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Q99873 (ANM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 1

EC=2.1.1.-
Alternative name(s):
Histone-arginine N-methyltransferase PRMT1
EC=2.1.1.125
Interferon receptor 1-bound protein 4
Gene names
Name:PRMT1
Synonyms:HMT2, HRMT1L2, IR1B4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Catalytic activity

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. Ref.9 Ref.10 Ref.16

Enzyme regulation

By BTG1, BTG2 and ILF3.

Subunit structure

Homodimer and heterodimer with PRMT8. The dimer can then associate to form a homohexamer. Interacts with ILF3, BTG1, BTG2, SUPT5H and interferon-alpha/beta receptor 1. Interacts with NFATC2IP By similarity. Ref.7 Ref.8 Ref.11 Ref.15

Subcellular location

Nucleus. Cytoplasmcytosol By similarity Ref.18.

Tissue specificity

Widely expressed. Ref.3

Sequence similarities

Belongs to the protein arginine N-methyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=1 µM for AdoMet Ref.16

KM=4.2 µM for H4

Vmax=1.2 nmol/min/mg enzyme toward AdoMet

Vmax=1.24 nmol/min/mg enzyme toward H4

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99873-1)

Also known as: V2;

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: Q99873-2)

Also known as: V3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MENFVATLANGMSLQPPLE → MVGVA
Isoform 3 (identifier: Q99873-3)

Also known as: V1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MENFVATLANGMSLQPPLE → M

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Protein arginine N-methyltransferase 1
PRO_0000212321

Sites

Binding site531S-adenosyl-L-methionine By similarity
Binding site621S-adenosyl-L-methionine By similarity
Binding site861S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1081S-adenosyl-L-methionine By similarity
Binding site1371S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue2991Phosphotyrosine Ref.12

Natural variations

Alternative sequence1 – 1919MENFV…QPPLE → MVGVA in isoform 2.
VSP_005208
Alternative sequence1 – 1919MENFV…QPPLE → M in isoform 3.
VSP_005209
Natural variant781K → M.
Corresponds to variant rs1804486 [ dbSNP | Ensembl ].
VAR_037501
Natural variant1581L → F.
Corresponds to variant rs11673683 [ dbSNP | Ensembl ].
VAR_037502

Experimental info

Sequence conflict1081E → V in CAA71763. Ref.1
Sequence conflict1081E → V in CAA71764. Ref.1
Sequence conflict1081E → V in CAA71765. Ref.1
Sequence conflict1081E → V in BAA11029. Ref.2
Sequence conflict147 – 17529DIIIS…RDKWL → ASSSASGWATASSTSPCSTP CSMPGTSV in BAA11029. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (V2) [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: A286D99B5AFC1860

FASTA36141,516
        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 


R 

« Hide

Isoform 2 (V3) [UniParc].

Checksum: 2546A25EF744E265
Show »

FASTA34739,929
Isoform 3 (V1) [UniParc].

Checksum: DFC413AC52F49754
Show »

FASTA34339,602

References

« Hide 'large scale' references
[1]"Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)."
Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A., Henry M.F.
Genomics 48:330-340(1998) [PubMed: 9545638] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[2]"Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant."
Nikawa J., Nakano H., Ohi N.
Gene 171:107-111(1996) [PubMed: 8675017] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Glial cell.
[3]"Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene."
Scorilas A., Black M.H., Talieri M., Diamandis E.P.
Biochem. Biophys. Res. Commun. 278:349-359(2000) [PubMed: 11097842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 3).
[7]"Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3."
Tang J., Kao P.N., Herschman H.R.
J. Biol. Chem. 275:19866-19876(2000) [PubMed: 10749851] [Abstract]
Cited for: INTERACTION WITH ILF3.
[8]"The structure and oligomerization of the yeast arginine methyltransferase, Hmt1."
Weiss V.H., McBride A.E., Soriano M.A., Filman D.J., Silver P.A., Hogle J.M.
Nat. Struct. Biol. 7:1165-1171(2000) [PubMed: 11101900] [Abstract]
Cited for: SUBUNIT.
[9]"Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1."
Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H., Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.
Curr. Biol. 11:996-1000(2001) [PubMed: 11448779] [Abstract]
Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY.
[10]"Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor."
Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H., Strahl B.D., Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.
Science 293:853-857(2001) [PubMed: 11387442] [Abstract]
Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY.
[11]"Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties."
Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B.
Mol. Cell 11:1055-1066(2003) [PubMed: 12718890] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUPT5H.
[12]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
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. expand/collapse author list , 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.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-299, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[13]"Regulation of estrogen rapid signaling through arginine methylation by PRMT1."
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S., Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.
Mol. Cell 31:212-221(2008) [PubMed: 18657504] [Abstract]
Cited for: FUNCTION.
[14]"PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells."
Miyata S., Mori Y., Tohyama M.
Neurosci. Lett. 445:162-165(2008) [PubMed: 18773938] [Abstract]
Cited for: FUNCTION.
[15]"Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state."
Pahlich S., Zakaryan R.P., Gehring H.
Proteins 72:1125-1137(2008) [PubMed: 18320585] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EWS AND PRMT8.
[16]"Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4."
Lakowski T.M., Frankel A.
Biochem. J. 421:253-261(2009) [PubMed: 19405910] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[17]"PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function."
Jobert L., Argentini M., Tora L.
Exp. Cell Res. 315:1273-1286(2009) [PubMed: 19124016] [Abstract]
Cited for: FUNCTION.
[18]"PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling."
Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.
Genes Dev. 23:118-132(2009) [PubMed: 19136629] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]"Protein-arginine methyltransferase 1 suppresses megakaryocytic differentiation via modulation of the p38 MAPK pathway in K562 cells."
Chang Y.I., Hua W.K., Yao C.L., Hwang S.M., Hung Y.C., Kuan C.J., Leou J.S., Lin W.J.
J. Biol. Chem. 285:20595-20606(2010) [PubMed: 20442406] [Abstract]
Cited for: FUNCTION.
[20]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10805 mRNA. Translation: CAA71763.1.
Y10806 mRNA. Translation: CAA71764.1.
Y10807 mRNA. Translation: CAA71765.1.
D66904 mRNA. Translation: BAA11029.1.
AF222689 Genomic DNA. Translation: AAF62893.1.
AF222689 Genomic DNA. Translation: AAF62894.1.
AF222689 Genomic DNA. Translation: AAF62895.1.
CR407608 mRNA. Translation: CAG28536.1.
AC011495 Genomic DNA. No translation available.
BC109282 mRNA. Translation: AAI09283.2.
BC109283 mRNA. Translation: AAI09284.2.
IPIIPI00382516.
IPI01014546.
IPI01018101.
RefSeqNP_001527.3. NM_001536.4.
UniGeneHs.20521.

3D structure databases

ProteinModelPortalQ99873.
SMRQ99873. Positions 49-361.
ModBaseSearch...

Protein-protein interaction databases

IntActQ99873. 29 interactions.
MINTMINT-4861475.
STRINGQ99873.

PTM databases

PhosphoSiteQ99873.

Polymorphism databases

DMDM161789011.

Proteomic databases

PRIDEQ99873.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351853; ENSP00000246789; ENSG00000126457.
GeneID3276.
KEGGhsa:3276.
UCSCuc002ppd.2. human.
uc002ppe.2. human.
uc010enf.1. human.

Organism-specific databases

CTD3276.
GeneCardsGC19P050181.
HGNCHGNC:5187. PRMT1.
HPACAB022550.
MIM602950. gene.
neXtProtNX_Q99873.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14340.
GeneTreeENSGT00550000074406.
HOVERGENHBG001793.
InParanoidQ99873.
OrthoDBEOG434W66.
PhylomeDBQ99873.

Gene expression databases

ArrayExpressQ99873.
BgeeQ99873.
CleanExHS_PRMT1.
GenevestigatorQ99873.
GermOnlineENSG00000126457. Homo sapiens.

Family and domain databases

InterProIPR010456. Ribosomal-L11_MeTrfase_PrmA.
[Graphical view]
KOK11434.
PfamPF06325. PrmA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio13013.
SOURCESearch...

Entry information

Entry nameANM1_HUMAN
AccessionPrimary (citable) accession number: Q99873
Secondary accession number(s): Q15529 expand/collapse secondary AC list , Q2VP93, Q6LEU5, Q99872, Q99874, Q9NZ04, Q9NZ05, Q9NZ06
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 99 of the entry and version 2 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

Human chromosome 19

Human chromosome 19: 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

SIMILARITY comments

Index of protein domains and families