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O14744 (ANM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:PRMT5
Synonyms:HRMT1L5, IBP72, JBP1, SKB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. 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. Ref.3 Ref.10 Ref.12 Ref.13 Ref.17 Ref.18 Ref.23 Ref.27 Ref.28 Ref.30 Ref.31

Catalytic activity

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. Ref.34

Enzyme regulation

Activity is increased by EGF, HGF, FGF1 or FGF2 treatments, and slightly decreased by NGF treatment. Ref.10

Subunit structure

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. Ref.1 Ref.3 Ref.10 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.30 Ref.31 Ref.34

Subcellular location

Cytoplasm. Nucleus Ref.10 Ref.25 Ref.30 Ref.31.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.

Contains 1 SAM-dependent MTase PRMT-type domain.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement Ref.2. Source: ProtInc

endothelial cell activation

Inferred from mutant phenotype Ref.31. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

histone H4-R3 methylation

Non-traceable author statement Ref.25. Source: UniProtKB

ncRNA metabolic process

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

peptidyl-arginine N-methylation

Inferred from direct assay PubMed 15369763. Source: MGI

peptidyl-arginine methylation

Inferred from mutant phenotype Ref.23. Source: UniProtKB

peptidyl-arginine methylation, to symmetrical-dimethyl arginine

Inferred from mutant phenotype Ref.23. Source: GOC

regulation of mitosis

Traceable author statement Ref.2. Source: ProtInc

regulation of transcription, DNA-templated

Inferred from Biological aspect of Ancestor. Source: RefGenome

spliceosomal snRNP assembly

Inferred from mutant phenotype Ref.23. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.24. Source: UniProtKB

methylosome

Inferred from direct assay Ref.24. Source: UniProtKB

nucleus

Non-traceable author statement Ref.25. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

histone-arginine N-methyltransferase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

methyltransferase activity

Inferred from direct assay PubMed 15369763. Source: MGI

protein binding

Inferred from physical interaction Ref.14Ref.25Ref.27Ref.31. Source: UniProtKB

protein-arginine omega-N symmetric methyltransferase activity

Inferred from mutant phenotype Ref.23. Source: UniProtKB

ribonucleoprotein complex binding

Inferred from physical interaction Ref.23. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seems to exist. According to EST sequences.
Isoform 1 (identifier: O14744-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O14744-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
Note: No experimental confirmation available.
Isoform 4 (identifier: O14744-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
     106-259: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: O14744-5)

The sequence of this isoform differs from the canonical sequence as follows:
     77-120: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O14744-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
     77-120: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 637637Protein arginine N-methyltransferase 5
PRO_0000212342
Initiator methionine11Removed; alternate Ref.11 Ref.15
Chain2 – 637636Protein arginine N-methyltransferase 5, N-terminally processed
PRO_0000417602

Regions

Domain308 – 615308SAM-dependent MTase PRMT-type
Region13 – 292280TIM barrel
Region333 – 3342S-adenosyl-L-methionine binding
Region419 – 4202S-adenosyl-L-methionine binding
Region465 – 637173Beta barrel
Region488 – 4947Dimerization

Sites

Active site4351Proton donor/acceptor Probable
Active site4441Proton donor/acceptor Probable
Binding site3041Peptide substrate
Binding site3071Peptide substrate
Binding site3241S-adenosyl-L-methionine
Binding site3921S-adenosyl-L-methionine
Site3271Critical for specifying symmetric addition of methyl groups By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.15 Ref.26 Ref.32 Ref.33

Natural variations

Alternative sequence1 – 3434MAAMA…LGAVA → MRGPNSGTEKGRLVIPE in isoform 2, isoform 3 and isoform 4.
VSP_043382
Alternative sequence77 – 12044Missing in isoform 3 and isoform 5.
VSP_054685
Alternative sequence106 – 259154Missing in isoform 4.
VSP_054768

Experimental info

Mutagenesis365 – 3695Missing: Increased MAPK1/MAPK3 phosphorylation in response to EGF. Ref.10 Ref.21
Mutagenesis367 – 3682GR → AA: Abolishes enzymatic activity. Ref.21
Sequence conflict1831E → K in BAG63592. Ref.4
Sequence conflict2471S → F in AAB66581. Ref.2
Sequence conflict4201M → T in BAG63592. Ref.4
Sequence conflict5531G → V in AAB66581. Ref.2

Secondary structure

........................................................................................................ 637
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 522E255B384F25E7

FASTA63772,684
        10         20         30         40         50         60 
MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFIQEPAK 

        70         80         90        100        110        120 
NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI RPDSKVEKIR RNSEAAMLQE LNFGAYLGLP 

       130        140        150        160        170        180 
AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDIIEN APTTHTEEYS 

       190        200        210        220        230        240 
GEEKTWMWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK 

       250        260        270        280        290        300 
KGFPVLSKMH QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF 

       310        320        330        340        350        360 
AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP EEEKDTNVQV 

       370        380        390        400        410        420 
LMVLGAGRGP LVNASLRAAK QADRRIKLYA VEKNPNAVVT LENWQFEEWG SQVTVVSSDM 

       430        440        450        460        470        480 
REWVAPEKAD IIVSELLGSF ADNELSPECL DGAQHFLKDD GVSIPGEYTS FLAPISSSKL 

       490        500        510        520        530        540 
YNEVRACREK DRDPEAQFEM PYVVRLHNFH QLSAPQPCFT FSHPNRDPMI DNNRYCTLEF 

       550        560        570        580        590        600 
PVEVNTVLHG FAGYFETVLY QDITLSIRPE THSPGMFSWF PILFPIKQPI TVREGQTICV 

       610        620        630 
RFWRCSNSKK VWYEWAVTAP VCSAIHNPTG RSYTIGL 

« Hide

Isoform 2 [UniParc].

Checksum: 0E489272643DD83C
Show »

FASTA62071,320
Isoform 4 [UniParc].

Checksum: 62386C5B867CF619
Show »

FASTA46653,580
Isoform 5 [UniParc].

Checksum: D609BFECAFB7D108
Show »

FASTA59367,674
Isoform 3 [UniParc].

Checksum: 988C2D288FC214A1
Show »

FASTA57666,311

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W., Boldt K., von Kriegsheim A.F.
Submitted (FEB-2008) to UniProtKB
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"Crystal structure of the human PRMT5:MEP50 complex."
Antonysamy S., Bonday Z., Campbell R.M., Doyle B., Druzina Z., Gheyi T., Han B., Jungheim L.N., Qian Y., Rauch C., Russell M., Sauder J.M., Wasserman S.R., Weichert K., Willard F.S., Zhang A., Emtage S.
Proc. Natl. Acad. Sci. U.S.A. 109:17960-17965(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41922.1. [O14744-2]
CCDS9579.1. [O14744-1]
PIRT03842.
RefSeqNP_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]
UniGeneHs.367854.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GQBX-ray2.06A1-637[»]
ProteinModelPortalO14744.
SMRO14744. Positions 13-637.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115688. 126 interactions.
DIPDIP-33172N.
IntActO14744. 63 interactions.
MINTMINT-1216859.
STRING9606.ENSP00000319169.

Chemistry

ChEMBLCHEMBL1795116.

PTM databases

PhosphoSiteO14744.

Proteomic databases

MaxQBO14744.
PaxDbO14744.
PeptideAtlasO14744.
PRIDEO14744.

Protocols and materials databases

DNASU10419.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216350; ENSP00000216350; ENSG00000100462.
ENST00000324366; ENSP00000319169; ENSG00000100462. [O14744-1]
ENST00000397440; ENSP00000380582; ENSG00000100462.
ENST00000397441; ENSP00000380583; ENSG00000100462. [O14744-2]
GeneID10419.
KEGGhsa:10419.
UCSCuc001whl.1. human. [O14744-2]
uc001whm.1. human. [O14744-1]

Organism-specific databases

CTD10419.
GeneCardsGC14M023389.
H-InvDBHIX0011525.
HGNCHGNC:10894. PRMT5.
HPACAB012459.
HPA005525.
MIM604045. gene.
neXtProtNX_O14744.
PharmGKBPA35794.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291156.
HOGENOMHOG000175933.
HOVERGENHBG057083.
InParanoidO14744.
KOK02516.
OMAIHNPAGR.
OrthoDBEOG7X6KZR.
PhylomeDBO14744.
TreeFamTF300626.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO14744.
BgeeO14744.
CleanExHS_PRMT5.
GenevestigatorO14744.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR10738. PTHR10738. 1 hit.
PfamPF05185. PRMT5. 1 hit.
[Graphical view]
PIRSFPIRSF015894. Skb1_MeTrfase. 1 hit.
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRMT5. human.
GeneWikiProtein_arginine_methyltransferase_5.
GenomeRNAi10419.
NextBio35464858.
PROO14744.
SOURCESearch...

Entry information

Entry nameANM5_HUMAN
AccessionPrimary (citable) accession number: O14744
Secondary accession number(s): A8MTP3 expand/collapse secondary AC list , A8MZ91, B4DX49, B4DY30, B5BU10, D3DS33, E2QRE7, Q6IBR1, Q9UKH1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 130 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM