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Protein

Protein arginine N-methyltransferase 8

Gene

PRMT8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS.3 Publications

Kineticsi

  1. KM=1.3 µM for GRGGFGGRGGFRGGRGG-NH21 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei86 – 861S-adenosyl-L-methionineBy similarity
    Binding sitei95 – 951S-adenosyl-L-methionineBy similarity
    Binding sitei119 – 1191S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei141 – 1411S-adenosyl-L-methionineBy similarity
    Binding sitei170 – 1701S-adenosyl-L-methionineBy similarity
    Active sitei185 – 1851By similarity
    Active sitei194 – 1941By similarity

    GO - Molecular functioni

    • histone-arginine N-methyltransferase activity Source: HGNC
    • identical protein binding Source: IntAct
    • protein-arginine omega-N asymmetric methyltransferase activity Source: UniProtKB
    • protein-arginine omega-N monomethyltransferase activity Source: UniProtKB
    • protein heterodimerization activity Source: HGNC
    • protein homodimerization activity Source: HGNC
    • S-adenosylmethionine-dependent methyltransferase activity Source: HGNC

    GO - Biological processi

    • histone arginine methylation Source: GOC
    • histone methylation Source: HGNC
    • peptidyl-arginine methylation Source: UniProtKB
    • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: HGNC
    • regulation of protein binding Source: HGNC
    • regulation of transcription, DNA-templated Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.125. 2681.
    SABIO-RKQ9NR22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein arginine N-methyltransferase 8 (EC:2.1.1.-)
    Alternative name(s):
    Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4
    Gene namesi
    Name:PRMT8
    Synonyms:HRMT1L3, HRMT1L4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:5188. PRMT8.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: GO_Central
    • plasma membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Loss of cell membrane localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA134903406.

    Chemistry

    ChEMBLiCHEMBL3108648.
    GuidetoPHARMACOLOGYi1259.

    Polymorphism and mutation databases

    BioMutaiPRMT8.
    DMDMi88983969.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved
    Chaini2 – 394393Protein arginine N-methyltransferase 8PRO_0000212329Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei58 – 581Omega-N-methylarginine; by autocatalysis1 Publication
    Modified residuei73 – 731Asymmetric dimethylarginine; by autocatalysis1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Myristate

    Proteomic databases

    EPDiQ9NR22.
    MaxQBiQ9NR22.
    PaxDbiQ9NR22.
    PRIDEiQ9NR22.

    PTM databases

    iPTMnetiQ9NR22.
    PhosphoSiteiQ9NR22.

    Expressioni

    Tissue specificityi

    Brain-specific.1 Publication

    Gene expression databases

    BgeeiQ9NR22.
    CleanExiHS_PRMT8.
    GenevisibleiQ9NR22. HS.

    Organism-specific databases

    HPAiHPA039747.

    Interactioni

    Subunit structurei

    Homodimers and heterodimers with PRMT1 or PRMT2, recruiting PRMT1 to the cell membrane. Interacts with PRMT2 and FYN (via the SH3 domain). Interacts with EWS; independently of EWS methylation status.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-745545,EBI-745545
    PRMT1Q998735EBI-10186886,EBI-78738
    SYNCRIPO605063EBI-745545,EBI-1024357

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • protein heterodimerization activity Source: HGNC
    • protein homodimerization activity Source: HGNC

    Protein-protein interaction databases

    BioGridi121140. 39 interactions.
    IntActiQ9NR22. 11 interactions.
    MINTiMINT-3072538.
    STRINGi9606.ENSP00000372067.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi83 – 919Combined sources
    Helixi93 – 10412Combined sources
    Helixi107 – 1104Combined sources
    Beta strandi114 – 1196Combined sources
    Helixi124 – 1318Combined sources
    Beta strandi135 – 1417Combined sources
    Helixi145 – 15511Combined sources
    Turni159 – 1613Combined sources
    Beta strandi162 – 1676Combined sources
    Turni169 – 1713Combined sources
    Beta strandi175 – 1773Combined sources
    Beta strandi179 – 1835Combined sources
    Turni192 – 1943Combined sources
    Helixi197 – 20711Combined sources
    Beta strandi208 – 2169Combined sources
    Beta strandi218 – 2269Combined sources
    Helixi229 – 2357Combined sources
    Helixi237 – 2404Combined sources
    Helixi248 – 2558Combined sources
    Beta strandi259 – 2613Combined sources
    Helixi265 – 2673Combined sources
    Beta strandi273 – 2797Combined sources
    Turni280 – 2823Combined sources
    Helixi285 – 2884Combined sources
    Beta strandi289 – 29810Combined sources
    Beta strandi300 – 31516Combined sources
    Beta strandi318 – 3203Combined sources
    Beta strandi322 – 3254Combined sources
    Beta strandi337 – 34812Combined sources
    Beta strandi353 – 36210Combined sources
    Beta strandi364 – 3663Combined sources
    Beta strandi369 – 37911Combined sources
    Beta strandi384 – 39310Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4X41X-ray3.50A/B61-394[»]
    5DSTX-ray2.96A/B/C/D/E/F/G/H/I/J/K/L/M/N/O68-394[»]
    ProteinModelPortaliQ9NR22.
    SMRiQ9NR22. Positions 82-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini73 – 394322SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi29 – 4214SH3-binding 1Add
    BLAST
    Motifi53 – 586SH3-binding 2

    Domaini

    The SH3-binding motifs mediate the interaction with SH3 domain-containing proteins such as PRMT2 and FYN, possibly leading to displace the N-terminal domain and activate the protein.1 Publication
    The N-terminal region (1-60) inhibits the enzymatic activity.1 Publication

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT8 subfamily.PROSITE-ProRule annotation
    Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiKOG1499. Eukaryota.
    ENOG410XQYH. LUCA.
    GeneTreeiENSGT00550000074406.
    HOGENOMiHOG000198521.
    HOVERGENiHBG001793.
    InParanoidiQ9NR22.
    KOiK11439.
    OMAiQMKPNER.
    OrthoDBiEOG7S7SDJ.
    PhylomeDBiQ9NR22.
    TreeFamiTF300608.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025799. Arg_MeTrfase.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PANTHERiPTHR11006. PTHR11006. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9NR22-1) [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
    MGMKHSSRCL LLRRKMAENA AESTEVNSPP SQPPQPVVPA KPVQCVHHVS
    60 70 80 90 100
    TQPSCPGRGK MSKLLNPEEM TSRDYYFDSY AHFGIHEEML KDEVRTLTYR
    110 120 130 140 150
    NSMYHNKHVF KDKVVLDVGS GTGILSMFAA KAGAKKVFGI ECSSISDYSE
    160 170 180 190 200
    KIIKANHLDN IITIFKGKVE EVELPVEKVD IIISEWMGYC LFYESMLNTV
    210 220 230 240 250
    IFARDKWLKP GGLMFPDRAA LYVVAIEDRQ YKDFKIHWWE NVYGFDMTCI
    260 270 280 290 300
    RDVAMKEPLV DIVDPKQVVT NACLIKEVDI YTVKTEELSF TSAFCLQIQR
    310 320 330 340 350
    NDYVHALVTY FNIEFTKCHK KMGFSTAPDA PYTHWKQTVF YLEDYLTVRR
    360 370 380 390
    GEEIYGTISM KPNAKNVRDL DFTVDLDFKG QLCETSVSND YKMR
    Length:394
    Mass (Da):45,291
    Last modified:February 21, 2006 - v2
    Checksum:i44B55438D16394CD
    GO
    Isoform 2 (identifier: Q9NR22-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: MGMKHSSRCLLLRRKMAENAAESTE → MESLASDGFKLKEVSS

    Note: No experimental confirmation available.
    Show »
    Length:385
    Mass (Da):44,169
    Checksum:i20E4A89EFD1C520D
    GO

    Sequence cautioni

    The sequence AAF91390.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAG37987.1 differs from that shown. Reason: Frameshift at position 45. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti150 – 1501E → Q in AAH22458 (PubMed:15489334).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2525MGMKH…AESTE → MESLASDGFKLKEVSS in isoform 2. 1 PublicationVSP_037466Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK315619 mRNA. Translation: BAG37987.1. Frameshift.
    AC005831 Genomic DNA. No translation available.
    AC005908 Genomic DNA. No translation available.
    AC005925 Genomic DNA. No translation available.
    BC022458 mRNA. Translation: AAH22458.2.
    AF263539 mRNA. Translation: AAF91390.1. Different initiation.
    CCDSiCCDS58200.1. [Q9NR22-2]
    CCDS8521.2. [Q9NR22-1]
    RefSeqiNP_001243465.1. NM_001256536.1. [Q9NR22-2]
    NP_062828.3. NM_019854.4. [Q9NR22-1]
    UniGeneiHs.504530.

    Genome annotation databases

    EnsembliENST00000382622; ENSP00000372067; ENSG00000111218. [Q9NR22-1]
    ENST00000452611; ENSP00000414507; ENSG00000111218. [Q9NR22-2]
    GeneIDi56341.
    KEGGihsa:56341.
    UCSCiuc001qmf.5. human. [Q9NR22-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK315619 mRNA. Translation: BAG37987.1. Frameshift.
    AC005831 Genomic DNA. No translation available.
    AC005908 Genomic DNA. No translation available.
    AC005925 Genomic DNA. No translation available.
    BC022458 mRNA. Translation: AAH22458.2.
    AF263539 mRNA. Translation: AAF91390.1. Different initiation.
    CCDSiCCDS58200.1. [Q9NR22-2]
    CCDS8521.2. [Q9NR22-1]
    RefSeqiNP_001243465.1. NM_001256536.1. [Q9NR22-2]
    NP_062828.3. NM_019854.4. [Q9NR22-1]
    UniGeneiHs.504530.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4X41X-ray3.50A/B61-394[»]
    5DSTX-ray2.96A/B/C/D/E/F/G/H/I/J/K/L/M/N/O68-394[»]
    ProteinModelPortaliQ9NR22.
    SMRiQ9NR22. Positions 82-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi121140. 39 interactions.
    IntActiQ9NR22. 11 interactions.
    MINTiMINT-3072538.
    STRINGi9606.ENSP00000372067.

    Chemistry

    ChEMBLiCHEMBL3108648.
    GuidetoPHARMACOLOGYi1259.

    PTM databases

    iPTMnetiQ9NR22.
    PhosphoSiteiQ9NR22.

    Polymorphism and mutation databases

    BioMutaiPRMT8.
    DMDMi88983969.

    Proteomic databases

    EPDiQ9NR22.
    MaxQBiQ9NR22.
    PaxDbiQ9NR22.
    PRIDEiQ9NR22.

    Protocols and materials databases

    DNASUi56341.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000382622; ENSP00000372067; ENSG00000111218. [Q9NR22-1]
    ENST00000452611; ENSP00000414507; ENSG00000111218. [Q9NR22-2]
    GeneIDi56341.
    KEGGihsa:56341.
    UCSCiuc001qmf.5. human. [Q9NR22-1]

    Organism-specific databases

    CTDi56341.
    GeneCardsiPRMT8.
    H-InvDBHIX0010342.
    HGNCiHGNC:5188. PRMT8.
    HPAiHPA039747.
    MIMi610086. gene.
    neXtProtiNX_Q9NR22.
    PharmGKBiPA134903406.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1499. Eukaryota.
    ENOG410XQYH. LUCA.
    GeneTreeiENSGT00550000074406.
    HOGENOMiHOG000198521.
    HOVERGENiHBG001793.
    InParanoidiQ9NR22.
    KOiK11439.
    OMAiQMKPNER.
    OrthoDBiEOG7S7SDJ.
    PhylomeDBiQ9NR22.
    TreeFamiTF300608.

    Enzyme and pathway databases

    BRENDAi2.1.1.125. 2681.
    SABIO-RKQ9NR22.

    Miscellaneous databases

    ChiTaRSiPRMT8. human.
    GenomeRNAii56341.
    NextBioi61985.
    PROiQ9NR22.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NR22.
    CleanExiHS_PRMT8.
    GenevisibleiQ9NR22. HS.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025799. Arg_MeTrfase.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PANTHERiPTHR11006. PTHR11006. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "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] (ISOFORM 2).
      Tissue: Neuroepithelioma.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Brain.
    4. "Transcripts in human map region 12p13.3."
      Lorenz B., Strom T.M.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-394 (ISOFORM 1).
      Tissue: Brain.
    5. "PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family."
      Lee J., Sayegh J., Daniel J., Clarke S., Bedford M.T.
      J. Biol. Chem. 280:32890-32896(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
    6. "Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain."
      Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G.
      J. Biol. Chem. 282:36444-36453(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, N-TERMINAL REGION DOMAIN, DOMAIN SH3-BINDING MOTIF, METHYLATION AT ARG-58 AND ARG-73, INTERACTION WITH PRMT2 AND FYN.
    7. "Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state."
      Pahlich S., Zakaryan R.P., Gehring H.
      Proteins 72:1125-1137(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INTERACTION WITH EWS.

    Entry informationi

    Entry nameiANM8_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR22
    Secondary accession number(s): B2RDP0, Q8TBJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: February 21, 2006
    Last modified: May 11, 2016
    This is version 123 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.