParc].

Checksum: 4A67AC40A78A7B01
Show »

FASTA46952,875

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ASN-508.
[2]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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), VARIANT ASN-508.
Tissue: Brain.
[4]"PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation."
Tang J., Gary J.D., Clarke S., Herschman H.R.
J. Biol. Chem. 273:16935-16945(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-531 (ISOFORM 1), VARIANT ASN-508.
[5]"DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo."
Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A., Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.
Oncogene 23:7761-7771(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPB41L3.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)."
Handrkova H., Petrak J., Halada P., Pospisilova D., Cmejla R.
Biochim. Biophys. Acta 1814:277-282(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-25 AND SER-27, MUTAGENESIS OF TYR-87, ABSENCE OF PHOSPHORYLATION AT TYR-87, INTERACTION WITH RPS2.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"The crystal structure of human HMT1 HNRNP methyltransferase-like 3 in complex with SAH."
Structural genomics consortium (SGC)
Submitted (MAR-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 211-531 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK300591 mRNA. Translation: BAG62289.1.
AC025972 Genomic DNA. No translation available.
AC108005 Genomic DNA. No translation available.
BC037544 mRNA. Translation: AAH37544.1.
BC064831 mRNA. Translation: AAH64831.1.
AF059531 mRNA. Translation: AAC39837.1.
CCDSCCDS44554.1. [O60678-2]
CCDS7853.1. [O60678-1]
RefSeqNP_005779.1. NM_005788.3.
UniGeneHs.152337.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FYTX-ray2.00A211-531[»]
3SMQX-ray2.00A211-531[»]
4HSGX-ray2.30A211-531[»]
ProteinModelPortalO60678.
SMRO60678. Positions 43-147, 221-531.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115491. 31 interactions.
IntActO60678. 5 interactions.
MINTMINT-6803908.
STRING9606.ENSP00000331879.

Chemistry

BindingDBO60678.
ChEMBLCHEMBL5891.

PTM databases

PhosphoSiteO60678.

Proteomic databases

MaxQBO60678.
PaxDbO60678.
PRIDEO60678.

Protocols and materials databases

DNASU10196.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331079; ENSP00000331879; ENSG00000185238. [O60678-1]
ENST00000437750; ENSP00000397766; ENSG00000185238. [O60678-2]
GeneID10196.
KEGGhsa:10196.
UCSCuc001mqb.3. human. [O60678-1]
uc010rdn.2. human. [O60678-2]

Organism-specific databases

CTD10196.
GeneCardsGC11P020373.
HGNCHGNC:30163. PRMT3.
HPACAB022083.
HPA007832.
MIM603190. gene.
neXtProtNX_O60678.
PharmGKBPA29462.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0500.
HOGENOMHOG000198521.
HOVERGENHBG001793.
KOK11436.
OMAAQDFVMH.
OrthoDBEOG7S7SDJ.
PhylomeDBO60678.
TreeFamTF323587.

Enzyme and pathway databases

SABIO-RKO60678.

Gene expression databases

ArrayExpressO60678.
BgeeO60678.
CleanExHS_PRMT3.
GenevestigatorO60678.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025799. Arg_MeTrfase.
IPR010456. Ribosomal-L11_MeTrfase_PrmA.
IPR029063. SAM-dependent_MTases-like.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERPTHR11006. PTHR11006. 1 hit.
PfamPF06325. PrmA. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS51678. SAM_MT_PRMT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO60678.
GeneWikiPRMT3.
GenomeRNAi10196.
NextBio38588.
PROO60678.
SOURCESearch...

Entry information

Entry nameANM3_HUMAN
AccessionPrimary (citable) accession number: O60678
Secondary accession number(s): B4DUC7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM