Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P33334

- PRP8_YEAST

UniProt

P33334 - PRP8_YEAST

Protein

Pre-mRNA-splicing factor 8

Gene

PRP8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 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.8 Publications

    GO - Molecular functioni

    1. pre-mRNA intronic binding Source: SGD
    2. protein binding Source: IntAct
    3. U1 snRNA binding Source: SGD
    4. U2 snRNA binding Source: SGD
    5. U5 snRNA binding Source: SGD
    6. U6 snRNA binding Source: SGD

    GO - Biological processi

    1. generation of catalytic spliceosome for second transesterification step Source: SGD
    2. mRNA 3'-splice site recognition Source: SGD
    3. spliceosomal tri-snRNP complex assembly Source: SGD

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31199-MONOMER.
    ReactomeiREACT_191540. mRNA Splicing - Minor Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pre-mRNA-splicing factor 8
    Gene namesi
    Name:PRP8
    Synonyms:DBF3, DNA39, RNA8, SLT21, USA2
    Ordered Locus Names:YHR165C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VIII

    Organism-specific databases

    CYGDiYHR165c.
    SGDiS000001208. PRP8.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nucleus Source: SGD
    2. spliceosomal complex Source: UniProtKB-KW
    3. U4/U6 x U5 tri-snRNP complex Source: SGD
    4. U5 snRNP Source: SGD

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1658 – 16581H → S: No effect on viability. 1 Publication
    Mutagenesisi1684 – 16841E → Q: No effect on viability. 1 Publication
    Mutagenesisi1687 – 16871H → S: No effect on viability. 1 Publication
    Mutagenesisi1700 – 17001D → N: No effect on viability. 1 Publication
    Mutagenesisi1735 – 17351D → N: No effect on viability. 1 Publication
    Mutagenesisi1853 – 18531D → A: Alters protein folding. Severely impaired growth. Strongly reduced growth at 35 degrees Celsius; when associated with A-1854. 3 Publications
    Mutagenesisi1853 – 18531D → N: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 3 Publications
    Mutagenesisi1854 – 18541D → A: 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. 2 Publications
    Mutagenesisi1854 – 18541D → N: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 2 Publications
    Mutagenesisi1855 – 18551T → A: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 1 Publication
    Mutagenesisi1936 – 19361T → A: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 1 Publication
    Mutagenesisi1937 – 19371R → K: Severely impaired growth. Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24132413Pre-mRNA-splicing factor 8PRO_0000097042Add
    BLAST

    Proteomic databases

    MaxQBiP33334.
    PaxDbiP33334.
    PRIDEiP33334.

    Expressioni

    Gene expression databases

    GenevestigatoriP33334.

    Interactioni

    Subunit structurei

    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 BRR2.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LIN1P388523EBI-465,EBI-570
    MYO3P360064EBI-465,EBI-11670
    MYO5Q044394EBI-465,EBI-11687
    SNP1Q009162EBI-465,EBI-724

    Protein-protein interaction databases

    BioGridi36599. 120 interactions.
    DIPiDIP-2427N.
    IntActiP33334. 63 interactions.
    MINTiMINT-599605.
    STRINGi4932.YHR165C.

    Structurei

    Secondary structure

    1
    2413
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi885 – 8928
    Helixi908 – 92417
    Helixi931 – 94515
    Helixi947 – 96014
    Beta strandi967 – 9693
    Helixi986 – 100520
    Beta strandi1013 – 10153
    Helixi1021 – 103313
    Turni1036 – 10394
    Beta strandi1046 – 10538
    Turni1056 – 10605
    Helixi1063 – 10719
    Helixi1076 – 108510
    Beta strandi1087 – 10926
    Beta strandi1095 – 10984
    Helixi1110 – 113526
    Beta strandi1138 – 11403
    Helixi1150 – 11545
    Beta strandi1156 – 11649
    Beta strandi1167 – 11748
    Helixi1176 – 118914
    Turni1197 – 12004
    Helixi1209 – 12113
    Helixi1217 – 123115
    Turni1236 – 12383
    Helixi1243 – 12453
    Beta strandi1246 – 12527
    Beta strandi1258 – 12625
    Beta strandi1265 – 12717
    Helixi1272 – 12743
    Beta strandi1283 – 12897
    Turni1291 – 12933
    Beta strandi1295 – 130410
    Helixi1306 – 132015
    Helixi1328 – 134619
    Helixi1348 – 13514
    Helixi1354 – 137522
    Helixi1385 – 13895
    Helixi1392 – 13943
    Helixi1409 – 14124
    Beta strandi1414 – 14174
    Beta strandi1422 – 14254
    Helixi1427 – 14293
    Beta strandi1434 – 14363
    Helixi1440 – 14434
    Helixi1447 – 147024
    Helixi1477 – 14793
    Turni1480 – 14823
    Turni1487 – 14904
    Helixi1491 – 14955
    Helixi1499 – 15024
    Helixi1508 – 15147
    Helixi1515 – 15173
    Helixi1530 – 15334
    Helixi1540 – 154910
    Helixi1552 – 15587
    Helixi1563 – 15653
    Helixi1603 – 161412
    Turni1617 – 16193
    Beta strandi1633 – 16364
    Helixi1641 – 16488
    Turni1649 – 16524
    Helixi1653 – 167018
    Turni1671 – 16777
    Beta strandi1678 – 16836
    Helixi1690 – 16923
    Beta strandi1700 – 171112
    Beta strandi1726 – 173914
    Beta strandi1743 – 17453
    Helixi1748 – 175912
    Beta strandi1763 – 17664
    Beta strandi1768 – 177811
    Turni1779 – 17824
    Beta strandi1783 – 17886
    Helixi1794 – 180815
    Helixi1810 – 182213
    Turni1837 – 18393
    Helixi1840 – 18445
    Beta strandi1845 – 18473
    Beta strandi1849 – 18535
    Beta strandi1857 – 18648
    Beta strandi1866 – 18683
    Beta strandi1870 – 18756
    Beta strandi1877 – 18826
    Turni1884 – 18863
    Beta strandi1888 – 18947
    Helixi1896 – 18994
    Helixi1905 – 192319
    Helixi1926 – 19283
    Beta strandi1931 – 19377
    Helixi1938 – 19403
    Helixi1941 – 19477
    Turni1948 – 19503
    Beta strandi1954 – 19574
    Beta strandi1959 – 19613
    Helixi1965 – 19706
    Helixi1972 – 19809
    Beta strandi1985 – 19906
    Turni1991 – 19944
    Helixi1995 – 19973
    Helixi2001 – 201717
    Helixi2019 – 20268
    Beta strandi2030 – 20323
    Beta strandi2039 – 20413
    Helixi2045 – 206723
    Helixi2071 – 20733
    Helixi2076 – 20849
    Helixi2149 – 215911
    Helixi2160 – 21678
    Beta strandi2168 – 21714
    Beta strandi2178 – 21803
    Beta strandi2182 – 21865
    Helixi2187 – 21959
    Beta strandi2199 – 22013
    Beta strandi2204 – 22118
    Beta strandi2218 – 22258
    Beta strandi2229 – 22313
    Beta strandi2236 – 22383
    Beta strandi2245 – 22473
    Beta strandi2254 – 226411
    Helixi2271 – 228111
    Turni2282 – 22843
    Beta strandi2289 – 22968
    Beta strandi2299 – 23079
    Helixi2309 – 23168
    Turni2317 – 23204
    Turni2323 – 23253
    Helixi2331 – 23333
    Beta strandi2334 – 234512
    Beta strandi2348 – 23525
    Helixi2360 – 23623
    Helixi2363 – 23653
    Beta strandi2374 – 23763
    Helixi2385 – 23873
    Helixi2391 – 23944

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OG4X-ray2.00A2147-2397[»]
    3E66X-ray2.05A/B1822-2095[»]
    3E9OX-ray2.00A1836-2087[»]
    3E9PX-ray2.10A/B1833-2087[»]
    3SBGX-ray3.28A1836-2397[»]
    3SBTX-ray1.80A1836-2092[»]
    3ZEFX-ray3.10B/E885-2413[»]
    4BGDX-ray3.10C2148-2395[»]
    4I43X-ray2.00B885-2413[»]
    4ILGX-ray2.10B1836-2090[»]
    C2147-2413[»]
    4ILHX-ray1.85A1836-2090[»]
    4ILJX-ray2.00A/B1836-2090[»]
    ProteinModelPortaliP33334.
    SMRiP33334. Positions 1835-2396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33334.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2178 – 2286109MPNAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni253 – 543291SNU114/CWC21 interacting domain (SCwid)Add
    BLAST
    Regioni885 – 1375491Reverse transcriptase homology domainAdd
    BLAST
    Regioni1376 – 1649274LinkerAdd
    BLAST
    Regioni1585 – 159814Important for branch point selectionAdd
    BLAST
    Regioni1653 – 1824172Restriction endonuclease homology domainAdd
    BLAST
    Regioni1839 – 2092254RNase H homology domainAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 95Poly-Pro
    Compositional biasi20 – 278Poly-Pro
    Compositional biasi50 – 567Poly-Pro
    Compositional biasi72 – 787Poly-Pro

    Domaini

    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.

    Sequence similaritiesi

    Contains 1 MPN (JAB/Mov34) domain.Curated

    Phylogenomic databases

    eggNOGiCOG5178.
    GeneTreeiENSGT00390000015210.
    HOGENOMiHOG000184103.
    KOiK12856.
    OMAiPPGWGAS.
    OrthoDBiEOG7PK96V.

    Family and domain databases

    InterProiIPR000555. JAMM/MPN+_dom.
    IPR012591. PRO8NT.
    IPR012592. PROCN.
    IPR012984. PROCT.
    IPR027652. PRP8.
    IPR021983. PRP8_domainIV.
    IPR019581. Prp8_U5-snRNA-bd.
    IPR019580. Prp8_U6-snRNA-bd.
    IPR012337. RNaseH-like_dom.
    IPR019582. RRM_spliceosomal_PrP8.
    [Graphical view]
    PANTHERiPTHR11140. PTHR11140. 1 hit.
    PfamiPF08082. PRO8NT. 1 hit.
    PF08083. PROCN. 1 hit.
    PF08084. PROCT. 1 hit.
    PF12134. PRP8_domainIV. 1 hit.
    PF10598. RRM_4. 1 hit.
    PF10597. U5_2-snRNA_bdg. 1 hit.
    PF10596. U6-snRNA_bdg. 1 hit.
    [Graphical view]
    ProDomiPD149576. Pre-mRNA-splicing_factor-8. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00232. JAB_MPN. 1 hit.
    [Graphical view]
    SUPFAMiSSF53098. SSF53098. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P33334-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGLPPPPPG FEEDSDLALP PPPPPPPGYE IEELDNPMVP SSVNEDTFLP     50
    PPPPPPSNFE INAEEIVDFT LPPPPPPPGL DELETKAEKK VELHGKRKLD 100
    IGKDTFVTRK SRKRAKKMTK KAKRSNLYTP KAEMPPEHLR KIINTHSDMA 150
    SKMYNTDKKA FLGALKYLPH AILKLLENMP HPWEQAKEVK VLYHTSGAIT 200
    FVNETPRVIE PVYTAQWSAT WIAMRREKRD RTHFKRMRFP PFDDDEPPLS 250
    YEQHIENIEP LDPINLPLDS QDDEYVKDWL YDSRPLEEDS KKVNGTSYKK 300
    WSFDLPEMSN LYRLSTPLRD EVTDKNYYYL FDKKSFFNGK ALNNAIPGGP 350
    KFEPLYPREE EEDYNEFNSI DRVIFRVPIR SEYKVAFPHL YNSRPRSVRI 400
    PWYNNPVSCI IQNDEEYDTP ALFFDPSLNP IPHFIDNNSS LNVSNTKENG 450
    DFTLPEDFAP LLAEEEELIL PNTKDAMSLY HSPFPFNRTK GKMVRAQDVA 500
    LAKKWFLQHP DEEYPVKVKV SYQKLLKNYV LNELHPTLPT NHNKTKLLKS 550
    LKNTKYFQQT TIDWVEAGLQ LCRQGHNMLN LLIHRKGLTY LHLDYNFNLK 600
    PTKTLTTKER KKSRLGNSFH LMRELLKMMK LIVDTHVQFR LGNVDAFQLA 650
    DGIHYILNHI GQLTGIYRYK YKVMHQIRAC KDLKHIIYYK FNKNLGKGPG 700
    CGFWQPAWRV WLNFLRGTIP LLERYIGNLI TRQFEGRSNE IVKTTTKQRL 750
    DAYYDLELRN SVMDDILEMM PESIRQKKAR TILQHLSEAW RCWKANIPWD 800
    VPGMPAPIKK IIERYIKSKA DAWVSAAHYN RERIKRGAHV EKTMVKKNLG 850
    RLTRLWIKNE QERQRQIQKN GPEITPEEAT TIFSVMVEWL ESRSFSPIPF 900
    PPLTYKNDTK ILVLALEDLK DVYASKVRLN ASEREELALI EEAYDNPHDT 950
    LNRIKKYLLT QRVFKPVDIT MMENYQNISP VYSVDPLEKI TDAYLDQYLW 1000
    YEADQRKLFP NWIKPSDSEI PPLLVYKWTQ GINNLSEIWD VSRGQSAVLL 1050
    ETTLGEMAEK IDFTLLNRLL RLIVDPNIAD YITAKNNVVI NFKDMSHVNK 1100
    YGLIRGLKFA SFIFQYYGLV IDLLLLGQER ATDLAGPANN PNEFMQFKSK 1150
    EVEKAHPIRL YTRYLDRIYM LFHFEEDEGE ELTDEYLAEN PDPNFENSIG 1200
    YNNRKCWPKD SRMRLIRQDV NLGRAVFWEI QSRVPTSLTS IKWENAFVSV 1250
    YSKNNPNLLF SMCGFEVRIL PRQRMEEVVS NDEGVWDLVD ERTKQRTAKA 1300
    YLKVSEEEIK KFDSRIRGIL MASGSTTFTK VAAKWNTSLI SLFTYFREAI 1350
    VATEPLLDIL VKGETRIQNR VKLGLNSKMP TRFPPAVFYT PKELGGLGMI 1400
    SASHILIPAS DLSWSKQTDT GITHFRAGMT HEDEKLIPTI FRYITTWENE 1450
    FLDSQRVWAE YATKRQEAIQ QNRRLAFEEL EGSWDRGIPR ISTLFQRDRH 1500
    TLAYDRGHRI RREFKQYSLE RNSPFWWTNS HHDGKLWNLN AYRTDVIQAL 1550
    GGIETILEHT LFKGTGFNSW EGLFWEKASG FEDSMQFKKL THAQRTGLSQ 1600
    IPNRRFTLWW SPTINRANVY VGFLVQLDLT GIFLHGKIPT LKISLIQIFR 1650
    AHLWQKIHES IVFDICQILD GELDVLQIES VTKETVHPRK SYKMNSSAAD 1700
    ITMESVHEWE VSKPSLLHET NDSFKGLITN KMWFDVQLRY GDYDSHDISR 1750
    YVRAKFLDYT TDNVSMYPSP TGVMIGIDLA YNMYDAYGNW FNGLKPLIQN 1800
    SMRTIMKANP ALYVLRERIR KGLQIYQSSV QEPFLNSSNY AELFNNDIKL 1850
    FVDDTNVYRV TVHKTFEGNV ATKAINGCIF TLNPKTGHLF LKIIHTSVWA 1900
    GQKRLSQLAK WKTAEEVSAL VRSLPKEEQP KQIIVTRKAM LDPLEVHMLD 1950
    FPNIAIRPTE LRLPFSAAMS IDKLSDVVMK ATEPQMVLFN IYDDWLDRIS 2000
    SYTAFSRLTL LLRALKTNEE SAKMILLSDP TITIKSYHLW PSFTDEQWIT 2050
    IESQMRDLIL TEYGRKYNVN ISALTQTEIK DIILGQNIKA PSVKRQKMAE 2100
    LEAARSEKQN DEEAAGASTV MKTKTINAQG EEIVVVASAD YESQTFSSKN 2150
    EWRKSAIANT LLYLRLKNIY VSADDFVEEQ NVYVLPKNLL KKFIEISDVK 2200
    IQVAAFIYGM SAKDHPKVKE IKTVVLVPQL GHVGSVQISN IPDIGDLPDT 2250
    EGLELLGWIH TQTEELKFMA ASEVATHSKL FADKKRDCID ISIFSTPGSV 2300
    SLSAYNLTDE GYQWGEENKD IMNVLSEGFE PTFSTHAQLL LSDRITGNFI 2350
    IPSGNVWNYT FMGTAFNQEG DYNFKYGIPL EFYNEMHRPV HFLQFSELAG 2400
    DEELEAEQID VFS 2413
    Length:2,413
    Mass (Da):279,504
    Last modified:February 1, 1994 - v1
    Checksum:i8F4F6F89D34D3508
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti388 – 42033PHLYN…EYDTP → LIYIIPGPVQCAYHGIIIQC RVLSRTMRSTTRL in AAA67044. (PubMed:7838707)CuratedAdd
    BLAST
    Sequence conflicti1132 – 11321T → S in AAA67044. (PubMed:7838707)Curated
    Sequence conflicti1575 – 15751W → C in AAA67044. (PubMed:7838707)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z24732 Genomic DNA. Translation: CAA80854.1.
    L29421 Genomic DNA. Translation: AAA67044.1.
    U00027 Genomic DNA. Translation: AAB68011.1.
    BK006934 Genomic DNA. Translation: DAA06858.1.
    PIRiS34670.
    RefSeqiNP_012035.1. NM_001179296.1.

    Genome annotation databases

    EnsemblFungiiYHR165C; YHR165C; YHR165C.
    GeneIDi856570.
    KEGGisce:YHR165C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z24732 Genomic DNA. Translation: CAA80854.1 .
    L29421 Genomic DNA. Translation: AAA67044.1 .
    U00027 Genomic DNA. Translation: AAB68011.1 .
    BK006934 Genomic DNA. Translation: DAA06858.1 .
    PIRi S34670.
    RefSeqi NP_012035.1. NM_001179296.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OG4 X-ray 2.00 A 2147-2397 [» ]
    3E66 X-ray 2.05 A/B 1822-2095 [» ]
    3E9O X-ray 2.00 A 1836-2087 [» ]
    3E9P X-ray 2.10 A/B 1833-2087 [» ]
    3SBG X-ray 3.28 A 1836-2397 [» ]
    3SBT X-ray 1.80 A 1836-2092 [» ]
    3ZEF X-ray 3.10 B/E 885-2413 [» ]
    4BGD X-ray 3.10 C 2148-2395 [» ]
    4I43 X-ray 2.00 B 885-2413 [» ]
    4ILG X-ray 2.10 B 1836-2090 [» ]
    C 2147-2413 [» ]
    4ILH X-ray 1.85 A 1836-2090 [» ]
    4ILJ X-ray 2.00 A/B 1836-2090 [» ]
    ProteinModelPortali P33334.
    SMRi P33334. Positions 1835-2396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36599. 120 interactions.
    DIPi DIP-2427N.
    IntActi P33334. 63 interactions.
    MINTi MINT-599605.
    STRINGi 4932.YHR165C.

    Proteomic databases

    MaxQBi P33334.
    PaxDbi P33334.
    PRIDEi P33334.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR165C ; YHR165C ; YHR165C .
    GeneIDi 856570.
    KEGGi sce:YHR165C.

    Organism-specific databases

    CYGDi YHR165c.
    SGDi S000001208. PRP8.

    Phylogenomic databases

    eggNOGi COG5178.
    GeneTreei ENSGT00390000015210.
    HOGENOMi HOG000184103.
    KOi K12856.
    OMAi PPGWGAS.
    OrthoDBi EOG7PK96V.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31199-MONOMER.
    Reactomei REACT_191540. mRNA Splicing - Minor Pathway.

    Miscellaneous databases

    EvolutionaryTracei P33334.
    NextBioi 982414.
    PROi P33334.

    Gene expression databases

    Genevestigatori P33334.

    Family and domain databases

    InterProi IPR000555. JAMM/MPN+_dom.
    IPR012591. PRO8NT.
    IPR012592. PROCN.
    IPR012984. PROCT.
    IPR027652. PRP8.
    IPR021983. PRP8_domainIV.
    IPR019581. Prp8_U5-snRNA-bd.
    IPR019580. Prp8_U6-snRNA-bd.
    IPR012337. RNaseH-like_dom.
    IPR019582. RRM_spliceosomal_PrP8.
    [Graphical view ]
    PANTHERi PTHR11140. PTHR11140. 1 hit.
    Pfami PF08082. PRO8NT. 1 hit.
    PF08083. PROCN. 1 hit.
    PF08084. PROCT. 1 hit.
    PF12134. PRP8_domainIV. 1 hit.
    PF10598. RRM_4. 1 hit.
    PF10597. U5_2-snRNA_bdg. 1 hit.
    PF10596. U6-snRNA_bdg. 1 hit.
    [Graphical view ]
    ProDomi PD149576. Pre-mRNA-splicing_factor-8. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00232. JAB_MPN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Extraordinary sequence conservation of the PRP8 splicing factor."
      Hodges P.E., Jackson S.P., Brown J.D., Beggs J.D.
      Yeast 11:337-342(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The budding yeast U5 snRNP Prp8 is a highly conserved protein which links RNA splicing with cell cycle progression."
      Shea J.E., Toyn J.H., Johnston L.H.
      Nucleic Acids Res. 22:5555-5564(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Cloning of the RNA8 gene of Saccharomyces cerevisiae, detection of the RNA8 protein, and demonstration that it is essential for nuclear pre-mRNA splicing."
      Jackson S.P., Lossky M., Beggs J.D.
      Mol. Cell. Biol. 8:1067-1075(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals."
      Abovich N., Rosbash M.
      Cell 89:403-412(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRP40.
    7. "Identification by mass spectrometry and functional analysis of novel proteins of the yeast [U4/U6.U5] tri-snRNP."
      Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R., Fabrizio P.
      EMBO J. 18:4535-4548(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Functional interactions of Prp8 with both splice sites at the spliceosomal catalytic center."
      Siatecka M., Reyes J.L., Konarska M.M.
      Genes Dev. 13:1983-1993(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "New roles for the Snp1 and Exo84 proteins in yeast pre-mRNA splicing."
      Awasthi S., Palmer R., Castro M., Mobarak C.D., Ruby S.W.
      J. Biol. Chem. 276:31004-31015(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNP1.
    10. "Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs."
      Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.
      Mol. Cell. Biol. 22:2011-2024(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CWC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Spatial organization of protein-RNA interactions in the branch site-3' splice site region during pre-mRNA splicing in yeast."
      McPheeters D.S., Muhlenkamp P.
      Mol. Cell. Biol. 23:4174-4186(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "prp8 mutations that cause human retinitis pigmentosa lead to a U5 snRNP maturation defect in yeast."
      Boon K.L., Grainger R.J., Ehsani P., Barrass J.D., Auchynnikava T., Inglehearn C.F., Beggs J.D.
      Nat. Struct. Mol. Biol. 14:1077-1083(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    14. "Structural elucidation of a PRP8 core domain from the heart of the spliceosome."
      Ritchie D.B., Schellenberg M.J., Gesner E.M., Raithatha S.A., Stuart D.T., Macmillan A.M.
      Nat. Struct. Mol. Biol. 15:1199-1205(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-1853 AND ASP-1854, LACK OF METAL-BINDING SITE.
    15. "Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNP by electron microscopy."
      Hacker I., Sander B., Golas M.M., Wolf E., Karagoz E., Kastner B., Stark H., Fabrizio P., Luhrmann R.
      Nat. Struct. Mol. Biol. 15:1206-1212(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, ELECTRON MICROSCOPY.
    16. "ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8."
      Maeder C., Kutach A.K., Guthrie C.
      Nat. Struct. Mol. Biol. 16:42-48(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRR2.
    17. "Physical and genetic interactions of yeast Cwc21p, an ortholog of human SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome."
      Grainger R.J., Barrass J.D., Jacquier A., Rain J.-C., Beggs J.D.
      RNA 15:2161-2173(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CWC21 AND SNU114.
    18. "Structure of a multipartite protein-protein interaction domain in splicing factor Prp8 and its link to retinitis pigmentosa."
      Pena V., Liu S., Bujnicki J.M., Luehrmann R., Wahl M.C.
      Mol. Cell 25:615-624(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2147-2413, ABSENCE OF METAL BINDING.
    19. "Structure and function of an RNase H domain at the heart of the spliceosome."
      Pena V., Rozov A., Fabrizio P., Luehrmann R., Wahl M.C.
      EMBO J. 27:2929-2940(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1827-2092, ABSENCE OF METAL BINDING, DOMAIN, MUTAGENESIS OF ASP-1853; ASP-1854; THR-1855; THR-1936 AND ARG-1937.
    20. "Crystal structure of the beta-finger domain of Prp8 reveals analogy to ribosomal proteins."
      Yang K., Zhang L., Xu T., Heroux A., Zhao R.
      Proc. Natl. Acad. Sci. U.S.A. 105:13817-13822(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1822-2095, ABSENCE OF METAL BINDING, FUNCTION, MUTAGENESIS OF ASP-1853.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1836-2092 IN COMPLEX WITH AAR2, INTERACTION WITH AAR2.
    22. "Crystal structure of Prp8 reveals active site cavity of the spliceosome."
      Galej W.P., Oubridge C., Newman A.J., Nagai K.
      Nature 493:638-643(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 885-2413 IN COMPLEX WITH AAR2, FUNCTION, DOMAIN, INTERACTION WITH AAR2, MUTAGENESIS OF HIS-1658; GLU-1684; HIS-1687; ASP-1700 AND ASP-1735.

    Entry informationi

    Entry nameiPRP8_YEAST
    AccessioniPrimary (citable) accession number: P33334
    Secondary accession number(s): D3DLB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 468 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

    External Data

    Dasty 3