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Q99873 (ANM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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) [Reference proteome]
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. Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity. Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Catalytic activity

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. Ref.11 Ref.12 Ref.18

Enzyme regulation

By BTG1, BTG2 and ILF3.

Subunit structure

Homodimer and heterodimer with PRMT8. Individual homodimers can associate to form a homohexamer. Interacts with BTG1, BTG2, NFATC2IP and IFNAR1 By similarity. Interacts with and methylates CHTOP, thereby enabling the interaction of CHTOP with the 5FMC complex By similarity. Interacts with ILF3 and SUPT5H. Interacts with and methylates FOXO1, leading to the nuclear retention of FOXO1 and the stimulation of FOXO1 transcriptional activity. Methylation of FOXO1 is increased upon oxidative stress. Ref.9 Ref.10 Ref.13 Ref.15 Ref.17

Subcellular location

Nucleus. Nucleusnucleoplasm By similarity. Cytoplasmcytosol By similarity. Note: Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction By similarity. Ref.20

Tissue specificity

Widely expressed. Ref.3

Sequence similarities

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

Contains 1 SAM-dependent MTase PRMT-type domain.

Biophysicochemical properties

Kinetic parameters:

KM=1 µM for AdoMet Ref.18

KM=4.2 µM for H4

Vmax=1.2 nmol/min/mg enzyme toward AdoMet

Vmax=1.24 nmol/min/mg enzyme toward H4

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell surface receptor signaling pathway

Traceable author statement PubMed 9029147. Source: ProtInc

histone H4-R3 methylation

Inferred from direct assay Ref.11. Source: UniProtKB

histone methylation

Inferred from direct assay Ref.18. Source: UniProtKB

negative regulation of megakaryocyte differentiation

Inferred from direct assay Ref.21. Source: UniProtKB

neuron projection development

Inferred from mutant phenotype Ref.16. Source: UniProtKB

peptidyl-arginine methylation

Inferred from direct assay Ref.14. Source: UniProtKB

peptidyl-arginine methylation, to asymmetrical-dimethyl arginine

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein methylation

Traceable author statement Ref.1. Source: ProtInc

regulation of transcription, DNA-templated

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytoplasm

Traceable author statement PubMed 9029147. Source: ProtInc

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.9. Source: MGI

   Molecular_functionN-methyltransferase activity

Inferred from direct assay Ref.14. Source: UniProtKB

histone methyltransferase activity

Inferred from direct assay Ref.18. Source: UniProtKB

histone methyltransferase activity (H4-R3 specific)

Inferred from direct assay Ref.11. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 16169070PubMed 23455924. Source: IntAct

methyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein-arginine omega-N asymmetric methyltransferase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 4 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
Isoform 4 (identifier: Q99873-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Protein arginine N-methyltransferase 1
PRO_0000212321

Regions

Domain40 – 361322SAM-dependent MTase PRMT-type

Sites

Active site1521 By similarity
Active site1611 By similarity
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 residue1241N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 1919MENFV…QPPLE → MVGVA in isoform 2.
VSP_005208
Alternative sequence1 – 1919MENFV…QPPLE → M in isoform 3.
VSP_005209
Alternative sequence1 – 1919MENFV…QPPLE → MAAAEAANCIM in isoform 4.
VSP_046334
Natural variant781K → M.
Corresponds to variant rs1804486 [ dbSNP | Ensembl ].
VAR_037501
Natural variant1581L → F.
Corresponds to variant rs11673683 [ dbSNP | Ensembl ].
VAR_037502

Experimental info

Mutagenesis821V → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. Ref.15
Mutagenesis831L → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. Ref.15
Mutagenesis841D → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. Ref.15
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
Sequence conflict2021K → E in BAG65435. Ref.4

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
Isoform 4 [UniParc].

Checksum: 1704BA3762F3E264
Show »

FASTA35340,548

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[4]"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 4).
Tissue: Uterus.
[5]"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).
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 3 AND 4).
Tissue: Lung.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ILF3.
[10]"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] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[11]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY.
[12]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY.
[13]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUPT5H.
[14]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Arginine methylation of FOXO transcription factors inhibits their phosphorylation by Akt."
Yamagata K., Daitoku H., Takahashi Y., Namiki K., Hisatake K., Kako K., Mukai H., Kasuya Y., Fukamizu A.
Mol. Cell 32:221-231(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FOXO1, MUTAGENESIS OF VAL-82; LEU-83 AND ASP-84.
[16]"PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells."
Miyata S., Mori Y., Tohyama M.
Neurosci. Lett. 445:162-165(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EWS AND PRMT8.
[18]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[19]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[21]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"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].
+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.
AK304660 mRNA. Translation: BAG65435.1.
CR407608 mRNA. Translation: CAG28536.1.
AC011495 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52521.1.
BC019268 mRNA. Translation: AAH19268.2.
BC109282 mRNA. Translation: AAI09283.2.
BC109283 mRNA. Translation: AAI09284.2.
RefSeqNP_001527.3. NM_001536.5.
NP_938074.2. NM_198318.4.
UniGeneHs.20521.

3D structure databases

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

Protein-protein interaction databases

BioGrid109512. 125 interactions.
DIPDIP-30878N.
IntActQ99873. 71 interactions.
MINTMINT-4861475.

Chemistry

BindingDBQ99873.
ChEMBLCHEMBL5524.

PTM databases

PhosphoSiteQ99873.

Polymorphism databases

DMDM161789011.

Proteomic databases

PaxDbQ99873.
PRIDEQ99873.

Protocols and materials databases

DNASU3276.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000391851; ENSP00000375724; ENSG00000126457. [Q99873-4]
GeneID3276.
KEGGhsa:3276.
UCSCuc002ppe.3. human.
uc021uxu.1. human. [Q99873-2]

Organism-specific databases

CTD3276.
GeneCardsGC19P050181.
HGNCHGNC:5187. PRMT1.
HPACAB022550.
MIM602950. gene.
neXtProtNX_Q99873.
PharmGKBPA29461.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0500.
HOVERGENHBG001793.
InParanoidQ99873.
KOK11434.
PhylomeDBQ99873.

Enzyme and pathway databases

SABIO-RKQ99873.
SignaLinkQ99873.

Gene expression databases

ArrayExpressQ99873.
BgeeQ99873.
CleanExHS_PRMT1.
GenevestigatorQ99873.

Family and domain databases

InterProIPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
[Graphical view]
PANTHERPTHR11006. PTHR11006. 1 hit.
PfamPF13847. Methyltransf_31. 1 hit.
[Graphical view]
PROSITEPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRMT1. human.
GeneWikiPRMT1.
GenomeRNAi3276.
NextBio13013.
PROQ99873.
SOURCESearch...

Entry information

Entry nameANM1_HUMAN
AccessionPrimary (citable) accession number: Q99873
Secondary accession number(s): B4E3C3 expand/collapse secondary AC list , G5E9B6, Q15529, Q2VP93, Q6LEU5, Q8WUW5, Q99872, Q99874, Q9NZ04, Q9NZ05, Q9NZ06
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 4, 2007
Last modified: April 16, 2014
This is version 124 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

SIMILARITY comments

Index of protein domains and families

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 19

Human chromosome 19: entries, gene names and cross-references to MIM