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O60678

- ANM3_HUMAN

UniProt

O60678 - ANM3_HUMAN

Protein

Protein arginine N-methyltransferase 3

Gene

PRMT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.

    Enzyme regulationi

    Inhibited by N-ethylmaleimide and high concentrations of zinc chloride.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei87 – 871Not phosphorylated
    Binding sitei230 – 2301S-adenosyl-L-methionineBy similarity
    Binding sitei239 – 2391S-adenosyl-L-methionine
    Binding sitei263 – 2631S-adenosyl-L-methionine; via carbonyl oxygen
    Binding sitei285 – 2851S-adenosyl-L-methionine
    Binding sitei314 – 3141S-adenosyl-L-methionine
    Active sitei329 – 3291By similarity
    Active sitei338 – 3381By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri48 – 7124C2H2-typeAdd
    BLAST

    GO - Molecular functioni

    1. histone-arginine N-methyltransferase activity Source: RefGenome
    2. metal ion binding Source: UniProtKB-KW
    3. methyltransferase activity Source: UniProtKB
    4. modified amino acid binding Source: Ensembl
    5. protein-arginine N-methyltransferase activity Source: UniProtKB
    6. protein-arginine omega-N asymmetric methyltransferase activity Source: RefGenome
    7. protein binding Source: UniProtKB

    GO - Biological processi

    1. histone arginine methylation Source: RefGenome
    2. negative regulation of protein ubiquitination Source: UniProtKB
    3. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: RefGenome
    4. regulation of transcription, DNA-templated Source: RefGenome

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, S-adenosyl-L-methionine, Zinc

    Enzyme and pathway databases

    SABIO-RKO60678.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein arginine N-methyltransferase 3 (EC:2.1.1.-)
    Alternative name(s):
    Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3
    Gene namesi
    Name:PRMT3
    Synonyms:HRMT1L3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:30163. PRMT3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: RefGenome
    3. ribosome Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi87 – 871Y → C: Markedly reduced affinity for RPS2. 1 Publication
    Mutagenesisi87 – 871Y → E: Markedly reduced affinity for RPS2. 1 Publication
    Mutagenesisi87 – 871Y → F: No effect on interaction with RPS2. 1 Publication

    Organism-specific databases

    PharmGKBiPA29462.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 531530Protein arginine N-methyltransferase 3PRO_0000212326Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylcysteine3 Publications
    Modified residuei25 – 251Phosphoserine4 Publications
    Modified residuei27 – 271Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60678.
    PaxDbiO60678.
    PRIDEiO60678.

    PTM databases

    PhosphoSiteiO60678.

    Expressioni

    Gene expression databases

    ArrayExpressiO60678.
    BgeeiO60678.
    CleanExiHS_PRMT3.
    GenevestigatoriO60678.

    Organism-specific databases

    HPAiCAB022083.
    HPA007832.

    Interactioni

    Subunit structurei

    Monomer or homodimer By similarity. Interacts with EPB41L3; this inhibits methylation of target proteins. Interacts with the 40S ribosomal protein RPS2.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SCN5AQ145242EBI-2809009,EBI-726858

    Protein-protein interaction databases

    BioGridi115491. 31 interactions.
    IntActiO60678. 5 interactions.
    MINTiMINT-6803908.
    STRINGi9606.ENSP00000331879.

    Structurei

    Secondary structure

    1
    531
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi223 – 2253
    Helixi227 – 2348
    Helixi237 – 24913
    Helixi251 – 2533
    Turni254 – 2563
    Beta strandi258 – 2636
    Helixi268 – 2758
    Beta strandi279 – 2879
    Helixi289 – 29911
    Turni303 – 3053
    Beta strandi306 – 3116
    Turni313 – 3153
    Beta strandi319 – 3213
    Beta strandi323 – 3286
    Turni336 – 3383
    Helixi340 – 35112
    Beta strandi352 – 3609
    Beta strandi362 – 3709
    Helixi373 – 3797
    Helixi381 – 3844
    Helixi392 – 3943
    Helixi395 – 3984
    Beta strandi403 – 4053
    Helixi409 – 4113
    Beta strandi417 – 4237
    Turni424 – 4263
    Helixi429 – 4324
    Beta strandi433 – 44210
    Beta strandi446 – 45914
    Beta strandi467 – 4704
    Beta strandi482 – 49312
    Beta strandi498 – 50710
    Beta strandi514 – 5218
    Beta strandi524 – 5307

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FYTX-ray2.00A211-531[»]
    3SMQX-ray2.00A211-531[»]
    4HSGX-ray2.30A211-531[»]
    ProteinModelPortaliO60678.
    SMRiO60678. Positions 43-147, 221-531.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60678.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini217 – 531315SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The zinc-finger is responsible for substrate specificity.By similarity

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
    Contains 1 C2H2-type zinc finger.Curated
    Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri48 – 7124C2H2-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0500.
    HOGENOMiHOG000198521.
    HOVERGENiHBG001793.
    KOiK11436.
    OMAiAQDFVMH.
    OrthoDBiEOG7S7SDJ.
    PhylomeDBiO60678.
    TreeFamiTF323587.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025799. Arg_MeTrfase.
    IPR010456. Ribosomal-L11_MeTrfase_PrmA.
    IPR029063. SAM-dependent_MTases-like.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    [Graphical view]
    PANTHERiPTHR11006. PTHR11006. 1 hit.
    PfamiPF06325. PrmA. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 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. Align

    Isoform 1 (identifier: O60678-1) [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

    MCSLASGATG GRGAVENEED LPELSDSGDE AAWEDEDDAD LPHGKQQTPC    50
    LFCNRLFTSA EETFSHCKSE HQFNIDSMVH KHGLEFYGYI KLINFIRLKN 100
    PTVEYMNSIY NPVPWEKEEY LKPVLEDDLL LQFDVEDLYE PVSVPFSYPN 150
    GLSENTSVVE KLKHMEARAL SAEAALARAR EDLQKMKQFA QDFVMHTDVR 200
    TCSSSTSVIA DLQEDEDGVY FSSYGHYGIH EEMLKDKIRT ESYRDFIYQN 250
    PHIFKDKVVL DVGCGTGILS MFAAKAGAKK VLGVDQSEIL YQAMDIIRLN 300
    KLEDTITLIK GKIEEVHLPV EKVDVIISEW MGYFLLFESM LDSVLYAKNK 350
    YLAKGGSVYP DICTISLVAV SDVNKHADRI AFWDDVYGFK MSCMKKAVIP 400
    EAVVEVLDPK TLISEPCGIK HIDCHTTSIS DLEFSSDFTL KITRTSMCTA 450
    IAGYFDIYFE KNCHNRVVFS TGPQSTKTHW KQTVFLLEKP FSVKAGEALK 500
    GKVTVHKSKK DPRSLTVTLT LNNSTQTYGL Q 531
    Length:531
    Mass (Da):59,876
    Last modified:January 11, 2011 - v3
    Checksum:iD02159E2BEDBE7B9
    GO
    Isoform 2 (identifier: O60678-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         11-99: GRGAVENEED...IKLINFIRLK → YSHLLKKHFHTVSLSISLILTAWFINM

    Note: No experimental confirmation available.

    Show »
    Length:469
    Mass (Da):52,875
    Checksum:i4A67AC40A78A7B01
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211L → E in AAC39837. (PubMed:9642256)Curated
    Sequence conflicti103 – 1031V → F in BAG62289. (PubMed:14702039)Curated
    Sequence conflicti510 – 5101K → R in BAG62289. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti440 – 4401L → V.
    Corresponds to variant rs3758805 [ dbSNP | Ensembl ].
    VAR_024584
    Natural varianti470 – 4701S → C.
    Corresponds to variant rs11025585 [ dbSNP | Ensembl ].
    VAR_030943
    Natural varianti508 – 5081S → N.3 Publications
    Corresponds to variant rs6483700 [ dbSNP | Ensembl ].
    VAR_024585

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei11 – 9989GRGAV…FIRLK → YSHLLKKHFHTVSLSISLIL TAWFINM in isoform 2. 1 PublicationVSP_040330Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK300591 mRNA. Translation: BAG62289.1.
    AC025972 Genomic DNA. No translation available.
    AC108005 Genomic DNA. No translation available.
    BC037544 mRNA. Translation: AAH37544.1.
    BC064831 mRNA. Translation: AAH64831.1.
    AF059531 mRNA. Translation: AAC39837.1.
    CCDSiCCDS44554.1. [O60678-2]
    CCDS7853.1. [O60678-1]
    RefSeqiNP_005779.1. NM_005788.3.
    UniGeneiHs.152337.

    Genome annotation databases

    EnsembliENST00000331079; ENSP00000331879; ENSG00000185238. [O60678-1]
    ENST00000437750; ENSP00000397766; ENSG00000185238. [O60678-2]
    GeneIDi10196.
    KEGGihsa:10196.
    UCSCiuc001mqb.3. human. [O60678-1]
    uc010rdn.2. human. [O60678-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK300591 mRNA. Translation: BAG62289.1 .
    AC025972 Genomic DNA. No translation available.
    AC108005 Genomic DNA. No translation available.
    BC037544 mRNA. Translation: AAH37544.1 .
    BC064831 mRNA. Translation: AAH64831.1 .
    AF059531 mRNA. Translation: AAC39837.1 .
    CCDSi CCDS44554.1. [O60678-2 ]
    CCDS7853.1. [O60678-1 ]
    RefSeqi NP_005779.1. NM_005788.3.
    UniGenei Hs.152337.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FYT X-ray 2.00 A 211-531 [» ]
    3SMQ X-ray 2.00 A 211-531 [» ]
    4HSG X-ray 2.30 A 211-531 [» ]
    ProteinModelPortali O60678.
    SMRi O60678. Positions 43-147, 221-531.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115491. 31 interactions.
    IntActi O60678. 5 interactions.
    MINTi MINT-6803908.
    STRINGi 9606.ENSP00000331879.

    Chemistry

    BindingDBi O60678.
    ChEMBLi CHEMBL5891.
    GuidetoPHARMACOLOGYi 1254.

    PTM databases

    PhosphoSitei O60678.

    Proteomic databases

    MaxQBi O60678.
    PaxDbi O60678.
    PRIDEi O60678.

    Protocols and materials databases

    DNASUi 10196.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331079 ; ENSP00000331879 ; ENSG00000185238 . [O60678-1 ]
    ENST00000437750 ; ENSP00000397766 ; ENSG00000185238 . [O60678-2 ]
    GeneIDi 10196.
    KEGGi hsa:10196.
    UCSCi uc001mqb.3. human. [O60678-1 ]
    uc010rdn.2. human. [O60678-2 ]

    Organism-specific databases

    CTDi 10196.
    GeneCardsi GC11P020373.
    HGNCi HGNC:30163. PRMT3.
    HPAi CAB022083.
    HPA007832.
    MIMi 603190. gene.
    neXtProti NX_O60678.
    PharmGKBi PA29462.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0500.
    HOGENOMi HOG000198521.
    HOVERGENi HBG001793.
    KOi K11436.
    OMAi AQDFVMH.
    OrthoDBi EOG7S7SDJ.
    PhylomeDBi O60678.
    TreeFami TF323587.

    Enzyme and pathway databases

    SABIO-RK O60678.

    Miscellaneous databases

    EvolutionaryTracei O60678.
    GeneWikii PRMT3.
    GenomeRNAii 10196.
    NextBioi 38588.
    PROi O60678.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60678.
    Bgeei O60678.
    CleanExi HS_PRMT3.
    Genevestigatori O60678.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025799. Arg_MeTrfase.
    IPR010456. Ribosomal-L11_MeTrfase_PrmA.
    IPR029063. SAM-dependent_MTases-like.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    [Graphical view ]
    PANTHERi PTHR11006. PTHR11006. 1 hit.
    Pfami PF06325. PrmA. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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), VARIANT ASN-508.
    2. 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), VARIANT ASN-508.
      Tissue: Brain.
    4. "PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation."
      Tang J., Gary J.D., Clarke S., Herschman H.R.
      J. Biol. Chem. 273:16935-16945(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-531 (ISOFORM 1), VARIANT ASN-508.
    5. "DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo."
      Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A., Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.
      Oncogene 23:7761-7771(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPB41L3.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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 CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)."
      Handrkova H., Petrak J., Halada P., Pospisilova D., Cmejla R.
      Biochim. Biophys. Acta 1814:277-282(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-25 AND SER-27, MUTAGENESIS OF TYR-87, ABSENCE OF PHOSPHORYLATION AT TYR-87, INTERACTION WITH RPS2.
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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 CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "The crystal structure of human HMT1 HNRNP methyltransferase-like 3 in complex with SAH."
      Structural genomics consortium (SGC)
      Submitted (MAR-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 211-531 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.

    Entry informationi

    Entry nameiANM3_HUMAN
    AccessioniPrimary (citable) accession number: O60678
    Secondary accession number(s): B4DUC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 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 11
      Human chromosome 11: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3