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Reviewed, UniProtKB/Swiss-Prot O60678 (ANM3_HUMAN)

Last modified November 25, 2008. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

May exist as a monomer or homodimer By similarity.

Subcellular location

Cytoplasm.

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 componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure

Gene Ontology (GO)

   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm Ref.2

Non-traceable author statement. Source: UniProtKB

   Molecular functionprotein-arginine N-methyltransferase activity Ref.2

Non-traceable author statement. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 531531Protein arginine N-methyltransferase 3
PRO_0000212326

Regions

Zinc finger48 – 7124C2H2-type

Sites

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

Natural variations

Natural variant4401L → V: dbSNP rs3758805.
VAR_024584
Natural variant4701S → C: dbSNP rs11025585.
VAR_030943
Natural variant5081N → S: dbSNP rs6483700.
VAR_024585

Experimental info

Sequence conflict211L → E in AAC39837. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O60678-1 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: 71EC59E2BEDBE7AC

FASTA53159,903
        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 GKVTVHKNKK DPRSLTVTLT LNNSTQTYGL Q 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Brain.
[2]"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: 9642256] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-531.
[3]"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.

Cross-references

Sequence databases

BC037544 mRNA. Translation: AAH37544.1.
BC064831 mRNA. Translation: AAH64831.1.
AF059531 mRNA. Translation: AAC39837.1.
RefSeqNP_005779.1.
UniGeneHs.152337

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2FYTX-ray2.00A211-531[»]
SMRO60678. Positions 43-147.
ModBaseSearch...

PTM databases

PhosphoSiteO60678.

Genome annotation databases

EnsemblENSG00000185238. Homo sapiens. [Contig view]
GeneID10196.
KEGGhsa:10196.

Organism-specific databases

H-InvDBHIX0026130.
HGNCHGNC:30163. PRMT3.
HPAHPA007832.
MIM603190. gene.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENO60678.

Gene expression databases

ArrayExpressO60678.
CleanExHS_PRMT3.
GermOnlineENSG00000185238. Homo sapiens.

Family and domain databases

InterProIPR013216. Methyltransf_11.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF08241. Methyltransf_11. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio38588.
SOURCESearch...

Entry information

Entry nameANM3_HUMAN
AccessionPrimary (citable) accession number: O60678
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 7, 2004
Last modified: November 25, 2008
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 11

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents