Full text data of SNRPD3
SNRPD3
[Confidence: low (only semi-automatic identification from reviews)]
Small nuclear ribonucleoprotein Sm D3; Sm-D3 (snRNP core protein D3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Small nuclear ribonucleoprotein Sm D3; Sm-D3 (snRNP core protein D3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62318
ID SMD3_HUMAN Reviewed; 126 AA.
AC P62318; B5BU13; P43331;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D3;
DE Short=Sm-D3;
DE AltName: Full=snRNP core protein D3;
GN Name=SNRPD3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7527560; DOI=10.1073/pnas.91.25.12317;
RA Lehmeier T., Raker V., Hermann H., Luehrmann R.;
RT "cDNA cloning of the Sm proteins D2 and D3 from human small nuclear
RT ribonucleoproteins: evidence for a direct D1-D2 interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12317-12321(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP METHYLATION.
RX PubMed=11747828; DOI=10.1016/S0960-9822(01)00592-9;
RA Meister G., Eggert C., Buehler D., Brahms H., Kambach C., Fischer U.;
RT "Methylation of Sm proteins by a complex containing PRMT5 and the
RT putative U snRNP assembly factor pICln.";
RL Curr. Biol. 11:1990-1994(2001).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE U7 SNRNP COMPLEX.
RX PubMed=11574479; DOI=10.1093/emboj/20.19.5470;
RA Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.;
RT "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10,
RT a new 14 kDa Sm D1-like protein.";
RL EMBO J. 20:5470-5479(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND MASS
RP SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R.,
RA Elbashir S., Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not
RT found in the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [10]
RP METHYLATION, AND INTERACTION WITH PRMT5 AND PRMT7.
RX PubMed=17709427; DOI=10.1083/jcb.200702147;
RA Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I.,
RA Matera A.G.;
RT "Two distinct arginine methyltransferases are required for biogenesis
RT of Sm-class ribonucleoproteins.";
RL J. Cell Biol. 178:733-740(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-75 IN COMPLEX WITH SNRPB.
RX PubMed=10025403; DOI=10.1016/S0092-8674(00)80550-4;
RA Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E.,
RA Raker V.A., Luehrmann R., Li J., Nagai K.;
RT "Crystal structures of two Sm protein complexes and their implications
RT for the assembly of the spliceosomal snRNPs.";
RL Cell 96:375-387(1999).
CC -!- FUNCTION: Appears to function in the U7 snRNP complex that is
CC involved in histone 3'-end processing. Binds to the downstream
CC cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent
CC manner.
CC -!- SUBUNIT: Component of the heptameric ring U7 snRNP complex, or U7
CC Sm protein core complex, at least composed of LSM10, LSM11, SNRPB,
CC SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Formation of the U7
CC snRNP is an ATP-dependent process mediated by a specialized SMN
CC complex containing at least the Sm protein core complex and
CC additionally, the U7-specific LSM10 and LSM11 proteins. Identified
CC in the spliceosome C complex. Component of the U11/U12 snRNPs that
CC are part of the U12-type spliceosome.
CC -!- INTERACTION:
CC P54105:CLNS1A; NbExp=6; IntAct=EBI-372789, EBI-724693;
CC Q9UK45:LSM7; NbExp=3; IntAct=EBI-372789, EBI-348372;
CC P14678:SNRPB; NbExp=2; IntAct=EBI-372789, EBI-372458;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Methylated on arginine residues by PRMT5 and PRMT7;
CC methylation is required for assembly and biogenesis of snRNPs.
CC -!- PTM: Arg-97 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- MISCELLANEOUS: In the autoimmune disease systemic lupus
CC erythematosus, antinuclear antibodies are developed with Sm
CC specificity.
CC -!- SIMILARITY: Belongs to the snRNP core protein family.
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DR EMBL; U15009; AAA57034.1; -; mRNA.
DR EMBL; CR456583; CAG30469.1; -; mRNA.
DR EMBL; AB451249; BAG70063.1; -; mRNA.
DR EMBL; AB451373; BAG70187.1; -; mRNA.
DR EMBL; CH471095; EAW59670.1; -; Genomic_DNA.
DR EMBL; BC000457; AAH00457.1; -; mRNA.
DR EMBL; BC003150; AAH03150.1; -; mRNA.
DR RefSeq; NP_001265585.1; NM_001278656.1.
DR RefSeq; NP_004166.1; NM_004175.4.
DR UniGene; Hs.356549; -.
DR PDB; 1D3B; X-ray; 2.00 A; A/C/E/G/I/K=1-75.
DR PDB; 2Y9A; X-ray; 3.60 A; D/K/R=1-126.
DR PDB; 2Y9B; X-ray; 3.60 A; D/K/R=1-126.
DR PDB; 2Y9C; X-ray; 3.60 A; D/K/R=1-126.
DR PDB; 2Y9D; X-ray; 3.60 A; D/K/R=1-126.
DR PDB; 3CW1; X-ray; 5.49 A; D/S/T/U=1-126.
DR PDB; 3PGW; X-ray; 4.40 A; W/Z=1-126.
DR PDB; 3VRI; X-ray; 1.60 A; C=54-63.
DR PDBsum; 1D3B; -.
DR PDBsum; 2Y9A; -.
DR PDBsum; 2Y9B; -.
DR PDBsum; 2Y9C; -.
DR PDBsum; 2Y9D; -.
DR PDBsum; 3CW1; -.
DR PDBsum; 3PGW; -.
DR PDBsum; 3VRI; -.
DR ProteinModelPortal; P62318; -.
DR SMR; P62318; 4-92.
DR DIP; DIP-31216N; -.
DR IntAct; P62318; 38.
DR MINT; MINT-5002679; -.
DR STRING; 9606.ENSP00000215829; -.
DR PhosphoSite; P62318; -.
DR DMDM; 51338667; -.
DR PaxDb; P62318; -.
DR PeptideAtlas; P62318; -.
DR PRIDE; P62318; -.
DR DNASU; 6634; -.
DR Ensembl; ENST00000215829; ENSP00000215829; ENSG00000100028.
DR Ensembl; ENST00000404603; ENSP00000456090; ENSG00000100028.
DR GeneID; 6634; -.
DR KEGG; hsa:6634; -.
DR UCSC; uc003aam.1; human.
DR CTD; 6634; -.
DR GeneCards; GC22P024951; -.
DR HGNC; HGNC:11160; SNRPD3.
DR HPA; HPA001170; -.
DR MIM; 601062; gene.
DR neXtProt; NX_P62318; -.
DR PharmGKB; PA36001; -.
DR eggNOG; COG1958; -.
DR HOGENOM; HOG000182712; -.
DR HOVERGEN; HBG105305; -.
DR InParanoid; P62318; -.
DR KO; K11088; -.
DR OMA; IMRANAR; -.
DR OrthoDB; EOG7VTDQF; -.
DR PhylomeDB; P62318; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR Reactome; REACT_78; Post-Elongation Processing of the Transcript.
DR EvolutionaryTrace; P62318; -.
DR GeneWiki; SNRPD3; -.
DR GenomeRNAi; 6634; -.
DR NextBio; 25845; -.
DR PRO; PR:P62318; -.
DR ArrayExpress; P62318; -.
DR Bgee; P62318; -.
DR CleanEx; HS_SNRPD3; -.
DR Genevestigator; P62318; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB.
DR GO; GO:0071208; F:histone pre-mRNA DCP binding; ISS:UniProtKB.
DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome.
DR GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
DR GO; GO:0034660; P:ncRNA metabolic process; TAS:Reactome.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; TAS:Reactome.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR010920; LSM_dom.
DR InterPro; IPR001163; Ribonucl_LSM.
DR InterPro; IPR006649; Ribonucl_LSM_euk/arc.
DR PANTHER; PTHR23338; PTHR23338; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW RNA-binding; Spliceosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 126 Small nuclear ribonucleoprotein Sm D3.
FT /FTId=PRO_0000122214.
FT REPEAT 110 111 1.
FT REPEAT 112 113 2.
FT REPEAT 114 115 3.
FT REPEAT 116 117 4.
FT REPEAT 118 119 5.
FT REGION 110 119 5 X 2 AA tandem repeats of [RM]-G.
FT COMPBIAS 84 126 Arg/Lys-rich (basic).
FT MOD_RES 2 2 N-acetylserine.
FT HELIX 6 12
FT TURN 13 15
FT STRAND 16 22
FT STRAND 27 35
FT STRAND 41 49
FT STRAND 55 63
FT HELIX 65 67
FT STRAND 68 73
SQ SEQUENCE 126 AA; 13916 MW; 59A6E78E860AA3E0 CRC64;
MSIGVPIKVL HEAEGHIVTC ETNTGEVYRG KLIEAEDNMN CQMSNITVTY RDGRVAQLEQ
VYIRGSKIRF LILPDMLKNA PMLKSMKNKN QGSGAGRGKA AILKAQVAAR GRGRGMGRGN
IFQKRR
//
ID SMD3_HUMAN Reviewed; 126 AA.
AC P62318; B5BU13; P43331;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D3;
DE Short=Sm-D3;
DE AltName: Full=snRNP core protein D3;
GN Name=SNRPD3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7527560; DOI=10.1073/pnas.91.25.12317;
RA Lehmeier T., Raker V., Hermann H., Luehrmann R.;
RT "cDNA cloning of the Sm proteins D2 and D3 from human small nuclear
RT ribonucleoproteins: evidence for a direct D1-D2 interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12317-12321(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP METHYLATION.
RX PubMed=11747828; DOI=10.1016/S0960-9822(01)00592-9;
RA Meister G., Eggert C., Buehler D., Brahms H., Kambach C., Fischer U.;
RT "Methylation of Sm proteins by a complex containing PRMT5 and the
RT putative U snRNP assembly factor pICln.";
RL Curr. Biol. 11:1990-1994(2001).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE U7 SNRNP COMPLEX.
RX PubMed=11574479; DOI=10.1093/emboj/20.19.5470;
RA Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.;
RT "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10,
RT a new 14 kDa Sm D1-like protein.";
RL EMBO J. 20:5470-5479(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND MASS
RP SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R.,
RA Elbashir S., Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not
RT found in the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [10]
RP METHYLATION, AND INTERACTION WITH PRMT5 AND PRMT7.
RX PubMed=17709427; DOI=10.1083/jcb.200702147;
RA Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I.,
RA Matera A.G.;
RT "Two distinct arginine methyltransferases are required for biogenesis
RT of Sm-class ribonucleoproteins.";
RL J. Cell Biol. 178:733-740(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-75 IN COMPLEX WITH SNRPB.
RX PubMed=10025403; DOI=10.1016/S0092-8674(00)80550-4;
RA Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E.,
RA Raker V.A., Luehrmann R., Li J., Nagai K.;
RT "Crystal structures of two Sm protein complexes and their implications
RT for the assembly of the spliceosomal snRNPs.";
RL Cell 96:375-387(1999).
CC -!- FUNCTION: Appears to function in the U7 snRNP complex that is
CC involved in histone 3'-end processing. Binds to the downstream
CC cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent
CC manner.
CC -!- SUBUNIT: Component of the heptameric ring U7 snRNP complex, or U7
CC Sm protein core complex, at least composed of LSM10, LSM11, SNRPB,
CC SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Formation of the U7
CC snRNP is an ATP-dependent process mediated by a specialized SMN
CC complex containing at least the Sm protein core complex and
CC additionally, the U7-specific LSM10 and LSM11 proteins. Identified
CC in the spliceosome C complex. Component of the U11/U12 snRNPs that
CC are part of the U12-type spliceosome.
CC -!- INTERACTION:
CC P54105:CLNS1A; NbExp=6; IntAct=EBI-372789, EBI-724693;
CC Q9UK45:LSM7; NbExp=3; IntAct=EBI-372789, EBI-348372;
CC P14678:SNRPB; NbExp=2; IntAct=EBI-372789, EBI-372458;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Methylated on arginine residues by PRMT5 and PRMT7;
CC methylation is required for assembly and biogenesis of snRNPs.
CC -!- PTM: Arg-97 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- MISCELLANEOUS: In the autoimmune disease systemic lupus
CC erythematosus, antinuclear antibodies are developed with Sm
CC specificity.
CC -!- SIMILARITY: Belongs to the snRNP core protein family.
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CC -----------------------------------------------------------------------
DR EMBL; U15009; AAA57034.1; -; mRNA.
DR EMBL; CR456583; CAG30469.1; -; mRNA.
DR EMBL; AB451249; BAG70063.1; -; mRNA.
DR EMBL; AB451373; BAG70187.1; -; mRNA.
DR EMBL; CH471095; EAW59670.1; -; Genomic_DNA.
DR EMBL; BC000457; AAH00457.1; -; mRNA.
DR EMBL; BC003150; AAH03150.1; -; mRNA.
DR RefSeq; NP_001265585.1; NM_001278656.1.
DR RefSeq; NP_004166.1; NM_004175.4.
DR UniGene; Hs.356549; -.
DR PDB; 1D3B; X-ray; 2.00 A; A/C/E/G/I/K=1-75.
DR PDB; 2Y9A; X-ray; 3.60 A; D/K/R=1-126.
DR PDB; 2Y9B; X-ray; 3.60 A; D/K/R=1-126.
DR PDB; 2Y9C; X-ray; 3.60 A; D/K/R=1-126.
DR PDB; 2Y9D; X-ray; 3.60 A; D/K/R=1-126.
DR PDB; 3CW1; X-ray; 5.49 A; D/S/T/U=1-126.
DR PDB; 3PGW; X-ray; 4.40 A; W/Z=1-126.
DR PDB; 3VRI; X-ray; 1.60 A; C=54-63.
DR PDBsum; 1D3B; -.
DR PDBsum; 2Y9A; -.
DR PDBsum; 2Y9B; -.
DR PDBsum; 2Y9C; -.
DR PDBsum; 2Y9D; -.
DR PDBsum; 3CW1; -.
DR PDBsum; 3PGW; -.
DR PDBsum; 3VRI; -.
DR ProteinModelPortal; P62318; -.
DR SMR; P62318; 4-92.
DR DIP; DIP-31216N; -.
DR IntAct; P62318; 38.
DR MINT; MINT-5002679; -.
DR STRING; 9606.ENSP00000215829; -.
DR PhosphoSite; P62318; -.
DR DMDM; 51338667; -.
DR PaxDb; P62318; -.
DR PeptideAtlas; P62318; -.
DR PRIDE; P62318; -.
DR DNASU; 6634; -.
DR Ensembl; ENST00000215829; ENSP00000215829; ENSG00000100028.
DR Ensembl; ENST00000404603; ENSP00000456090; ENSG00000100028.
DR GeneID; 6634; -.
DR KEGG; hsa:6634; -.
DR UCSC; uc003aam.1; human.
DR CTD; 6634; -.
DR GeneCards; GC22P024951; -.
DR HGNC; HGNC:11160; SNRPD3.
DR HPA; HPA001170; -.
DR MIM; 601062; gene.
DR neXtProt; NX_P62318; -.
DR PharmGKB; PA36001; -.
DR eggNOG; COG1958; -.
DR HOGENOM; HOG000182712; -.
DR HOVERGEN; HBG105305; -.
DR InParanoid; P62318; -.
DR KO; K11088; -.
DR OMA; IMRANAR; -.
DR OrthoDB; EOG7VTDQF; -.
DR PhylomeDB; P62318; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR Reactome; REACT_78; Post-Elongation Processing of the Transcript.
DR EvolutionaryTrace; P62318; -.
DR GeneWiki; SNRPD3; -.
DR GenomeRNAi; 6634; -.
DR NextBio; 25845; -.
DR PRO; PR:P62318; -.
DR ArrayExpress; P62318; -.
DR Bgee; P62318; -.
DR CleanEx; HS_SNRPD3; -.
DR Genevestigator; P62318; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB.
DR GO; GO:0071208; F:histone pre-mRNA DCP binding; ISS:UniProtKB.
DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome.
DR GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
DR GO; GO:0034660; P:ncRNA metabolic process; TAS:Reactome.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; TAS:Reactome.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR010920; LSM_dom.
DR InterPro; IPR001163; Ribonucl_LSM.
DR InterPro; IPR006649; Ribonucl_LSM_euk/arc.
DR PANTHER; PTHR23338; PTHR23338; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW RNA-binding; Spliceosome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 126 Small nuclear ribonucleoprotein Sm D3.
FT /FTId=PRO_0000122214.
FT REPEAT 110 111 1.
FT REPEAT 112 113 2.
FT REPEAT 114 115 3.
FT REPEAT 116 117 4.
FT REPEAT 118 119 5.
FT REGION 110 119 5 X 2 AA tandem repeats of [RM]-G.
FT COMPBIAS 84 126 Arg/Lys-rich (basic).
FT MOD_RES 2 2 N-acetylserine.
FT HELIX 6 12
FT TURN 13 15
FT STRAND 16 22
FT STRAND 27 35
FT STRAND 41 49
FT STRAND 55 63
FT HELIX 65 67
FT STRAND 68 73
SQ SEQUENCE 126 AA; 13916 MW; 59A6E78E860AA3E0 CRC64;
MSIGVPIKVL HEAEGHIVTC ETNTGEVYRG KLIEAEDNMN CQMSNITVTY RDGRVAQLEQ
VYIRGSKIRF LILPDMLKNA PMLKSMKNKN QGSGAGRGKA AILKAQVAAR GRGRGMGRGN
IFQKRR
//
MIM
601062
*RECORD*
*FIELD* NO
601062
*FIELD* TI
*601062 SMALL NUCLEAR RIBONUCLEOPROTEIN POLYPEPTIDE D3; SNRPD3
*FIELD* TX
CLONING
read more
See also SNRPD2 (601061) and SNRPD1 (601063). Lehmeier et al. (1994)
obtained partial amino acid sequence for the D2 and D3 protein
components of small nuclear ribonucleoproteins (snRNPs). Degenerate
oligomers were designed and used to isolate 2 cDNAs from a HeLa cell
library. The sequence of the D3 cDNA predicts a 126-amino acid protein
with 29% identity to the D1 polypeptide. Recombinantly expressed protein
could be precipitated with anti-Sm antibodies.
*FIELD* RF
1. Lehmeier, T.; Raker, V.; Hermann, H.; Luhrmann, R.: cDNA cloning
of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins:
evidence for a direct D1-D2 interaction. Proc. Nat. Acad. Sci. 91:
12317-12321, 1994.
*FIELD* CD
Alan F. Scott: 2/12/1996
*FIELD* ED
alopez: 04/06/2010
alopez: 2/11/1999
mark: 2/12/1996
*RECORD*
*FIELD* NO
601062
*FIELD* TI
*601062 SMALL NUCLEAR RIBONUCLEOPROTEIN POLYPEPTIDE D3; SNRPD3
*FIELD* TX
CLONING
read more
See also SNRPD2 (601061) and SNRPD1 (601063). Lehmeier et al. (1994)
obtained partial amino acid sequence for the D2 and D3 protein
components of small nuclear ribonucleoproteins (snRNPs). Degenerate
oligomers were designed and used to isolate 2 cDNAs from a HeLa cell
library. The sequence of the D3 cDNA predicts a 126-amino acid protein
with 29% identity to the D1 polypeptide. Recombinantly expressed protein
could be precipitated with anti-Sm antibodies.
*FIELD* RF
1. Lehmeier, T.; Raker, V.; Hermann, H.; Luhrmann, R.: cDNA cloning
of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins:
evidence for a direct D1-D2 interaction. Proc. Nat. Acad. Sci. 91:
12317-12321, 1994.
*FIELD* CD
Alan F. Scott: 2/12/1996
*FIELD* ED
alopez: 04/06/2010
alopez: 2/11/1999
mark: 2/12/1996