SNRPD3

Protein-coding gene in the species Homo sapiens

SNRPD3

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1D3B, 3CW1, 3PGW, 3VRI, 4PJO, 4WZJ, 3JCR

Identifiers

Aliases

SNRPD3 , SMD3, Sm-D3, small nuclear ribonucleoprotein D3 polypeptide

External IDs

OMIM: 601062; MGI: 1914582; HomoloGene: 3078; GeneCards: SNRPD3; OMA:SNRPD3 - orthologs

Gene location (Human)
Chromosome 22 (human)
Chr.	Chromosome 22 (human) ^[1]
Chromosome 22 (human) Genomic location for SNRPD3 Genomic location for SNRPD3
Band	22q11.23	Start	24,555,958 bp ^[1]
Band	22q11.23	End	24,582,052 bp ^[1]

Gene location (Mouse)
Chromosome 10 (mouse)
Chr.	Chromosome 10 (mouse)^[2]
Chromosome 10 (mouse) Genomic location for SNRPD3 Genomic location for SNRPD3
Band	10\|10 C1	Start	75,353,385 bp ^[2]
Band	10\|10 C1	End	75,373,215 bp ^[2]

RNA expression pattern

Bgee

Human	Mouse (ortholog)
Top expressed in ganglionic eminence islet of Langerhans ventricular zone white blood cell monocyte appendix muscle of thigh granulocyte olfactory zone of nasal mucosa duodenum	Top expressed in abdominal wall otic placode ventricular zone somite migratory enteric neural crest cell mandibular prominence maxillary prominence endocardial cushion dermis hand
More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	histone pre-mRNA DCP binding U2 snRNA binding protein binding enzyme binding U7 snRNA binding telomerase RNA binding U1 snRNP binding RNA binding
Cellular component	SMN-Sm protein complex cytosol prespliceosome catalytic step 2 spliceosome spliceosomal tri-snRNP complex U5 snRNP U12-type spliceosomal complex U2 snRNP nucleoplasm methylosome U7 snRNP precatalytic spliceosome small nuclear ribonucleoprotein complex pICln-Sm protein complex telomerase holoenzyme complex spliceosomal complex commitment complex U4 snRNP extracellular exosome nucleus U1 snRNP cytoplasm nuclear body U4/U6 x U5 tri-snRNP complex U2-type precatalytic spliceosome U2-type catalytic step 2 spliceosome
Biological process	mRNA splicing, via spliceosome termination of RNA polymerase II transcription RNA processing mRNA processing spliceosomal complex assembly RNA splicing histone mRNA metabolic process protein methylation import into nucleus spliceosomal snRNP assembly
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


6634


67332

Ensembl


ENSG00000100028


ENSMUSG00000020180

UniProt


P62318


P62320

RefSeq (mRNA)

NM_001278656
NM_004175

NM_026095

RefSeq (protein)

NP_001265585
NP_004166

NP_080371

Location (UCSC)

Chr 22: 24.56 – 24.58 Mb

Chr 10: 75.35 – 75.37 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human View/Edit Mouse

Small nuclear ribonucleoprotein Sm D3 is a protein that in humans is encoded by the SNRPD3 gene.^[5]^[6]^[7]

Function

[edit ]

The protein encoded by this gene belongs to the small nuclear ribonucleoprotein core protein family. It is required for pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis.^[7]

Interactions

[edit ]

SNRPD3 has been shown to interact with:

CDC5L,^[8]
CLNS1A,^[9]
DDX20,^[10] and
Protein arginine methyltransferase 5.^[9]

References

[edit ]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100028 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020180 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Lehmeier T, Foulaki K, Lührmann 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.
^ Lehmeier T, Raker V, Hermann H, Lührmann 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. Bibcode:1994PNAS...9112317L. doi:10.1073/pnas.91.25.12317 . PMC 45428 . PMID 7527560.
^ ^a ^b "Entrez Gene: SNRPD3 small nuclear ribonucleoprotein D3 polypeptide 18kDa".
^ Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (Dec 2000). "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.
^ ^a ^b Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, 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. 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. PMC 99994 . PMID 11713266.
^ Charroux B, Pellizzoni L, Perkinson RA, 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. 147 (6): 1181–94. doi:10.1083/jcb.147.6.1181. PMC 2168095 . PMID 10601333.

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, Avis JM, de la Fortelle E, Raker VA, Lührmann R, Li J, Nagai K (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, Shevchenko A, Mann M, Dreyfuss G (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, Yong J, Shevchenko A, Mann M, Dreyfuss G (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.
Brahms H, Raymackers J, Union A, de Keyser F, Meheus L, Lührmann R (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 . hdl:11858/00-001M-0000-0012-F7F0-E . PMID 10747894.
Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (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.
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, Wyce A, Dreyfuss G (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.
Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G, Rappsilber J, Mann M, Dreyfuss G (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, Rappsilber J, Mann M, Dreyfuss G (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.
Meister G, Eggert C, Bühler D, Brahms H, Kambach C, Fischer U (2002). "Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln". Curr. Biol. 11 (24): 1990–4. doi:10.1016/S0960-9822(01)00592-9. hdl:11858/00-001M-0000-0012-F501-7 . PMID 11747828. S2CID 14742376.
Pellizzoni L, Baccon J, Rappsilber J, Mann M, Dreyfuss G (2002). "Purification of native survival of motor neurons complexes and identification of Gemin6 as a novel component". J. Biol. Chem. 277 (9): 7540–5. doi:10.1074/jbc.M110141200 . PMID 11748230.
Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, Dreyfuss G (2002). "A novel WD repeat protein component of the methylosome binds Sm proteins". J. Biol. Chem. 277 (10): 8243–7. doi:10.1074/jbc.M109984200 . PMID 11756452.
Fong YW, Zhou Q (2002). "Stimulatory effect of splicing factors on transcriptional elongation". Nature. 414 (6866): 929–33. doi:10.1038/414929a. PMID 11780068. S2CID 1518837.
Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9 . PMID 11790298.
Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ (2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA. 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266 . PMID 11991638.
Baccon J, Pellizzoni L, Rappsilber J, Mann M, Dreyfuss G (2002). "Identification and characterization of Gemin7, a novel component of the survival of motor neuron complex". J. Biol. Chem. 277 (35): 31957–62. doi:10.1074/jbc.M203478200 . PMID 12065586.

v t e PDB gallery
1d3b: CRYSTAL STRUCTURE OF THE D3B SUBCOMPLEX OF THE HUMAN CORE SNRNP DOMAIN AT 2.0A RESOLUTION 1d3b: CRYSTAL STRUCTURE OF THE D3B SUBCOMPLEX OF THE HUMAN CORE SNRNP DOMAIN AT 2.0A RESOLUTION

v t e RNA-binding protein: Ribonucleoproteins
snRNP	A A1 B B2 C D1 D2 D3 E F G N 70K/U1 spliceosomal RNA SNRNP200
hnRNP	A0 C L R
Other transcription	Telomerase
Translation	Ribosome
Vault ribonucleoprotein particles	Major vault protein
Other	Signal recognition particle

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Function

Interactions

References

Further reading