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P33334

- PRP8_YEAST

UniProt

P33334 - PRP8_YEAST

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Protein
Pre-mRNA-splicing factor 8
Gene
PRP8, DBF3, DNA39, RNA8, SLT21, USA2, YHR165C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

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
Complete GO annotation...

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

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 8
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP33334.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni253 – 543291SNU114/CWC21 interacting domain (SCwid)
Add
BLAST
Regioni885 – 1375491Reverse transcriptase homology domain
Add
BLAST
Regioni1376 – 1649274Linker
Add
BLAST
Regioni1585 – 159814Important for branch point selection
Add
BLAST
Regioni1653 – 1824172Restriction endonuclease homology domain
Add
BLAST
Regioni1839 – 2092254RNase H homology domain
Add
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.2 Publications
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.2 Publications
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.2 Publications
Contains a region with structural similarity to RNase H, but lacks RNase H activity.2 Publications

Sequence similaritiesi

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

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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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti388 – 42033PHLYN…EYDTP → LIYIIPGPVQCAYHGIIIQC RVLSRTMRSTTRL in AAA67044. 1 Publication
Add
BLAST
Sequence conflicti1132 – 11321T → S in AAA67044. 1 Publication
Sequence conflicti1575 – 15751W → C in AAA67044. 1 Publication

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.
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Publicationsi

« Hide 'large scale' publications
  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: September 3, 2014
This is version 132 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.

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

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