Reviewed, UniProtKB/Swiss-Prot Q99873 (ANM1_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein arginine N-methyltransferase 1
    EC=2.1.1.-
Alternative name(s):
    Interferon receptor 1-bound protein 4

Gene names

Name:	PRMT1
Synonyms:	HMT2, HRMT1L2, IR1B4

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H and EWS. Ref.8 Ref.10
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.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the protein arginine N-methyltransferase family.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell surface receptor linked signal transduction Traceable author statement. Source: ProtInc protein amino acid methylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Traceable author statement. Source: ProtInc nucleus Ref.6 Inferred from direct assay. Source: MGI
Molecular function	N-methyltransferase activity Traceable author statement. Source: ProtInc protein binding Ref.6 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DHX9	Q08211	1	EBI-78738,EBI-352022
HABP4	Q9NYJ2	1	EBI-78738,EBI-710278
ILF3	Q12906	2	EBI-78738,EBI-78756
SSSCA1	O60232	1	EBI-78738,EBI-741415

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 361	361	Protein arginine N-methyltransferase 1		PRO_0000212321
Sites
	Binding site	53	1	S-adenosyl-L-methionine By similarity
	Binding site	62	1	S-adenosyl-L-methionine By similarity
	Binding site	86	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	108	1	S-adenosyl-L-methionine By similarity
	Binding site	137	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	299	1	Phosphotyrosine Ref.9
Natural variations
	Alternative sequence	1 – 19	19	MENFV…QPPLE → MVGVA in isoform 2.		VSP_005208
	Alternative sequence	1 – 19	19	MENFV…QPPLE → M in isoform 3.		VSP_005209
	Natural variant	78	1	K → M: dbSNP rs1804486.		VAR_037501
	Natural variant	158	1	L → F: dbSNP rs11673683.		VAR_037502
Experimental info
	Sequence conflict	108	1	E → V in CAA71763. Ref.1
	Sequence conflict	108	1	E → V in CAA71764. Ref.1
	Sequence conflict	108	1	E → V in CAA71765. Ref.1
	Sequence conflict	108	1	E → V in BAA11029. Ref.2
	Sequence conflict	147 – 175	29	DIIIS…RDKWL → ASSSASGWATASSTSPCSTP CSMPGTSV in BAA11029. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (V2) [UniParc]. Last modified December 4, 2007. Version 2. Checksum: A286D99B5AFC1860	FASTA	361	41,516
	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
	Isoform 2 (V3). Checksum: 2546A25EF744E265	FASTA	347	39,929
	10 20 30 40 50 60 MVGVAEVSCG QAESSEKPNA EDMTSKDYYF DSYAHFGIHE EMLKDEVRTL TYRNSMFHNR 70 80 90 100 110 120 HLFKDKVVLD VGSGTGILCM FAAKAGARKV IGIECSSISD YAVKIVKANK LDHVVTIIKG 130 140 150 160 170 180 KVEEVELPVE KVDIIISEWM GYCLFYESML NTVLYARDKW LAPDGLIFPD RATLYVTAIE 190 200 210 220 230 240 DRQYKDYKIH WWENVYGFDM SCIKDVAIKE PLVDVVDPKQ LVTNACLIKE VDIYTVKVED 250 260 270 280 290 300 LTFTSPFCLQ VKRNDYVHAL VAYFNIEFTR CHKRTGFSTS PESPYTHWKQ TVFYMEDYLT 310 320 330 340 VKTGEEIFGT IGMRPNAKNN RDLDFTIDLD FKGQLCELSC STDYRMR
	Isoform 3 (V1). Checksum: DFC413AC52F49754	FASTA	343	39,602
	10 20 30 40 50 60 MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK DEVRTLTYRN SMFHNRHLFK 70 80 90 100 110 120 DKVVLDVGSG TGILCMFAAK AGARKVIGIE CSSISDYAVK IVKANKLDHV VTIIKGKVEE 130 140 150 160 170 180 VELPVEKVDI IISEWMGYCL FYESMLNTVL YARDKWLAPD GLIFPDRATL YVTAIEDRQY 190 200 210 220 230 240 KDYKIHWWEN VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY TVKVEDLTFT 250 260 270 280 290 300 SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY MEDYLTVKTG 310 320 330 340 EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY RMR

References

	« Hide 'large scale' referencesShow '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]	"Molecular characterization, mapping and tissue expression of the human protein arginine N-methyltransferase 1 (PRMT1/HRMT1L2) gene." Scorilas A., Black M.H., Diamandis E.P. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[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 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).
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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. , 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.
[10]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. BC109282 mRNA. Translation: AAI09283.2. BC109283 mRNA. Translation: AAI09284.2.
IPI	IPI00018522. IPI00215734. IPI00914913.
RefSeq	NP_001527.3. NP_938075.2.
UniGene	Hs.20521
3D structure databases
HSSP	HSSP built from PDB template 1ORI based on UniProtKB Q63009.
SMR	Q99873. Positions 49-361.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99873. 29 interactions.
STRING	Q99873.
PTM databases
PhosphoSite	Q99873.
Proteomic databases
PRIDE	Q99873.
Genome annotation databases
Ensembl	ENST00000351853; ENSP00000246789; ENSG00000126457; Homo sapiens. [Genome view] ENST00000391849; ENSP00000375723; ENSG00000126457; Homo sapiens. [Genome view] ENST00000391851; ENSP00000375724; ENSG00000126457; Homo sapiens. [Genome view] ENST00000408976; ENSP00000386204; ENSG00000126457; Homo sapiens. [Genome view] ENST00000419451; ENSP00000401618; ENSG00000126457; Homo sapiens. [Genome view] ENST00000449059; ENSP00000388162; ENSG00000126457; Homo sapiens. [Genome view] ENST00000454376; ENSP00000406162; ENSG00000126457; Homo sapiens. [Genome view]
GeneID	3276.
KEGG	hsa:3276.
UCSC	uc002ppd.2. human. uc002ppe.2. human. uc010enf.1. human.
Organism-specific databases
CTD	3276.
GeneCards	GC19P054873.
H-InvDB	HIX0039961.
HGNC	HGNC:5187. PRMT1.
HPA	CAB022550.
MIM	602950. gene.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q99873.
Gene expression databases
ArrayExpress	Q99873.
Bgee	Q99873.
CleanEx	HS_PRMT1.
Genevestigator	Q99873.
GermOnline	ENSG00000126457. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	13013.
SOURCE	Search...

Entry information

Entry name

ANM1_HUMAN

Accession

Primary (citable) accession number: Q99873
Secondary accession number(s): Q15529 , 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:	October 13, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.