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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: 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

  • pre-mRNA intronic binding Source: SGD
  • U1 snRNA binding Source: SGD
  • U2 snRNA binding Source: SGD
  • U5 snRNA binding Source: SGD
  • U6 snRNA binding Source: SGD

GO - Biological processi

  • generation of catalytic spliceosome for second transesterification step Source: SGD
  • mRNA 3'-splice site recognition Source: SGD
  • 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.
BRENDAi3.1.13.2. 984.
ReactomeiR-SCE-72165. 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
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR165C.
SGDiS000001208. PRP8.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: GO_Central
  • nucleus Source: SGD
  • U4/U6 x U5 tri-snRNP complex Source: SGD
  • U5 snRNP Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1658H → S: No effect on viability. 1 Publication1
Mutagenesisi1684E → Q: No effect on viability. 1 Publication1
Mutagenesisi1687H → S: No effect on viability. 1 Publication1
Mutagenesisi1700D → N: No effect on viability. 1 Publication1
Mutagenesisi1735D → N: No effect on viability. 1 Publication1
Mutagenesisi1853D → A: Alters protein folding. Severely impaired growth. Strongly reduced growth at 35 degrees Celsius; when associated with A-1854. 3 Publications1
Mutagenesisi1853D → N: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 3 Publications1
Mutagenesisi1854D → 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 Publications1
Mutagenesisi1854D → N: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 2 Publications1
Mutagenesisi1855T → A: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 1 Publication1
Mutagenesisi1936T → A: Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 1 Publication1
Mutagenesisi1937R → K: Severely impaired growth. Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000970421 – 2413Pre-mRNA-splicing factor 8Add BLAST2413

Proteomic databases

MaxQBiP33334.
PRIDEiP33334.

PTM databases

iPTMnetiP33334.

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. 122 interactors.
DIPiDIP-2427N.
IntActiP33334. 63 interactors.
MINTiMINT-599605.

Structurei

Secondary structure

12413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi885 – 892Combined sources8
Helixi908 – 924Combined sources17
Helixi931 – 945Combined sources15
Helixi947 – 960Combined sources14
Beta strandi967 – 969Combined sources3
Helixi986 – 1005Combined sources20
Beta strandi1013 – 1015Combined sources3
Helixi1021 – 1033Combined sources13
Turni1036 – 1039Combined sources4
Beta strandi1046 – 1053Combined sources8
Turni1056 – 1060Combined sources5
Helixi1063 – 1071Combined sources9
Helixi1076 – 1085Combined sources10
Beta strandi1087 – 1092Combined sources6
Beta strandi1095 – 1098Combined sources4
Helixi1110 – 1135Combined sources26
Beta strandi1138 – 1140Combined sources3
Helixi1150 – 1154Combined sources5
Beta strandi1156 – 1164Combined sources9
Beta strandi1167 – 1174Combined sources8
Helixi1176 – 1189Combined sources14
Turni1197 – 1200Combined sources4
Helixi1209 – 1211Combined sources3
Helixi1217 – 1231Combined sources15
Turni1236 – 1238Combined sources3
Helixi1243 – 1245Combined sources3
Beta strandi1246 – 1252Combined sources7
Beta strandi1258 – 1262Combined sources5
Beta strandi1265 – 1271Combined sources7
Helixi1272 – 1274Combined sources3
Beta strandi1283 – 1289Combined sources7
Turni1291 – 1293Combined sources3
Beta strandi1295 – 1304Combined sources10
Helixi1306 – 1320Combined sources15
Helixi1328 – 1346Combined sources19
Helixi1348 – 1351Combined sources4
Helixi1354 – 1375Combined sources22
Helixi1385 – 1389Combined sources5
Helixi1392 – 1394Combined sources3
Helixi1409 – 1412Combined sources4
Beta strandi1414 – 1417Combined sources4
Beta strandi1422 – 1425Combined sources4
Helixi1427 – 1429Combined sources3
Beta strandi1434 – 1436Combined sources3
Helixi1440 – 1443Combined sources4
Helixi1447 – 1470Combined sources24
Helixi1477 – 1479Combined sources3
Turni1480 – 1482Combined sources3
Turni1487 – 1490Combined sources4
Helixi1491 – 1495Combined sources5
Helixi1499 – 1502Combined sources4
Helixi1508 – 1514Combined sources7
Helixi1515 – 1517Combined sources3
Helixi1530 – 1533Combined sources4
Helixi1540 – 1549Combined sources10
Helixi1552 – 1558Combined sources7
Helixi1563 – 1565Combined sources3
Helixi1603 – 1614Combined sources12
Turni1617 – 1619Combined sources3
Beta strandi1633 – 1636Combined sources4
Helixi1641 – 1648Combined sources8
Turni1649 – 1652Combined sources4
Helixi1653 – 1670Combined sources18
Turni1671 – 1677Combined sources7
Beta strandi1678 – 1683Combined sources6
Helixi1690 – 1692Combined sources3
Beta strandi1700 – 1711Combined sources12
Beta strandi1726 – 1739Combined sources14
Beta strandi1743 – 1745Combined sources3
Helixi1748 – 1759Combined sources12
Beta strandi1763 – 1766Combined sources4
Beta strandi1768 – 1778Combined sources11
Turni1779 – 1782Combined sources4
Beta strandi1783 – 1788Combined sources6
Helixi1794 – 1808Combined sources15
Helixi1810 – 1822Combined sources13
Turni1837 – 1839Combined sources3
Helixi1840 – 1844Combined sources5
Beta strandi1845 – 1847Combined sources3
Beta strandi1849 – 1853Combined sources5
Beta strandi1857 – 1864Combined sources8
Beta strandi1866 – 1868Combined sources3
Beta strandi1870 – 1875Combined sources6
Beta strandi1877 – 1882Combined sources6
Turni1884 – 1886Combined sources3
Beta strandi1888 – 1894Combined sources7
Helixi1896 – 1899Combined sources4
Helixi1905 – 1923Combined sources19
Helixi1926 – 1928Combined sources3
Beta strandi1931 – 1937Combined sources7
Helixi1938 – 1940Combined sources3
Helixi1941 – 1947Combined sources7
Turni1948 – 1950Combined sources3
Beta strandi1954 – 1957Combined sources4
Beta strandi1959 – 1961Combined sources3
Helixi1965 – 1970Combined sources6
Helixi1972 – 1980Combined sources9
Beta strandi1985 – 1990Combined sources6
Turni1991 – 1994Combined sources4
Helixi1995 – 1997Combined sources3
Helixi2001 – 2017Combined sources17
Helixi2019 – 2026Combined sources8
Beta strandi2030 – 2032Combined sources3
Beta strandi2039 – 2041Combined sources3
Helixi2045 – 2067Combined sources23
Helixi2071 – 2073Combined sources3
Helixi2076 – 2084Combined sources9
Helixi2149 – 2159Combined sources11
Helixi2160 – 2167Combined sources8
Beta strandi2168 – 2171Combined sources4
Beta strandi2178 – 2180Combined sources3
Beta strandi2182 – 2186Combined sources5
Helixi2187 – 2195Combined sources9
Beta strandi2199 – 2201Combined sources3
Beta strandi2204 – 2211Combined sources8
Beta strandi2218 – 2225Combined sources8
Beta strandi2229 – 2231Combined sources3
Beta strandi2236 – 2238Combined sources3
Beta strandi2245 – 2247Combined sources3
Beta strandi2254 – 2264Combined sources11
Helixi2271 – 2281Combined sources11
Turni2282 – 2284Combined sources3
Beta strandi2289 – 2296Combined sources8
Beta strandi2299 – 2307Combined sources9
Helixi2309 – 2316Combined sources8
Turni2317 – 2320Combined sources4
Turni2323 – 2325Combined sources3
Helixi2331 – 2333Combined sources3
Beta strandi2334 – 2345Combined sources12
Beta strandi2348 – 2352Combined sources5
Helixi2360 – 2362Combined sources3
Helixi2363 – 2365Combined sources3
Beta strandi2374 – 2376Combined sources3
Helixi2385 – 2387Combined sources3
Helixi2389 – 2396Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OG4X-ray2.00A2147-2397[»]
3E66X-ray2.05A/B1822-2095[»]
3E9OX-ray2.00A1836-2087[»]
3E9PX-ray2.10A/B1833-2087[»]
3JCMelectron microscopy3.80A1-2413[»]
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[»]
5DCAX-ray2.80J2148-2398[»]
5GAMelectron microscopy3.70A1-735[»]
5GANelectron microscopy3.60A1-2413[»]
5GAOelectron microscopy3.60A2147-2413[»]
5GAPelectron microscopy3.60A1-2413[»]
5GM6electron microscopy3.50A128-2413[»]
5GMKelectron microscopy3.40A1-2413[»]
5LJ3electron microscopy3.80A1-2413[»]
5LJ5electron microscopy3.80A1-2413[»]
5LQWelectron microscopy5.80A1-2413[»]
ProteinModelPortaliP33334.
SMRiP33334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33334.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2178 – 2286MPNAdd BLAST109

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni253 – 543SNU114/CWC21 interacting domain (SCwid)Add BLAST291
Regioni885 – 1375Reverse transcriptase homology domainAdd BLAST491
Regioni1376 – 1649LinkerAdd BLAST274
Regioni1585 – 1598Important for branch point selectionAdd BLAST14
Regioni1653 – 1824Restriction endonuclease homology domainAdd BLAST172
Regioni1839 – 2092RNase H homology domainAdd BLAST254

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi5 – 9Poly-Pro5
Compositional biasi20 – 27Poly-Pro8
Compositional biasi50 – 56Poly-Pro7
Compositional biasi72 – 78Poly-Pro7

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

GeneTreeiENSGT00390000015210.
HOGENOMiHOG000184103.
InParanoidiP33334.
KOiK12856.
OMAiAGMSHED.
OrthoDBiEOG092C3X6Q.

Family and domain databases

CDDicd13838. RNase_H_like_Prp8_IV. 1 hit.
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. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti388 – 420PHLYN…EYDTP → LIYIIPGPVQCAYHGIIIQC RVLSRTMRSTTRL in AAA67044 (PubMed:7838707).CuratedAdd BLAST33
Sequence conflicti1132T → S in AAA67044 (PubMed:7838707).Curated1
Sequence conflicti1575W → C in AAA67044 (PubMed:7838707).Curated1

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.
PIRiS34670.
RefSeqiNP_012035.1. NM_001179296.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OG4X-ray2.00A2147-2397[»]
3E66X-ray2.05A/B1822-2095[»]
3E9OX-ray2.00A1836-2087[»]
3E9PX-ray2.10A/B1833-2087[»]
3JCMelectron microscopy3.80A1-2413[»]
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[»]
5DCAX-ray2.80J2148-2398[»]
5GAMelectron microscopy3.70A1-735[»]
5GANelectron microscopy3.60A1-2413[»]
5GAOelectron microscopy3.60A2147-2413[»]
5GAPelectron microscopy3.60A1-2413[»]
5GM6electron microscopy3.50A128-2413[»]
5GMKelectron microscopy3.40A1-2413[»]
5LJ3electron microscopy3.80A1-2413[»]
5LJ5electron microscopy3.80A1-2413[»]
5LQWelectron microscopy5.80A1-2413[»]
ProteinModelPortaliP33334.
SMRiP33334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36599. 122 interactors.
DIPiDIP-2427N.
IntActiP33334. 63 interactors.
MINTiMINT-599605.

PTM databases

iPTMnetiP33334.

Proteomic databases

MaxQBiP33334.
PRIDEiP33334.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YHR165C.
SGDiS000001208. PRP8.

Phylogenomic databases

GeneTreeiENSGT00390000015210.
HOGENOMiHOG000184103.
InParanoidiP33334.
KOiK12856.
OMAiAGMSHED.
OrthoDBiEOG092C3X6Q.

Enzyme and pathway databases

BioCyciYEAST:G3O-31199-MONOMER.
BRENDAi3.1.13.2. 984.
ReactomeiR-SCE-72165. mRNA Splicing - Minor Pathway.

Miscellaneous databases

EvolutionaryTraceiP33334.
PROiP33334.

Family and domain databases

CDDicd13838. RNase_H_like_Prp8_IV. 1 hit.
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. 2 hits.
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.
ProtoNetiSearch...

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 30, 2016
This is version 157 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.