Reviewed, UniProtKB/Swiss-Prot P55345 (ANM2_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein arginine N-methyltransferase 2
    EC=2.1.1.-

Gene names

Name:	PRMT2
Synonyms:	HMT1, HRMT1L1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably methylates the guanidino nitrogens of arginyl residues in some proteins. May play a role in transcriptional coactivation.
Subunit structure	Interacts with NCOA6 coactivator. Interacts (via SH3 domain) with PRMT8. Ref.5
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the protein arginine N-methyltransferase family. Contains 1 SH3 domain.

Ontologies

Keywords
Domain	SH3 domain
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein amino acid methylation Ref.1 Traceable author statement. Source: ProtInc signal transduction Ref.1 Traceable author statement. Source: ProtInc
Cellular component	nucleus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	identical protein binding Ref.5 Inferred from physical interaction. Source: IntAct methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-78458,EBI-78458
BAT2	P48634	1	EBI-78458,EBI-347545
E2F1	Q01094	1	EBI-78458,EBI-448924
ESR1	P03372	2	EBI-78458,EBI-78473
ESR2	Q92731	1	EBI-78458,EBI-78505
NCOA6	Q14686	1	EBI-78458,EBI-78670
NPM1	P06748	1	EBI-78458,EBI-78579
PGR	P06401	1	EBI-78458,EBI-78539
PPARA	Q07869	1	EBI-78458,EBI-78615
RB1	P06400	3	EBI-78458,EBI-491274
RXRA	P19793	1	EBI-78458,EBI-78598
SCARB1	Q8WTV0	1	EBI-78458,EBI-78657
THRB	P10828	1	EBI-78458,EBI-78558

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 433

433

Protein arginine N-methyltransferase 2

PRO_0000212324

Regions

Domain

30 – 89

60

SH3

Sites

Binding site

112

1

S-adenosyl-L-methionine By similarity

Binding site

121

1

S-adenosyl-L-methionine By similarity

Binding site

145

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Binding site

168

1

S-adenosyl-L-methionine By similarity

Binding site

197

1

S-adenosyl-L-methionine By similarity

Experimental info

Sequence conflict

256 – 260

5

KDYRS → RIIVA in AAB48437. Ref.2

Sequence conflict

402

1

R → I in AAH00727. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

433

Helix Strand Turn

Details...

Beta strand

34 – 39

6

Beta strand

56 – 61

6

Beta strand

64 – 71

8

Beta strand

77 – 85

9

Sequences

	Sequence		Length	Mass (Da)
	P55345-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 6DEE0350C15ECD4F	FASTA	433	49,042
	10 20 30 40 50 60 MATSGDCPRS ESQGEEPAEC SEAGLLQEGV QPEEFVAIAD YAATDETQLS FLRGEKILIL 70 80 90 100 110 120 RQTTADWWWG ERAGCCGYIP ANHVGKHVDE YDPEDTWQDE EYFGSYGTLK LHLEMLADQP 130 140 150 160 170 180 RTTKYHSVIL QNKESLTDKV ILDVGCGTGI ISLFCAHYAR PRAVYAVEAS EMAQHTGQLV 190 200 210 220 230 240 LQNGFADIIT VYQQKVEDVV LPEKVDVLVS EWMGTCLLFE FMIESILYAR DAWLKEDGVI 250 260 270 280 290 300 WPTMAALHLV PCSADKDYRS KVLFWDNAYE FNLSALKSLA VKEFFSKPKY NHILKPEDCL 310 320 330 340 350 360 SEPCTILQLD MRTVQISDLE TLRGELRFDI RKAGTLHGFT AWFSVHFQSL QEGQPPQVLS 370 380 390 400 410 420 TGPFHPTTHW KQTLFMMDDP VPVHTGDVVT GSVVLQRNPV WRRHMSVALS WAVTSRQDPT 430 SQKVGEKVFP IWR

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].
[2]	"Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene." Katsanis N., Yaspo M.-L., Fisher E.M.C. Mamm. Genome 8:526-529(1997) [PubMed: 9196002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: Kidney.
[4]	The European IMAGE consortium Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-277.
[5]	"Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha." Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J. J. Biol. Chem. 277:28624-28630(2002) [PubMed: 12039952] [Abstract] Cited for: INTERACTION WITH NCOA6.
[6]	"Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain." Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G. J. Biol. Chem. 282:36444-36453(2007) [PubMed: 17925405] [Abstract] Cited for: INTERACTION WITH PRMT8.
[7]	"Solution structure of the SH3 domain of the protein arginine N-methyltransferase 2." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 33-87.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X99209 mRNA. Translation: CAA67599.1.
U80213 mRNA. Translation: AAB48437.1.
BC000727 mRNA. Translation: AAH00727.1.
AL109794 mRNA. Translation: CAB52454.1.

IPI

IPI00297265.

RefSeq

NP_001526.2.
NP_996845.1.

UniGene

Hs.154163

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X2P	NMR	-	A	33-87	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P55345. 14 interactions.

Proteomic databases

PRIDE

P55345.

Genome annotation databases

Ensembl

ENSG00000160310. Homo sapiens. [Contig view]

GeneID

3275.

KEGG

hsa:3275.

Organism-specific databases

GeneCards

GC21P046880.

H-InvDB

HIX0016196.

HGNC

HGNC:5186. PRMT2.

MIM

601961. gene.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P55345.

HOVERGEN

P55345.

OMA

P55345. SLFCAHH.

Gene expression databases

ArrayExpress

P55345.

Bgee

P55345.

CleanEx

HS_PRMT2.

GermOnline

ENSG00000160310. Homo sapiens.

Family and domain databases

InterPro

IPR001452. SH3_domain.
IPR007848. Small_mtfrase.
[Graphical view]

Pfam

PF05175. MTS. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

ProDom

PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00326. SH3. 1 hit.
[Graphical view]

PROSITE

PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

13007.

SOURCE

Search...

Entry information

Entry name

ANM2_HUMAN

Accession

Primary (citable) accession number: P55345
Secondary accession number(s): P78350, Q9BW15, Q9UMC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)