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Protein

Protein arginine N-methyltransferase 7

Gene

PRMT7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N(omega)-methyl-L-arginine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei144By similarity1
Active sitei153By similarity1

GO - Molecular functioni

  • [myelin basic protein]-arginine N-methyltransferase activity Source: HGNC
  • histone-arginine N-methyltransferase activity Source: HGNC
  • histone binding Source: HGNC
  • histone methyltransferase activity (H4-R3 specific) Source: UniProtKB
  • protein-arginine N-methyltransferase activity Source: Reactome
  • protein-arginine omega-N asymmetric methyltransferase activity Source: GO_Central
  • protein-arginine omega-N monomethyltransferase activity Source: UniProtKB
  • protein-arginine omega-N symmetric methyltransferase activity Source: UniProtKB
  • ribonucleoprotein complex binding Source: UniProtKB
  • S-adenosylmethionine-dependent methyltransferase activity Source: HGNC

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • DNA methylation involved in gamete generation Source: UniProtKB
  • histone arginine methylation Source: UniProtKB
  • histone methylation Source: HGNC
  • peptidyl-arginine methylation Source: UniProtKB
  • regulation of gene expression by genetic imprinting Source: UniProtKB
  • regulation of protein binding Source: HGNC
  • regulation of transcription, DNA-templated Source: GO_Central
  • spliceosomal snRNP assembly Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:HS05660-MONOMER.
ZFISH:HS05660-MONOMER.
BRENDAi2.1.1.125. 2681.
ReactomeiR-HSA-3214858. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 7 (EC:2.1.1.3211 Publication)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT7
[Myelin basic protein]-arginine N-methyltransferase PRMT7
Gene namesi
Name:PRMT7
Synonyms:KIAA1933
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:25557. PRMT7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in PRMT7 are associated with mild intellectual disabilityy, obesity and symmetrical shortening of the digits and posterior metacarpals and metatarsals. The phenotype is a phenocopy of pseudohypoparathyroidism (PHP).

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi54496.
OpenTargetsiENSG00000132600.
PharmGKBiPA143485581.

Chemistry databases

ChEMBLiCHEMBL3562175.
GuidetoPHARMACOLOGYi1258.

Polymorphism and mutation databases

BioMutaiPRMT7.
DMDMi20137529.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002123351 – 692Protein arginine N-methyltransferase 7Add BLAST692

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32Omega-N-methylarginineBy similarity1

Keywords - PTMi

Methylation

Proteomic databases

EPDiQ9NVM4.
MaxQBiQ9NVM4.
PaxDbiQ9NVM4.
PeptideAtlasiQ9NVM4.
PRIDEiQ9NVM4.

PTM databases

iPTMnetiQ9NVM4.
PhosphoSitePlusiQ9NVM4.

Expressioni

Gene expression databases

BgeeiENSG00000132600.
CleanExiHS_PRMT7.
ExpressionAtlasiQ9NVM4. baseline and differential.
GenevisibleiQ9NVM4. HS.

Organism-specific databases

HPAiHPA044241.

Interactioni

Subunit structurei

Homodimer and heterodimer (By similarity). Interacts with CTCFL (By similarity). Interacts with PRMT5 and SNRPD3.By similarity1 Publication

GO - Molecular functioni

  • histone binding Source: HGNC

Protein-protein interaction databases

BioGridi119992. 24 interactors.
IntActiQ9NVM4. 10 interactors.
MINTiMINT-4831330.
STRINGi9606.ENSP00000343103.

Structurei

3D structure databases

ProteinModelPortaliQ9NVM4.
SMRiQ9NVM4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 345SAM-dependent MTase PRMT-type 1PROSITE-ProRule annotationAdd BLAST332
Domaini358 – 684SAM-dependent MTase PRMT-type 2PROSITE-ProRule annotationAdd BLAST327

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.PROSITE-ProRule annotation
Contains 2 SAM-dependent MTase PRMT-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410INRX. Eukaryota.
COG0500. LUCA.
GeneTreeiENSGT00860000133873.
HOGENOMiHOG000033951.
HOVERGENiHBG018729.
InParanoidiQ9NVM4.
KOiK11438.
OMAiGENSWQE.
OrthoDBiEOG091G07KL.
PhylomeDBiQ9NVM4.
TreeFamiTF315221.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR025799. Arg_MeTrfase.
IPR014644. MeTrfase_PRMT7.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PIRSFiPIRSF036946. Arg_N-mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51678. SAM_MT_PRMT. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NVM4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKIFCSRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNVKYYQ
60 70 80 90 100
GIRAAVSRVK DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA
110 120 130 140 150
DAAVKIVEKN GFSDKIKVIN KHSTEVTVGP EGDMPCRANI LVTELFDTEL
160 170 180 190 200
IGEGALPSYE HAHRHLVEEN CEAVPHRATV YAQLVESGRM WSWNKLFPIH
210 220 230 240 250
VQTSLGEQVI VPPVDVESCP GAPSVCDIQL NQVSPADFTV LSDVLPMFSI
260 270 280 290 300
DFSKQVSSSA ACHSRRFEPL TSGRAQVVLS WWDIEMDPEG KIKCTMAPFW
310 320 330 340 350
AHSDPEEMQW RDHWMQCVYF LPQEEPVVQG SALYLVAHHD DYCVWYSLQR
360 370 380 390 400
TSPEKNERVR QMRPVCDCQA HLLWNRPRFG EINDQDRTDR YVQALRTVLK
410 420 430 440 450
PDSVCLCVSD GSLLSVLAHH LGVEQVFTVE SSAASHKLLR KIFKANHLED
460 470 480 490 500
KINIIEKRPE LLTNEDLQGR KVSLLLGEPF FTTSLLPWHN LYFWYVRTAV
510 520 530 540 550
DQHLGPGAMV MPQAASLHAV VVEFRDLWRI RSPCGDCEGF DVHIMDDMIK
560 570 580 590 600
RALDFRESRE AEPHPLWEYP CRSLSEPWQI LTFDFQQPVP LQPLCAEGTV
610 620 630 640 650
ELRRPGQSHA AVLWMEYHLT PECTLSTGLL EPADPEGGCC WNPHCKQAVY
660 670 680 690
FFSPAPDPRA LLGGPRTVSY AVEFHPDTGD IIMEFRHADT PD
Length:692
Mass (Da):78,459
Last modified:October 1, 2000 - v1
Checksum:i9E0DB9530154231C
GO
Isoform 2 (identifier: Q9NVM4-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:544
Mass (Da):62,118
Checksum:iF979828D17B27191
GO
Isoform 3 (identifier: Q9NVM4-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:642
Mass (Da):73,154
Checksum:i6CF17C684932B869
GO
Isoform 4 (identifier: Q9NVM4-4) [UniParc]FASTAAdd to basket

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.
Show »
Length:567
Mass (Da):63,806
Checksum:iA283D1FC9EBA086C
GO

Sequence cautioni

The sequence BAB14215 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti218S → G in BAG53431 (PubMed:14702039).Curated1
Sequence conflicti246P → L in BAG53431 (PubMed:14702039).Curated1
Sequence conflicti258S → G in BAG51772 (PubMed:14702039).Curated1
Sequence conflicti633A → S in BAB14215 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07632932R → T Found in patients with mild intellectual disability, obesity and acrodysostosis. 1 PublicationCorresponds to variant rs149170494dbSNPEnsembl.1
Natural variantiVAR_076330387R → G Found in patients with mild intellectual disability, obesity and acrodysostosis. 1 PublicationCorresponds to variant rs762515973dbSNPEnsembl.1
Natural variantiVAR_076331494W → R Found in patients with mild intellectual disability, obesity and acrodysostosis. 1 PublicationCorresponds to variant rs751670999dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03725345 – 94Missing in isoform 3. 1 PublicationAdd BLAST50
Alternative sequenceiVSP_00521395 – 168Missing in isoform 2. 1 PublicationAdd BLAST74
Alternative sequenceiVSP_005214399 – 472Missing in isoform 2. 1 PublicationAdd BLAST74
Alternative sequenceiVSP_037254526 – 567DLWRI…PHPLW → VCREQQDVPLVLAATLPCVL AGGCGWGCSFLTGPVADPEP LW in isoform 4. 1 PublicationAdd BLAST42
Alternative sequenceiVSP_037255568 – 692Missing in isoform 4. 1 PublicationAdd BLAST125

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10866.1. [Q9NVM4-1]
CCDS54033.1. [Q9NVM4-3]
RefSeqiNP_001171753.1. NM_001184824.1. [Q9NVM4-3]
NP_001276947.1. NM_001290018.1. [Q9NVM4-1]
NP_061896.1. NM_019023.2. [Q9NVM4-1]
XP_016878783.1. XM_017023294.1. [Q9NVM4-1]
XP_016878784.1. XM_017023295.1. [Q9NVM4-1]
UniGeneiHs.640229.
Hs.653193.

Genome annotation databases

EnsembliENST00000339507; ENSP00000343103; ENSG00000132600. [Q9NVM4-1]
ENST00000441236; ENSP00000409324; ENSG00000132600. [Q9NVM4-1]
ENST00000449359; ENSP00000414716; ENSG00000132600. [Q9NVM4-3]
GeneIDi54496.
KEGGihsa:54496.
UCSCiuc010vlg.3. human. [Q9NVM4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10866.1. [Q9NVM4-1]
CCDS54033.1. [Q9NVM4-3]
RefSeqiNP_001171753.1. NM_001184824.1. [Q9NVM4-3]
NP_001276947.1. NM_001290018.1. [Q9NVM4-1]
NP_061896.1. NM_019023.2. [Q9NVM4-1]
XP_016878783.1. XM_017023294.1. [Q9NVM4-1]
XP_016878784.1. XM_017023295.1. [Q9NVM4-1]
UniGeneiHs.640229.
Hs.653193.

3D structure databases

ProteinModelPortaliQ9NVM4.
SMRiQ9NVM4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119992. 24 interactors.
IntActiQ9NVM4. 10 interactors.
MINTiMINT-4831330.
STRINGi9606.ENSP00000343103.

Chemistry databases

ChEMBLiCHEMBL3562175.
GuidetoPHARMACOLOGYi1258.

PTM databases

iPTMnetiQ9NVM4.
PhosphoSitePlusiQ9NVM4.

Polymorphism and mutation databases

BioMutaiPRMT7.
DMDMi20137529.

Proteomic databases

EPDiQ9NVM4.
MaxQBiQ9NVM4.
PaxDbiQ9NVM4.
PeptideAtlasiQ9NVM4.
PRIDEiQ9NVM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000339507; ENSP00000343103; ENSG00000132600. [Q9NVM4-1]
ENST00000441236; ENSP00000409324; ENSG00000132600. [Q9NVM4-1]
ENST00000449359; ENSP00000414716; ENSG00000132600. [Q9NVM4-3]
GeneIDi54496.
KEGGihsa:54496.
UCSCiuc010vlg.3. human. [Q9NVM4-1]

Organism-specific databases

CTDi54496.
DisGeNETi54496.
GeneCardsiPRMT7.
HGNCiHGNC:25557. PRMT7.
HPAiHPA044241.
MIMi610087. gene.
neXtProtiNX_Q9NVM4.
OpenTargetsiENSG00000132600.
PharmGKBiPA143485581.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INRX. Eukaryota.
COG0500. LUCA.
GeneTreeiENSGT00860000133873.
HOGENOMiHOG000033951.
HOVERGENiHBG018729.
InParanoidiQ9NVM4.
KOiK11438.
OMAiGENSWQE.
OrthoDBiEOG091G07KL.
PhylomeDBiQ9NVM4.
TreeFamiTF315221.

Enzyme and pathway databases

BioCyciMetaCyc:HS05660-MONOMER.
ZFISH:HS05660-MONOMER.
BRENDAi2.1.1.125. 2681.
ReactomeiR-HSA-3214858. RMTs methylate histone arginines.

Miscellaneous databases

ChiTaRSiPRMT7. human.
GenomeRNAii54496.
PROiQ9NVM4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132600.
CleanExiHS_PRMT7.
ExpressionAtlasiQ9NVM4. baseline and differential.
GenevisibleiQ9NVM4. HS.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR025799. Arg_MeTrfase.
IPR014644. MeTrfase_PRMT7.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PIRSFiPIRSF036946. Arg_N-mtase. 1 hit.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51678. SAM_MT_PRMT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANM7_HUMAN
AccessioniPrimary (citable) accession number: Q9NVM4
Secondary accession number(s): B3KPR0
, B3KUG9, B4E379, Q96PV5, Q9H9L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.