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O14744

- ANM5_HUMAN

UniProt

O14744 - ANM5_HUMAN

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Protein

Protein arginine N-methyltransferase 5

Gene

PRMT5

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. 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. 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. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation. Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter.11 Publications

Catalytic activityi

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei304 – 3041Peptide substrate1 Publication
Binding sitei307 – 3071Peptide substrate1 Publication
Binding sitei324 – 3241S-adenosyl-L-methionine1 Publication
Sitei327 – 3271Critical for specifying symmetric addition of methyl groupsBy similarity
Binding sitei392 – 3921S-adenosyl-L-methionine1 Publication
Active sitei435 – 4351Proton donor/acceptor1 Publication
Active sitei444 – 4441Proton donor/acceptor1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. core promoter sequence-specific DNA binding Source: UniProtKB
  3. histone-arginine N-methyltransferase activity Source: RefGenome
  4. methyltransferase activity Source: MGI
  5. protein-arginine omega-N symmetric methyltransferase activity Source: UniProtKB
  6. ribonucleoprotein complex binding Source: UniProtKB
  7. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. circadian regulation of gene expression Source: UniProtKB
  3. endothelial cell activation Source: UniProtKB
  4. gene expression Source: Reactome
  5. histone H4-R3 methylation Source: UniProtKB
  6. ncRNA metabolic process Source: Reactome
  7. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  8. peptidyl-arginine methylation Source: UniProtKB
  9. peptidyl-arginine methylation, to symmetrical-dimethyl arginine Source: GOC
  10. peptidyl-arginine N-methylation Source: MGI
  11. regulation of mitosis Source: ProtInc
  12. regulation of transcription, DNA-templated Source: RefGenome
  13. RNA metabolic process Source: Reactome
  14. spliceosomal snRNP assembly Source: UniProtKB
  15. transcription, DNA-templated Source: UniProtKB-KW
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

ReactomeiREACT_11066. snRNP Assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 5 (EC:2.1.1.-)
Alternative name(s):
72 kDa ICln-binding protein
Histone-arginine N-methyltransferase PRMT5 (EC:2.1.1.125)
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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:10894. PRMT5.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. methylosome Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi365 – 3695Missing: Increased MAPK1/MAPK3 phosphorylation in response to EGF. 1 Publication
Mutagenesisi367 – 3682GR → AA: Abolishes enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA35794.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Protein arginine N-methyltransferase 5PRO_0000212342Add
BLAST
Initiator methioninei1 – 11Removed; alternate5 Publications
Chaini2 – 637636Protein arginine N-methyltransferase 5, N-terminally processedPRO_0000417602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO14744.
PaxDbiO14744.
PeptideAtlasiO14744.
PRIDEiO14744.

PTM databases

PhosphoSiteiO14744.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO14744.
CleanExiHS_PRMT5.
ExpressionAtlasiO14744. baseline and differential.
GenevestigatoriO14744.

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 and WDR77/MEP50. 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 (By similarity). 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.By similarity19 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
NUDCD2Q8WVJ22EBI-351098,EBI-1052153
RBM23Q86U063EBI-351098,EBI-780319
SRGAP2O750444EBI-351098,EBI-1051034
TRIB3Q96RU72EBI-351098,EBI-492476
WDR77Q9BQA16EBI-351098,EBI-1237307
YWHAZP631042EBI-351098,EBI-347088

Protein-protein interaction databases

BioGridi115688. 133 interactions.
DIPiDIP-33172N.
IntActiO14744. 63 interactions.
MINTiMINT-1216859.
STRINGi9606.ENSP00000319169.

Structurei

Secondary structure

1
637
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 194Combined sources
Helixi26 – 3510Combined sources
Beta strandi39 – 468Combined sources
Beta strandi54 – 563Combined sources
Helixi59 – 613Combined sources
Helixi70 – 723Combined sources
Helixi75 – 817Combined sources
Beta strandi82 – 854Combined sources
Helixi97 – 11721Combined sources
Beta strandi120 – 1256Combined sources
Helixi132 – 14211Combined sources
Beta strandi150 – 1589Combined sources
Helixi160 – 1634Combined sources
Helixi181 – 1833Combined sources
Helixi184 – 19512Combined sources
Turni196 – 1983Combined sources
Beta strandi202 – 2076Combined sources
Helixi215 – 2195Combined sources
Turni220 – 2234Combined sources
Beta strandi226 – 2327Combined sources
Helixi233 – 2353Combined sources
Helixi248 – 25912Combined sources
Beta strandi263 – 2686Combined sources
Helixi273 – 2753Combined sources
Helixi279 – 28911Combined sources
Helixi296 – 3005Combined sources
Beta strandi309 – 3113Combined sources
Turni314 – 3163Combined sources
Helixi321 – 3277Combined sources
Helixi331 – 34818Combined sources
Helixi351 – 3533Combined sources
Turni354 – 3563Combined sources
Beta strandi358 – 3658Combined sources
Helixi370 – 38112Combined sources
Beta strandi385 – 3939Combined sources
Helixi395 – 40713Combined sources
Helixi410 – 4123Combined sources
Beta strandi413 – 4186Combined sources
Turni420 – 4223Combined sources
Beta strandi429 – 4335Combined sources
Helixi442 – 4443Combined sources
Helixi446 – 4538Combined sources
Helixi454 – 4563Combined sources
Beta strandi457 – 4659Combined sources
Beta strandi467 – 47610Combined sources
Helixi478 – 4858Combined sources
Helixi496 – 4994Combined sources
Beta strandi516 – 5249Combined sources
Beta strandi534 – 5418Combined sources
Beta strandi546 – 56015Combined sources
Beta strandi563 – 5664Combined sources
Helixi569 – 5713Combined sources
Beta strandi582 – 59211Combined sources
Beta strandi597 – 60610Combined sources
Beta strandi608 – 62114Combined sources
Helixi628 – 6303Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GQBX-ray2.06A1-637[»]
ProteinModelPortaliO14744.
SMRiO14744. Positions 13-637.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini308 – 615308SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 292280TIM barrel1 PublicationAdd
BLAST
Regioni333 – 3342S-adenosyl-L-methionine binding1 Publication
Regioni419 – 4202S-adenosyl-L-methionine binding1 Publication
Regioni465 – 637173Beta barrel1 PublicationAdd
BLAST
Regioni488 – 4947Dimerization1 Publication

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

eggNOGiNOG291156.
GeneTreeiENSGT00390000001141.
HOGENOMiHOG000175933.
HOVERGENiHBG057083.
InParanoidiO14744.
KOiK02516.
OMAiIHNPAGR.
OrthoDBiEOG7X6KZR.
PhylomeDBiO14744.
TreeFamiTF300626.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
IPR029063. SAM-dependent_MTases-like.
[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. Align

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831E → K in BAG63592. (PubMed:14702039)Curated
Sequence conflicti247 – 2471S → F in AAB66581. (PubMed:9843966)Curated
Sequence conflicti420 – 4201M → T in BAG63592. (PubMed:14702039)Curated
Sequence conflicti553 – 5531G → V in AAB66581. (PubMed:9843966)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434MAAMA…LGAVA → MRGPNSGTEKGRLVIPE in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_043382Add
BLAST
Alternative sequencei77 – 12044Missing in isoform 3 and isoform 5. 1 PublicationVSP_054685Add
BLAST
Alternative sequencei106 – 259154Missing in isoform 4. 1 PublicationVSP_054768Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.1. human. [O14744-2]
uc001whm.1. human. [O14744-1]
uc001whn.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS41922.1. [O14744-2 ]
CCDS61394.1. [O14744-3 ]
CCDS61395.1. [O14744-4 ]
CCDS61396.1. [O14744-5 ]
CCDS9579.1. [O14744-1 ]
PIRi T03842.
RefSeqi NP_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 ]
UniGenei Hs.367854.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GQB X-ray 2.06 A 1-637 [» ]
ProteinModelPortali O14744.
SMRi O14744. Positions 13-637.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115688. 133 interactions.
DIPi DIP-33172N.
IntActi O14744. 63 interactions.
MINTi MINT-1216859.
STRINGi 9606.ENSP00000319169.

Chemistry

ChEMBLi CHEMBL1795116.

PTM databases

PhosphoSitei O14744.

Proteomic databases

MaxQBi O14744.
PaxDbi O14744.
PeptideAtlasi O14744.
PRIDEi O14744.

Protocols and materials databases

DNASUi 10419.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216350 ; ENSP00000216350 ; ENSG00000100462 . [O14744-3 ]
ENST00000324366 ; ENSP00000319169 ; ENSG00000100462 . [O14744-1 ]
ENST00000397440 ; ENSP00000380582 ; ENSG00000100462 . [O14744-4 ]
ENST00000397441 ; ENSP00000380583 ; ENSG00000100462 . [O14744-2 ]
ENST00000553897 ; ENSP00000452555 ; ENSG00000100462 . [O14744-5 ]
GeneIDi 10419.
KEGGi hsa:10419.
UCSCi uc001whl.1. human. [O14744-2 ]
uc001whm.1. human. [O14744-1 ]
uc001whn.1. human.

Organism-specific databases

CTDi 10419.
GeneCardsi GC14M023389.
H-InvDB HIX0011525.
HGNCi HGNC:10894. PRMT5.
HPAi CAB012459.
HPA005525.
MIMi 604045. gene.
neXtProti NX_O14744.
PharmGKBi PA35794.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG291156.
GeneTreei ENSGT00390000001141.
HOGENOMi HOG000175933.
HOVERGENi HBG057083.
InParanoidi O14744.
KOi K02516.
OMAi IHNPAGR.
OrthoDBi EOG7X6KZR.
PhylomeDBi O14744.
TreeFami TF300626.

Enzyme and pathway databases

Reactomei REACT_11066. snRNP Assembly.

Miscellaneous databases

ChiTaRSi PRMT5. human.
GeneWikii Protein_arginine_methyltransferase_5.
GenomeRNAii 10419.
NextBioi 35464858.
PROi O14744.
SOURCEi Search...

Gene expression databases

Bgeei O14744.
CleanExi HS_PRMT5.
ExpressionAtlasi O14744. baseline and differential.
Genevestigatori O14744.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR10738. PTHR10738. 1 hit.
Pfami PF05185. PRMT5. 1 hit.
[Graphical view ]
PIRSFi PIRSF015894. Skb1_MeTrfase. 1 hit.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology."
    Krapivinsky G., Pu W., Wickman K., Krapivinsky L., Clapham D.E.
    J. Biol. Chem. 273:10811-10814(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CLNS1A.
  2. "Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs."
    Gilbreth M., Yang P., Bartholomeusz G., Pimental R.A., Kansra S., Gadiraju R., Marcus S.
    Proc. Natl. Acad. Sci. U.S.A. 95:14781-14786(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity."
    Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S.
    J. Biol. Chem. 274:31531-31542(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH JAK2.
  4. "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] (ISOFORMS 2; 3 AND 5).
    Tissue: Testis and Thyroid.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
  6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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).
    Tissue: Skin.
  10. "Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF."
    Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., Avila M.A., Recio J.A.
    Sci. Signal. 4:RA58-RA58(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-13 AND 594-601, FUNCTION IN THE REGULATION OF MAPK1/MAPK3 SIGNALING PATHWAY, INTERACTION WITH BRAF AND RAF1, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 365-GLY--GLY-369.
  11. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Tissue: Platelet.
  12. "Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs."
    Meister G., Fischer U.
    EMBO J. 21:5853-5863(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  13. "The tumor suppressor DAL-1/4.1B modulates protein arginine N-methyltransferase 5 activity in a substrate-specific manner."
    Jiang W., Roemer M.E., Newsham I.F.
    Biochem. Biophys. Res. Commun. 329:522-530(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EPB41L3.
  14. "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes."
    Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C., Fischer U., Schuemperli D.
    J. Biol. Chem. 280:34435-34440(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LSM11.
  15. Cited for: PROTEIN SEQUENCE OF 2-13; 19-49; 52-60; 69-95; 155-193; 201-248; 334-343; 349-377; 386-393; 422-428; 459-485 AND 489-526, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma and Mammary carcinoma.
  16. "Interaction of the somatostatin receptor subtype 1 with the human homolog of the Shk1 kinase-binding protein from yeast."
    Schwaerzler A., Kreienkamp H.-J., Richter D.
    J. Biol. Chem. 275:9557-9562(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSTR1.
  17. "Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family."
    Rho J., Choi S., Seong Y.R., Cho W.-K., Kim S.H., Im D.-S.
    J. Biol. Chem. 276:11393-11401(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  18. "Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln."
    Meister G., Eggert C., Buehler D., Brahms H., Kambach C., Fischer U.
    Curr. Biol. 11:1990-1994(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE METHYLATION AT SNRPD1 AND SNRPD3.
  19. "Negative regulation of transcription by the type II arginine methyltransferase PRMT5."
    Fabbrizio E., El Messaoudi S., Polanowska J., Paul C., Cook J.R., Lee J.-H., Negre V., Rousset M., Pestka S., Le Cam A., Sardet C.
    EMBO Rep. 3:641-645(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF THE CERC COMPLEX.
  20. "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties."
    Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B.
    Mol. Cell 11:1055-1066(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUPT5H.
  21. "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes."
    Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.
    Mol. Cell. Biol. 24:9630-9645(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE SWI/SNF COMPLEX, MUTAGENESIS OF 367-GLY-ARG-368, METHYLATION OF HISTONE H3.
  22. "A putative transcriptional elongation factor hIws1 is essential for mammalian cell proliferation."
    Liu Z., Zhou Z., Chen G., Bao S.
    Biochem. Biophys. Res. Commun. 353:47-53(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IWS1.
  23. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRMT7 AND SNRPD3.
  24. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
    Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
    Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE METHYLOSOME COMPLEX.
  25. "The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5."
    Lacroix M., Messaoudi S.E., Rodier G., Le Cam A., Sardet C., Fabbrizio E.
    EMBO Rep. 9:452-458(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COPRS, SUBCELLULAR LOCATION.
  26. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis."
    Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.
    J. Biol. Chem. 285:12695-12705(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPS10.
  28. "srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization."
    Guo S., Bao S.
    J. Biol. Chem. 285:35133-35141(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH SRGAP2.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation."
    Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J., Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T., Tsai C.H., Hung M.C.
    Nat. Cell Biol. 13:174-181(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EGFR SIGNALING, SUBCELLULAR LOCATION, FUNCTION IN EGFR METHYLATION, INTERACTION WITH EGFR.
  31. "HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules."
    Bandyopadhyay S., Harris D.P., Adams G.N., Lause G.E., McHugh A., Tillmaand E.G., Money A., Willard B., Fox P.L., Dicorleto P.E.
    Mol. Cell. Biol. 32:1202-1213(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOXA9.
  32. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) IN COMPLEX WITH WDR77; S-ADENOSYLMETHIONINE ANALOG AND HISTONE H4 PEPTIDE, CATALYTIC ACTIVITY, ACTIVE SITE, SUBSTRATE-BINDING SITES, SUBUNIT.

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: October 29, 2014
This is version 133 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

External Data

Dasty 3