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SNRPF SNRPF SNRPB SNRPB SNRPE SNRPE SNRNP70 SNRNP70 MAGOH MAGOH SMN1 SMN1 SNRPD2 SNRPD2 SNRPD3 SNRPD3 SF3A2 SF3A2 SNRPG SNRPG SNRPD1 SNRPD1
"SNRPD1" - small nuclear ribonucleoprotein D1 polypeptide 16kDa in Homo sapiens
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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protein of unknown 3D structure
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SNRPD1small nuclear ribonucleoprotein D1 polypeptide 16kDa; May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA (119 aa)    
Predicted Functional Partners:
SNRPD2
small nuclear ribonucleoprotein D2 polypeptide 16.5kDa; Required for pre-mRNA splicing. Required for snRNP biogenesis (By similarity) (118 aa)
      score_image score_image score_image score_image   0.999
SNRPD3
small nuclear ribonucleoprotein D3 polypeptide 18kDa; Appears to function in the U7 snRNP complex that is involved in histone 3’-end processing. Binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner (126 aa)
      score_image score_image score_image score_image   0.999
SNRPE
small nuclear ribonucleoprotein polypeptide E; Appears to function in the U7 snRNP complex that is involved in histone 3’-end processing. Associated with snRNP U1, U2, U4/U6 and U5 (92 aa)
      score_image score_image score_image score_image   0.999
SNRPB
small nuclear ribonucleoprotein polypeptides B and B1; Appears to function in the U7 snRNP complex that is involved in histone 3’-end processing. Associated with snRNP U1, U2, U4/U6 and U5. May have a functional role in the pre-mRNA splicing or in snRNP structure. Binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner (By similarity) (240 aa)
      score_image score_image score_image score_image   0.999
SNRNP70
small nuclear ribonucleoprotein 70kDa (U1) (437 aa)
      score_image score_image score_image score_image   0.999
SNRPF
small nuclear ribonucleoprotein polypeptide F; Appears to function in the U7 snRNP complex that is involved in histone 3’-end processing. Associated with snRNP U1, U2, U4/U6 and U5 (86 aa)
      score_image score_image score_image score_image   0.999
SMN1
survival of motor neuron 1, telomeric; The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus. It may also play a role in the metabolism of snoRNPs (294 aa)
      score_image score_image score_image score_image   0.999
SNRPG
small nuclear ribonucleoprotein polypeptide G; Appears to function in the U7 snRNP complex that is involved in histone 3’-end processing. Associated with snRNP U1, U2, U4/U6 and U5 (76 aa)
      score_image score_image score_image score_image   0.999
SF3A2
splicing factor 3a, subunit 2, 66kDa; Subunit of the splicing factor SF3A required for ’A’ complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the ’E’ complex (464 aa)
      score_image score_image score_image score_image   0.999
MAGOH
mago-nashi homolog, proliferation-associated (Drosophila); Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mR [...] (146 aa)
      score_image score_image score_image score_image   0.999
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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