SMD1_HUMAN
ID SMD1_HUMAN Reviewed; 119 AA.
AC P62314; B5BTZ1; P13641;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D1;
DE Short=Sm-D1;
DE AltName: Full=Sm-D autoantigen;
DE AltName: Full=snRNP core protein D1;
GN Name=SNRPD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-11.
RC TISSUE=Placenta;
RX PubMed=3260384; DOI=10.1073/pnas.85.13.4832;
RA Rokeach L.A., Haselby J.A., Hoch S.O.;
RT "Molecular cloning of a cDNA encoding the human Sm-D autoantigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4832-4836(1988).
RN [2]
RP SEQUENCE REVISION.
RA Rokeach L.A.;
RL Submitted (JUL-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2528429;
RA Renz M., Heim C., Braeunling O., Czichos A., Wieland C., Seelig H.P.;
RT "Expression of the major human ribonucleoprotein (RNP) autoantigens in
RT Escherichia coli and their use in an EIA for screening sera from patients
RT with autoimmune diseases.";
RL Clin. Chem. 35:1861-1863(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH SMN1.
RX PubMed=10500148; DOI=10.1073/pnas.96.20.11167;
RA Pellizzoni L., Charroux B., Dreyfuss G.;
RT "SMN mutants of spinal muscular atrophy patients are defective in binding
RT to snRNP proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11167-11172(1999).
RN [9]
RP METHYLATION, INTERACTION WITH CLNS1A, AND MUTAGENESIS OF LEU-58 AND ILE-60.
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 putative
RT U snRNP assembly factor pICln.";
RL Curr. Biol. 11:1990-1994(2001).
RN [10]
RP INTERACTION WITH SMN1.
RX PubMed=11135666; DOI=10.1038/83014;
RA Selenko P., Sprangers R., Stier G., Buhler D., Fischer U., Sattler M.;
RT "SMN tudor domain structure and its interaction with the Sm proteins.";
RL Nat. Struct. Biol. 8:27-31(2001).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
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 [12]
RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S.,
RA Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in
RT the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [13]
RP IDENTIFICATION IN THE SMN-SM COMPLEX.
RX PubMed=16314521; DOI=10.1128/mcb.25.24.10989-11004.2005;
RA Golembe T.J., Yong J., Dreyfuss G.;
RT "Specific sequence features, recognized by the SMN complex, identify snRNAs
RT and determine their fate as snRNPs.";
RL Mol. Cell. Biol. 25:10989-11004(2005).
RN [14]
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 of
RT Sm-class ribonucleoproteins.";
RL J. Cell Biol. 178:733-740(2007).
RN [15]
RP FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX,
RP IDENTIFICATION IN SMN-SM COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
RA Englbrecht C., Sickmann A., Stark H., Fischer U.;
RT "An assembly chaperone collaborates with the SMN complex to generate
RT spliceosomal SnRNPs.";
RL Cell 135:497-509(2008).
RN [16]
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., Buerckstuemmer T.,
RA 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-86, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-81 IN COMPLEX WITH SNRPD2.
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., Raker V.A.,
RA Luehrmann R., Li J., Nagai K.;
RT "Crystal structures of two Sm protein complexes and their implications for
RT the assembly of the spliceosomal snRNPs.";
RL Cell 96:375-387(1999).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) IN SPLICEOSOMAL U1 SNRNP, FUNCTION,
RP AND SUBUNIT.
RX PubMed=19325628; DOI=10.1038/nature07851;
RA Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.;
RT "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution.";
RL Nature 458:475-480(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (4.40 ANGSTROMS) IN SPLICEOSOMAL U1 SNRNP,
RP SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21113136; DOI=10.1038/emboj.2010.295;
RA Weber G., Trowitzsch S., Kastner B., Luhrmann R., Wahl M.C.;
RT "Functional organization of the Sm core in the crystal structure of human
RT U1 snRNP.";
RL EMBO J. 29:4172-4184(2010).
RN [21] {ECO:0007744|PDB:5XJL}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SNRPD2; SNRPE;
RP SNRPF; SNRPG; SMN1 AND GEMIN2, AND INTERACTION WITH GEMIN2 AND SNRPD2.
RX PubMed=21816274; DOI=10.1016/j.cell.2011.06.043;
RA Zhang R., So B.R., Li P., Yong J., Glisovic T., Wan L., Dreyfuss G.;
RT "Structure of a key intermediate of the SMN complex reveals Gemin2's
RT crucial function in snRNP assembly.";
RL Cell 146:384-395(2011).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP, AND
RP SUBUNIT.
RX PubMed=21516107; DOI=10.1038/nature09956;
RA Leung A.K., Nagai K., Li J.;
RT "Structure of the spliceosomal U4 snRNP core domain and its implication for
RT snRNP biogenesis.";
RL Nature 473:536-539(2011).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN 6S PICLN-SM COMPLEX,
RP IDENTIFICATION IN 6S PICLN-SM COMPLEX, AND FUNCTION IN CORE U1 SNRNP
RP BIOGENESIS.
RX PubMed=23333303; DOI=10.1016/j.molcel.2012.12.009;
RA Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K.,
RA Stark H., Schindelin H., Fischer U.;
RT "Structural basis of assembly chaperone-mediated snRNP formation.";
RL Mol. Cell 49:692-703(2013).
RN [24] {ECO:0007744|PDB:4PJO}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 2-85, AND SUBUNIT.
RX PubMed=25555158; DOI=10.7554/elife.04986;
RA Kondo Y., Oubridge C., van Roon A.M., Nagai K.;
RT "Crystal structure of human U1 snRNP, a small nuclear ribonucleoprotein
RT particle, reveals the mechanism of 5' splice site recognition.";
RL Elife 4:0-0(2015).
RN [25] {ECO:0007744|PDB:3JCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION,
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26912367; DOI=10.1126/science.aad2085;
RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H.,
RA Luhrmann R., Stark H.;
RT "Molecular architecture of the human U4/U6.U5 tri-snRNP.";
RL Science 351:1416-1420(2016).
RN [26] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [27] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
RN [28] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
RN [29] {ECO:0007744|PDB:5XJQ, ECO:0007744|PDB:5XJR, ECO:0007744|PDB:5XJS}
RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 1-82 IN COMPLEX WITH GEMIN2;
RP SNRPD2; SNRPE; SNRPF; SNRPG AND SMN1, AND INTERACTION WITH GEMIN2 AND
RP SNRPD2.
RX PubMed=31799625; DOI=10.1093/nar/gkz1135;
RA Yi H., Mu L., Shen C., Kong X., Wang Y., Hou Y., Zhang R.;
RT "Negative cooperativity between Gemin2 and RNA provides insights into RNA
RT selection and the SMN complex's release in snRNP assembly.";
RL Nucleic Acids Res. 48:895-911(2020).
CC -!- FUNCTION: Plays a role in pre-mRNA splicing as a core component of the
CC spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC (snRNPs), the building blocks of the spliceosome (PubMed:11991638,
CC PubMed:18984161, PubMed:19325628, PubMed:23333303, PubMed:25555158,
CC PubMed:26912367, PubMed:28502770, PubMed:28781166, PubMed:28076346).
CC Component of both the pre-catalytic spliceosome B complex and activated
CC spliceosome C complexes (PubMed:11991638, PubMed:26912367,
CC PubMed:28502770, PubMed:28781166, PubMed:28076346). Is also a component
CC of the minor U12 spliceosome (PubMed:15146077). May act as a charged
CC protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP
CC interactions through non-specific electrostatic contacts with RNA
CC (Probable). {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15146077,
CC ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:19325628,
CC ECO:0000269|PubMed:23333303, ECO:0000269|PubMed:25555158,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166,
CC ECO:0000305|PubMed:23333303}.
CC -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small
CC nuclear ribonucleoproteins (snRNPs), the building blocks of the
CC spliceosome (PubMed:11991638, PubMed:19325628, PubMed:25555158,
CC PubMed:26912367, PubMed:28502770, PubMed:28781166, PubMed:28076346).
CC Most spliceosomal snRNPs contain a common set of Sm proteins, SNRPB,
CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a
CC heptameric protein ring on the Sm site of the small nuclear RNA to form
CC the core snRNP (PubMed:10025403, PubMed:19325628, PubMed:21113136,
CC PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166,
CC PubMed:28076346). Component of the U1 snRNP (PubMed:19325628,
CC PubMed:21113136, PubMed:25555158). The U1 snRNP is composed of the U1
CC snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC SNRPF and SNRPG, and at least three U1 snRNP-specific proteins
CC SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C (PubMed:19325628,
CC PubMed:21113136, PubMed:25555158). Component of the U4/U6-U5 tri-snRNP
CC complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4,
CC PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1
CC and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8
CC (PubMed:26912367). Component of the U11/U12 snRNPs that are part of the
CC U12-type spliceosome (PubMed:15146077). Part of the SMN-Sm complex that
CC contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6,
CC GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly
CC (PubMed:16314521). Forms a 6S pICln-Sm complex composed of
CC CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like
CC structure where CLNS1A/pICln mimics additional Sm proteins and which is
CC unable to assemble into the core snRNP. Interacts (via C-terminus) with
CC SMN1 (via Tudor domain); the interaction is direct (PubMed:10500148,
CC PubMed:11135666). Interacts with GEMIN2; the interaction is direct
CC (PubMed:21816274). Interacts with SNRPD2; the interaction is direct
CC (PubMed:21816274, PubMed:31799625). {ECO:0000269|PubMed:10025403,
CC ECO:0000269|PubMed:10500148, ECO:0000269|PubMed:11135666,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15146077,
CC ECO:0000269|PubMed:16314521, ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:21113136,
CC ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:23333303,
CC ECO:0000269|PubMed:25555158, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:31799625}.
CC -!- INTERACTION:
CC P62314; P54105: CLNS1A; NbExp=12; IntAct=EBI-372177, EBI-724693;
CC P62314; Q8WXD5: GEMIN6; NbExp=2; IntAct=EBI-372177, EBI-752301;
CC P62314; Q16637: SMN2; NbExp=6; IntAct=EBI-372177, EBI-395421;
CC P62314; P62316: SNRPD2; NbExp=3; IntAct=EBI-372177, EBI-297993;
CC P62314; PRO_0000037573 [P27958]; Xeno; NbExp=7; IntAct=EBI-372177, EBI-3649474;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}.
CC Nucleus {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:21113136,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. Note=SMN-
CC mediated assembly into core snRNPs occurs in the cytosol before SMN-
CC mediated transport to the nucleus to be included in spliceosomes.
CC {ECO:0000305}.
CC -!- PTM: Methylated on arginine residues by PRMT5 and PRMT7; probable
CC asymmetric dimethylation which is required for assembly and biogenesis
CC of snRNPs. {ECO:0000269|PubMed:11747828, ECO:0000269|PubMed:17709427}.
CC -!- MISCELLANEOUS: In the autoimmune disease systemic lupus erythematosus,
CC antinuclear antibodies are developed with Sm specificity.
CC -!- SIMILARITY: Belongs to the snRNP core protein family. {ECO:0000305}.
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DR EMBL; J03798; AAA36620.1; -; mRNA.
DR EMBL; L36188; AAA85339.1; -; Genomic_DNA.
DR EMBL; L36182; AAA85339.1; JOINED; Genomic_DNA.
DR EMBL; L36186; AAA85339.1; JOINED; Genomic_DNA.
DR EMBL; L36187; AAA85339.1; JOINED; Genomic_DNA.
DR EMBL; CR542239; CAG47035.1; -; mRNA.
DR EMBL; AB451227; BAG70041.1; -; mRNA.
DR EMBL; AB451350; BAG70164.1; -; mRNA.
DR EMBL; CH471088; EAX01130.1; -; Genomic_DNA.
DR EMBL; BC001721; AAH01721.1; -; mRNA.
DR EMBL; BC072427; AAH72427.1; -; mRNA.
DR CCDS; CCDS32801.1; -.
DR PIR; A94201; A27668.
DR RefSeq; NP_001278845.1; NM_001291916.1.
DR RefSeq; NP_008869.1; NM_006938.3.
DR PDB; 1B34; X-ray; 2.50 A; A=1-119.
DR PDB; 3CW1; X-ray; 5.49 A; B/M/N/O=1-119.
DR PDB; 3JCR; EM; 7.00 A; P/p=1-119.
DR PDB; 3PGW; X-ray; 4.40 A; U/X=1-119.
DR PDB; 4F7U; X-ray; 1.90 A; A/C=1-119.
DR PDB; 4PJO; X-ray; 3.30 A; C/Q/c/q=2-85.
DR PDB; 4V98; X-ray; 3.10 A; AA/AI/AQ/AY/Ag/Ao/Aw/BA/BI/BQ/BY/Bg/Bo/Bw/CA/CI/CQ/CY/Cg/Co=1-119.
DR PDB; 4WZJ; X-ray; 3.60 A; AB/AI/AP/BB/BI/BP/CB/CI/CP/DB/DI/DP=1-119.
DR PDB; 5MQF; EM; 5.90 A; g/n=1-119.
DR PDB; 5O9Z; EM; 4.50 A; Z/g/n=1-119.
DR PDB; 5XJC; EM; 3.60 A; c/j=1-119.
DR PDB; 5XJL; X-ray; 2.50 A; A=1-119.
DR PDB; 5XJQ; X-ray; 3.28 A; A=1-82.
DR PDB; 5XJR; X-ray; 3.12 A; A=1-82.
DR PDB; 5XJS; X-ray; 3.38 A; A=1-82.
DR PDB; 5XJT; X-ray; 2.92 A; A=1-82.
DR PDB; 5XJU; X-ray; 2.58 A; A=1-82.
DR PDB; 5YZG; EM; 4.10 A; c/j=1-119.
DR PDB; 5Z56; EM; 5.10 A; c/j=1-119.
DR PDB; 5Z57; EM; 6.50 A; c/j=1-119.
DR PDB; 5Z58; EM; 4.90 A; c/j=1-119.
DR PDB; 6AH0; EM; 5.70 A; V/g/j=1-119.
DR PDB; 6AHD; EM; 3.80 A; V/b/j=1-119.
DR PDB; 6FF7; EM; 4.50 A; g/n=1-119.
DR PDB; 6ICZ; EM; 3.00 A; c/j=1-119.
DR PDB; 6ID0; EM; 2.90 A; c/j=1-119.
DR PDB; 6ID1; EM; 2.86 A; c/j=1-119.
DR PDB; 6QDV; EM; 3.30 A; h/l=1-78.
DR PDB; 6QW6; EM; 2.92 A; 41/51=1-119.
DR PDB; 6QX9; EM; 3.28 A; 11/21/41/51=1-119.
DR PDB; 6Y53; EM; 7.10 A; n=1-119.
DR PDB; 6Y5Q; EM; 7.10 A; n=1-119.
DR PDB; 7A5P; EM; 5.00 A; c/n=1-119.
DR PDB; 7ABG; EM; 7.80 A; g/n=1-119.
DR PDB; 7ABI; EM; 8.00 A; g/n=1-119.
DR PDB; 7B0Y; EM; 3.60 A; k=1-119.
DR PDB; 7DVQ; EM; 2.89 A; c/j=1-119.
DR PDBsum; 1B34; -.
DR PDBsum; 3CW1; -.
DR PDBsum; 3JCR; -.
DR PDBsum; 3PGW; -.
DR PDBsum; 4F7U; -.
DR PDBsum; 4PJO; -.
DR PDBsum; 4V98; -.
DR PDBsum; 4WZJ; -.
DR PDBsum; 5MQF; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5XJL; -.
DR PDBsum; 5XJQ; -.
DR PDBsum; 5XJR; -.
DR PDBsum; 5XJS; -.
DR PDBsum; 5XJT; -.
DR PDBsum; 5XJU; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6ID0; -.
DR PDBsum; 6ID1; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 6Y53; -.
DR PDBsum; 6Y5Q; -.
DR PDBsum; 7A5P; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7B0Y; -.
DR PDBsum; 7DVQ; -.
DR AlphaFoldDB; P62314; -.
DR SMR; P62314; -.
DR BioGRID; 112516; 249.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-2392; U1 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-6033; Sm complex.
DR CORUM; P62314; -.
DR DIP; DIP-31207N; -.
DR IntAct; P62314; 85.
DR MINT; P62314; -.
DR STRING; 9606.ENSP00000300413; -.
DR GlyGen; P62314; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62314; -.
DR PhosphoSitePlus; P62314; -.
DR SwissPalm; P62314; -.
DR BioMuta; SNRPD1; -.
DR DMDM; 51338665; -.
DR EPD; P62314; -.
DR jPOST; P62314; -.
DR MassIVE; P62314; -.
DR MaxQB; P62314; -.
DR PaxDb; P62314; -.
DR PeptideAtlas; P62314; -.
DR PRIDE; P62314; -.
DR ProteomicsDB; 57391; -.
DR TopDownProteomics; P62314; -.
DR ABCD; P62314; 7 sequenced antibodies.
DR Antibodypedia; 7243; 181 antibodies from 27 providers.
DR DNASU; 6632; -.
DR Ensembl; ENST00000300413.10; ENSP00000300413.4; ENSG00000167088.11.
DR GeneID; 6632; -.
DR KEGG; hsa:6632; -.
DR MANE-Select; ENST00000300413.10; ENSP00000300413.4; NM_006938.4; NP_008869.1.
DR UCSC; uc002ktj.2; human.
DR CTD; 6632; -.
DR DisGeNET; 6632; -.
DR GeneCards; SNRPD1; -.
DR HGNC; HGNC:11158; SNRPD1.
DR HPA; ENSG00000167088; Low tissue specificity.
DR MIM; 601063; gene.
DR neXtProt; NX_P62314; -.
DR OpenTargets; ENSG00000167088; -.
DR PharmGKB; PA164742464; -.
DR VEuPathDB; HostDB:ENSG00000167088; -.
DR eggNOG; KOG3428; Eukaryota.
DR GeneTree; ENSGT00510000047245; -.
DR HOGENOM; CLU_123956_3_0_1; -.
DR InParanoid; P62314; -.
DR OMA; SVTPQMN; -.
DR OrthoDB; 1579192at2759; -.
DR PhylomeDB; P62314; -.
DR TreeFam; TF314224; -.
DR PathwayCommons; P62314; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR SignaLink; P62314; -.
DR BioGRID-ORCS; 6632; 795 hits in 1014 CRISPR screens.
DR ChiTaRS; SNRPD1; human.
DR EvolutionaryTrace; P62314; -.
DR GeneWiki; Small_nuclear_ribonucleoprotein_D1; -.
DR GenomeRNAi; 6632; -.
DR Pharos; P62314; Tbio.
DR PRO; PR:P62314; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P62314; protein.
DR Bgee; ENSG00000167088; Expressed in ganglionic eminence and 204 other tissues.
DR ExpressionAtlas; P62314; baseline and differential.
DR Genevisible; P62314; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0000243; C:commitment complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0034709; C:methylosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034715; C:pICln-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc.
DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IPI:ComplexPortal.
DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005685; C:U1 snRNP; IDA:UniProtKB.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0005687; C:U4 snRNP; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB.
DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990446; F:U1 snRNP binding; IEA:Ensembl.
DR GO; GO:0036261; P:7-methylguanosine cap hypermethylation; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000245; P:spliceosomal complex assembly; TAS:ProtInc.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR CDD; cd01724; Sm_D1; 1.
DR IDEAL; IID00159; -.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR034102; Sm_D1.
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; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Methylation; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Ribonucleoprotein; Spliceosome; Ubl conjugation.
FT CHAIN 1..119
FT /note="Small nuclear ribonucleoprotein Sm D1"
FT /id="PRO_0000122201"
FT REGION 1..80
FT /note="Sufficient for interaction with CLNS1A"
FT /evidence="ECO:0000269|PubMed:11747828"
FT REGION 69..119
FT /note="Required for interaction with SMN1"
FT /evidence="ECO:0000269|PubMed:11135666"
FT REGION 88..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 58
FT /note="L->K: Loss of interaction with CLNS1A."
FT /evidence="ECO:0000269|PubMed:11747828"
FT MUTAGEN 60
FT /note="I->R: Loss of interaction with CLNS1A."
FT /evidence="ECO:0000269|PubMed:11747828"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:1B34"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1B34"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:1B34"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:1B34"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5XJR"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1B34"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1B34"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1B34"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1B34"
SQ SEQUENCE 119 AA; 13282 MW; 0C81C94BF98E0810 CRC64;
MKLVRFLMKL SHETVTIELK NGTQVHGTIT GVDVSMNTHL KAVKMTLKNR EPVQLETLSI
RGNNIRYFIL PDSLPLDTLL VDVEPKVKSK KREAVAGRGR GRGRGRGRGR GRGRGGPRR
