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 04-NOV-2026, entry version 203. 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; DOI=10.1093/clinchem/35.9.1861; 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 MINOR SPLICEOSOME, AND IDENTIFICATION RP 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 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 IN SPLICEOSOMAL U1 SNRNP, FUNCTION, 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 IN SPLICEOSOMAL U1 SNRNP, SUBCELLULAR LOCATION, RP 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 IN COMPLEX WITH SNRPD2; SNRPE; SNRPF; SNRPG; SMN1 AND RP 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 IN SPLICEOSOMAL CORE U4 SNRNP, AND 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 IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN 6S PICLN-SM RP COMPLEX, AND FUNCTION IN CORE U1 SNRNP 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, 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, SUBCELLULAR LOCATION, SUBUNIT, AND RP 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, FUNCTION, SUBCELLULAR LOCATION, AND RP 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, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, RP 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, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, RP 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 IN COMPLEX WITH GEMIN2; SNRPD2; SNRPE; SNRPF; SNRPG RP AND SMN1, AND INTERACTION WITH GEMIN2 AND 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). RN [30] {ECO:0007744|PDB:6Y5Q} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH THE 17S U2 SNRNP COMPLEX, RP FUNCTION, AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=32494006; DOI=10.1038/s41586-020-2344-3; RA Zhang Z., Will C.L., Bertram K., Dybkov O., Hartmuth K., Agafonov D.E., RA Hofele R., Urlaub H., Kastner B., Luehrmann R., Stark H.; RT "Molecular architecture of the human 17S U2 snRNP."; RL Nature 583:310-313(2020). RN [31] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY, AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). RN [32] {ECO:0007744|PDB:8HK1} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH THE 17S U2 SNRNP COMPLEX, RP AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=36797247; DOI=10.1038/s41467-023-36489-x; RA Yang F., Bian T., Zhan X., Chen Z., Xing Z., Larsen N.A., Zhang X., Shi Y.; RT "Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP RT assembly."; RL Nat. Commun. 14:897-897(2023). 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:28076346, PubMed:28502770, PubMed:28781166, CC PubMed:32494006). Component of both the pre-catalytic spliceosome B CC complex and activated spliceosome C complexes (PubMed:11991638, CC PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166). As CC a component of the minor spliceosome, involved in the splicing of U12- CC type introns in pre-mRNAs (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 (PubMed:23333303). {ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:18984161, CC ECO:0000269|PubMed:19325628, 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:32494006, 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:28076346, PubMed:28502770, PubMed:28781166, CC PubMed:32494006, PubMed:36797247). Most spliceosomal snRNPs contain a CC common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF CC and SNRPG that assemble in a heptameric protein ring on the Sm site of CC the small nuclear RNA to form the core snRNP (PubMed:10025403, CC PubMed:19325628, PubMed:21113136, PubMed:25555158, PubMed:26912367, CC PubMed:28076346, PubMed:28502770, PubMed:28781166). Component of the U1 CC snRNP (PubMed:19325628, PubMed:21113136, PubMed:25555158). The U1 snRNP CC is composed of the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, CC SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP- CC specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C CC (PubMed:19325628, PubMed:21113136, PubMed:25555158). Component of the CC U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at CC least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, CC PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, CC LSM6, LSM7 and LSM8 (PubMed:26912367). Component of the minor CC spliceosome, which splices U12-type introns (PubMed:15146077, CC PubMed:33509932). Part of the SMN-Sm complex that contains SMN1, CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, CC SNRPF and SNRPG; catalyzes core snRNPs assembly (PubMed:16314521). CC Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, CC SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics CC additional Sm proteins and which is unable to assemble into the core CC snRNP. Interacts (via C-terminus) with SMN1 (via Tudor domain); the CC interaction is direct (PubMed:10500148, PubMed:11135666). Interacts CC with GEMIN2; the interaction is direct (PubMed:21816274). Interacts CC with SNRPD2; the interaction is direct (PubMed:21816274, CC 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 ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:33509932, CC ECO:0000269|PubMed:36797247}. CC -!- INTERACTION: CC P62314; P54105: CLNS1A; NbExp=13; IntAct=EBI-372177, EBI-724693; CC P62314; Q8WXD5: GEMIN6; NbExp=2; IntAct=EBI-372177, EBI-752301; CC P62314; Q15428: SF3A2; NbExp=2; IntAct=EBI-372177, EBI-2462271; CC P62314; Q16637: SMN2; NbExp=7; IntAct=EBI-372177, EBI-395421; CC P62314; P62316: SNRPD2; NbExp=4; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001291916.2. DR RefSeq; NP_008869.1; NM_006938.4. 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; C/CC/CCC/CCCC/J/JJ/JJJ/JJJJ/Q/QQ/QQQ/QQQQ=1-118. 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=1-80. 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 PDB; 7EVO; EM; 2.50 A; g=1-119. DR PDB; 7QTT; EM; 3.10 A; k=1-119. DR PDB; 7VPX; EM; 3.00 A; g/h=1-119. DR PDB; 7W59; EM; 3.60 A; c/j=1-119. DR PDB; 7W5A; EM; 3.60 A; c/j=1-119. DR PDB; 7W5B; EM; 4.30 A; c/j=1-119. DR PDB; 8C6J; EM; 2.80 A; c/l=1-119. DR PDB; 8CH6; EM; 5.90 A; 5/k=1-119. DR PDB; 8H6E; EM; 3.20 A; 2b/4b/5b=1-119. DR PDB; 8H6J; EM; 3.25 A; 2b/4b/5b=1-119. DR PDB; 8H6K; EM; 2.70 A; 2b/4b/5b=1-119. DR PDB; 8H6L; EM; 2.60 A; 2b/4b/5b=1-119. DR PDB; 8HK1; EM; 2.70 A; g=1-119. DR PDB; 8I0P; EM; 3.40 A; b/n=1-119. DR PDB; 8I0R; EM; 3.00 A; b/n=1-119. DR PDB; 8I0S; EM; 4.20 A; b/n=1-119. DR PDB; 8I0T; EM; 3.00 A; b/n=1-119. DR PDB; 8I0U; EM; 3.30 A; b/n=1-119. DR PDB; 8I0V; EM; 3.00 A; b/n=1-119. DR PDB; 8I0W; EM; 3.40 A; b/j=1-119. DR PDB; 8Q7Q; EM; 3.20 A; a=1-119. DR PDB; 8Q7V; EM; 3.80 A; a=1-119. DR PDB; 8Q7W; EM; 3.90 A; a=1-119. DR PDB; 8Q7X; EM; 4.60 A; a=1-119. DR PDB; 8Q91; EM; 3.10 A; i=1-119. DR PDB; 8QO9; EM; 5.29 A; 21/41/51=1-119. DR PDB; 8QXD; EM; 9.60 A; 21/41=1-119, 51=1-82. DR PDB; 8QZS; EM; 4.10 A; 21/41/51=1-119. DR PDB; 8R08; EM; 6.10 A; 11/21/41/51=1-119. DR PDB; 8R09; EM; 4.30 A; 21/41/51=1-119. DR PDB; 8R0A; EM; 5.80 A; 21/41/51=1-119. DR PDB; 8R0B; EM; 4.40 A; 21/41/51=1-119. DR PDB; 8R7N; EM; 3.40 A; h=1-119. DR PDB; 8RC0; EM; 3.20 A; i=1-119. DR PDB; 8RM5; EM; 6.90 A; 21/41/51=1-119. DR PDB; 8RO2; EM; 3.50 A; c=1-119. DR PDB; 8Y6O; EM; 3.38 A; b/i/p=1-119. DR PDB; 8Y7E; EM; 4.66 A; j=1-119. DR PDB; 9E3B; EM; 3.06 A; M/N/O/P=1-119. DR PDB; 9E3C; EM; 3.19 A; M=1-119. DR PDB; 9FMD; EM; 3.30 A; c/j=1-119. DR PDB; 9GBW; EM; 3.50 A; h=1-119. DR PDB; 9GC0; EM; 3.20 A; h=1-119. DR PDB; 9GCL; EM; 3.00 A; h=1-119. DR PDB; 9QEQ; EM; 3.50 A; k=1-119. DR PDB; 9R8V; EM; 8.50 A; 21/51=1-119. DR AlphaFoldDB; P62314; -. DR EMDB; EMD-10689; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-11972; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16452; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-18229; -. DR EMDB; EMD-18234; -. DR EMDB; EMD-18235; -. DR EMDB; EMD-18237; -. DR EMDB; EMD-18267; -. DR EMDB; EMD-18529; -. DR EMDB; EMD-18718; -. DR EMDB; EMD-18781; -. DR EMDB; EMD-18786; -. DR EMDB; EMD-18787; -. DR EMDB; EMD-18788; -. DR EMDB; EMD-18789; -. DR EMDB; EMD-18984; -. DR EMDB; EMD-19041; -. DR EMDB; EMD-19349; -. DR EMDB; EMD-19399; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-31334; -. DR EMDB; EMD-32074; -. DR EMDB; EMD-32317; -. DR EMDB; EMD-32319; -. DR EMDB; EMD-32321; -. DR EMDB; EMD-34500; -. DR EMDB; EMD-34505; -. DR EMDB; EMD-34507; -. DR EMDB; EMD-34508; -. DR EMDB; EMD-34841; -. DR EMDB; EMD-35105; -. DR EMDB; EMD-35107; -. DR EMDB; EMD-35108; -. DR EMDB; EMD-35109; -. DR EMDB; EMD-35110; -. DR EMDB; EMD-35111; -. DR EMDB; EMD-35113; -. DR EMDB; EMD-3545; -. DR EMDB; EMD-3766; -. DR EMDB; EMD-38993; -. DR EMDB; EMD-39013; -. DR EMDB; EMD-4525; -. DR EMDB; EMD-4658; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-47477; -. DR EMDB; EMD-47478; -. DR EMDB; EMD-51223; -. DR EMDB; EMD-51226; -. DR EMDB; EMD-51233; -. DR EMDB; EMD-53087; -. DR EMDB; EMD-53843; -. DR EMDB; EMD-6721; -. DR EMDB; EMD-6864; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR EMDB; EMD-9645; -. DR EMDB; EMD-9646; -. DR EMDB; EMD-9647; -. DR SMR; P62314; -. DR BioGRID; 112516; 377. 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-26417; U4 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26421; U5 small nuclear ribonucleoprotein complete complex. DR ComplexPortal; CPX-26429; Major Spliceosomal Pre-B complex. DR ComplexPortal; CPX-26435; Major Spliceosomal B complex. DR ComplexPortal; CPX-26441; Major Spliceosomal Pre-B-act complex. DR ComplexPortal; CPX-26448; Major Spliceosomal B-act-I complex. DR ComplexPortal; CPX-26450; Major Spliceosomal B-act-II complex. DR ComplexPortal; CPX-26451; Major Spliceosomal B-act-III complex. DR ComplexPortal; CPX-26454; Major Spliceosomal B-act-IV complex. DR ComplexPortal; CPX-26458; Major Spliceosomal Post-B-act complex. DR ComplexPortal; CPX-26463; Major Spliceosomal C complex. DR ComplexPortal; CPX-26465; Major Spliceosomal Pre-C*-I complex. DR ComplexPortal; CPX-26467; Major Spliceosomal Pre-C*-II complex. DR ComplexPortal; CPX-26472; Major Spliceosomal C* complex. DR ComplexPortal; CPX-26479; Major Post-catalytic P Spliceosome complex. DR ComplexPortal; CPX-26480; Intron Lariat Spliceosome, type 1 complex. DR ComplexPortal; CPX-26481; Intron Lariat Spliceosome, type 2 complex. DR ComplexPortal; CPX-26485; U11 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26487; U12 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26489; U11/U12 di-small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26495; U4atac small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26502; U4atac/U6atac.U5 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-26506; Minor Spliceosomal Pre-B complex. DR ComplexPortal; CPX-26509; Minor Spliceosomal B-act complex. DR ComplexPortal; CPX-26552; U5 small nuclear ribonucleoprotein complex, AAR2 variant. DR ComplexPortal; CPX-6033; Sm complex. DR CORUM; P62314; -. DR DIP; DIP-31207N; -. DR FunCoup; P62314; 2939. DR IntAct; P62314; 140. DR NDEx; IQUERY-CP-SNRPD1; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000300413; -. DR BindingDB; P62314; -. DR ChEMBL; CHEMBL6066339; -. DR GlyCosmos; P62314; 1 site, 1 glycan. DR GlyGen; P62314; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P62314; -. DR PhosphoSitePlus; P62314; -. DR SwissPalm; P62314; -. DR BioMuta; SNRPD1; -. DR DMDM; 51338665; -. DR jPOST; P62314; -. DR MassIVE; P62314; -. DR PaxDb; 9606-ENSP00000300413; -. DR PeptideAtlas; P62314; -. DR PRIDE; P62314; -. DR ProteomicsDB; 57391; -. DR Pumba; P62314; -. DR TopDownProteomics; P62314; -. DR ABCD; P62314; 7 sequenced antibodies. DR Antibodypedia; 7243; 207 antibodies from 29 providers. DR DNASU; 6632; -. DR Ensembl; ENST00000300413.10; ENSP00000300413.4; ENSG00000167088.12. 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 AGR; HGNC:11158; -. DR ClinPGx; PA164742464; -. 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 OpenTargets; ENSG00000167088; -. DR VEuPathDB; HostDB:ENSG00000167088; -. DR eggNOG; KOG3428; Eukaryota. DR GeneTree; ENSGT00510000047245; -. DR HOGENOM; CLU_123956_3_0_1; -. DR InParanoid; P62314; -. DR OMA; ACRFLMK; -. DR OrthoDB; 9626941at2759; -. DR PAN-GO; P62314; 12 GO annotations based on evolutionary models. DR PhylomeDB; P62314; -. 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 Reactome; R-HSA-9770562; mRNA Polyadenylation. DR Reactome; R-HSA-9918481; Dengue Virus-Host Interactions. DR Reactome; R-HSA-9943411; CHD1 and CHD2 subfamily. DR SignaLink; P62314; -. DR SIGNOR; P62314; -. DR Agora; ENSG00000167088; -. DR BioGRID-ORCS; 6632; 830 hits in 1097 CRISPR screens. DR CD-CODE; 6F24707C; Cajal body. 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 206 other cell types or tissues. DR ExpressionAtlas; P62314; baseline and differential. 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:0071014; C:post-mRNA release spliceosomal complex; IPI:ComplexPortal. DR GO; GO:0071020; C:post-spliceosomal complex; IPI:ComplexPortal. DR GO; GO:0071011; C:precatalytic spliceosome; IPI:ComplexPortal. 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:0034693; C:U11/U12 snRNP; IPI:ComplexPortal. DR GO; GO:0071018; C:U12-type catalytic step 2 spliceosome; IPI:ComplexPortal. DR GO; GO:0071016; C:U12-type precatalytic spliceosome; IPI:ComplexPortal. DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central. DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IPI:ComplexPortal. 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:0005684; C:U2-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0005687; C:U4 snRNP; IDA:UniProtKB. DR GO; GO:0071001; C:U4/U6 snRNP; NAS:ComplexPortal. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB. DR GO; GO:0005690; C:U4atac snRNP; NAS:ComplexPortal. DR GO; GO:0071002; C:U4atac/U6atac snRNP; NAS:ComplexPortal. DR GO; GO:0071009; C:U4atac/U6atac x U5 tri-snRNP complex; NAS:ComplexPortal. 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; NAS:ComplexPortal. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; NAS:ComplexPortal. 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:0000244; P:spliceosomal tri-snRNP complex assembly; NAS:ComplexPortal. DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); NAS:ComplexPortal. DR GO; GO:1903241; P:U2-type prespliceosome assembly; NAS:ComplexPortal. DR CDD; cd01724; Sm_D1; 1. DR FunFam; 2.30.30.100:FF:000016; Small nuclear ribonucleoprotein Sm D1; 1. DR Gene3D; 2.30.30.100; -; 2. DR IDEAL; IID00159; -. DR InterPro; IPR027141; LSm4/Sm_D1/D3. DR InterPro; IPR010920; LSM_dom_sf. DR InterPro; IPR047575; Sm. DR InterPro; IPR034102; Sm_D1. DR InterPro; IPR001163; Sm_dom_euk/arc. DR PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 1. DR Pfam; PF01423; LSM; 1. DR SMART; SM00651; Sm; 1. DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1. DR PROSITE; PS52002; SM; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond; KW Methylation; mRNA processing; mRNA splicing; Nucleus; KW Proteomics identification; Reference proteome; Repeat; Ribonucleoprotein; KW Spliceosome; Ubl conjugation. FT CHAIN 1..119 FT /note="Small nuclear ribonucleoprotein Sm D1" FT /id="PRO_0000122201" FT DOMAIN 2..74 FT /note="Sm" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346" 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 99..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:8H6L" FT STRAND 14..19 FT /evidence="ECO:0007829|PDB:1B34" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:8I0R" FT STRAND 24..32 FT /evidence="ECO:0007829|PDB:1B34" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:8C6J" 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" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:9E3B" SQ SEQUENCE 119 AA; 13282 MW; 0C81C94BF98E0810 CRC64; MKLVRFLMKL SHETVTIELK NGTQVHGTIT GVDVSMNTHL KAVKMTLKNR EPVQLETLSI RGNNIRYFIL PDSLPLDTLL VDVEPKVKSK KREAVAGRGR GRGRGRGRGR GRGRGGPRR //