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Q99873

- ANM1_HUMAN

UniProt

Q99873 - ANM1_HUMAN

Protein

Protein arginine N-methyltransferase 1

Gene

PRMT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (04 Dec 2007)
      Previous versions | rss
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    Functioni

    Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity.10 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].3 Publications

    Enzyme regulationi

    By BTG1, BTG2 and ILF3.

    Kineticsi

    1. KM=1 µM for AdoMet1 Publication
    2. KM=4.2 µM for H41 Publication

    Vmax=1.2 nmol/min/mg enzyme toward AdoMet1 Publication

    Vmax=1.24 nmol/min/mg enzyme toward H41 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531S-adenosyl-L-methionineBy similarity
    Binding sitei62 – 621S-adenosyl-L-methionineBy similarity
    Binding sitei86 – 861S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei108 – 1081S-adenosyl-L-methionineBy similarity
    Binding sitei137 – 1371S-adenosyl-L-methionineBy similarity
    Active sitei152 – 1521By similarity
    Active sitei161 – 1611By similarity

    GO - Molecular functioni

    1. histone methyltransferase activity Source: UniProtKB
    2. histone methyltransferase activity (H4-R3 specific) Source: UniProtKB
    3. identical protein binding Source: IntAct
    4. methyltransferase activity Source: ProtInc
    5. N-methyltransferase activity Source: UniProtKB
    6. poly(A) RNA binding Source: UniProtKB
    7. protein-arginine omega-N asymmetric methyltransferase activity Source: RefGenome
    8. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. histone H4-R3 methylation Source: UniProtKB
    3. histone methylation Source: UniProtKB
    4. negative regulation of megakaryocyte differentiation Source: UniProtKB
    5. neuron projection development Source: UniProtKB
    6. peptidyl-arginine methylation Source: UniProtKB
    7. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: RefGenome
    8. protein methylation Source: ProtInc
    9. regulation of transcription, DNA-templated Source: RefGenome

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    SABIO-RKQ99873.
    SignaLinkiQ99873.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein arginine N-methyltransferase 1 (EC:2.1.1.-)
    Alternative name(s):
    Histone-arginine N-methyltransferase PRMT1 (EC:2.1.1.125)
    Interferon receptor 1-bound protein 4
    Gene namesi
    Name:PRMT1
    Synonyms:HMT2, HRMT1L2, IR1B4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:5187. PRMT1.

    Subcellular locationi

    Nucleus 1 Publication. Nucleusnucleoplasm By similarity. Cytoplasmcytosol By similarity
    Note: Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: RefGenome
    3. nucleoplasm Source: UniProtKB-SubCell
    4. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi82 – 821V → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. 1 Publication
    Mutagenesisi83 – 831L → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. 1 Publication
    Mutagenesisi84 – 841D → A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA29461.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 361361Protein arginine N-methyltransferase 1PRO_0000212321Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei124 – 1241N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiQ99873.
    PaxDbiQ99873.
    PRIDEiQ99873.

    PTM databases

    PhosphoSiteiQ99873.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ99873.
    BgeeiQ99873.
    CleanExiHS_PRMT1.
    GenevestigatoriQ99873.

    Organism-specific databases

    HPAiCAB022550.

    Interactioni

    Subunit structurei

    Homodimer and heterodimer with PRMT8. Individual homodimers can associate to form a homohexamer. Interacts with BTG1, BTG2, NFATC2IP and IFNAR1 By similarity. Interacts with and methylates CHTOP, thereby enabling the interaction of CHTOP with the 5FMC complex By similarity. Interacts with ILF3 and SUPT5H. Interacts with and methylates FOXO1, leading to the nuclear retention of FOXO1 and the stimulation of FOXO1 transcriptional activity. Methylation of FOXO1 is increased upon oxidative stress.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-78738,EBI-78738
    CHTOPQ9Y3Y22EBI-78738,EBI-347794
    DCAF8Q5TAQ92EBI-78738,EBI-740686
    DHX9Q082112EBI-78738,EBI-352022
    EWSR1Q018442EBI-78738,EBI-739737
    FAM9AQ8IZU12EBI-78738,EBI-8468186
    gagP045912EBI-78738,EBI-6179727From a different organism.
    HABP4Q5JVS02EBI-78738,EBI-523625
    HNRNPKP619783EBI-78738,EBI-304185
    ILF3Q129062EBI-78738,EBI-78756
    NRIP1P485524EBI-78738,EBI-746484
    OFCC1Q8IZS52EBI-78738,EBI-8477661
    PRMT8Q9NR223EBI-78738,EBI-745545
    SCN5AQ145242EBI-78738,EBI-726858
    SPSB1Q96BD62EBI-78738,EBI-2659201
    SPSB2Q996192EBI-78738,EBI-2323209
    SYNCRIPO605062EBI-78738,EBI-1024357
    VHLP403372EBI-78738,EBI-301246

    Protein-protein interaction databases

    BioGridi109512. 128 interactions.
    DIPiDIP-30878N.
    IntActiQ99873. 72 interactions.
    MINTiMINT-4861475.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99873.
    SMRiQ99873. Positions 49-361.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 361322SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
    BLAST

    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

    eggNOGiCOG0500.
    HOVERGENiHBG001793.
    InParanoidiQ99873.
    KOiK11434.
    PhylomeDBiQ99873.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025799. Arg_MeTrfase.
    IPR025714. Methyltranfer_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR11006. PTHR11006. 1 hit.
    PfamiPF13847. Methyltransf_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99873-1) [UniParc]FASTAAdd to Basket

    Also known as: V2

    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

    MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK DYYFDSYAHF    50
    GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG 100
    ARKVIGIECS SISDYAVKIV KANKLDHVVT IIKGKVEEVE LPVEKVDIII 150
    SEWMGYCLFY ESMLNTVLYA RDKWLAPDGL IFPDRATLYV TAIEDRQYKD 200
    YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVTNAC LIKEVDIYTV 250
    KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG FSTSPESPYT 300
    HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT IDLDFKGQLC 350
    ELSCSTDYRM R 361
    Length:361
    Mass (Da):41,516
    Last modified:December 4, 2007 - v2
    Checksum:iA286D99B5AFC1860
    GO
    Isoform 2 (identifier: Q99873-2) [UniParc]FASTAAdd to Basket

    Also known as: V3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: MENFVATLANGMSLQPPLE → MVGVA

    Show »
    Length:347
    Mass (Da):39,929
    Checksum:i2546A25EF744E265
    GO
    Isoform 3 (identifier: Q99873-3) [UniParc]FASTAAdd to Basket

    Also known as: V1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: MENFVATLANGMSLQPPLE → M

    Show »
    Length:343
    Mass (Da):39,602
    Checksum:iDFC413AC52F49754
    GO
    Isoform 4 (identifier: Q99873-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: MENFVATLANGMSLQPPLE → MAAAEAANCIM

    Show »
    Length:353
    Mass (Da):40,548
    Checksum:i1704BA3762F3E264
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081E → V in CAA71763. (PubMed:9545638)Curated
    Sequence conflicti108 – 1081E → V in CAA71764. (PubMed:9545638)Curated
    Sequence conflicti108 – 1081E → V in CAA71765. (PubMed:9545638)Curated
    Sequence conflicti108 – 1081E → V in BAA11029. (PubMed:8675017)Curated
    Sequence conflicti147 – 17529DIIIS…RDKWL → ASSSASGWATASSTSPCSTP CSMPGTSV in BAA11029. (PubMed:8675017)CuratedAdd
    BLAST
    Sequence conflicti202 – 2021K → E in BAG65435. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti78 – 781K → M.
    Corresponds to variant rs1804486 [ dbSNP | Ensembl ].
    VAR_037501
    Natural varianti158 – 1581L → F.
    Corresponds to variant rs11673683 [ dbSNP | Ensembl ].
    VAR_037502

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1919MENFV…QPPLE → MVGVA in isoform 2. 1 PublicationVSP_005208Add
    BLAST
    Alternative sequencei1 – 1919MENFV…QPPLE → M in isoform 3. 1 PublicationVSP_005209Add
    BLAST
    Alternative sequencei1 – 1919MENFV…QPPLE → MAAAEAANCIM in isoform 4. 2 PublicationsVSP_046334Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10805 mRNA. Translation: CAA71763.1.
    Y10806 mRNA. Translation: CAA71764.1.
    Y10807 mRNA. Translation: CAA71765.1.
    D66904 mRNA. Translation: BAA11029.1.
    AF222689 Genomic DNA. Translation: AAF62893.1.
    AF222689 Genomic DNA. Translation: AAF62894.1.
    AF222689 Genomic DNA. Translation: AAF62895.1.
    AK304660 mRNA. Translation: BAG65435.1.
    CR407608 mRNA. Translation: CAG28536.1.
    AC011495 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52521.1.
    BC019268 mRNA. Translation: AAH19268.2.
    BC109282 mRNA. Translation: AAI09283.2.
    BC109283 mRNA. Translation: AAI09284.2.
    CCDSiCCDS42592.1. [Q99873-4]
    RefSeqiNP_001527.3. NM_001536.5.
    NP_938074.2. NM_198318.4. [Q99873-4]
    UniGeneiHs.20521.

    Genome annotation databases

    EnsembliENST00000391851; ENSP00000375724; ENSG00000126457. [Q99873-4]
    GeneIDi3276.
    KEGGihsa:3276.
    UCSCiuc002ppe.3. human.
    uc021uxu.1. human. [Q99873-2]

    Polymorphism databases

    DMDMi161789011.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10805 mRNA. Translation: CAA71763.1 .
    Y10806 mRNA. Translation: CAA71764.1 .
    Y10807 mRNA. Translation: CAA71765.1 .
    D66904 mRNA. Translation: BAA11029.1 .
    AF222689 Genomic DNA. Translation: AAF62893.1 .
    AF222689 Genomic DNA. Translation: AAF62894.1 .
    AF222689 Genomic DNA. Translation: AAF62895.1 .
    AK304660 mRNA. Translation: BAG65435.1 .
    CR407608 mRNA. Translation: CAG28536.1 .
    AC011495 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52521.1 .
    BC019268 mRNA. Translation: AAH19268.2 .
    BC109282 mRNA. Translation: AAI09283.2 .
    BC109283 mRNA. Translation: AAI09284.2 .
    CCDSi CCDS42592.1. [Q99873-4 ]
    RefSeqi NP_001527.3. NM_001536.5.
    NP_938074.2. NM_198318.4. [Q99873-4 ]
    UniGenei Hs.20521.

    3D structure databases

    ProteinModelPortali Q99873.
    SMRi Q99873. Positions 49-361.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109512. 128 interactions.
    DIPi DIP-30878N.
    IntActi Q99873. 72 interactions.
    MINTi MINT-4861475.

    Chemistry

    BindingDBi Q99873.
    ChEMBLi CHEMBL5524.
    GuidetoPHARMACOLOGYi 1252.

    PTM databases

    PhosphoSitei Q99873.

    Polymorphism databases

    DMDMi 161789011.

    Proteomic databases

    MaxQBi Q99873.
    PaxDbi Q99873.
    PRIDEi Q99873.

    Protocols and materials databases

    DNASUi 3276.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000391851 ; ENSP00000375724 ; ENSG00000126457 . [Q99873-4 ]
    GeneIDi 3276.
    KEGGi hsa:3276.
    UCSCi uc002ppe.3. human.
    uc021uxu.1. human. [Q99873-2 ]

    Organism-specific databases

    CTDi 3276.
    GeneCardsi GC19P050181.
    HGNCi HGNC:5187. PRMT1.
    HPAi CAB022550.
    MIMi 602950. gene.
    neXtProti NX_Q99873.
    PharmGKBi PA29461.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0500.
    HOVERGENi HBG001793.
    InParanoidi Q99873.
    KOi K11434.
    PhylomeDBi Q99873.

    Enzyme and pathway databases

    SABIO-RK Q99873.
    SignaLinki Q99873.

    Miscellaneous databases

    ChiTaRSi PRMT1. human.
    GeneWikii PRMT1.
    GenomeRNAii 3276.
    NextBioi 13013.
    PROi Q99873.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99873.
    Bgeei Q99873.
    CleanExi HS_PRMT1.
    Genevestigatori Q99873.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025799. Arg_MeTrfase.
    IPR025714. Methyltranfer_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR11006. PTHR11006. 1 hit.
    Pfami PF13847. Methyltransf_31. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)."
      Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A., Henry M.F.
      Genomics 48:330-340(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    2. "Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant."
      Nikawa J., Nakano H., Ohi N.
      Gene 171:107-111(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Glial cell.
    3. "Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene."
      Scorilas A., Black M.H., Talieri M., Diamandis E.P.
      Biochem. Biophys. Res. Commun. 278:349-359(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    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] (ISOFORM 4).
      Tissue: Uterus.
    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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    6. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 3 AND 4).
      Tissue: Lung.
    9. "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3."
      Tang J., Kao P.N., Herschman H.R.
      J. Biol. Chem. 275:19866-19876(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ILF3.
    10. "The structure and oligomerization of the yeast arginine methyltransferase, Hmt1."
      Weiss V.H., McBride A.E., Soriano M.A., Filman D.J., Silver P.A., Hogle J.M.
      Nat. Struct. Biol. 7:1165-1171(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1."
      Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H., Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.
      Curr. Biol. 11:996-1000(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY.
    12. "Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor."
      Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H., Strahl B.D., Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.
      Science 293:853-857(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY.
    13. "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: FUNCTION, INTERACTION WITH SUPT5H.
    14. Cited for: FUNCTION.
    15. "Arginine methylation of FOXO transcription factors inhibits their phosphorylation by Akt."
      Yamagata K., Daitoku H., Takahashi Y., Namiki K., Hisatake K., Kako K., Mukai H., Kasuya Y., Fukamizu A.
      Mol. Cell 32:221-231(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FOXO1, MUTAGENESIS OF VAL-82; LEU-83 AND ASP-84.
    16. "PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells."
      Miyata S., Mori Y., Tohyama M.
      Neurosci. Lett. 445:162-165(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "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, INTERACTION WITH EWS AND PRMT8.
    18. "Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4."
      Lakowski T.M., Frankel A.
      Biochem. J. 421:253-261(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    19. "PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function."
      Jobert L., Argentini M., Tora L.
      Exp. Cell Res. 315:1273-1286(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling."
      Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.
      Genes Dev. 23:118-132(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    21. "Protein-arginine methyltransferase 1 suppresses megakaryocytic differentiation via modulation of the p38 MAPK pathway in K562 cells."
      Chang Y.I., Hua W.K., Yao C.L., Hwang S.M., Hung Y.C., Kuan C.J., Leou J.S., Lin W.J.
      J. Biol. Chem. 285:20595-20606(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiANM1_HUMAN
    AccessioniPrimary (citable) accession number: Q99873
    Secondary accession number(s): B4E3C3
    , G5E9B6, Q15529, Q2VP93, Q6LEU5, Q8WUW5, Q99872, Q99874, Q9NZ04, Q9NZ05, Q9NZ06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 4, 2007
    Last modified: October 1, 2014
    This is version 129 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3