P33334 · PRP8_YEAST

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcatalytic step 2 spliceosome
Cellular Componentcytoplasm
Cellular Componentnucleus
Cellular Componentspliceosomal complex
Cellular ComponentU4/U6 x U5 tri-snRNP complex
Cellular ComponentU5 snRNP
Molecular Functionmetallopeptidase activity
Molecular FunctionmRNA binding
Molecular Functionpre-mRNA intronic binding
Molecular FunctionU1 snRNA binding
Molecular FunctionU2 snRNA binding
Molecular FunctionU5 snRNA binding
Molecular FunctionU6 snRNA binding
Biological Processgeneration of catalytic spliceosome for second transesterification step
Biological ProcessmRNA 3'-splice site recognition
Biological ProcessmRNA 5'-splice site recognition
Biological ProcessmRNA splicing, via spliceosome
Biological Processspliceosomal snRNP assembly
Biological Processspliceosomal tri-snRNP complex assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pre-mRNA-splicing factor 8

Gene names

    • Name
      PRP8
    • Synonyms
      DBF3, DNA39, RNA8, SLT21, USA2
    • Ordered locus names
      YHR165C

Organism names

Accessions

  • Primary accession
    P33334
  • Secondary accessions
    • D3DLB4

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis1658No effect on viability.
Mutagenesis1684No effect on viability.
Mutagenesis1687No effect on viability.
Mutagenesis1700No effect on viability.
Mutagenesis1735No effect on viability.
Mutagenesis1853Alters protein folding. Severely impaired growth. Strongly reduced growth at 35 degrees Celsius; when associated with A-1854.
Mutagenesis1853Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius.
Mutagenesis1854Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Strongly reduced growth at 35 degrees Celsius; when associated with A-1853.
Mutagenesis1854Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius.
Mutagenesis1855Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius.
Mutagenesis1936Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius.
Mutagenesis1937Severely impaired growth. Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000970421-2413Pre-mRNA-splicing factor 8

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

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-31Pro residues
Region1-60Disordered
Region253-543SNU114/CWC21 interacting domain (SCwid)
Region885-1375Reverse transcriptase homology domain
Region1376-1649Linker
Region1585-1598Important for branch point selection
Region1653-1824Restriction endonuclease homology domain
Region1839-2092RNase H homology domain
Domain2182-2311MPN

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 status
    Complete
  • Length
    2,413
  • Mass (Da)
    279,504
  • Last updated
    1994-02-01 v1
  • Checksum
    8F4F6F89D34D3508
MSGLPPPPPGFEEDSDLALPPPPPPPPGYEIEELDNPMVPSSVNEDTFLPPPPPPPSNFEINAEEIVDFTLPPPPPPPGLDELETKAEKKVELHGKRKLDIGKDTFVTRKSRKRAKKMTKKAKRSNLYTPKAEMPPEHLRKIINTHSDMASKMYNTDKKAFLGALKYLPHAILKLLENMPHPWEQAKEVKVLYHTSGAITFVNETPRVIEPVYTAQWSATWIAMRREKRDRTHFKRMRFPPFDDDEPPLSYEQHIENIEPLDPINLPLDSQDDEYVKDWLYDSRPLEEDSKKVNGTSYKKWSFDLPEMSNLYRLSTPLRDEVTDKNYYYLFDKKSFFNGKALNNAIPGGPKFEPLYPREEEEDYNEFNSIDRVIFRVPIRSEYKVAFPHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTPALFFDPSLNPIPHFIDNNSSLNVSNTKENGDFTLPEDFAPLLAEEEELILPNTKDAMSLYHSPFPFNRTKGKMVRAQDVALAKKWFLQHPDEEYPVKVKVSYQKLLKNYVLNELHPTLPTNHNKTKLLKSLKNTKYFQQTTIDWVEAGLQLCRQGHNMLNLLIHRKGLTYLHLDYNFNLKPTKTLTTKERKKSRLGNSFHLMRELLKMMKLIVDTHVQFRLGNVDAFQLADGIHYILNHIGQLTGIYRYKYKVMHQIRACKDLKHIIYYKFNKNLGKGPGCGFWQPAWRVWLNFLRGTIPLLERYIGNLITRQFEGRSNEIVKTTTKQRLDAYYDLELRNSVMDDILEMMPESIRQKKARTILQHLSEAWRCWKANIPWDVPGMPAPIKKIIERYIKSKADAWVSAAHYNRERIKRGAHVEKTMVKKNLGRLTRLWIKNEQERQRQIQKNGPEITPEEATTIFSVMVEWLESRSFSPIPFPPLTYKNDTKILVLALEDLKDVYASKVRLNASEREELALIEEAYDNPHDTLNRIKKYLLTQRVFKPVDITMMENYQNISPVYSVDPLEKITDAYLDQYLWYEADQRKLFPNWIKPSDSEIPPLLVYKWTQGINNLSEIWDVSRGQSAVLLETTLGEMAEKIDFTLLNRLLRLIVDPNIADYITAKNNVVINFKDMSHVNKYGLIRGLKFASFIFQYYGLVIDLLLLGQERATDLAGPANNPNEFMQFKSKEVEKAHPIRLYTRYLDRIYMLFHFEEDEGEELTDEYLAENPDPNFENSIGYNNRKCWPKDSRMRLIRQDVNLGRAVFWEIQSRVPTSLTSIKWENAFVSVYSKNNPNLLFSMCGFEVRILPRQRMEEVVSNDEGVWDLVDERTKQRTAKAYLKVSEEEIKKFDSRIRGILMASGSTTFTKVAAKWNTSLISLFTYFREAIVATEPLLDILVKGETRIQNRVKLGLNSKMPTRFPPAVFYTPKELGGLGMISASHILIPASDLSWSKQTDTGITHFRAGMTHEDEKLIPTIFRYITTWENEFLDSQRVWAEYATKRQEAIQQNRRLAFEELEGSWDRGIPRISTLFQRDRHTLAYDRGHRIRREFKQYSLERNSPFWWTNSHHDGKLWNLNAYRTDVIQALGGIETILEHTLFKGTGFNSWEGLFWEKASGFEDSMQFKKLTHAQRTGLSQIPNRRFTLWWSPTINRANVYVGFLVQLDLTGIFLHGKIPTLKISLIQIFRAHLWQKIHESIVFDICQILDGELDVLQIESVTKETVHPRKSYKMNSSAADITMESVHEWEVSKPSLLHETNDSFKGLITNKMWFDVQLRYGDYDSHDISRYVRAKFLDYTTDNVSMYPSPTGVMIGIDLAYNMYDAYGNWFNGLKPLIQNSMRTIMKANPALYVLRERIRKGLQIYQSSVQEPFLNSSNYAELFNNDIKLFVDDTNVYRVTVHKTFEGNVATKAINGCIFTLNPKTGHLFLKIIHTSVWAGQKRLSQLAKWKTAEEVSALVRSLPKEEQPKQIIVTRKAMLDPLEVHMLDFPNIAIRPTELRLPFSAAMSIDKLSDVVMKATEPQMVLFNIYDDWLDRISSYTAFSRLTLLLRALKTNEESAKMILLSDPTITIKSYHLWPSFTDEQWITIESQMRDLILTEYGRKYNVNISALTQTEIKDIILGQNIKAPSVKRQKMAELEAARSEKQNDEEAAGASTVMKTKTINAQGEEIVVVASADYESQTFSSKNEWRKSAIANTLLYLRLKNIYVSADDFVEEQNVYVLPKNLLKKFIEISDVKIQVAAFIYGMSAKDHPKVKEIKTVVLVPQLGHVGSVQISNIPDIGDLPDTEGLELLGWIHTQTEELKFMAASEVATHSKLFADKKRDCIDISIFSTPGSVSLSAYNLTDEGYQWGEENKDIMNVLSEGFEPTFSTHAQLLLSDRITGNFIIPSGNVWNYTFMGTAFNQEGDYNFKYGIPLEFYNEMHRPVHFLQFSELAGDEELEAEQIDVFS

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-31Pro residues
Sequence conflict388-420in Ref. 2; AAA67044
Sequence conflict1132in Ref. 2; AAA67044
Sequence conflict1575in Ref. 2; AAA67044

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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