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P33334

- PRP8_YEAST

UniProt

P33334 - PRP8_YEAST

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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

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. U1 snRNA binding Source: SGD
  3. U2 snRNA binding Source: SGD
  4. U5 snRNA binding Source: SGD
  5. 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
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. nucleus Source: SGD
  2. spliceosomal complex Source: UniProtKB-KW
  3. U4/U6 x U5 tri-snRNP complex Source: SGD
  4. U5 snRNP Source: SGD
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 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. 121 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 – 8928Combined sources
Helixi908 – 92417Combined sources
Helixi931 – 94515Combined sources
Helixi947 – 96014Combined sources
Beta strandi967 – 9693Combined sources
Helixi986 – 100520Combined sources
Beta strandi1013 – 10153Combined sources
Helixi1021 – 103313Combined sources
Turni1036 – 10394Combined sources
Beta strandi1046 – 10538Combined sources
Turni1056 – 10605Combined sources
Helixi1063 – 10719Combined sources
Helixi1076 – 108510Combined sources
Beta strandi1087 – 10926Combined sources
Beta strandi1095 – 10984Combined sources
Helixi1110 – 113526Combined sources
Beta strandi1138 – 11403Combined sources
Helixi1150 – 11545Combined sources
Beta strandi1156 – 11649Combined sources
Beta strandi1167 – 11748Combined sources
Helixi1176 – 118914Combined sources
Turni1197 – 12004Combined sources
Helixi1209 – 12113Combined sources
Helixi1217 – 123115Combined sources
Turni1236 – 12383Combined sources
Helixi1243 – 12453Combined sources
Beta strandi1246 – 12527Combined sources
Beta strandi1258 – 12625Combined sources
Beta strandi1265 – 12717Combined sources
Helixi1272 – 12743Combined sources
Beta strandi1283 – 12897Combined sources
Turni1291 – 12933Combined sources
Beta strandi1295 – 130410Combined sources
Helixi1306 – 132015Combined sources
Helixi1328 – 134619Combined sources
Helixi1348 – 13514Combined sources
Helixi1354 – 137522Combined sources
Helixi1385 – 13895Combined sources
Helixi1392 – 13943Combined sources
Helixi1409 – 14124Combined sources
Beta strandi1414 – 14174Combined sources
Beta strandi1422 – 14254Combined sources
Helixi1427 – 14293Combined sources
Beta strandi1434 – 14363Combined sources
Helixi1440 – 14434Combined sources
Helixi1447 – 147024Combined sources
Helixi1477 – 14793Combined sources
Turni1480 – 14823Combined sources
Turni1487 – 14904Combined sources
Helixi1491 – 14955Combined sources
Helixi1499 – 15024Combined sources
Helixi1508 – 15147Combined sources
Helixi1515 – 15173Combined sources
Helixi1530 – 15334Combined sources
Helixi1540 – 154910Combined sources
Helixi1552 – 15587Combined sources
Helixi1563 – 15653Combined sources
Helixi1603 – 161412Combined sources
Turni1617 – 16193Combined sources
Beta strandi1633 – 16364Combined sources
Helixi1641 – 16488Combined sources
Turni1649 – 16524Combined sources
Helixi1653 – 167018Combined sources
Turni1671 – 16777Combined sources
Beta strandi1678 – 16836Combined sources
Helixi1690 – 16923Combined sources
Beta strandi1700 – 171112Combined sources
Beta strandi1726 – 173914Combined sources
Beta strandi1743 – 17453Combined sources
Helixi1748 – 175912Combined sources
Beta strandi1763 – 17664Combined sources
Beta strandi1768 – 177811Combined sources
Turni1779 – 17824Combined sources
Beta strandi1783 – 17886Combined sources
Helixi1794 – 180815Combined sources
Helixi1810 – 182213Combined sources
Turni1837 – 18393Combined sources
Helixi1840 – 18445Combined sources
Beta strandi1845 – 18473Combined sources
Beta strandi1849 – 18535Combined sources
Beta strandi1857 – 18648Combined sources
Beta strandi1866 – 18683Combined sources
Beta strandi1870 – 18756Combined sources
Beta strandi1877 – 18826Combined sources
Turni1884 – 18863Combined sources
Beta strandi1888 – 18947Combined sources
Helixi1896 – 18994Combined sources
Helixi1905 – 192319Combined sources
Helixi1926 – 19283Combined sources
Beta strandi1931 – 19377Combined sources
Helixi1938 – 19403Combined sources
Helixi1941 – 19477Combined sources
Turni1948 – 19503Combined sources
Beta strandi1954 – 19574Combined sources
Beta strandi1959 – 19613Combined sources
Helixi1965 – 19706Combined sources
Helixi1972 – 19809Combined sources
Beta strandi1985 – 19906Combined sources
Turni1991 – 19944Combined sources
Helixi1995 – 19973Combined sources
Helixi2001 – 201717Combined sources
Helixi2019 – 20268Combined sources
Beta strandi2030 – 20323Combined sources
Beta strandi2039 – 20413Combined sources
Helixi2045 – 206723Combined sources
Helixi2071 – 20733Combined sources
Helixi2076 – 20849Combined sources
Helixi2149 – 215911Combined sources
Helixi2160 – 21678Combined sources
Beta strandi2168 – 21714Combined sources
Beta strandi2178 – 21803Combined sources
Beta strandi2182 – 21865Combined sources
Helixi2187 – 21959Combined sources
Beta strandi2199 – 22013Combined sources
Beta strandi2204 – 22118Combined sources
Beta strandi2218 – 22258Combined sources
Beta strandi2229 – 22313Combined sources
Beta strandi2236 – 22383Combined sources
Beta strandi2245 – 22473Combined sources
Beta strandi2254 – 226411Combined sources
Helixi2271 – 228111Combined sources
Turni2282 – 22843Combined sources
Beta strandi2289 – 22968Combined sources
Beta strandi2299 – 23079Combined sources
Helixi2309 – 23168Combined sources
Turni2317 – 23204Combined sources
Turni2323 – 23253Combined sources
Helixi2331 – 23333Combined sources
Beta strandi2334 – 234512Combined sources
Beta strandi2348 – 23525Combined sources
Helixi2360 – 23623Combined sources
Helixi2363 – 23653Combined sources
Beta strandi2374 – 23763Combined sources
Helixi2385 – 23873Combined sources
Helixi2391 – 23944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP33334.
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

        10         20         30         40         50
MSGLPPPPPG FEEDSDLALP PPPPPPPGYE IEELDNPMVP SSVNEDTFLP
60 70 80 90 100
PPPPPPSNFE INAEEIVDFT LPPPPPPPGL DELETKAEKK VELHGKRKLD
110 120 130 140 150
IGKDTFVTRK SRKRAKKMTK KAKRSNLYTP KAEMPPEHLR KIINTHSDMA
160 170 180 190 200
SKMYNTDKKA FLGALKYLPH AILKLLENMP HPWEQAKEVK VLYHTSGAIT
210 220 230 240 250
FVNETPRVIE PVYTAQWSAT WIAMRREKRD RTHFKRMRFP PFDDDEPPLS
260 270 280 290 300
YEQHIENIEP LDPINLPLDS QDDEYVKDWL YDSRPLEEDS KKVNGTSYKK
310 320 330 340 350
WSFDLPEMSN LYRLSTPLRD EVTDKNYYYL FDKKSFFNGK ALNNAIPGGP
360 370 380 390 400
KFEPLYPREE EEDYNEFNSI DRVIFRVPIR SEYKVAFPHL YNSRPRSVRI
410 420 430 440 450
PWYNNPVSCI IQNDEEYDTP ALFFDPSLNP IPHFIDNNSS LNVSNTKENG
460 470 480 490 500
DFTLPEDFAP LLAEEEELIL PNTKDAMSLY HSPFPFNRTK GKMVRAQDVA
510 520 530 540 550
LAKKWFLQHP DEEYPVKVKV SYQKLLKNYV LNELHPTLPT NHNKTKLLKS
560 570 580 590 600
LKNTKYFQQT TIDWVEAGLQ LCRQGHNMLN LLIHRKGLTY LHLDYNFNLK
610 620 630 640 650
PTKTLTTKER KKSRLGNSFH LMRELLKMMK LIVDTHVQFR LGNVDAFQLA
660 670 680 690 700
DGIHYILNHI GQLTGIYRYK YKVMHQIRAC KDLKHIIYYK FNKNLGKGPG
710 720 730 740 750
CGFWQPAWRV WLNFLRGTIP LLERYIGNLI TRQFEGRSNE IVKTTTKQRL
760 770 780 790 800
DAYYDLELRN SVMDDILEMM PESIRQKKAR TILQHLSEAW RCWKANIPWD
810 820 830 840 850
VPGMPAPIKK IIERYIKSKA DAWVSAAHYN RERIKRGAHV EKTMVKKNLG
860 870 880 890 900
RLTRLWIKNE QERQRQIQKN GPEITPEEAT TIFSVMVEWL ESRSFSPIPF
910 920 930 940 950
PPLTYKNDTK ILVLALEDLK DVYASKVRLN ASEREELALI EEAYDNPHDT
960 970 980 990 1000
LNRIKKYLLT QRVFKPVDIT MMENYQNISP VYSVDPLEKI TDAYLDQYLW
1010 1020 1030 1040 1050
YEADQRKLFP NWIKPSDSEI PPLLVYKWTQ GINNLSEIWD VSRGQSAVLL
1060 1070 1080 1090 1100
ETTLGEMAEK IDFTLLNRLL RLIVDPNIAD YITAKNNVVI NFKDMSHVNK
1110 1120 1130 1140 1150
YGLIRGLKFA SFIFQYYGLV IDLLLLGQER ATDLAGPANN PNEFMQFKSK
1160 1170 1180 1190 1200
EVEKAHPIRL YTRYLDRIYM LFHFEEDEGE ELTDEYLAEN PDPNFENSIG
1210 1220 1230 1240 1250
YNNRKCWPKD SRMRLIRQDV NLGRAVFWEI QSRVPTSLTS IKWENAFVSV
1260 1270 1280 1290 1300
YSKNNPNLLF SMCGFEVRIL PRQRMEEVVS NDEGVWDLVD ERTKQRTAKA
1310 1320 1330 1340 1350
YLKVSEEEIK KFDSRIRGIL MASGSTTFTK VAAKWNTSLI SLFTYFREAI
1360 1370 1380 1390 1400
VATEPLLDIL VKGETRIQNR VKLGLNSKMP TRFPPAVFYT PKELGGLGMI
1410 1420 1430 1440 1450
SASHILIPAS DLSWSKQTDT GITHFRAGMT HEDEKLIPTI FRYITTWENE
1460 1470 1480 1490 1500
FLDSQRVWAE YATKRQEAIQ QNRRLAFEEL EGSWDRGIPR ISTLFQRDRH
1510 1520 1530 1540 1550
TLAYDRGHRI RREFKQYSLE RNSPFWWTNS HHDGKLWNLN AYRTDVIQAL
1560 1570 1580 1590 1600
GGIETILEHT LFKGTGFNSW EGLFWEKASG FEDSMQFKKL THAQRTGLSQ
1610 1620 1630 1640 1650
IPNRRFTLWW SPTINRANVY VGFLVQLDLT GIFLHGKIPT LKISLIQIFR
1660 1670 1680 1690 1700
AHLWQKIHES IVFDICQILD GELDVLQIES VTKETVHPRK SYKMNSSAAD
1710 1720 1730 1740 1750
ITMESVHEWE VSKPSLLHET NDSFKGLITN KMWFDVQLRY GDYDSHDISR
1760 1770 1780 1790 1800
YVRAKFLDYT TDNVSMYPSP TGVMIGIDLA YNMYDAYGNW FNGLKPLIQN
1810 1820 1830 1840 1850
SMRTIMKANP ALYVLRERIR KGLQIYQSSV QEPFLNSSNY AELFNNDIKL
1860 1870 1880 1890 1900
FVDDTNVYRV TVHKTFEGNV ATKAINGCIF TLNPKTGHLF LKIIHTSVWA
1910 1920 1930 1940 1950
GQKRLSQLAK WKTAEEVSAL VRSLPKEEQP KQIIVTRKAM LDPLEVHMLD
1960 1970 1980 1990 2000
FPNIAIRPTE LRLPFSAAMS IDKLSDVVMK ATEPQMVLFN IYDDWLDRIS
2010 2020 2030 2040 2050
SYTAFSRLTL LLRALKTNEE SAKMILLSDP TITIKSYHLW PSFTDEQWIT
2060 2070 2080 2090 2100
IESQMRDLIL TEYGRKYNVN ISALTQTEIK DIILGQNIKA PSVKRQKMAE
2110 2120 2130 2140 2150
LEAARSEKQN DEEAAGASTV MKTKTINAQG EEIVVVASAD YESQTFSSKN
2160 2170 2180 2190 2200
EWRKSAIANT LLYLRLKNIY VSADDFVEEQ NVYVLPKNLL KKFIEISDVK
2210 2220 2230 2240 2250
IQVAAFIYGM SAKDHPKVKE IKTVVLVPQL GHVGSVQISN IPDIGDLPDT
2260 2270 2280 2290 2300
EGLELLGWIH TQTEELKFMA ASEVATHSKL FADKKRDCID ISIFSTPGSV
2310 2320 2330 2340 2350
SLSAYNLTDE GYQWGEENKD IMNVLSEGFE PTFSTHAQLL LSDRITGNFI
2360 2370 2380 2390 2400
IPSGNVWNYT FMGTAFNQEG DYNFKYGIPL EFYNEMHRPV HFLQFSELAG
2410
DEELEAEQID VFS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 121 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.
InParanoidi P33334.
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

« 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: November 26, 2014
This is version 135 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