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DNAJC8 DNAJC8 SNRPG SNRPG SNRPA1 SNRPA1 SART1 SART1 SRSF1 SRSF1 PHF5A PHF5A SNRPD3 SNRPD3 SF3A1 SF3A1 PRPF8 PRPF8 SNRPD2 SNRPD2 SF3A3 SF3A3 SF3B3 SF3B3 DHX15 DHX15 SF3B2 SF3B2 SNRPB SNRPB SF3B1 SF3B1 SF3B5 SF3B5 SF3A2 SF3A2 U2AF2 U2AF2 CHERP CHERP SF3B14 SF3B14 DDX42 DDX42 RBM17 RBM17 DDX46 DDX46 U2SURP U2SURP SMNDC1 SMNDC1
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Network nodes represent proteins
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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small nodes:
protein of unknown 3D structure
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large nodes:
some 3D structure is known or predicted
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colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
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experimentally determined
Predicted Interactions
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textmining
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SF3A1splicing factor 3a, subunit 1, 120kDa; 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 (793 aa)
SNRPD3small 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)
PHF5APHD finger protein 5A; Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER- alpha. Also involved in pre-mRNA splicing (110 aa)
SF3A2splicing 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)
SF3B14Pre-mRNA branch site protein p14 ; Necessary for the splicing of pre-mRNA. Directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing. Enters the spliceosome and associates with the pre-mRNA branch site as part of the 17S U2 or, in the case of the minor spliceosome, as part of the 18S U11/U12 snRNP complex, and thus may facilitate the interaction of these snRNP with the branch sites of U2 and U12 respectively (125 aa)
SNRPA1small nuclear ribonucleoprotein polypeptide A’; This protein is associated with sn-RNP U2. It helps the A’ protein to bind stem loop IV of U2 snRNA (255 aa)
SRSF1serine/arginine-rich splicing factor 1; Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5’- and 3’-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5’-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5’-RGAAGAAC-3’ (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5’- CGAGGCG-3’ motif in vitro. Three copies of the octame [...] (248 aa)
DNAJC8DnaJ (Hsp40) homolog, subfamily C, member 8 (253 aa)
SNRPGsmall 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)
PRPF8PRP8 pre-mRNA processing factor 8 homolog (S. cerevisiae); Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5’ and the 3’ splice site (2335 aa)
SF3B3splicing factor 3b, subunit 3, 130kDa; Subunit of the splicing factor SF3B 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. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (1217 aa)
U2AF2U2 small nuclear RNA auxiliary factor 2; Necessary for the splicing of pre-mRNA. Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10 (475 aa)
SART1squamous cell carcinoma antigen recognized by T cells; Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA (800 aa)
SF3B2splicing factor 3b, subunit 2, 145kDa; Subunit of the splicing factor SF3B 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. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (895 aa)
U2SURPU2 snRNP-associated SURP domain containing (1029 aa)
SF3B1splicing factor 3b, subunit 1, 155kDa; Subunit of the splicing factor SF3B 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. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (1304 aa)
DHX15DEAH (Asp-Glu-Ala-His) box polypeptide 15; Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA (By similarity) (795 aa)
SNRPD2small nuclear ribonucleoprotein D2 polypeptide 16.5kDa; Required for pre-mRNA splicing. Required for snRNP biogenesis (By similarity) (118 aa)
DDX46DEAD (Asp-Glu-Ala-Asp) box polypeptide 46; Plays an essential role in splicing, either prior to, or during splicing A complex formation (1031 aa)
SF3B5splicing factor 3b, subunit 5, 10kDa (86 aa)
SMNDC1survival motor neuron domain containing 1; Necessary for spliceosome assembly. Overexpression causes apoptosis (238 aa)
SF3A3splicing factor 3a, subunit 3, 60kDa; 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 (501 aa)
RBM17RNA binding motif protein 17; Splice factor that binds to the single stranded 3’AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia (401 aa)
DDX42DEAD (Asp-Glu-Ala-Asp) box polypeptide 42; ATP-dependent RNA helicase. Binds to partially double- stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity- ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and [...] (938 aa)
SNRPBsmall 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)
CHERPcalcium homeostasis endoplasmic reticulum protein; Involved in calcium homeostasis, growth and proliferation (916 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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