Q9NVM4 (ANM7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein arginine N-methyltransferase 7
EC=2.1.1.-

Alternative name(s):
Histone-arginine N-methyltransferase PRMT7
EC=2.1.1.125
[Myelin basic protein]-arginine N-methyltransferase PRMT7
EC=2.1.1.126

Gene names

Name:	PRMT7
Synonyms:	KIAA1933

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	692 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo. Ref.4 Ref.5 Ref.6 Ref.9
Catalytic activity	S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. S-adenosyl-L-methionine + [myelin basic protein]-arginine = S-adenosyl-L-homocysteine + [myelin basic protein]-N(omega)-methyl-arginine.
Subunit structure	Homodimer and heterodimer By similarity. Interacts with CTCFL By similarity. Interacts with PRMT5 and SNRPD3. Ref.6
Subcellular location	Cytoplasm › cytosol. Nucleus Ref.5.
Miscellaneous	May be involved in etoposide-induced cytotoxicity, a chemotherapeutic agent frequently used for testicular cancer and small-cell lung cancer that can cause cytotoxicity in the treatment of other cancers. Down-regulation confers increased sensitivity to the Top1 inhibitor camptothecin (CPT).
Sequence similarities	Belongs to the protein arginine N-methyltransferase family. PRMT7 subfamily.
Sequence caution	The sequence BAB14215.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Differentiation Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA methylation involved in gamete generation Inferred from sequence or structural similarity. Source: UniProtKB cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW regulation of gene expression by genetic imprinting Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein binding Inferred by curator Ref.4. Source: HGNC regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW spliceosomal snRNP assembly Inferred from mutant phenotype Ref.6. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay Ref.5. Source: UniProtKB nucleus Inferred from direct assay Ref.5. Source: UniProtKB
Molecular function	[myelin basic protein]-arginine N-methyltransferase activity Inferred from direct assay Ref.5. Source: HGNC histone binding Inferred by curator Ref.5. Source: HGNC histone methyltransferase activity (H4-R3 specific) Inferred from sequence or structural similarity. Source: UniProtKB protein-arginine omega-N monomethyltransferase activity Inferred from direct assay Ref.9. Source: UniProtKB protein-arginine omega-N symmetric methyltransferase activity Inferred from direct assay Ref.9. Source: UniProtKB ribonucleoprotein complex binding Inferred from physical interaction Ref.6. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NVM4-1)

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: Q9NVM4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     95-168: Missing.
     399-472: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9NVM4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     45-94: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9NVM4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     526-567: DLWRIRSPCG...SREAEPHPLW → VCREQQDVPL...GPVADPEPLW
     568-692: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 692	692	Protein arginine N-methyltransferase 7		PRO_0000212335
Natural variations
	Alternative sequence	45 – 94	50	Missing in isoform 3.		VSP_037253
	Alternative sequence	95 – 168	74	Missing in isoform 2.		VSP_005213
	Alternative sequence	399 – 472	74	Missing in isoform 2.		VSP_005214
	Alternative sequence	526 – 567	42	DLWRI…PHPLW → VCREQQDVPLVLAATLPCVL AGGCGWGCSFLTGPVADPEP LW in isoform 4.		VSP_037254
	Alternative sequence	568 – 692	125	Missing in isoform 4.		VSP_037255
Experimental info
	Sequence conflict	218	1	S → G in BAG53431. Ref.1
	Sequence conflict	246	1	P → L in BAG53431. Ref.1
	Sequence conflict	258	1	S → G in BAG51772. Ref.1
	Sequence conflict	633	1	A → S in BAB14215. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 9E0DB9530154231C	FASTA	692	78,459
	10 20 30 40 50 60 MKIFCSRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNVKYYQ GIRAAVSRVK 70 80 90 100 110 120 DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA DAAVKIVEKN GFSDKIKVIN 130 140 150 160 170 180 KHSTEVTVGP EGDMPCRANI LVTELFDTEL IGEGALPSYE HAHRHLVEEN CEAVPHRATV 190 200 210 220 230 240 YAQLVESGRM WSWNKLFPIH VQTSLGEQVI VPPVDVESCP GAPSVCDIQL NQVSPADFTV 250 260 270 280 290 300 LSDVLPMFSI DFSKQVSSSA ACHSRRFEPL TSGRAQVVLS WWDIEMDPEG KIKCTMAPFW 310 320 330 340 350 360 AHSDPEEMQW RDHWMQCVYF LPQEEPVVQG SALYLVAHHD DYCVWYSLQR TSPEKNERVR 370 380 390 400 410 420 QMRPVCDCQA HLLWNRPRFG EINDQDRTDR YVQALRTVLK PDSVCLCVSD GSLLSVLAHH 430 440 450 460 470 480 LGVEQVFTVE SSAASHKLLR KIFKANHLED KINIIEKRPE LLTNEDLQGR KVSLLLGEPF 490 500 510 520 530 540 FTTSLLPWHN LYFWYVRTAV DQHLGPGAMV MPQAASLHAV VVEFRDLWRI RSPCGDCEGF 550 560 570 580 590 600 DVHIMDDMIK RALDFRESRE AEPHPLWEYP CRSLSEPWQI LTFDFQQPVP LQPLCAEGTV 610 620 630 640 650 660 ELRRPGQSHA AVLWMEYHLT PECTLSTGLL EPADPEGGCC WNPHCKQAVY FFSPAPDPRA 670 680 690 LLGGPRTVSY AVEFHPDTGD IIMEFRHADT PD
	Isoform 2 [UniParc]. Checksum: F979828D17B27191	FASTA	544	62,118
	10 20 30 40 50 60 MKIFCSRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNVKYYQ GIRAAVSRVK 70 80 90 100 110 120 DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEENCEAV PHRATVYAQL VESGRMWSWN 130 140 150 160 170 180 KLFPIHVQTS LGEQVIVPPV DVESCPGAPS VCDIQLNQVS PADFTVLSDV LPMFSIDFSK 190 200 210 220 230 240 QVSSSAACHS RRFEPLTSGR AQVVLSWWDI EMDPEGKIKC TMAPFWAHSD PEEMQWRDHW 250 260 270 280 290 300 MQCVYFLPQE EPVVQGSALY LVAHHDDYCV WYSLQRTSPE KNERVRQMRP VCDCQAHLLW 310 320 330 340 350 360 NRPRFGEIND QDRTDRYVQA LRTVSLLLGE PFFTTSLLPW HNLYFWYVRT AVDQHLGPGA 370 380 390 400 410 420 MVMPQAASLH AVVVEFRDLW RIRSPCGDCE GFDVHIMDDM IKRALDFRES REAEPHPLWE 430 440 450 460 470 480 YPCRSLSEPW QILTFDFQQP VPLQPLCAEG TVELRRPGQS HAAVLWMEYH LTPECTLSTG 490 500 510 520 530 540 LLEPADPEGG CCWNPHCKQA VYFFSPAPDP RALLGGPRTV SYAVEFHPDT GDIIMEFRHA DTPD
	Isoform 3 [UniParc]. Checksum: 6CF17C684932B869	FASTA	642	73,154
	10 20 30 40 50 60 MKIFCSRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRVFKPMA DAAVKIVEKN 70 80 90 100 110 120 GFSDKIKVIN KHSTEVTVGP EGDMPCRANI LVTELFDTEL IGEGALPSYE HAHRHLVEEN 130 140 150 160 170 180 CEAVPHRATV YAQLVESGRM WSWNKLFPIH VQTSLGEQVI VPPVDVESCP GAPSVCDIQL 190 200 210 220 230 240 NQVSPADFTV LSDVLPMFSI DFSKQVSSSA ACHSRRFEPL TSGRAQVVLS WWDIEMDPEG 250 260 270 280 290 300 KIKCTMAPFW AHSDPEEMQW RDHWMQCVYF LPQEEPVVQG SALYLVAHHD DYCVWYSLQR 310 320 330 340 350 360 TSPEKNERVR QMRPVCDCQA HLLWNRPRFG EINDQDRTDR YVQALRTVLK PDSVCLCVSD 370 380 390 400 410 420 GSLLSVLAHH LGVEQVFTVE SSAASHKLLR KIFKANHLED KINIIEKRPE LLTNEDLQGR 430 440 450 460 470 480 KVSLLLGEPF FTTSLLPWHN LYFWYVRTAV DQHLGPGAMV MPQAASLHAV VVEFRDLWRI 490 500 510 520 530 540 RSPCGDCEGF DVHIMDDMIK RALDFRESRE AEPHPLWEYP CRSLSEPWQI LTFDFQQPVP 550 560 570 580 590 600 LQPLCAEGTV ELRRPGQSHA AVLWMEYHLT PECTLSTGLL EPADPEGGCC WNPHCKQAVY 610 620 630 640 FFSPAPDPRA LLGGPRTVSY AVEFHPDTGD IIMEFRHADT PD
	Isoform 4 [UniParc]. Checksum: A283D1FC9EBA086C	FASTA	567	63,806
	10 20 30 40 50 60 MKIFCSRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNVKYYQ GIRAAVSRVK 70 80 90 100 110 120 DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA DAAVKIVEKN GFSDKIKVIN 130 140 150 160 170 180 KHSTEVTVGP EGDMPCRANI LVTELFDTEL IGEGALPSYE HAHRHLVEEN CEAVPHRATV 190 200 210 220 230 240 YAQLVESGRM WSWNKLFPIH VQTSLGEQVI VPPVDVESCP GAPSVCDIQL NQVSPADFTV 250 260 270 280 290 300 LSDVLPMFSI DFSKQVSSSA ACHSRRFEPL TSGRAQVVLS WWDIEMDPEG KIKCTMAPFW 310 320 330 340 350 360 AHSDPEEMQW RDHWMQCVYF LPQEEPVVQG SALYLVAHHD DYCVWYSLQR TSPEKNERVR 370 380 390 400 410 420 QMRPVCDCQA HLLWNRPRFG EINDQDRTDR YVQALRTVLK PDSVCLCVSD GSLLSVLAHH 430 440 450 460 470 480 LGVEQVFTVE SSAASHKLLR KIFKANHLED KINIIEKRPE LLTNEDLQGR KVSLLLGEPF 490 500 510 520 530 540 FTTSLLPWHN LYFWYVRTAV DQHLGPGAMV MPQAASLHAV VVEFRVCREQ QDVPLVLAAT 550 560 LPCVLAGGCG WGCSFLTGPV ADPEPLW

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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). Tissue: Brain, Spleen and Uterus.
[2]	"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 1). Tissue: Placenta.
[3]	"Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins." Nagase T., Kikuno R., Ohara O. DNA Res. 8:179-187(2001) [PubMed: 11572484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-692 (ISOFORM 2). Tissue: Brain.
[4]	"PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity." Miranda T.B., Miranda M., Frankel A., Clarke S. J. Biol. Chem. 279:22902-22907(2004) [PubMed: 15044439] [Abstract] Cited for: FUNCTION.
[5]	"PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine." Lee J.-H., Cook J.R., Yang Z.-H., Mirochnitchenko O., Gunderson S.I., Felix A.M., Herth N., Hoffmann R., Pestka S. J. Biol. Chem. 280:3656-3664(2005) [PubMed: 15494416] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins." Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I., Matera A.G. J. Cell Biol. 178:733-740(2007) [PubMed: 17709427] [Abstract] Cited for: FUNCTION, INTERACTION WITH PRMT5 AND SNRPD3.
[7]	"Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential target for the sensitization of tumor cells to camptothecins." Verbiest V., Montaudon D., Tautu M.T., Moukarzel J., Portail J.-P., Markovits J., Robert J., Ichas F., Pourquier P. FEBS Lett. 582:1483-1489(2008) [PubMed: 18381071] [Abstract] Cited for: INCREASED SENSITIVITY TO CAMPTOTHECIN.
[8]	"Identification of genomic regions contributing to etoposide-induced cytotoxicity." Bleibel W.K., Duan S., Huang R.S., Kistner E.O., Shukla S.J., Wu X., Badner J.A., Dolan M.E. Hum. Genet. 125:173-180(2009) [PubMed: 19089452] [Abstract] Cited for: POSSIBLE INVOLVEMENT IN ETOPOSIDE-INDUCED CYTOTOXICITY.
[9]	"Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry." Wang H., Straubinger R.M., Aletta J.M., Cao J., Duan X., Yu H., Qu J. J. Am. Soc. Mass Spectrom. 20:507-519(2009) [PubMed: 19110445] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK001502 mRNA. Translation: BAA91726.1. AK022739 mRNA. Translation: BAB14215.1. Different initiation. AK056647 mRNA. Translation: BAG51772.1. AK097175 mRNA. Translation: BAG53431.1. AK304605 mRNA. Translation: BAG65391.1. BC000146 mRNA. Translation: AAH00146.1. AB067520 mRNA. Translation: BAB67826.1.
IPI	IPI00004567. IPI00219090. IPI00643634. IPI00909654.
RefSeq	NP_001171753.1. NM_001184824.1. NP_061896.1. NM_019023.2.
UniGene	Hs.653193.
3D structure databases
ProteinModelPortal	Q9NVM4.
SMR	Q9NVM4. Positions 62-178.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NVM4. 1 interaction.
STRING	Q9NVM4.
Polymorphism databases
DMDM	20137529.
Proteomic databases
PRIDE	Q9NVM4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000339507; ENSP00000343103; ENSG00000132600. ENST00000449359; ENSP00000414716; ENSG00000132600.
GeneID	54496.
KEGG	hsa:54496.
UCSC	uc002evy.1. human. uc002evz.1. human.
Organism-specific databases
CTD	54496.
GeneCards	GC16P068344.
HGNC	HGNC:25557. PRMT7.
MIM	610087. gene.
neXtProt	NX_Q9NVM4.
PharmGKB	PA143485581.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10708.
GeneTree	ENSGT00530000063495.
HOGENOM	HBG377790.
HOVERGEN	HBG018729.
InParanoid	Q9NVM4.
OMA	YDIQLNQ.
OrthoDB	EOG48KR9T.
PhylomeDB	Q9NVM4.
Gene expression databases
ArrayExpress	Q9NVM4.
Bgee	Q9NVM4.
CleanEx	HS_PRMT7.
Genevestigator	Q9NVM4.
GermOnline	ENSG00000132600. Homo sapiens.
Family and domain databases
InterPro	IPR014644. Arg_N-MeTrfase. IPR010456. Ribosomal-L11_MeTrfase_PrmA. [Graphical view]
KO	K11438.
Pfam	PF06325. PrmA. 1 hit. [Graphical view]
PIRSF	PIRSF036946. Arg_N-mtase. 1 hit.
ProtoNet	Search...
Other
NextBio	56828.
SOURCE	Search...

Entry information

Entry name

ANM7_HUMAN

Accession

Primary (citable) accession number: Q9NVM4
Secondary accession number(s): B3KPR0 , B3KUG9, B4E379, Q96PV5, Q9H9L0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 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.