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SF3B1 SF3B1 LSM8 LSM8 SF3B3 SF3B3 SNRPD2 SNRPD2 SNRPG SNRPG SMU1 SMU1 LSM4 LSM4 EFTUD2 EFTUD2 ZMAT2 ZMAT2 LSM3 LSM3 SNRPD1 SNRPD1 SNRPD3 SNRPD3 NHP2L1 NHP2L1 PHF5A PHF5A DDX23 DDX23 PPIH PPIH SNRPE SNRPE LSM5 LSM5 PRPF38A PRPF38A LSM2 LSM2 LSM1 LSM1 SF3B5 SF3B5 LSM6 LSM6 PRPF3 PRPF3 LSM7 LSM7 SNRPF SNRPF
Nodes:
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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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SNRPD3Small nuclear ribonucleoprotein Sm D3; Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3’-end processing (126 aa)
PHF5APHD finger-like domain-containing protein 5A; Involved with the PAF1 complex (PAF1C) in transcriptional elongation by RNA polymerase II, and in regulation of development and maintenance of embryonic stem cell (ESC) pluripotency. Required for maintenance of ESCs self-renewal and cellular reprogramming of stem cells. Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes. Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 ’Lys-79’ (H3K79me2) a [...] (110 aa)
LSM8U6 snRNA-associated Sm-like protein LSm8; Binds specifically to the 3’-terminal U-tract of U6 snRNA and is probably a component of the spliceosome; Belongs to the snRNP Sm proteins family (96 aa)
LSM7U6 snRNA-associated Sm-like protein LSm7; Binds specifically to the 3’-terminal U-tract of U6 snRNA and is probably a component of the spliceosome; Belongs to the snRNP Sm proteins family (103 aa)
PRPF38APre-mRNA-splicing factor 38A; May be required for pre-mRNA splicing; Belongs to the PRP38 family (312 aa)
SNRPFSmall nuclear ribonucleoprotein F; Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3’-end processing (86 aa)
SNRPGSmall nuclear ribonucleoprotein G; Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Appears to function in the U7 snRNP complex that is involved in histone 3’-end processing (76 aa)
ZMAT2Zinc finger matrin-type 2; Spliceosomal B complex (199 aa)
SNRPD1Small nuclear ribonucleoprotein Sm D1; Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP- snRNP interactions through nonspecific [...] (119 aa)
LSM3U6 snRNA-associated Sm-like protein LSm3; Binds specifically to the 3’-terminal U-tract of U6 snRNA; Belongs to the snRNP Sm proteins family (102 aa)
SF3B3Splicing factor 3B subunit 3; Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is 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)
PPIHPeptidyl-prolyl cis-trans isomerase H; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone; Cyclophilin peptidylprolyl isomerases (177 aa)
LSM1U6 snRNA-associated Sm-like protein LSm1; Plays a role in the degradation of histone mRNAs, the only eukaryotic mRNAs that are not polyadenylated. Probably also part of an LSm subunits- containing complex involved in the general process of mRNA degradation (By similarity); Belongs to the snRNP Sm proteins family (133 aa)
DDX23Probable ATP-dependent RNA helicase DDX23; Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation; DEAD-box helicases (820 aa)
PRPF3U4/U6 small nuclear ribonucleoprotein Prp3; Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome; U4/U6 small nucleolar ribonucleoprotein (683 aa)
SF3B1Splicing factor 3B subunit 1; Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is 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; Armadillo-like helical d [...] (1304 aa)
SNRPD2Small nuclear ribonucleoprotein Sm D2; Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (118 aa)
SF3B5Splicing factor 3B subunit 5; Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is 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 (86 aa)
LSM2U6 snRNA-associated Sm-like protein LSm2; Binds specifically to the 3’-terminal U-tract of U6 snRNA. May be involved in pre-mRNA splicing; Belongs to the snRNP Sm proteins family (95 aa)
SMU1WD40 repeat-containing protein SMU1; Auxiliary spliceosomal protein that regulates selection of alternative splice sites in a small set of target pre-mRNA species (Probable). Regulates alternative splicing of the HSPG2 pre-mRNA (By similarity). Required for normal mitotic spindle assembly and normal progress through mitosis. Required for normal accumulation of IK; Belongs to the WD repeat SMU1 family (513 aa)
NHP2L1NHP2-like protein 1; Binds to the 5’-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding (128 aa)
EFTUD2116 kDa U5 small nuclear ribonucleoprotein component; Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily (972 aa)
SNRPESmall nuclear ribonucleoprotein E; Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3’-end processing. May indirectly play a role in hair development (92 aa)
LSM5U6 snRNA-associated Sm-like protein LSm5; Plays a role in U6 snRNP assembly and function. Binds to the 3’ end of U6 snRNA, thereby facilitating formation of the spliceosomal U4/U6 duplex formation in vitro; LSm proteins (91 aa)
LSM6U6 snRNA-associated Sm-like protein LSm6; Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5’-to-3’ mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 d [...] (80 aa)
LSM4U6 snRNA-associated Sm-like protein LSm4; Binds specifically to the 3’-terminal U-tract of U6 snRNA; Belongs to the snRNP Sm proteins family (139 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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