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Q8CIG8

- ANM5_MOUSE

UniProt

Q8CIG8 - ANM5_MOUSE

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Protein
Protein arginine N-methyltransferase 5
Gene
Prmt5, Jbp1, Skb1
Organism
Mus musculus (Mouse)
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.4 Publications

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei304 – 3041Peptide substrate By similarity
Binding sitei307 – 3071Peptide substrate By similarity
Binding sitei324 – 3241S-adenosyl-L-methionine By similarity
Sitei327 – 3271Critical for specifying symmetric addition of methyl groups By similarity
Binding sitei392 – 3921S-adenosyl-L-methionine By similarity
Active sitei435 – 4351Proton donor/acceptor By similarity
Active sitei444 – 4441Proton donor/acceptor By similarity

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. histone-arginine N-methyltransferase activity Source: RefGenome
  3. methyltransferase activity Source: MGI
  4. protein binding Source: UniProtKB
  5. protein-arginine omega-N symmetric methyltransferase activity Source: UniProtKB
  6. ribonucleoprotein complex binding Source: Ensembl

GO - Biological processi

  1. endothelial cell activation Source: Ensembl
  2. histone arginine methylation Source: RefGenome
  3. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  4. peptidyl-arginine N-methylation Source: MGI
  5. peptidyl-arginine methylation Source: UniProtKB
  6. peptidyl-arginine methylation, to symmetrical-dimethyl arginine Source: RefGenome
  7. spliceosomal snRNP assembly Source: UniProtKB
  8. 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_206812. snRNP Assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 5 (EC:2.1.1.-)
Alternative name(s):
Histone-arginine N-methyltransferase PRMT5 (EC:2.1.1.125)
Jak-binding protein 1
Shk1 kinase-binding protein 1 homolog
Short name:
SKB1 homolog
Gene namesi
Name:Prmt5
Synonyms:Jbp1, Skb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1351645. Prmt5.

Subcellular locationi

Cytoplasm By similarity. Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 637636Protein arginine N-methyltransferase 5
PRO_0000212344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8CIG8.
PaxDbiQ8CIG8.
PRIDEiQ8CIG8.

PTM databases

PhosphoSiteiQ8CIG8.

Expressioni

Gene expression databases

ArrayExpressiQ8CIG8.
BgeeiQ8CIG8.
CleanExiMM_PRMT5.
GenevestigatoriQ8CIG8.

Interactioni

Subunit structurei

Forms, at least, homodimers and homotetramers. Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1 and WDR77/MEP50. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Also interacts with Sm proteins, JAK2 and SSTR1. Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with LSM11, PRMT7 and SNRPD3. Interacts with COPRS; promoting its recruitment on histone H4 By similarity. Interacts with PRDM1. Interacts with RPS10. Interacts with EGFR; methylates EGFR and stimulates EGFR-mediated ERK activation By similarity. Interacts with BRAF and with active RAF1 By similarity. Interacts with HOXA9 By similarity. Interacts with SRGAP2. Interacts with EPB41L3; this modulates methylation of target proteins By similarity. 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. Interacts with IWS1 By similarity. Interacts with CRY1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ccnd1P253225EBI-2527009,EBI-847243
ChtopQ9CY574EBI-2527009,EBI-6393116

Protein-protein interaction databases

BioGridi205181. 14 interactions.
IntActiQ8CIG8. 7 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8CIG8.
SMRiQ8CIG8. Positions 13-637.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini308 – 615308SAM-dependent MTase PRMT-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 292280TIM barrel By similarity
Add
BLAST
Regioni333 – 3342S-adenosyl-L-methionine binding By similarity
Regioni419 – 4202S-adenosyl-L-methionine binding By similarity
Regioni465 – 637173Beta barrel By similarity
Add
BLAST
Regioni488 – 4947Dimerization By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG291156.
GeneTreeiENSGT00390000001141.
HOGENOMiHOG000175933.
HOVERGENiHBG057083.
InParanoidiQ8CIG8.
KOiK02516.
OrthoDBiEOG7X6KZR.
PhylomeDBiQ8CIG8.
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]

Sequencei

Sequence statusi: Complete.

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

Q8CIG8-1 [UniParc]FASTAAdd to Basket

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MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF    50
KREFIQEPAK NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI HPDSKVEKIR 100
RNSEAAMLQE LNFGAYLGLP AFLLPLNQED NTNLARVLTN HIHTGHHSSM 150
FWMRVPLVAP EDLRDDVIAN APTTHTEEYS GEEKTWMWWH NFRTLCDYSK 200
RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK KGFPVLSKVQ 250
QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF 300
AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP 350
EEEKETNVQV LMVLGAGRGP LVNASLRAAK QAERRIRLYA VEKNPNAVVT 400
LENWQFEEWG SQVTVVSSDM REWVAPEKAD IIVSELLGSF ADNELSPECL 450
DGAQHFLKDD GVSIPGEYTS FLAPISSSKL YNEVRACREK DRDPEAQFEM 500
PYVVRLHNFH QLSAPKPCFT FSHPNRDPMI DNNRYCTLEF PVEVNTVLHG 550
FAGYFETVLY RDITLSIRPE THSPGMFSWF PIFFPIKQPI TVHEGQNICV 600
RFWRCSNSKK VWYEWAVTAP VCSSIHNPTG RSYTIGL 637
Length:637
Mass (Da):72,680
Last modified:January 23, 2007 - v3
Checksum:iE8014CA172B30543
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691A → E in BAE21155. 1 Publication
Sequence conflicti169 – 1691A → E in BAE38057. 1 Publication
Sequence conflicti376 – 3761L → F in AAF04503. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK132414 mRNA. Translation: BAE21155.1.
AK165165 mRNA. Translation: BAE38057.1.
BC023905 mRNA. Translation: AAH23905.1.
AF167573 mRNA. Translation: AAF04503.1.
CCDSiCCDS27091.1.
RefSeqiNP_038796.2. NM_013768.3.
UniGeneiMm.196585.

Genome annotation databases

EnsembliENSMUST00000023873; ENSMUSP00000023873; ENSMUSG00000023110.
GeneIDi27374.
KEGGimmu:27374.
UCSCiuc007twf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK132414 mRNA. Translation: BAE21155.1 .
AK165165 mRNA. Translation: BAE38057.1 .
BC023905 mRNA. Translation: AAH23905.1 .
AF167573 mRNA. Translation: AAF04503.1 .
CCDSi CCDS27091.1.
RefSeqi NP_038796.2. NM_013768.3.
UniGenei Mm.196585.

3D structure databases

ProteinModelPortali Q8CIG8.
SMRi Q8CIG8. Positions 13-637.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205181. 14 interactions.
IntActi Q8CIG8. 7 interactions.

PTM databases

PhosphoSitei Q8CIG8.

Proteomic databases

MaxQBi Q8CIG8.
PaxDbi Q8CIG8.
PRIDEi Q8CIG8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023873 ; ENSMUSP00000023873 ; ENSMUSG00000023110 .
GeneIDi 27374.
KEGGi mmu:27374.
UCSCi uc007twf.2. mouse.

Organism-specific databases

CTDi 10419.
MGIi MGI:1351645. Prmt5.

Phylogenomic databases

eggNOGi NOG291156.
GeneTreei ENSGT00390000001141.
HOGENOMi HOG000175933.
HOVERGENi HBG057083.
InParanoidi Q8CIG8.
KOi K02516.
OrthoDBi EOG7X6KZR.
PhylomeDBi Q8CIG8.
TreeFami TF300626.

Enzyme and pathway databases

Reactomei REACT_206812. snRNP Assembly.

Miscellaneous databases

NextBioi 305288.
PROi Q8CIG8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8CIG8.
Bgeei Q8CIG8.
CleanExi MM_PRMT5.
Genevestigatori Q8CIG8.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  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] OF 7-637.
  4. "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: FUNCTION IN METHYLATION OF HISTONE H3.
  5. "Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells."
    Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., Kouzarides T., Surani M.A.
    Nat. Cell Biol. 8:623-630(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRDM1.
  6. "Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members."
    Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S., Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.
    Genes Dev. 23:1749-1762(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN METHYLATION OF PIWI PROTEINS.
  7. Cited for: FUNCTION, INTERACTION WITH CHTOP.
  8. "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: FUNCTION IN THE REGULATION OF MAPK1/MAPK3 SIGNALING PATHWAY, RAF1 METHYLATION.
  9. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
    Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
    Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHTOP, SUBCELLULAR LOCATION.
  10. "The histone- and PRMT5-associated protein COPR5 is required for myogenic differentiation."
    Paul C., Sardet C., Fabbrizio E.
    Cell Death Differ. 19:900-908(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COPRS, IDENTIFICATION IN A COMPLEX WITH PRMT5; RUNX1 AND CBFB.
  11. "Role of type II protein arginine methyltransferase 5 in the regulation of Circadian Per1 gene."
    Na J., Lee K., Kim H.G., Shin J.Y., Na W., Jeong H., Lee J.W., Cho S., Kim W.S., Ju B.G.
    PLoS ONE 7:E48152-E48152(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CRY1.

Entry informationi

Entry nameiANM5_MOUSE
AccessioniPrimary (citable) accession number: Q8CIG8
Secondary accession number(s): Q3TNN1, Q9QZS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi