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P33334 (PRP8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-mRNA-splicing factor 8
Gene names
Name:PRP8
Synonyms:DBF3, DNA39, RNA8, SLT21, USA2
Ordered Locus Names:YHR165C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length2413 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 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. Ref.5 Ref.6 Ref.8 Ref.11 Ref.13 Ref.17 Ref.21 Ref.23

Subunit structure

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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.13 Ref.16 Ref.17 Ref.18 Ref.22 Ref.23

Subcellular location

Nucleus Ref.5 Ref.13.

Domain

The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion. Ref.20 Ref.23

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. Ref.20 Ref.23

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. Ref.20 Ref.23

Contains a region with structural similarity to RNase H, but lacks RNase H activity. Ref.20 Ref.23

Miscellaneous

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

Sequence similarities

Contains 1 MPN (JAB/Mov34) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LIN1P388523EBI-465,EBI-570
SNP1Q009163EBI-465,EBI-724

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24132413Pre-mRNA-splicing factor 8
PRO_0000097042

Regions

Domain2178 – 2286109MPN
Region253 – 543291SNU114/CWC21 interacting domain (SCwid)
Region885 – 1375491Reverse transcriptase homology domain
Region1376 – 1649274Linker
Region1585 – 159814Important for branch point selection
Region1653 – 1824172Restriction endonuclease homology domain
Region1839 – 2092254RNase H homology domain
Compositional bias5 – 95Poly-Pro
Compositional bias20 – 278Poly-Pro
Compositional bias50 – 567Poly-Pro
Compositional bias72 – 787Poly-Pro

Amino acid modifications

Modified residue3641Phosphotyrosine Ref.14

Experimental info

Mutagenesis16581H → S: No effect on viability. Ref.23
Mutagenesis16841E → Q: No effect on viability. Ref.23
Mutagenesis16871H → S: No effect on viability. Ref.23
Mutagenesis17001D → N: No effect on viability. Ref.23
Mutagenesis17351D → N: No effect on viability. Ref.23
Mutagenesis18531D → A: Alters protein folding. Severely impaired growth. Strongly reduced growth at 35 degrees Celsius; when associated with A-1854. Ref.15 Ref.20 Ref.21
Mutagenesis18531D → N: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Ref.15 Ref.20 Ref.21
Mutagenesis18541D → 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. Ref.15 Ref.20
Mutagenesis18541D → N: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Ref.15 Ref.20
Mutagenesis18551T → A: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Ref.20
Mutagenesis19361T → A: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Ref.20
Mutagenesis19371R → K: Severely impaired growth. Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Ref.20
Sequence conflict388 – 42033PHLYN…EYDTP → LIYIIPGPVQCAYHGIIIQC RVLSRTMRSTTRL in AAA67044. Ref.2
Sequence conflict11321T → S in AAA67044. Ref.2
Sequence conflict15751W → C in AAA67044. Ref.2

Secondary structure

1 ................................................................................................................................................................................................................................................ 2413
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33334 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 8F4F6F89D34D3508

FASTA2,413279,504
        10         20         30         40         50         60 
MSGLPPPPPG FEEDSDLALP PPPPPPPGYE IEELDNPMVP SSVNEDTFLP PPPPPPSNFE 

        70         80         90        100        110        120 
INAEEIVDFT LPPPPPPPGL DELETKAEKK VELHGKRKLD IGKDTFVTRK SRKRAKKMTK 

       130        140        150        160        170        180 
KAKRSNLYTP KAEMPPEHLR KIINTHSDMA SKMYNTDKKA FLGALKYLPH AILKLLENMP 

       190        200        210        220        230        240 
HPWEQAKEVK VLYHTSGAIT FVNETPRVIE PVYTAQWSAT WIAMRREKRD RTHFKRMRFP 

       250        260        270        280        290        300 
PFDDDEPPLS YEQHIENIEP LDPINLPLDS QDDEYVKDWL YDSRPLEEDS KKVNGTSYKK 

       310        320        330        340        350        360 
WSFDLPEMSN LYRLSTPLRD EVTDKNYYYL FDKKSFFNGK ALNNAIPGGP KFEPLYPREE 

       370        380        390        400        410        420 
EEDYNEFNSI DRVIFRVPIR SEYKVAFPHL YNSRPRSVRI PWYNNPVSCI IQNDEEYDTP 

       430        440        450        460        470        480 
ALFFDPSLNP IPHFIDNNSS LNVSNTKENG DFTLPEDFAP LLAEEEELIL PNTKDAMSLY 

       490        500        510        520        530        540 
HSPFPFNRTK GKMVRAQDVA LAKKWFLQHP DEEYPVKVKV SYQKLLKNYV LNELHPTLPT 

       550        560        570        580        590        600 
NHNKTKLLKS LKNTKYFQQT TIDWVEAGLQ LCRQGHNMLN LLIHRKGLTY LHLDYNFNLK 

       610        620        630        640        650        660 
PTKTLTTKER KKSRLGNSFH LMRELLKMMK LIVDTHVQFR LGNVDAFQLA DGIHYILNHI 

       670        680        690        700        710        720 
GQLTGIYRYK YKVMHQIRAC KDLKHIIYYK FNKNLGKGPG CGFWQPAWRV WLNFLRGTIP 

       730        740        750        760        770        780 
LLERYIGNLI TRQFEGRSNE IVKTTTKQRL DAYYDLELRN SVMDDILEMM PESIRQKKAR 

       790        800        810        820        830        840 
TILQHLSEAW RCWKANIPWD VPGMPAPIKK IIERYIKSKA DAWVSAAHYN RERIKRGAHV 

       850        860        870        880        890        900 
EKTMVKKNLG RLTRLWIKNE QERQRQIQKN GPEITPEEAT TIFSVMVEWL ESRSFSPIPF 

       910        920        930        940        950        960 
PPLTYKNDTK ILVLALEDLK DVYASKVRLN ASEREELALI EEAYDNPHDT LNRIKKYLLT 

       970        980        990       1000       1010       1020 
QRVFKPVDIT MMENYQNISP VYSVDPLEKI TDAYLDQYLW YEADQRKLFP NWIKPSDSEI 

      1030       1040       1050       1060       1070       1080 
PPLLVYKWTQ GINNLSEIWD VSRGQSAVLL ETTLGEMAEK IDFTLLNRLL RLIVDPNIAD 

      1090       1100       1110       1120       1130       1140 
YITAKNNVVI NFKDMSHVNK YGLIRGLKFA SFIFQYYGLV IDLLLLGQER ATDLAGPANN 

      1150       1160       1170       1180       1190       1200 
PNEFMQFKSK EVEKAHPIRL YTRYLDRIYM LFHFEEDEGE ELTDEYLAEN PDPNFENSIG 

      1210       1220       1230       1240       1250       1260 
YNNRKCWPKD SRMRLIRQDV NLGRAVFWEI QSRVPTSLTS IKWENAFVSV YSKNNPNLLF 

      1270       1280       1290       1300       1310       1320 
SMCGFEVRIL PRQRMEEVVS NDEGVWDLVD ERTKQRTAKA YLKVSEEEIK KFDSRIRGIL 

      1330       1340       1350       1360       1370       1380 
MASGSTTFTK VAAKWNTSLI SLFTYFREAI VATEPLLDIL VKGETRIQNR VKLGLNSKMP 

      1390       1400       1410       1420       1430       1440 
TRFPPAVFYT PKELGGLGMI SASHILIPAS DLSWSKQTDT GITHFRAGMT HEDEKLIPTI 

      1450       1460       1470       1480       1490       1500 
FRYITTWENE FLDSQRVWAE YATKRQEAIQ QNRRLAFEEL EGSWDRGIPR ISTLFQRDRH 

      1510       1520       1530       1540       1550       1560 
TLAYDRGHRI RREFKQYSLE RNSPFWWTNS HHDGKLWNLN AYRTDVIQAL GGIETILEHT 

      1570       1580       1590       1600       1610       1620 
LFKGTGFNSW EGLFWEKASG FEDSMQFKKL THAQRTGLSQ IPNRRFTLWW SPTINRANVY 

      1630       1640       1650       1660       1670       1680 
VGFLVQLDLT GIFLHGKIPT LKISLIQIFR AHLWQKIHES IVFDICQILD GELDVLQIES 

      1690       1700       1710       1720       1730       1740 
VTKETVHPRK SYKMNSSAAD ITMESVHEWE VSKPSLLHET NDSFKGLITN KMWFDVQLRY 

      1750       1760       1770       1780       1790       1800 
GDYDSHDISR YVRAKFLDYT TDNVSMYPSP TGVMIGIDLA YNMYDAYGNW FNGLKPLIQN 

      1810       1820       1830       1840       1850       1860 
SMRTIMKANP ALYVLRERIR KGLQIYQSSV QEPFLNSSNY AELFNNDIKL FVDDTNVYRV 

      1870       1880       1890       1900       1910       1920 
TVHKTFEGNV ATKAINGCIF TLNPKTGHLF LKIIHTSVWA GQKRLSQLAK WKTAEEVSAL 

      1930       1940       1950       1960       1970       1980 
VRSLPKEEQP KQIIVTRKAM LDPLEVHMLD FPNIAIRPTE LRLPFSAAMS IDKLSDVVMK 

      1990       2000       2010       2020       2030       2040 
ATEPQMVLFN IYDDWLDRIS SYTAFSRLTL LLRALKTNEE SAKMILLSDP TITIKSYHLW 

      2050       2060       2070       2080       2090       2100 
PSFTDEQWIT IESQMRDLIL TEYGRKYNVN ISALTQTEIK DIILGQNIKA PSVKRQKMAE 

      2110       2120       2130       2140       2150       2160 
LEAARSEKQN DEEAAGASTV MKTKTINAQG EEIVVVASAD YESQTFSSKN EWRKSAIANT 

      2170       2180       2190       2200       2210       2220 
LLYLRLKNIY VSADDFVEEQ NVYVLPKNLL KKFIEISDVK IQVAAFIYGM SAKDHPKVKE 

      2230       2240       2250       2260       2270       2280 
IKTVVLVPQL GHVGSVQISN IPDIGDLPDT EGLELLGWIH TQTEELKFMA ASEVATHSKL 

      2290       2300       2310       2320       2330       2340 
FADKKRDCID ISIFSTPGSV SLSAYNLTDE GYQWGEENKD IMNVLSEGFE PTFSTHAQLL 

      2350       2360       2370       2380       2390       2400 
LSDRITGNFI IPSGNVWNYT FMGTAFNQEG DYNFKYGIPL EFYNEMHRPV HFLQFSELAG 

      2410 
DEELEAEQID VFS

« Hide

References

« Hide 'large scale' references
[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]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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, 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: MASS SPECTROMETRY, IDENTIFICATION IN THE CWC COMPLEX.
[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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364, MASS SPECTROMETRY.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"Mechanism for Aar2p function as a U5 snRNP assembly factor."
Weber G., Cristao V.F., de Lima Alves F., Santos K.F., Holton N., Rappsilber J., Beggs J.D., Wahl M.C.
Genes Dev. 25:1601-1612(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1836-2092 IN COMPLEX WITH AAR2, INTERACTION WITH AAR2.
[23]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z24732 Genomic DNA. Translation: CAA80854.1.
L29421 Genomic DNA. Translation: AAA67044.1.
U00027 Genomic DNA. Translation: AAB68011.1.
BK006934 Genomic DNA. Translation: DAA06858.1.
PIRS34670.
RefSeqNP_012035.1. NM_001179296.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
4I43X-ray2.00B885-2413[»]
4ILGX-ray2.10B1836-2090[»]
C2147-2413[»]
4ILJX-ray2.00A/B1836-2090[»]
ProteinModelPortalP33334.
SMRP33334. Positions 1835-2396.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2427N.
IntActP33334. 61 interactions.
MINTMINT-599605.
STRING4932.YHR165C.

Proteomic databases

PaxDbP33334.
PRIDEP33334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR165C; YHR165C; YHR165C.
GeneID856570.
KEGGsce:YHR165C.

Organism-specific databases

CYGDYHR165c.
SGDS000001208. PRP8.

Phylogenomic databases

eggNOGCOG5178.
GeneTreeENSGT00390000015210.
HOGENOMHOG000184103.
KOK12856.
OMAEEFTHRD.
OrthoDBEOG4Q2HPK.

Gene expression databases

GenevestigatorP33334.
GermOnlineYHR165C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000555. JAB1_Mov34_MPN_PAD1.
IPR012591. Pre-mRNA-splicing_factor-8.
IPR012984. PRO_C.
IPR012592. PROCN.
IPR021983. PRP8_domainIV.
IPR019581. Prp8_U5-snRNA-bd.
IPR019580. Prp8_U6-snRNA-bd.
IPR019582. RRM_spliceosomal_PrP8.
[Graphical view]
PfamPF08082. 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]
ProDomPD149576. Pre-mRNA-splicing_factor-8. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
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EvolutionaryTraceP33334.
NextBio982414.

Entry information

Entry namePRP8_YEAST
AccessionPrimary (citable) accession number: P33334
Secondary accession number(s): D3DLB4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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