O60678 (ANM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein arginine N-methyltransferase 3
EC=2.1.1.-

Alternative name(s):
Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3

Gene names

Name:	PRMT3
Synonyms:	HRMT1L3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.
Enzyme regulation	Inhibited by N-ethylmaleimide and high concentrations of zinc chloride By similarity.
Subunit structure	May exist as a monomer or homodimer By similarity.
Subcellular location	Cytoplasm.
Domain	The zinc-finger is responsible for substrate specificity By similarity.
Sequence similarities	Belongs to the protein arginine N-methyltransferase family. Contains 1 C2H2-type zinc finger.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Non-traceable author statement Ref.4. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara ribosome Inferred from electronic annotation. Source: Compara
Molecular_function	protein-arginine N-methyltransferase activity Non-traceable author statement Ref.4. Source: UniProtKB protein-arginine omega-N asymmetric methyltransferase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O60678-1)

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: O60678-2)

The sequence of this isoform differs from the canonical sequence as follows:
     11-99: GRGAVENEED...IKLINFIRLK → YSHLLKKHFHTVSLSISLILTAWFINM

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 531

531

Protein arginine N-methyltransferase 3

PRO_0000212326

Regions

Zinc finger

48 – 71

24

C2H2-type

Sites

Active site

329

1

By similarity

Active site

338

1

By similarity

Binding site

230

1

S-adenosyl-L-methionine By similarity

Binding site

239

1

S-adenosyl-L-methionine

Binding site

263

1

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

285

1

S-adenosyl-L-methionine

Binding site

314

1

S-adenosyl-L-methionine

Amino acid modifications

Modified residue

25

1

Phosphoserine Ref.6 Ref.7 Ref.9

Modified residue

27

1

Phosphoserine Ref.6 Ref.7 Ref.9

Natural variations

Alternative sequence

11 – 99

89

GRGAV…FIRLK → YSHLLKKHFHTVSLSISLIL TAWFINM in isoform 2.

VSP_040330

Natural variant

440

1

L → V.
Corresponds to variant rs3758805 [ dbSNP | Ensembl ].

VAR_024584

Natural variant

470

1

S → C.
Corresponds to variant rs11025585 [ dbSNP | Ensembl ].

VAR_030943

Natural variant

508

1

S → N. Ref.1 Ref.3 Ref.4
Corresponds to variant rs6483700 [ dbSNP | Ensembl ].

VAR_024585

Experimental info

Sequence conflict

21

1

L → E in AAC39837. Ref.4

Sequence conflict

103

1

V → F in BAG62289. Ref.1

Sequence conflict

510

1

K → R in BAG62289. Ref.1

Secondary structure

1

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531

Helix Strand Turn

Details...

Helix

223 – 225

3

Helix

227 – 234

8

Helix

237 – 249

13

Helix

251 – 253

3

Turn

254 – 256

3

Beta strand

258 – 263

6

Helix

268 – 275

8

Beta strand

279 – 287

9

Helix

289 – 299

11

Turn

303 – 305

3

Beta strand

306 – 311

6

Turn

313 – 315

3

Beta strand

319 – 321

3

Beta strand

323 – 328

6

Turn

336 – 338

3

Helix

340 – 351

12

Beta strand

352 – 360

9

Beta strand

362 – 370

9

Helix

373 – 379

7

Helix

381 – 384

4

Helix

392 – 394

3

Helix

395 – 398

4

Beta strand

403 – 405

3

Helix

409 – 411

3

Beta strand

417 – 423

7

Turn

424 – 426

3

Helix

429 – 432

4

Beta strand

433 – 442

10

Beta strand

446 – 459

14

Beta strand

467 – 470

4

Beta strand

482 – 493

12

Beta strand

498 – 507

10

Beta strand

514 – 521

8

Beta strand

524 – 530

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: D02159E2BEDBE7B9	FASTA	531	59,876
	10 20 30 40 50 60 MCSLASGATG GRGAVENEED LPELSDSGDE AAWEDEDDAD LPHGKQQTPC LFCNRLFTSA 70 80 90 100 110 120 EETFSHCKSE HQFNIDSMVH KHGLEFYGYI KLINFIRLKN PTVEYMNSIY NPVPWEKEEY 130 140 150 160 170 180 LKPVLEDDLL LQFDVEDLYE PVSVPFSYPN GLSENTSVVE KLKHMEARAL SAEAALARAR 190 200 210 220 230 240 EDLQKMKQFA QDFVMHTDVR TCSSSTSVIA DLQEDEDGVY FSSYGHYGIH EEMLKDKIRT 250 260 270 280 290 300 ESYRDFIYQN PHIFKDKVVL DVGCGTGILS MFAAKAGAKK VLGVDQSEIL YQAMDIIRLN 310 320 330 340 350 360 KLEDTITLIK GKIEEVHLPV EKVDVIISEW MGYFLLFESM LDSVLYAKNK YLAKGGSVYP 370 380 390 400 410 420 DICTISLVAV SDVNKHADRI AFWDDVYGFK MSCMKKAVIP EAVVEVLDPK TLISEPCGIK 430 440 450 460 470 480 HIDCHTTSIS DLEFSSDFTL KITRTSMCTA IAGYFDIYFE KNCHNRVVFS TGPQSTKTHW 490 500 510 520 530 KQTVFLLEKP FSVKAGEALK GKVTVHKSKK DPRSLTVTLT LNNSTQTYGL Q
	Isoform 2 [UniParc]. Checksum: 4A67AC40A78A7B01	FASTA	469	52,875
	10 20 30 40 50 60 MCSLASGATG YSHLLKKHFH TVSLSISLIL TAWFINMNPT VEYMNSIYNP VPWEKEEYLK 70 80 90 100 110 120 PVLEDDLLLQ FDVEDLYEPV SVPFSYPNGL SENTSVVEKL KHMEARALSA EAALARARED 130 140 150 160 170 180 LQKMKQFAQD FVMHTDVRTC SSSTSVIADL QEDEDGVYFS SYGHYGIHEE MLKDKIRTES 190 200 210 220 230 240 YRDFIYQNPH IFKDKVVLDV GCGTGILSMF AAKAGAKKVL GVDQSEILYQ AMDIIRLNKL 250 260 270 280 290 300 EDTITLIKGK IEEVHLPVEK VDVIISEWMG YFLLFESMLD SVLYAKNKYL AKGGSVYPDI 310 320 330 340 350 360 CTISLVAVSD VNKHADRIAF WDDVYGFKMS CMKKAVIPEA VVEVLDPKTL ISEPCGIKHI 370 380 390 400 410 420 DCHTTSISDL EFSSDFTLKI TRTSMCTAIA GYFDIYFEKN CHNRVVFSTG PQSTKTHWKQ 430 440 450 460 TVFLLEKPFS VKAGEALKGK VTVHKSKKDP RSLTVTLTLN NSTQTYGLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , 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 2), VARIANT ASN-508.
[2]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-508. Tissue: Brain.
[4]	"PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation." Tang J., Gary J.D., Clarke S., Herschman H.R. J. Biol. Chem. 273:16935-16945(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-531 (ISOFORM 1), VARIANT ASN-508.
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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].
[9]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, MASS SPECTROMETRY.
[10]	"The crystal structure of human HMT1 HNRNP methyltransferase-like 3 in complex with SAH." Structural genomics consortium (SGC) Submitted (MAR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 211-531 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK300591 mRNA. Translation: BAG62289.1.
AC025972 Genomic DNA. No translation available.
AC108005 Genomic DNA. No translation available.
BC037544 mRNA. Translation: AAH37544.1.
BC064831 mRNA. Translation: AAH64831.1.
AF059531 mRNA. Translation: AAC39837.1.

IPI

IPI00401321.
IPI00909714.

RefSeq

NP_005779.1. NM_005788.3.

UniGene

Hs.152337.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FYT	X-ray	2.00	A	211-531	[»]
3SMQ	X-ray	2.00	A	211-531	[»]
4HSG	X-ray	2.30	A	211-531	[»]

ProteinModelPortal

O60678.

SMR

O60678. Positions 43-147, 221-531.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60678. 1 interaction.

MINT

MINT-6803908.

STRING

9606.ENSP00000331879.

PTM databases

PhosphoSite

O60678.

Proteomic databases

PaxDb

O60678.

PRIDE

O60678.

Protocols and materials databases

DNASU

10196.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000331079; ENSP00000331879; ENSG00000185238.
ENST00000437750; ENSP00000397766; ENSG00000185238.

GeneID

10196.

KEGG

hsa:10196.

UCSC

uc001mqb.3. human.
uc010rdn.2. human.

Organism-specific databases

CTD

10196.

GeneCards

GC11P020373.

HGNC

HGNC:30163. PRMT3.

HPA

CAB022083.
HPA007832.

MIM

603190. gene.

neXtProt

NX_O60678.

PharmGKB

PA29462.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0500.

HOGENOM

HOG000198521.

HOVERGEN

HBG001793.

KO

K11436.

OMA

ITKTSMC.

Enzyme and pathway databases

SABIO-RK

O60678.

Gene expression databases

ArrayExpress

O60678.

Bgee

O60678.

CleanEx

HS_PRMT3.

Genevestigator

O60678.

GermOnline

ENSG00000185238. Homo sapiens.

Family and domain databases

InterPro

IPR025799. Arg_MeTrfase.
IPR010456. Ribosomal-L11_MeTrfase_PrmA.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]

PANTHER

PTHR11006. PTHR11006. 1 hit.

Pfam

PF06325. PrmA. 1 hit.
[Graphical view]

SMART

SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O60678.

ChEMBL

CHEMBL5891.

EvolutionaryTrace

O60678.

GenomeRNAi

10196.

NextBio

38588.

SOURCE

Search...

Entry information

Entry name

ANM3_HUMAN

Accession

Primary (citable) accession number: O60678
Secondary accession number(s): B4DUC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 11, 2011
Last modified:	April 3, 2013
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.