Small nuclear ribonucleoprotein D1

Small nuclear ribonucleoprotein D1 polypeptide 16kDa

PDB rendering based on 1b34.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1B34, 1VU2, 1VU3, 2Y9A, 2Y9B, 2Y9C, 2Y9D, 3CW1, 3PGW, 3S6N, 4F77, 4F7U

Identifiers

Symbols

SNRPD1 ; HsT2456; SMD1; SNRPD; Sm-D1

External IDs

OMIM: 601063 MGI: 98344 HomoloGene: 107532 GeneCards: SNRPD1 Gene

Gene ontology
Molecular function	• RNA binding • protein binding • poly(A) RNA binding
Cellular component	• nucleus • nucleoplasm • U1 snRNP • U4 snRNP • U12-type spliceosomal complex • cytosol • small nuclear ribonucleoprotein complex • methylosome • pICln-Sm protein complex • SMN-Sm protein complex • catalytic step 2 spliceosome
Biological process	• spliceosomal complex assembly • spliceosomal snRNP assembly • mRNA splicing, via spliceosome • RNA splicing • gene expression • RNA metabolic process • ncRNA metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 18:
19.19 – 19.21 Mb

Chr 18:
10.62 – 10.63 Mb

PubMed search

Small nuclear ribonucleoprotein Sm D1 is a protein that in humans is encoded by the SNRPD1 gene.^[1]^[2]

This gene encodes a small nuclear ribonucleoprotein that belongs to the SNRNP core protein family. The protein may act as a charged protein scaffold to promote SNRNP assembly or strengthen SNRNP-SNRNP interactions through nonspecific electrostatic contacts with RNA.^[3]

Interactions

Small nuclear ribonucleoprotein D1 has been shown to interact with DDX20,^[4] CLNS1A,^[5] CDC5L,^[6] Small nuclear ribonucleoprotein D2^[7]^[8] and SMN1.^[9]^[10]^[11]

References

↑ Lehmeier T, Raker V, Hermann H, Luhrmann R (January 1995). "cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction". Proc Natl Acad Sci U S A 91 (25): 12317–21. doi:10.1073/pnas.91.25.12317. PMC 45428. PMID 7527560.
↑ Lehmeier T, Foulaki K, Luhrmann R (January 1991). "Evidence for three distinct D proteins, which react differentially with anti-Sm autoantibodies, in the cores of the major snRNPs U1, U2, U4/U6 and U5". Nucleic Acids Res 18 (22): 6475–84. doi:10.1093/nar/18.22.6475. PMC 332598. PMID 1701240.
↑ "Entrez Gene: SNRPD1 small nuclear ribonucleoprotein D1 polypeptide 16kDa".
↑ Charroux, B; Pellizzoni L; Perkinson R A; Shevchenko A; Mann M; Dreyfuss G (Dec 1999). "Gemin3: A Novel Dead Box Protein That Interacts with Smn, the Spinal Muscular Atrophy Gene Product, and Is a Component of Gems". J. Cell Biol. (UNITED STATES) 147 (6): 1181–94. doi:10.1083/jcb.147.6.1181. ISSN 0021-9525. PMC 2168095. PMID 10601333.
↑ Friesen, W J; Paushkin S; Wyce A; Massenet S; Pesiridis G S; Van Duyne G; Rappsilber J; Mann M; Dreyfuss G (Dec 2001). "The Methylosome, a 20S Complex Containing JBP1 and pICln, Produces Dimethylarginine-Modified Sm Proteins". Mol. Cell. Biol. (United States) 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. ISSN 0270-7306. PMC 99994. PMID 11713266.
↑ Ajuh, P; Kuster B; Panov K; Zomerdijk J C; Mann M; Lamond A I (Dec 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. (ENGLAND) 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. ISSN 0261-4189. PMC 305846. PMID 11101529.
↑ Fury, M G; Zhang W; Christodoulopoulos I; Zieve G W (November 1997). "Multiple protein: protein interactions between the snRNP common core proteins". Exp. Cell Res. (UNITED STATES) 237 (1): 63–9. doi:10.1006/excr.1997.3750. ISSN 0014-4827. PMID 9417867.
↑ Kambach, C; Walke S; Young R; Avis J M; de la Fortelle E; Raker V A; Lührmann R; Li J; Nagai K (February 1999). "Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs". Cell (UNITED STATES) 96 (3): 375–87. doi:10.1016/S0092-8674(00)80550-4. ISSN 0092-8674. PMID 10025403.
↑ Meister, G; Bühler D; Laggerbauer B; Zobawa M; Lottspeich F; Fischer U (August 2000). "Characterization of a nuclear 20S complex containing the survival of motor neurons (SMN) protein and a specific subset of spliceosomal Sm proteins". Hum. Mol. Genet. (ENGLAND) 9 (13): 1977–86. doi:10.1093/hmg/9.13.1977. ISSN 0964-6906. PMID 10942426.
↑ Liu, Q; Fischer U; Wang F; Dreyfuss G (September 1997). "The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins". Cell (UNITED STATES) 90 (6): 1013–21. doi:10.1016/S0092-8674(00)80367-0. ISSN 0092-8674. PMID 9323129.
↑ Friesen, W J; Dreyfuss G (August 2000). "Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN)". J. Biol. Chem. (UNITED STATES) 275 (34): 26370–5. doi:10.1074/jbc.M003299200. ISSN 0021-9258. PMID 10851237.

Renz M, Heim C, Bräunling O et al. (1989). "Expression of the major human ribonucleoprotein (RNP) autoantigens in Escherichia coli and their use in an EIA for screening sera from patients with autoimmune diseases". Clin. Chem. 35 (9): 1861–3. PMID 2528429.
Rokeach LA, Haselby JA, Hoch SO (1988). "Molecular cloning of a cDNA encoding the human Sm-D autoantigen". Proc. Natl. Acad. Sci. U.S.A. 85 (13): 4832–6. doi:10.1073/pnas.85.13.4832. PMC 280530. PMID 3260384.
Sun D, Ou YC, Hoch SO (1997). "Analysis of genes for human snRNP Sm-D1 protein and identification of the promoter sequence which shows segmental homology to the promoters of Sm-E and U1 snRNA genes". Gene 189 (2): 245–54. doi:10.1016/S0378-1119(96)00858-X. PMID 9168134.
Liu Q, Fischer U, Wang F, Dreyfuss G (1997). "The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins". Cell 90 (6): 1013–21. doi:10.1016/S0092-8674(00)80367-0. PMID 9323129.
Fury MG, Zhang W, Christodoulopoulos I, Zieve GW (1998). "Multiple protein: protein interactions between the snRNP common core proteins". Exp. Cell Res. 237 (1): 63–9. doi:10.1006/excr.1997.3750. PMID 9417867.
Kambach C, Walke S, Young R et al. (1999). "Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs". Cell 96 (3): 375–87. doi:10.1016/S0092-8674(00)80550-4. PMID 10025403.
Charroux B, Pellizzoni L, Perkinson RA et al. (2000). "Gemin3: A Novel Dead Box Protein That Interacts with Smn, the Spinal Muscular Atrophy Gene Product, and Is a Component of Gems". J. Cell Biol. 147 (6): 1181–94. doi:10.1083/jcb.147.6.1181. PMC 2168095. PMID 10601333.
Charroux B, Pellizzoni L, Perkinson RA et al. (2000). "Gemin4: A Novel Component of the Smn Complex That Is Found in Both Gems and Nucleoli". J. Cell Biol. 148 (6): 1177–86. doi:10.1083/jcb.148.6.1177. PMC 2174312. PMID 10725331.
Mammoto A, Sasaki T, Kim Y, Takai Y (2000). "Physical and functional interaction of rabphilin-11 with mammalian Sec13 protein. Implication in vesicle trafficking". J. Biol. Chem. 275 (18): 13167–70. doi:10.1074/jbc.C000096200. PMID 10747849.
Brahms H, Raymackers J, Union A et al. (2000). "The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies". J. Biol. Chem. 275 (22): 17122–9. doi:10.1074/jbc.M000300200. PMID 10747894.
Meister G, Bühler D, Laggerbauer B et al. (2000). "Characterization of a nuclear 20S complex containing the survival of motor neurons (SMN) protein and a specific subset of spliceosomal Sm proteins". Hum. Mol. Genet. 9 (13): 1977–86. doi:10.1093/hmg/9.13.1977. PMID 10942426.
Ajuh P, Kuster B, Panov K et al. (2001). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.
Selenko P, Sprangers R, Stier G et al. (2001). "SMN tudor domain structure and its interaction with the Sm proteins". Nat. Struct. Biol. 8 (1): 27–31. doi:10.1038/83014. PMID 11135666.
Urlaub H, Raker VA, Kostka S, Lührmann R (2001). "Sm protein–Sm site RNA interactions within the inner ring of the spliceosomal snRNP core structure". EMBO J. 20 (1–2): 187–96. doi:10.1093/emboj/20.1.187. PMC 140196. PMID 11226169.
Friesen WJ, Massenet S, Paushkin S et al. (2001). "SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets". Mol. Cell 7 (5): 1111–7. doi:10.1016/S1097-2765(01)00244-1. PMID 11389857.
Park JW, Voss PG, Grabski S et al. (2001). "Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein". Nucleic Acids Res. 29 (17): 3595–602. doi:10.1093/nar/29.17.3595. PMC 55878. PMID 11522829.
Friesen WJ, Paushkin S, Wyce A et al. (2001). "The Methylosome, a 20S Complex Containing JBP1 and pICln, Produces Dimethylarginine-Modified Sm Proteins". Mol. Cell. Biol. 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. PMC 99994. PMID 11713266.
Gubitz AK, Mourelatos Z, Abel L et al. (2002). "Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins". J. Biol. Chem. 277 (7): 5631–6. doi:10.1074/jbc.M109448200. PMID 11714716.

PDB gallery

1b34: CRYSTAL STRUCTURE OF THE D1D2 SUB-COMPLEX FROM THE HUMAN SNRNP CORE DOMAIN

RNA-binding protein: Ribonucleoproteins

snRNP

70K/U1 spliceosomal RNA

SNRNP200

hnRNP

Other transcription

Telomerase

Translation

Ribosome

Vault ribonucleoprotein
particles

Major vault protein

Other

Signal recognition particle

Index of genetics

Description	Gene expression DNA replication cycle recombination repair binding proteins Transcription factors regulators nucleic acids RNA RNA binding proteins ribonucleoproteins repeated sequence modification Translation ribosome modification nexins Proteins domains Structure primary secondary tertiary quaternary

Disease	Replication and repair Transcription factor Transcription Translation

Small nuclear ribonucleoprotein D1

Interactions

References

Further reading