P33334 · PRP8_YEAST
- ProteinPre-mRNA-splicing factor 8
- GenePRP8
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2413 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for association of BRR2 with the spliceosomal U5 snRNP, and the subsequent assembly of the U4/U6-U5 tri-snRNP complex. Functions as a 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, as well as the branch region. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region. Also has a role in cell cycle.
Miscellaneous
Present with 468 molecules/cell in log phase SD medium.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | catalytic step 2 spliceosome | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | spliceosomal complex | |
Cellular Component | U4/U6 x U5 tri-snRNP complex | |
Cellular Component | U5 snRNP | |
Molecular Function | metallopeptidase activity | |
Molecular Function | mRNA binding | |
Molecular Function | pre-mRNA intronic binding | |
Molecular Function | U1 snRNA binding | |
Molecular Function | U2 snRNA binding | |
Molecular Function | U5 snRNA binding | |
Molecular Function | U6 snRNA binding | |
Biological Process | generation of catalytic spliceosome for second transesterification step | |
Biological Process | mRNA 3'-splice site recognition | |
Biological Process | mRNA 5'-splice site recognition | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | spliceosomal snRNP assembly | |
Biological Process | spliceosomal tri-snRNP complex assembly |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePre-mRNA-splicing factor 8
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP33334
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1658 | No effect on viability. | ||||
Sequence: H → S | ||||||
Mutagenesis | 1684 | No effect on viability. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 1687 | No effect on viability. | ||||
Sequence: H → S | ||||||
Mutagenesis | 1700 | No effect on viability. | ||||
Sequence: D → N | ||||||
Mutagenesis | 1735 | No effect on viability. | ||||
Sequence: D → N | ||||||
Mutagenesis | 1853 | Alters protein folding. Severely impaired growth. Strongly reduced growth at 35 degrees Celsius; when associated with A-1854. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1853 | Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. | ||||
Sequence: D → N | ||||||
Mutagenesis | 1854 | Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Strongly reduced growth at 35 degrees Celsius; when associated with A-1853. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1854 | Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. | ||||
Sequence: D → N | ||||||
Mutagenesis | 1855 | Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. | ||||
Sequence: T → A | ||||||
Mutagenesis | 1936 | Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. | ||||
Sequence: T → A | ||||||
Mutagenesis | 1937 | Severely impaired growth. Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. | ||||
Sequence: R → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 24 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000097042 | 1-2413 | Pre-mRNA-splicing factor 8 | |||
Sequence: MSGLPPPPPGFEEDSDLALPPPPPPPPGYEIEELDNPMVPSSVNEDTFLPPPPPPPSNFEINAEEIVDFTLPPPPPPPGLDELETKAEKKVELHGKRKLDIGKDTFVTRKSRKRAKKMTKKAKRSNLYTPKAEMPPEHLRKIINTHSDMASKMYNTDKKAFLGALKYLPHAILKLLENMPHPWEQAKEVKVLYHTSGAITFVNETPRVIEPVYTAQWSATWIAMRREKRDRTHFKRMRFPPFDDDEPPLSYEQHIENIEPLDPINLPLDSQDDEYVKDWLYDSRPLEEDSKKVNGTSYKKWSFDLPEMSNLYRLSTPLRDEVTDKNYYYLFDKKSFFNGKALNNAIPGGPKFEPLYPREEEEDYNEFNSIDRVIFRVPIRSEYKVAFPHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTPALFFDPSLNPIPHFIDNNSSLNVSNTKENGDFTLPEDFAPLLAEEEELILPNTKDAMSLYHSPFPFNRTKGKMVRAQDVALAKKWFLQHPDEEYPVKVKVSYQKLLKNYVLNELHPTLPTNHNKTKLLKSLKNTKYFQQTTIDWVEAGLQLCRQGHNMLNLLIHRKGLTYLHLDYNFNLKPTKTLTTKERKKSRLGNSFHLMRELLKMMKLIVDTHVQFRLGNVDAFQLADGIHYILNHIGQLTGIYRYKYKVMHQIRACKDLKHIIYYKFNKNLGKGPGCGFWQPAWRVWLNFLRGTIPLLERYIGNLITRQFEGRSNEIVKTTTKQRLDAYYDLELRNSVMDDILEMMPESIRQKKARTILQHLSEAWRCWKANIPWDVPGMPAPIKKIIERYIKSKADAWVSAAHYNRERIKRGAHVEKTMVKKNLGRLTRLWIKNEQERQRQIQKNGPEITPEEATTIFSVMVEWLESRSFSPIPFPPLTYKNDTKILVLALEDLKDVYASKVRLNASEREELALIEEAYDNPHDTLNRIKKYLLTQRVFKPVDITMMENYQNISPVYSVDPLEKITDAYLDQYLWYEADQRKLFPNWIKPSDSEIPPLLVYKWTQGINNLSEIWDVSRGQSAVLLETTLGEMAEKIDFTLLNRLLRLIVDPNIADYITAKNNVVINFKDMSHVNKYGLIRGLKFASFIFQYYGLVIDLLLLGQERATDLAGPANNPNEFMQFKSKEVEKAHPIRLYTRYLDRIYMLFHFEEDEGEELTDEYLAENPDPNFENSIGYNNRKCWPKDSRMRLIRQDVNLGRAVFWEIQSRVPTSLTSIKWENAFVSVYSKNNPNLLFSMCGFEVRILPRQRMEEVVSNDEGVWDLVDERTKQRTAKAYLKVSEEEIKKFDSRIRGILMASGSTTFTKVAAKWNTSLISLFTYFREAIVATEPLLDILVKGETRIQNRVKLGLNSKMPTRFPPAVFYTPKELGGLGMISASHILIPASDLSWSKQTDTGITHFRAGMTHEDEKLIPTIFRYITTWENEFLDSQRVWAEYATKRQEAIQQNRRLAFEELEGSWDRGIPRISTLFQRDRHTLAYDRGHRIRREFKQYSLERNSPFWWTNSHHDGKLWNLNAYRTDVIQALGGIETILEHTLFKGTGFNSWEGLFWEKASGFEDSMQFKKLTHAQRTGLSQIPNRRFTLWWSPTINRANVYVGFLVQLDLTGIFLHGKIPTLKISLIQIFRAHLWQKIHESIVFDICQILDGELDVLQIESVTKETVHPRKSYKMNSSAADITMESVHEWEVSKPSLLHETNDSFKGLITNKMWFDVQLRYGDYDSHDISRYVRAKFLDYTTDNVSMYPSPTGVMIGIDLAYNMYDAYGNWFNGLKPLIQNSMRTIMKANPALYVLRERIRKGLQIYQSSVQEPFLNSSNYAELFNNDIKLFVDDTNVYRVTVHKTFEGNVATKAINGCIFTLNPKTGHLFLKIIHTSVWAGQKRLSQLAKWKTAEEVSALVRSLPKEEQPKQIIVTRKAMLDPLEVHMLDFPNIAIRPTELRLPFSAAMSIDKLSDVVMKATEPQMVLFNIYDDWLDRISSYTAFSRLTLLLRALKTNEESAKMILLSDPTITIKSYHLWPSFTDEQWITIESQMRDLILTEYGRKYNVNISALTQTEIKDIILGQNIKAPSVKRQKMAELEAARSEKQNDEEAAGASTVMKTKTINAQGEEIVVVASADYESQTFSSKNEWRKSAIANTLLYLRLKNIYVSADDFVEEQNVYVLPKNLLKKFIEISDVKIQVAAFIYGMSAKDHPKVKEIKTVVLVPQLGHVGSVQISNIPDIGDLPDTEGLELLGWIHTQTEELKFMAASEVATHSKLFADKKRDCIDISIFSTPGSVSLSAYNLTDEGYQWGEENKDIMNVLSEGFEPTFSTHAQLLLSDRITGNFIIPSGNVWNYTFMGTAFNQEGDYNFKYGIPLEFYNEMHRPVHFLQFSELAGDEELEAEQIDVFS |
Proteomic databases
PTM databases
Interaction
Subunit
Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with PRP40 and SNP1. Interacts (via SCwid domain) with CWC21. Interacts (via SCwid domain) with SNU114 (via N-terminus). Interacts (via RNase H homology domain and MPN domain) with BRR2; this modulates BRR2 ATPase and helicase activity. Interacts (via RNase H homology domain) with AAR2. AAR2 and BRR2 compete for PRP8 binding, and during U5 snRNP maturation BRR2 displaces the initially bound AAR2. Is associated with snRNP U5, together with SNU114 and BRR2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P33334 | AAR2 P32357 | 12 | EBI-465, EBI-340 | |
BINARY | P33334 | BRR2 P32639 | 26 | EBI-465, EBI-861 | |
BINARY | P33334 | MYO3 P36006 | 4 | EBI-465, EBI-11670 | |
BINARY | P33334 | MYO5 Q04439 | 4 | EBI-465, EBI-11687 | |
BINARY | P33334 | SNP1 Q00916 | 3 | EBI-465, EBI-724 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-31 | Pro residues | ||||
Sequence: MSGLPPPPPGFEEDSDLALPPPPPPPPGYEI | ||||||
Region | 1-60 | Disordered | ||||
Sequence: MSGLPPPPPGFEEDSDLALPPPPPPPPGYEIEELDNPMVPSSVNEDTFLPPPPPPPSNFE | ||||||
Region | 253-543 | SNU114/CWC21 interacting domain (SCwid) | ||||
Sequence: QHIENIEPLDPINLPLDSQDDEYVKDWLYDSRPLEEDSKKVNGTSYKKWSFDLPEMSNLYRLSTPLRDEVTDKNYYYLFDKKSFFNGKALNNAIPGGPKFEPLYPREEEEDYNEFNSIDRVIFRVPIRSEYKVAFPHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTPALFFDPSLNPIPHFIDNNSSLNVSNTKENGDFTLPEDFAPLLAEEEELILPNTKDAMSLYHSPFPFNRTKGKMVRAQDVALAKKWFLQHPDEEYPVKVKVSYQKLLKNYVLNELHPTLPTNHN | ||||||
Region | 885-1375 | Reverse transcriptase homology domain | ||||
Sequence: VMVEWLESRSFSPIPFPPLTYKNDTKILVLALEDLKDVYASKVRLNASEREELALIEEAYDNPHDTLNRIKKYLLTQRVFKPVDITMMENYQNISPVYSVDPLEKITDAYLDQYLWYEADQRKLFPNWIKPSDSEIPPLLVYKWTQGINNLSEIWDVSRGQSAVLLETTLGEMAEKIDFTLLNRLLRLIVDPNIADYITAKNNVVINFKDMSHVNKYGLIRGLKFASFIFQYYGLVIDLLLLGQERATDLAGPANNPNEFMQFKSKEVEKAHPIRLYTRYLDRIYMLFHFEEDEGEELTDEYLAENPDPNFENSIGYNNRKCWPKDSRMRLIRQDVNLGRAVFWEIQSRVPTSLTSIKWENAFVSVYSKNNPNLLFSMCGFEVRILPRQRMEEVVSNDEGVWDLVDERTKQRTAKAYLKVSEEEIKKFDSRIRGILMASGSTTFTKVAAKWNTSLISLFTYFREAIVATEPLLDILVKGETRIQNRVKLGL | ||||||
Region | 1376-1649 | Linker | ||||
Sequence: NSKMPTRFPPAVFYTPKELGGLGMISASHILIPASDLSWSKQTDTGITHFRAGMTHEDEKLIPTIFRYITTWENEFLDSQRVWAEYATKRQEAIQQNRRLAFEELEGSWDRGIPRISTLFQRDRHTLAYDRGHRIRREFKQYSLERNSPFWWTNSHHDGKLWNLNAYRTDVIQALGGIETILEHTLFKGTGFNSWEGLFWEKASGFEDSMQFKKLTHAQRTGLSQIPNRRFTLWWSPTINRANVYVGFLVQLDLTGIFLHGKIPTLKISLIQIF | ||||||
Region | 1585-1598 | Important for branch point selection | ||||
Sequence: MQFKKLTHAQRTGL | ||||||
Region | 1653-1824 | Restriction endonuclease homology domain | ||||
Sequence: LWQKIHESIVFDICQILDGELDVLQIESVTKETVHPRKSYKMNSSAADITMESVHEWEVSKPSLLHETNDSFKGLITNKMWFDVQLRYGDYDSHDISRYVRAKFLDYTTDNVSMYPSPTGVMIGIDLAYNMYDAYGNWFNGLKPLIQNSMRTIMKANPALYVLRERIRKGLQ | ||||||
Region | 1839-2092 | RNase H homology domain | ||||
Sequence: NYAELFNNDIKLFVDDTNVYRVTVHKTFEGNVATKAINGCIFTLNPKTGHLFLKIIHTSVWAGQKRLSQLAKWKTAEEVSALVRSLPKEEQPKQIIVTRKAMLDPLEVHMLDFPNIAIRPTELRLPFSAAMSIDKLSDVVMKATEPQMVLFNIYDDWLDRISSYTAFSRLTLLLRALKTNEESAKMILLSDPTITIKSYHLWPSFTDEQWITIESQMRDLILTEYGRKYNVNISALTQTEIKDIILGQNIKAPS | ||||||
Domain | 2182-2311 | MPN | ||||
Sequence: VYVLPKNLLKKFIEISDVKIQVAAFIYGMSAKDHPKVKEIKTVVLVPQLGHVGSVQISNIPDIGDLPDTEGLELLGWIHTQTEELKFMAASEVATHSKLFADKKRDCIDISIFSTPGSVSLSAYNLTDEG |
Domain
The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion.
Contains a region with structural similarity to reverse transcripase, presenting the classical thumb, fingers and palm architecture, but lacks enzyme activity, since the essential metal-binding residues are not conserved.
Contains a region with structural similarity to type-2 restriction endonucleases, but the residues that would bind catalytic metal ions in endonucleases are instead involved in hydrogen bonds that stabilize a highly conserved loop.
Contains a region with structural similarity to RNase H, but lacks RNase H activity.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,413
- Mass (Da)279,504
- Last updated1994-02-01 v1
- Checksum8F4F6F89D34D3508
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-31 | Pro residues | ||||
Sequence: MSGLPPPPPGFEEDSDLALPPPPPPPPGYEI | ||||||
Sequence conflict | 388-420 | in Ref. 2; AAA67044 | ||||
Sequence: PHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTP → LIYIIPGPVQCAYHGIIIQCRVLSRTMRSTTRL | ||||||
Sequence conflict | 1132 | in Ref. 2; AAA67044 | ||||
Sequence: T → S | ||||||
Sequence conflict | 1575 | in Ref. 2; AAA67044 | ||||
Sequence: W → C |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z24732 EMBL· GenBank· DDBJ | CAA80854.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L29421 EMBL· GenBank· DDBJ | AAA67044.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00027 EMBL· GenBank· DDBJ | AAB68011.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006934 EMBL· GenBank· DDBJ | DAA06858.1 EMBL· GenBank· DDBJ | Genomic DNA |