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UniProtKB/Swiss-Prot entry Q99873


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ANM1_HUMAN
Primary accession number Q99873
Secondary accession numbers Q15529 Q2VP93 Q6LEU5 Q99872 Q99874 Q9NZ04 Q9NZ05 Q9NZ06
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on December 4, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 72)
Name and origin of the protein
Protein name Protein arginine N-methyltransferase 1
Synonyms EC 2.1.1.-
Interferon receptor 1-bound protein 4
Gene name
Name: PRMT1
Synonyms: HMT2, HRMT1L2, IR1B4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
DOI=10.1006/geno.1997.5190; PubMed=9545638 [NCBI, ExPASy, EBI, Israel, Japan]
Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A., Henry M.F.;
"Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2).";
Genomics 48:330-340(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Glial cell;
DOI=10.1016/0378-1119(96)00073-X; PubMed=8675017 [NCBI, ExPASy, EBI, Israel, Japan]
Nikawa J., Nakano H., Ohi N.;
"Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant.";
Gene 171:107-111(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
Scorilas A., Black M.H., Diamandis E.P.;
"Molecular characterization, mapping and tissue expression of the human protein arginine N-methyltransferase 1 (PRMT1/HRMT1L2) gene.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH ILF3.
DOI=10.1074/jbc.M000023200; PubMed=10749851 [NCBI, ExPASy, EBI, Israel, Japan]
Tang J., Kao P.N., Herschman H.R.;
"Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3.";
J. Biol. Chem. 275:19866-19876(2000).
[7]
SUBUNIT.
DOI=10.1038/82028; PubMed=11101900 [NCBI, ExPASy, EBI, Israel, Japan]
Weiss V.H., McBride A.E., Soriano M.A., Filman D.J., Silver P.A., Hogle J.M.;
"The structure and oligomerization of the yeast arginine methyltransferase, Hmt1.";
Nat. Struct. Biol. 7:1165-1171(2000).
[8]
FUNCTION, AND INTERACTION WITH SUPT5H.
DOI=10.1016/S1097-2765(03)00101-1; PubMed=12718890 [NCBI, ExPASy, EBI, Israel, Japan]
Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B.;
"Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties.";
Mol. Cell 11:1055-1066(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-299, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[10]
FUNCTION, AND INTERACTION WITH EWS AND PRMT8.
DOI=10.1002/prot.22004; PubMed=18320585 [NCBI, ExPASy, EBI, Israel, Japan]
Pahlich S., Zakaryan R.P., Gehring H.;
"Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state.";
Proteins 72:1125-1137(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y10805; CAA71763.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y10806; CAA71764.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y10807; CAA71765.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D66904; BAA11029.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF222689; AAF62893.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF222689; AAF62894.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF222689; AAF62895.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR407608; CAG28536.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC109282; AAI09283.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC109283; AAI09284.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00018522; -.
IPI00215734; -.
IPI00914913; -.
RefSeq NP_001527.3; -.
NP_938075.2; -.
UniGene Hs.20521
3D structure databases
HSSP Q63009; 1ORI. [HSSP ENTRY / PDB]
SMR Q99873; 49-361.
ModBase Q99873.
Protein-protein interaction databases
IntAct Q99873; 29.
PTM databases
PhosphoSite Q99873; -.
Organism-specific databases
GeneCards GC19P054873; -.
H-InvDB HIX0039961; -.
HGNC HGNC:5187; PRMT1.
GenAtlas PRMT1.
MIM 602950; gene. [NCBI / EBI]
Gene expression databases
ArrayExpress Q99873; -.
Bgee Q99873; -.
CleanEx HS_PRMT1; -.
GermOnline ENSG00000126457; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005634; Cellular component: nucleus (inferred from direct assay from MGI).
GO:0008170; Molecular function: N-methyltransferase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0007166; Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
GO:0006479; Biological process: protein amino acid methylation (traceable author statement from ProtInc).
QuickGo view.
Proteomic databases
PRIDE Q99873; -.
Genome annotation databases
Ensembl ENSG00000126457; Homo sapiens. [Contig view]
GeneID 3276; -.
KEGG hsa:3276; -.
Phylogenomic databases
HOVERGEN Q99873; -.
Other
NextBio 13013; -.
SOURCE PRMT1; Homo sapiens.
ProtoNet Q99873.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; S-adenosyl-L-methionine; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   361  361     Protein arginine N-methyltransferase 1. PRO_0000212321
BINDING   53    53        S-adenosyl-L-methionine (By similarity). 
BINDING   62    62        S-adenosyl-L-methionine (By similarity). 
BINDING   86    86        S-adenosyl-L-methionine; via carbonyl oxygen (By similarity). 
BINDING   108   108        S-adenosyl-L-methionine (By similarity). 
BINDING   137   137        S-adenosyl-L-methionine (By similarity). 
MOD_RES   299   299        Phosphotyrosine. 
VAR_SEQ   1    19        MENFVATLANGMSLQPPLE -> MVGVA (in isoform 2). VSP_005208
VAR_SEQ   1    19        MENFVATLANGMSLQPPLE -> M (in isoform 3). VSP_005209
VARIANT   78    78  1     K -> M (in dbSNP:rs1804486 [NCBI]). VAR_037501 
VARIANT   158   158  1     L -> F (in dbSNP:rs11673683 [NCBI]). VAR_037502 
CONFLICT   108   108        E -> V (in Ref. 1; CAA71763/CAA71764/CAA71765 and 2; BAA11029). 
CONFLICT   147   175        DIIISEWMGYCLFYESMLNTVLYARDKWL -> ASSSASGWATASSTSPCSTPCSMPGTSV (in Ref. 2; BAA11029). 
Sequence information
Length: 361 AA [This is the length of the unprocessed precursor] Molecular weight: 41516 Da [This is the MW of the unprocessed precursor] CRC64: A286D99B5AFC1860 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK DYYFDSYAHF GIHEEMLKDE 

        70         80         90        100        110        120 
VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG ARKVIGIECS SISDYAVKIV 

       130        140        150        160        170        180 
KANKLDHVVT IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVLYA RDKWLAPDGL 

       190        200        210        220        230        240 
IFPDRATLYV TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVTNAC 

       250        260        270        280        290        300 
LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG FSTSPESPYT 

       310        320        330        340        350        360 
HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT IDLDFKGQLC ELSCSTDYRM 


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Q99873 in FASTA format

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