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Protein

Protein arginine N-methyltransferase 5

Gene

PRMT5

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 (PubMed:10531356, PubMed:11152681, PubMed:11747828, PubMed:12411503, PubMed:15737618, PubMed:17709427, PubMed:20159986, PubMed:20810653, PubMed:21258366, PubMed:21917714, PubMed:22269951). 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 (PubMed:12411503, PubMed:11747828, PubMed:17709427). Methylates SUPT5H and may regulate its transcriptional elongation properties (PubMed:12718890). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation (PubMed:21917714, PubMed:21258366). Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 (PubMed:22269951). Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (PubMed:20810653). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation (PubMed:20421892). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed:26700805).By similarity15 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-N(omega),N(omega')-dimethyl-L-arginine.1 Publication

Enzyme regulationi

Activity is increased by EGF, HGF, FGF1 or FGF2 treatments, and slightly decreased by NGF treatment.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei304Peptide substrate1 Publication1
Binding sitei307Peptide substrate1 Publication1
Binding sitei324S-adenosyl-L-methionine1 Publication1
Sitei327Critical for specifying symmetric addition of methyl groupsBy similarity1
Binding sitei392S-adenosyl-L-methionine1 Publication1
Active sitei435Proton donor/acceptor1 Publication1
Active sitei444Proton donor/acceptor1 Publication1

GO - Molecular functioni

  • core promoter sequence-specific DNA binding Source: UniProtKB
  • histone-arginine N-methyltransferase activity Source: Reactome
  • histone methyltransferase activity (H4-R3 specific) Source: UniProtKB
  • methyl-CpG binding Source: UniProtKB
  • methyltransferase activity Source: MGI
  • protein-arginine N-methyltransferase activity Source: UniProtKB
  • protein-arginine omega-N symmetric methyltransferase activity Source: UniProtKB
  • protein heterodimerization activity Source: MGI
  • ribonucleoprotein complex binding Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: ProtInc
  • circadian regulation of gene expression Source: UniProtKB
  • DNA-templated transcription, termination Source: UniProtKB
  • endothelial cell activation Source: UniProtKB
  • Golgi ribbon formation Source: UniProtKB
  • histone H4-R3 methylation Source: UniProtKB
  • liver regeneration Source: Ensembl
  • negative regulation of cell differentiation Source: Ensembl
  • peptidyl-arginine methylation Source: UniProtKB
  • peptidyl-arginine N-methylation Source: WormBase
  • positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway Source: WormBase
  • positive regulation of oligodendrocyte differentiation Source: Ensembl
  • regulation of DNA methylation Source: Ensembl
  • regulation of ERK1 and ERK2 cascade Source: Ensembl
  • regulation of mitotic nuclear division Source: ProtInc
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription, DNA-templated Source: GO_Central
  • spliceosomal snRNP assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:HS02092-MONOMER.
ZFISH:HS02092-MONOMER.
BRENDAi2.1.1.125. 2681.
ReactomeiR-HSA-191859. snRNP Assembly.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
SIGNORiO14744.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 5 (EC:2.1.1.3201 Publication)
Alternative name(s):
72 kDa ICln-binding protein
Histone-arginine N-methyltransferase PRMT5
Jak-binding protein 1
Shk1 kinase-binding protein 1 homolog
Short name:
SKB1 homolog
Short name:
SKB1Hs
Cleaved into the following chain:
Gene namesi
Name:PRMT5
Synonyms:HRMT1L5, IBP72, JBP1, SKB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:10894. PRMT5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: CACAO
  • cytosol Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • histone methyltransferase complex Source: ParkinsonsUK-UCL
  • methylosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi365 – 369Missing : Increased MAPK1/MAPK3 phosphorylation in response to EGF. 1 Publication5
Mutagenesisi367 – 368GR → AA: Abolishes enzymatic activity. 1 Publication2

Organism-specific databases

DisGeNETi10419.
OpenTargetsiENSG00000100462.
PharmGKBiPA35794.

Chemistry databases

ChEMBLiCHEMBL1795116.
GuidetoPHARMACOLOGYi1256.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002123421 – 637Protein arginine N-methyltransferase 5Add BLAST637
Initiator methionineiRemoved; alternateCombined sources2 Publications
ChainiPRO_00004176022 – 637Protein arginine N-methyltransferase 5, N-terminally processedAdd BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine; in Protein arginine N-methyltransferase 5, N-terminally processedCombined sources1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO14744.
MaxQBiO14744.
PaxDbiO14744.
PeptideAtlasiO14744.
PRIDEiO14744.

PTM databases

iPTMnetiO14744.
PhosphoSitePlusiO14744.
SwissPalmiO14744.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000100462.
CleanExiHS_PRMT5.
ExpressionAtlasiO14744. baseline and differential.
GenevisibleiO14744. HS.

Organism-specific databases

HPAiCAB012459.
HPA005525.

Interactioni

Subunit structurei

Forms, at least, homodimers and homotetramers. Interacts with PRDM1 (By similarity). Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH. Interacts with EGFR; methylates EGFR and stimulates EGFR-mediated ERK activation. Interacts with HOXA9. Interacts with SRGAP2. Found in a complex with COPRS, RUNX1 AND CBFB. Interacts with CHTOP; the interaction symmetrically methylates CHTOP, but seems to require the presence of PRMT1 (PubMed:25284789). Interacts with EPB41L3; this modulates methylation of target proteins. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with JAK2, SSTR1, SUPT5H, BRAF and with active RAF1. Interacts with LSM11, PRMT7 and SNRPD3. Interacts with COPRS; promoting its recruitment on histone H4. Interacts with CLNS1A/pICln. Identified in a complex with CLNS1A/pICln and Sm proteins. Interacts with RPS10. Interacts with WDR77. Interacts with IWS1. Interacts with CRY1. Interacts with POLR2A. Interacts with SMN1/SMN2.By similarity21 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDYL2Q8N8U22EBI-351098,EBI-8467076
CLNS1AP541053EBI-351098,EBI-724693
COPRSQ9NQ926EBI-351098,EBI-1642558
E2F1Q010948EBI-351098,EBI-448924
GRHL3Q8TE852EBI-351098,EBI-8469396
GTPBP2Q9BX102EBI-351098,EBI-6115579
HIST2H4BP628053EBI-351098,EBI-302023
HOXA9P312694EBI-351098,EBI-742314
NP034182EBI-351098,EBI-6930799From a different organism.
NUDCD2Q8WVJ22EBI-351098,EBI-1052153
RBM23Q86U063EBI-351098,EBI-780319
RIOK1Q9BRS24EBI-351098,EBI-7307838
SRGAP2O750444EBI-351098,EBI-1051034
TRIB3Q96RU72EBI-351098,EBI-492476
WDR77Q9BQA17EBI-351098,EBI-1237307
YWHAZP631042EBI-351098,EBI-347088

GO - Molecular functioni

  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi115688. 180 interactors.
DIPiDIP-33172N.
IntActiO14744. 92 interactors.
MINTiMINT-1216859.
STRINGi9606.ENSP00000319169.

Chemistry databases

BindingDBiO14744.

Structurei

Secondary structure

1637
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 19Combined sources4
Helixi26 – 35Combined sources10
Beta strandi39 – 46Combined sources8
Beta strandi54 – 56Combined sources3
Helixi59 – 61Combined sources3
Helixi70 – 72Combined sources3
Helixi75 – 81Combined sources7
Beta strandi82 – 85Combined sources4
Helixi97 – 117Combined sources21
Beta strandi120 – 125Combined sources6
Helixi132 – 142Combined sources11
Beta strandi144 – 146Combined sources3
Beta strandi150 – 158Combined sources9
Helixi160 – 163Combined sources4
Helixi181 – 183Combined sources3
Helixi184 – 195Combined sources12
Turni196 – 198Combined sources3
Beta strandi202 – 207Combined sources6
Helixi215 – 219Combined sources5
Turni220 – 223Combined sources4
Beta strandi226 – 232Combined sources7
Helixi233 – 235Combined sources3
Helixi248 – 259Combined sources12
Beta strandi263 – 268Combined sources6
Helixi273 – 275Combined sources3
Helixi279 – 289Combined sources11
Helixi296 – 300Combined sources5
Helixi302 – 304Combined sources3
Beta strandi309 – 311Combined sources3
Turni314 – 316Combined sources3
Helixi321 – 327Combined sources7
Helixi331 – 348Combined sources18
Helixi351 – 353Combined sources3
Turni354 – 356Combined sources3
Beta strandi358 – 365Combined sources8
Turni367 – 369Combined sources3
Helixi370 – 381Combined sources12
Beta strandi385 – 393Combined sources9
Helixi395 – 407Combined sources13
Helixi410 – 412Combined sources3
Beta strandi413 – 418Combined sources6
Turni420 – 422Combined sources3
Beta strandi429 – 433Combined sources5
Helixi442 – 444Combined sources3
Helixi446 – 453Combined sources8
Helixi454 – 456Combined sources3
Beta strandi457 – 465Combined sources9
Beta strandi467 – 476Combined sources10
Helixi478 – 485Combined sources8
Helixi496 – 499Combined sources4
Beta strandi502 – 505Combined sources4
Beta strandi516 – 524Combined sources9
Beta strandi527 – 529Combined sources3
Beta strandi534 – 541Combined sources8
Beta strandi546 – 560Combined sources15
Beta strandi563 – 566Combined sources4
Helixi569 – 571Combined sources3
Beta strandi582 – 592Combined sources11
Beta strandi597 – 606Combined sources10
Beta strandi608 – 621Combined sources14
Helixi628 – 630Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GQBX-ray2.06A1-637[»]
4X60X-ray2.35A2-637[»]
4X61X-ray2.85A2-637[»]
4X63X-ray3.05A2-637[»]
5C9ZX-ray2.36A2-637[»]
5EMJX-ray2.27A2-637[»]
5EMKX-ray2.52A2-637[»]
5EMLX-ray2.39A2-637[»]
5EMMX-ray2.37A2-637[»]
5FA5X-ray2.34A1-637[»]
ProteinModelPortaliO14744.
SMRiO14744.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini308 – 615SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST308

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 292TIM barrel1 PublicationAdd BLAST280
Regioni333 – 334S-adenosyl-L-methionine binding1 Publication2
Regioni419 – 420S-adenosyl-L-methionine binding1 Publication2
Regioni465 – 637Beta barrel1 PublicationAdd BLAST173
Regioni488 – 494Dimerization1 Publication7

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0822. Eukaryota.
ENOG410XNZM. LUCA.
GeneTreeiENSGT00390000001141.
HOGENOMiHOG000175933.
HOVERGENiHBG057083.
InParanoidiO14744.
KOiK02516.
OMAiINPLTHT.
OrthoDBiEOG091G03PD.
PhylomeDBiO14744.
TreeFamiTF300626.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10738. PTHR10738. 1 hit.
PfamiPF05185. PRMT5. 1 hit.
[Graphical view]
PIRSFiPIRSF015894. Skb1_MeTrfase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seems to exist. According to EST sequences.
Isoform 1 (identifier: O14744-1) [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
MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF
60 70 80 90 100
KREFIQEPAK NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI RPDSKVEKIR
110 120 130 140 150
RNSEAAMLQE LNFGAYLGLP AFLLPLNQED NTNLARVLTN HIHTGHHSSM
160 170 180 190 200
FWMRVPLVAP EDLRDDIIEN APTTHTEEYS GEEKTWMWWH NFRTLCDYSK
210 220 230 240 250
RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK KGFPVLSKMH
260 270 280 290 300
QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF
310 320 330 340 350
AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP
360 370 380 390 400
EEEKDTNVQV LMVLGAGRGP LVNASLRAAK QADRRIKLYA VEKNPNAVVT
410 420 430 440 450
LENWQFEEWG SQVTVVSSDM REWVAPEKAD IIVSELLGSF ADNELSPECL
460 470 480 490 500
DGAQHFLKDD GVSIPGEYTS FLAPISSSKL YNEVRACREK DRDPEAQFEM
510 520 530 540 550
PYVVRLHNFH QLSAPQPCFT FSHPNRDPMI DNNRYCTLEF PVEVNTVLHG
560 570 580 590 600
FAGYFETVLY QDITLSIRPE THSPGMFSWF PILFPIKQPI TVREGQTICV
610 620 630
RFWRCSNSKK VWYEWAVTAP VCSAIHNPTG RSYTIGL
Length:637
Mass (Da):72,684
Last modified:January 23, 2007 - v4
Checksum:i522E255B384F25E7
GO
Isoform 2 (identifier: O14744-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE

Note: No experimental confirmation available.
Show »
Length:620
Mass (Da):71,320
Checksum:i0E489272643DD83C
GO
Isoform 4 (identifier: O14744-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
     106-259: Missing.

Note: No experimental confirmation available.
Show »
Length:466
Mass (Da):53,580
Checksum:i62386C5B867CF619
GO
Isoform 5 (identifier: O14744-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-120: Missing.

Note: No experimental confirmation available.
Show »
Length:593
Mass (Da):67,674
Checksum:iD609BFECAFB7D108
GO
Isoform 3 (identifier: O14744-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
     77-120: Missing.

Note: No experimental confirmation available.
Show »
Length:576
Mass (Da):66,311
Checksum:i988C2D288FC214A1
GO

Sequence cautioni

The sequence BC005820 differs from that shown. Reason: Frameshift at position 370.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti183E → K in BAG63592 (PubMed:14702039).Curated1
Sequence conflicti247S → F in AAB66581 (PubMed:9843966).Curated1
Sequence conflicti420M → T in BAG63592 (PubMed:14702039).Curated1
Sequence conflicti553G → V in AAB66581 (PubMed:9843966).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0433821 – 34MAAMA…LGAVA → MRGPNSGTEKGRLVIPE in isoform 2, isoform 3 and isoform 4. 2 PublicationsAdd BLAST34
Alternative sequenceiVSP_05468577 – 120Missing in isoform 3 and isoform 5. 1 PublicationAdd BLAST44
Alternative sequenceiVSP_054768106 – 259Missing in isoform 4. 1 PublicationAdd BLAST154

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015913 mRNA. Translation: AAB66581.1.
AF167572 mRNA. Translation: AAF04502.1.
AK075251 mRNA. Translation: BAG52095.1.
AK301812 mRNA. Translation: BAG63261.1.
AK302240 mRNA. Translation: BAG63592.1.
CR456741 mRNA. Translation: CAG33022.1.
AB451246 mRNA. Translation: BAG70060.1.
AB451370 mRNA. Translation: BAG70184.1.
AL132780 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66218.1.
CH471078 Genomic DNA. Translation: EAW66219.1.
CH471078 Genomic DNA. Translation: EAW66220.1.
CH471078 Genomic DNA. Translation: EAW66221.1.
BC005820 mRNA. No translation available.
BC025979 mRNA. Translation: AAH25979.1.
CCDSiCCDS41922.1. [O14744-2]
CCDS61394.1. [O14744-3]
CCDS61395.1. [O14744-4]
CCDS61396.1. [O14744-5]
CCDS9579.1. [O14744-1]
PIRiT03842.
RefSeqiNP_001034708.1. NM_001039619.2. [O14744-2]
NP_001269882.1. NM_001282953.1. [O14744-3]
NP_001269884.1. NM_001282955.1. [O14744-5]
NP_001269885.1. NM_001282956.1. [O14744-4]
NP_006100.2. NM_006109.4. [O14744-1]
UniGeneiHs.367854.

Genome annotation databases

EnsembliENST00000216350; ENSP00000216350; ENSG00000100462. [O14744-3]
ENST00000324366; ENSP00000319169; ENSG00000100462. [O14744-1]
ENST00000397440; ENSP00000380582; ENSG00000100462. [O14744-4]
ENST00000397441; ENSP00000380583; ENSG00000100462. [O14744-2]
ENST00000553897; ENSP00000452555; ENSG00000100462. [O14744-5]
GeneIDi10419.
KEGGihsa:10419.
UCSCiuc001whl.3. human. [O14744-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015913 mRNA. Translation: AAB66581.1.
AF167572 mRNA. Translation: AAF04502.1.
AK075251 mRNA. Translation: BAG52095.1.
AK301812 mRNA. Translation: BAG63261.1.
AK302240 mRNA. Translation: BAG63592.1.
CR456741 mRNA. Translation: CAG33022.1.
AB451246 mRNA. Translation: BAG70060.1.
AB451370 mRNA. Translation: BAG70184.1.
AL132780 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66218.1.
CH471078 Genomic DNA. Translation: EAW66219.1.
CH471078 Genomic DNA. Translation: EAW66220.1.
CH471078 Genomic DNA. Translation: EAW66221.1.
BC005820 mRNA. No translation available.
BC025979 mRNA. Translation: AAH25979.1.
CCDSiCCDS41922.1. [O14744-2]
CCDS61394.1. [O14744-3]
CCDS61395.1. [O14744-4]
CCDS61396.1. [O14744-5]
CCDS9579.1. [O14744-1]
PIRiT03842.
RefSeqiNP_001034708.1. NM_001039619.2. [O14744-2]
NP_001269882.1. NM_001282953.1. [O14744-3]
NP_001269884.1. NM_001282955.1. [O14744-5]
NP_001269885.1. NM_001282956.1. [O14744-4]
NP_006100.2. NM_006109.4. [O14744-1]
UniGeneiHs.367854.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GQBX-ray2.06A1-637[»]
4X60X-ray2.35A2-637[»]
4X61X-ray2.85A2-637[»]
4X63X-ray3.05A2-637[»]
5C9ZX-ray2.36A2-637[»]
5EMJX-ray2.27A2-637[»]
5EMKX-ray2.52A2-637[»]
5EMLX-ray2.39A2-637[»]
5EMMX-ray2.37A2-637[»]
5FA5X-ray2.34A1-637[»]
ProteinModelPortaliO14744.
SMRiO14744.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115688. 180 interactors.
DIPiDIP-33172N.
IntActiO14744. 92 interactors.
MINTiMINT-1216859.
STRINGi9606.ENSP00000319169.

Chemistry databases

BindingDBiO14744.
ChEMBLiCHEMBL1795116.
GuidetoPHARMACOLOGYi1256.

PTM databases

iPTMnetiO14744.
PhosphoSitePlusiO14744.
SwissPalmiO14744.

Proteomic databases

EPDiO14744.
MaxQBiO14744.
PaxDbiO14744.
PeptideAtlasiO14744.
PRIDEiO14744.

Protocols and materials databases

DNASUi10419.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216350; ENSP00000216350; ENSG00000100462. [O14744-3]
ENST00000324366; ENSP00000319169; ENSG00000100462. [O14744-1]
ENST00000397440; ENSP00000380582; ENSG00000100462. [O14744-4]
ENST00000397441; ENSP00000380583; ENSG00000100462. [O14744-2]
ENST00000553897; ENSP00000452555; ENSG00000100462. [O14744-5]
GeneIDi10419.
KEGGihsa:10419.
UCSCiuc001whl.3. human. [O14744-1]

Organism-specific databases

CTDi10419.
DisGeNETi10419.
GeneCardsiPRMT5.
H-InvDBHIX0011525.
HGNCiHGNC:10894. PRMT5.
HPAiCAB012459.
HPA005525.
MIMi604045. gene.
neXtProtiNX_O14744.
OpenTargetsiENSG00000100462.
PharmGKBiPA35794.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0822. Eukaryota.
ENOG410XNZM. LUCA.
GeneTreeiENSGT00390000001141.
HOGENOMiHOG000175933.
HOVERGENiHBG057083.
InParanoidiO14744.
KOiK02516.
OMAiINPLTHT.
OrthoDBiEOG091G03PD.
PhylomeDBiO14744.
TreeFamiTF300626.

Enzyme and pathway databases

BioCyciMetaCyc:HS02092-MONOMER.
ZFISH:HS02092-MONOMER.
BRENDAi2.1.1.125. 2681.
ReactomeiR-HSA-191859. snRNP Assembly.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
SIGNORiO14744.

Miscellaneous databases

ChiTaRSiPRMT5. human.
GeneWikiiProtein_arginine_methyltransferase_5.
GenomeRNAii10419.
PROiO14744.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100462.
CleanExiHS_PRMT5.
ExpressionAtlasiO14744. baseline and differential.
GenevisibleiO14744. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10738. PTHR10738. 1 hit.
PfamiPF05185. PRMT5. 1 hit.
[Graphical view]
PIRSFiPIRSF015894. Skb1_MeTrfase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANM5_HUMAN
AccessioniPrimary (citable) accession number: O14744
Secondary accession number(s): A8MTP3
, A8MZ91, B4DX49, B4DY30, B5BU10, D3DS33, E2QRE7, Q6IBR1, Q9UKH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 157 of the entry and version 4 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.