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O14744

- ANM5_HUMAN

UniProt

O14744 - ANM5_HUMAN

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
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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 substrate
    Binding sitei307 – 3071Peptide substrate
    Binding sitei324 – 3241S-adenosyl-L-methionine
    Sitei327 – 3271Critical for specifying symmetric addition of methyl groupsBy similarity
    Binding sitei392 – 3921S-adenosyl-L-methionine
    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. protein binding Source: UniProtKB
    7. ribonucleoprotein complex binding Source: UniProtKB
    8. 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

    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

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

    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

    ArrayExpressiO14744.
    BgeeiO14744.
    CleanExiHS_PRMT5.
    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. 126 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 – 194
    Helixi26 – 3510
    Beta strandi39 – 468
    Beta strandi54 – 563
    Helixi59 – 613
    Helixi70 – 723
    Helixi75 – 817
    Beta strandi82 – 854
    Helixi97 – 11721
    Beta strandi120 – 1256
    Helixi132 – 14211
    Beta strandi150 – 1589
    Helixi160 – 1634
    Helixi181 – 1833
    Helixi184 – 19512
    Turni196 – 1983
    Beta strandi202 – 2076
    Helixi215 – 2195
    Turni220 – 2234
    Beta strandi226 – 2327
    Helixi233 – 2353
    Helixi248 – 25912
    Beta strandi263 – 2686
    Helixi273 – 2753
    Helixi279 – 28911
    Helixi296 – 3005
    Beta strandi309 – 3113
    Turni314 – 3163
    Helixi321 – 3277
    Helixi331 – 34818
    Helixi351 – 3533
    Turni354 – 3563
    Beta strandi358 – 3658
    Helixi370 – 38112
    Beta strandi385 – 3939
    Helixi395 – 40713
    Helixi410 – 4123
    Beta strandi413 – 4186
    Turni420 – 4223
    Beta strandi429 – 4335
    Helixi442 – 4443
    Helixi446 – 4538
    Helixi454 – 4563
    Beta strandi457 – 4659
    Beta strandi467 – 47610
    Helixi478 – 4858
    Helixi496 – 4994
    Beta strandi516 – 5249
    Beta strandi534 – 5418
    Beta strandi546 – 56015
    Beta strandi563 – 5664
    Helixi569 – 5713
    Beta strandi582 – 59211
    Beta strandi597 – 60610
    Beta strandi608 – 62114
    Helixi628 – 6303

    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 barrelAdd
    BLAST
    Regioni333 – 3342S-adenosyl-L-methionine binding
    Regioni419 – 4202S-adenosyl-L-methionine binding
    Regioni465 – 637173Beta barrelAdd
    BLAST
    Regioni488 – 4947Dimerization

    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.
    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

    MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF    50
    KREFIQEPAK NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI RPDSKVEKIR 100
    RNSEAAMLQE LNFGAYLGLP AFLLPLNQED NTNLARVLTN HIHTGHHSSM 150
    FWMRVPLVAP EDLRDDIIEN APTTHTEEYS GEEKTWMWWH NFRTLCDYSK 200
    RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK KGFPVLSKMH 250
    QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF 300
    AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP 350
    EEEKDTNVQV LMVLGAGRGP LVNASLRAAK QADRRIKLYA VEKNPNAVVT 400
    LENWQFEEWG SQVTVVSSDM REWVAPEKAD IIVSELLGSF ADNELSPECL 450
    DGAQHFLKDD GVSIPGEYTS FLAPISSSKL YNEVRACREK DRDPEAQFEM 500
    PYVVRLHNFH QLSAPQPCFT FSHPNRDPMI DNNRYCTLEF PVEVNTVLHG 550
    FAGYFETVLY QDITLSIRPE THSPGMFSWF PILFPIKQPI TVREGQTICV 600
    RFWRCSNSKK VWYEWAVTAP VCSAIHNPTG RSYTIGL 637
    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. 126 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.
    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

    ArrayExpressi O14744.
    Bgeei O14744.
    CleanExi HS_PRMT5.
    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

    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 1, 2014
    This is version 132 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