Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P62318

- SMD3_HUMAN

UniProt

P62318 - SMD3_HUMAN

Protein

Small nuclear ribonucleoprotein Sm D3

Gene

SNRPD3

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

    Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing.2 Publications

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. histone pre-mRNA DCP binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. histone mRNA metabolic process Source: Reactome
    3. mRNA 3'-end processing Source: Reactome
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. ncRNA metabolic process Source: Reactome
    6. RNA metabolic process Source: Reactome
    7. RNA splicing Source: Reactome
    8. spliceosomal snRNP assembly Source: UniProtKB
    9. termination of RNA polymerase II transcription Source: Reactome
    10. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_11066. snRNP Assembly.
    REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Small nuclear ribonucleoprotein Sm D3
    Short name:
    Sm-D3
    Alternative name(s):
    snRNP core protein D3
    Gene namesi
    Name:SNRPD3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:11160. SNRPD3.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Nucleus 1 Publication
    Note: SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytosol Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. methylosome Source: UniProtKB
    6. nucleoplasm Source: Reactome
    7. nucleus Source: HPA
    8. pICln-Sm protein complex Source: UniProtKB
    9. small nuclear ribonucleoprotein complex Source: ProtInc
    10. SMN-Sm protein complex Source: UniProtKB
    11. spliceosomal complex Source: ProtInc
    12. U12-type spliceosomal complex Source: UniProtKB
    13. U1 snRNP Source: UniProtKB
    14. U4 snRNP Source: UniProtKB
    15. U7 snRNP Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36001.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 126125Small nuclear ribonucleoprotein Sm D3PRO_0000122214Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Post-translational modificationi

    Methylated on arginine residues by PRMT5 and PRMT7; probable asymmetric dimethylation which is required for assembly and biogenesis of snRNPs.2 Publications

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    MaxQBiP62318.
    PaxDbiP62318.
    PeptideAtlasiP62318.
    PRIDEiP62318.

    PTM databases

    PhosphoSiteiP62318.

    Expressioni

    Gene expression databases

    ArrayExpressiP62318.
    BgeeiP62318.
    CleanExiHS_SNRPD3.
    GenevestigatoriP62318.

    Organism-specific databases

    HPAiHPA001170.

    Interactioni

    Subunit structurei

    U1 snRNP is for instance composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of the U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CLNS1AP541056EBI-372789,EBI-724693
    LSM7Q9UK453EBI-372789,EBI-348372
    SNRPBP146782EBI-372789,EBI-372458

    Protein-protein interaction databases

    BioGridi112518. 88 interactions.
    DIPiDIP-31216N.
    IntActiP62318. 38 interactions.
    MINTiMINT-5002679.
    STRINGi9606.ENSP00000215829.

    Structurei

    Secondary structure

    1
    126
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 127
    Turni13 – 153
    Beta strandi16 – 227
    Beta strandi27 – 359
    Beta strandi41 – 499
    Beta strandi55 – 639
    Helixi65 – 673
    Beta strandi68 – 736

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D3BX-ray2.00A/C/E/G/I/K1-75[»]
    2Y9AX-ray3.60D/K/R1-126[»]
    2Y9BX-ray3.60D/K/R1-126[»]
    2Y9CX-ray3.60D/K/R1-126[»]
    2Y9DX-ray3.60D/K/R1-126[»]
    3CW1X-ray5.49D/S/T/U1-126[»]
    3PGWX-ray4.40W/Z1-126[»]
    3VRIX-ray1.60C54-63[»]
    ProteinModelPortaliP62318.
    SMRiP62318. Positions 4-92.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62318.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati110 – 11121
    Repeati112 – 11322
    Repeati114 – 11523
    Repeati116 – 11724
    Repeati118 – 11925

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 119105 X 2 AA tandem repeats of [RM]-G

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi84 – 12643Arg/Lys-rich (basic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the snRNP core protein family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1958.
    HOGENOMiHOG000182712.
    HOVERGENiHBG105305.
    InParanoidiP62318.
    KOiK11088.
    OMAiIMRANAR.
    OrthoDBiEOG7VTDQF.
    PhylomeDBiP62318.
    TreeFamiTF354302.

    Family and domain databases

    InterProiIPR027141. LSm4/Sm_D1/D3.
    IPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    [Graphical view]
    PANTHERiPTHR23338. PTHR23338. 1 hit.
    PfamiPF01423. LSM. 1 hit.
    [Graphical view]
    SMARTiSM00651. Sm. 1 hit.
    [Graphical view]
    SUPFAMiSSF50182. SSF50182. 1 hit.

    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: P62318-1) [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

    MSIGVPIKVL HEAEGHIVTC ETNTGEVYRG KLIEAEDNMN CQMSNITVTY    50
    RDGRVAQLEQ VYIRGSKIRF LILPDMLKNA PMLKSMKNKN QGSGAGRGKA 100
    AILKAQVAAR GRGRGMGRGN IFQKRR 126
    Length:126
    Mass (Da):13,916
    Last modified:July 5, 2004 - v1
    Checksum:i59A6E78E860AA3E0
    GO
    Isoform 2 (identifier: P62318-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         107-126: VAARGRGRGMGRGNIFQKRR → GYLSSLEWVLVHIC

    Note: No experimental confirmation available.

    Show »
    Length:120
    Mass (Da):13,292
    Checksum:iFAEF4075E9ED6E9D
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei107 – 12620VAARG…FQKRR → GYLSSLEWVLVHIC in isoform 2. 1 PublicationVSP_056478Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15009 mRNA. Translation: AAA57034.1.
    CR456583 mRNA. Translation: CAG30469.1.
    AK296173 mRNA. Translation: BAG58909.1.
    AB451249 mRNA. Translation: BAG70063.1.
    AB451373 mRNA. Translation: BAG70187.1.
    AP000356 Genomic DNA. No translation available.
    CH471095 Genomic DNA. Translation: EAW59670.1.
    BC000457 mRNA. Translation: AAH00457.1.
    BC003150 mRNA. Translation: AAH03150.1.
    CCDSiCCDS13828.1.
    RefSeqiNP_001265585.1. NM_001278656.1.
    NP_004166.1. NM_004175.4.
    UniGeneiHs.356549.

    Genome annotation databases

    EnsembliENST00000215829; ENSP00000215829; ENSG00000100028.
    ENST00000402849; ENSP00000385266; ENSG00000100028.
    ENST00000404603; ENSP00000456090; ENSG00000100028.
    GeneIDi6634.
    KEGGihsa:6634.
    UCSCiuc003aam.1. human.

    Polymorphism databases

    DMDMi51338667.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15009 mRNA. Translation: AAA57034.1 .
    CR456583 mRNA. Translation: CAG30469.1 .
    AK296173 mRNA. Translation: BAG58909.1 .
    AB451249 mRNA. Translation: BAG70063.1 .
    AB451373 mRNA. Translation: BAG70187.1 .
    AP000356 Genomic DNA. No translation available.
    CH471095 Genomic DNA. Translation: EAW59670.1 .
    BC000457 mRNA. Translation: AAH00457.1 .
    BC003150 mRNA. Translation: AAH03150.1 .
    CCDSi CCDS13828.1.
    RefSeqi NP_001265585.1. NM_001278656.1.
    NP_004166.1. NM_004175.4.
    UniGenei Hs.356549.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D3B X-ray 2.00 A/C/E/G/I/K 1-75 [» ]
    2Y9A X-ray 3.60 D/K/R 1-126 [» ]
    2Y9B X-ray 3.60 D/K/R 1-126 [» ]
    2Y9C X-ray 3.60 D/K/R 1-126 [» ]
    2Y9D X-ray 3.60 D/K/R 1-126 [» ]
    3CW1 X-ray 5.49 D/S/T/U 1-126 [» ]
    3PGW X-ray 4.40 W/Z 1-126 [» ]
    3VRI X-ray 1.60 C 54-63 [» ]
    ProteinModelPortali P62318.
    SMRi P62318. Positions 4-92.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112518. 88 interactions.
    DIPi DIP-31216N.
    IntActi P62318. 38 interactions.
    MINTi MINT-5002679.
    STRINGi 9606.ENSP00000215829.

    PTM databases

    PhosphoSitei P62318.

    Polymorphism databases

    DMDMi 51338667.

    Proteomic databases

    MaxQBi P62318.
    PaxDbi P62318.
    PeptideAtlasi P62318.
    PRIDEi P62318.

    Protocols and materials databases

    DNASUi 6634.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215829 ; ENSP00000215829 ; ENSG00000100028 .
    ENST00000402849 ; ENSP00000385266 ; ENSG00000100028 .
    ENST00000404603 ; ENSP00000456090 ; ENSG00000100028 .
    GeneIDi 6634.
    KEGGi hsa:6634.
    UCSCi uc003aam.1. human.

    Organism-specific databases

    CTDi 6634.
    GeneCardsi GC22P024951.
    HGNCi HGNC:11160. SNRPD3.
    HPAi HPA001170.
    MIMi 601062. gene.
    neXtProti NX_P62318.
    PharmGKBi PA36001.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1958.
    HOGENOMi HOG000182712.
    HOVERGENi HBG105305.
    InParanoidi P62318.
    KOi K11088.
    OMAi IMRANAR.
    OrthoDBi EOG7VTDQF.
    PhylomeDBi P62318.
    TreeFami TF354302.

    Enzyme and pathway databases

    Reactomei REACT_11066. snRNP Assembly.
    REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    EvolutionaryTracei P62318.
    GeneWikii SNRPD3.
    GenomeRNAii 6634.
    NextBioi 25845.
    PROi P62318.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62318.
    Bgeei P62318.
    CleanExi HS_SNRPD3.
    Genevestigatori P62318.

    Family and domain databases

    InterProi IPR027141. LSm4/Sm_D1/D3.
    IPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    [Graphical view ]
    PANTHERi PTHR23338. PTHR23338. 1 hit.
    Pfami PF01423. LSM. 1 hit.
    [Graphical view ]
    SMARTi SM00651. Sm. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50182. SSF50182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction."
      Lehmeier T., Raker V., Hermann H., Luehrmann R.
      Proc. Natl. Acad. Sci. U.S.A. 91:12317-12321(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "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: Thalamus.
    4. "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).
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Lung.
    8. "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: METHYLATION.
    9. "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein."
      Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.
      EMBO J. 20:5470-5479(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE U7 SNRNP COMPLEX.
    10. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    11. "The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
      Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
      RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "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: METHYLATION, INTERACTION WITH PRMT5 AND PRMT7.
    13. "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: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN SMN-SM COMPLEX, SUBCELLULAR LOCATION.
    14. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs."
      Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E., Raker V.A., Luehrmann R., Li J., Nagai K.
      Cell 96:375-387(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-75 IN COMPLEX WITH SNRPB.
    17. "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
      Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
      Nature 458:475-480(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) IN SPLICEOSOMAL U1 SNRNP.
    18. "Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis."
      Leung A.K., Nagai K., Li J.
      Nature 473:536-539(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP.

    Entry informationi

    Entry nameiSMD3_HUMAN
    AccessioniPrimary (citable) accession number: P62318
    Secondary accession number(s): B4DJP7, B5BU13, P43331
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 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

    Miscellaneous

    In the autoimmune disease systemic lupus erythematosus, antinuclear antibodies are developed with Sm specificity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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