Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pre-mRNA-processing-splicing factor 8

Gene

Prpf8

Organism
Mus musculus (Mouse)
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 the 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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-processing-splicing factor 8
Alternative name(s):
Splicing factor Prp8
Gene namesi
Name:Prpf8
Synonyms:Prp8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2179381. Prpf8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000970412 – 2335Pre-mRNA-processing-splicing factor 8Add BLAST2334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei859PhosphoserineBy similarity1
Modified residuei1358PhosphoserineBy similarity1
Modified residuei1425N6,N6-dimethyllysineBy similarity1
Modified residuei1463N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ99PV0.
MaxQBiQ99PV0.
PaxDbiQ99PV0.
PeptideAtlasiQ99PV0.
PRIDEiQ99PV0.

PTM databases

iPTMnetiQ99PV0.
PhosphoSitePlusiQ99PV0.

Expressioni

Tissue specificityi

Strongly expressed in testis (preferentially in the outer cell layer), and moderately in ovary (preferentially in granulosa cells).1 Publication

Developmental stagei

During embryogenesis, is highly expressed at day 9.5 of gestation, and its expression decreases progressively during embryogenesis.1 Publication

Gene expression databases

BgeeiENSMUSG00000020850.
CleanExiMM_PRPF8.
ExpressionAtlasiQ99PV0. baseline and differential.
GenevisibleiQ99PV0. MM.

Interactioni

Subunit structurei

Part of the U5 snRNP complex. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Component of the U5.U4atac/U6atac snRNP complexes in U12-dependent spliceosomes. Found in a mRNA splicing-dependent exon junction complex (EJC) with SRRM1. Interacts with U5 snRNP proteins SNRP116 and SNRNP40. Interacts with EFTUD2 and SNRNP200. Interacts (via the MPN (JAB/Mov34) domain) with PRPF3 ('Lys-63'-linked polyubiquitinated); may stabilize the U4/U6-U5 tri-snRNP complex.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi228650. 55 interactors.
IntActiQ99PV0. 59 interactors.
MINTiMINT-1868113.
STRINGi10090.ENSMUSP00000018449.

Structurei

3D structure databases

ProteinModelPortaliQ99PV0.
SMRiQ99PV0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2099 – 2233MPNAdd BLAST135

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni812 – 1303Reverse transcriptase homology domainAdd BLAST492
Regioni1304 – 1577LinkerAdd BLAST274
Regioni1513 – 1526Important for branch point selectionBy similarityAdd BLAST14
Regioni1581 – 1752Restriction endonuclease homology domainAdd BLAST172
Regioni1669 – 2034Involved in interaction with pre-mRNA 5' splice siteBy similarityAdd BLAST366
Regioni1767 – 2020RNase H homology domainAdd BLAST254
Regioni2301 – 2335Required for interaction with EFTUD2 and SNRNP200By similarityAdd BLAST35

Domaini

The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion.By similarity
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.By similarity
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 the protein structure.By similarity
Contains a region with structural similarity to RNase H, but lacks RNase H activity.By similarity

Sequence similaritiesi

Contains 1 MPN (JAB/Mov34) domain.Curated

Phylogenomic databases

eggNOGiKOG1795. Eukaryota.
COG5178. LUCA.
GeneTreeiENSGT00390000015210.
HOVERGENiHBG052796.
InParanoidiQ99PV0.
KOiK12856.
OMAiRNQNEEF.
OrthoDBiEOG091G003B.
PhylomeDBiQ99PV0.
TreeFamiTF105613.

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. 1 hit.
PfamiPF01398. JAB. 1 hit.
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]
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99PV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK
60 70 80 90 100
FGFVDAQKED MPPEHVRKII RDHGDMTNRK FRHDKRVYLG ALKYMPHAVL
110 120 130 140 150
KLLENMPMPW EQIRDVPVLY HITGAISFVN EIPWVIEPVY ISQWGSMWIM
160 170 180 190 200
MRREKRDRRH FKRMRFPPFD DEEPPLDYAD NILDVEPLEA IQLELDPEED
210 220 230 240 250
APVLDWFYDH QPLRDSRKYV NGSTYQRWQF TLPMMSTLYR LANQLLTDLV
260 270 280 290 300
DDNYFYLFDL KAFFTSKALN MAIPGGPKFE PLVRDINLQD EDWNEFNDIN
310 320 330 340 350
KIIIRQPIRT EYKIAFPYLY NNLPHHVHLT WYHTPNVVFI KTEDPDLPAF
360 370 380 390 400
YFDPLINPIS HRHSVKSQEP LPDDDEEFEL PEFVEPFLKD TPLYTDNTAN
410 420 430 440 450
GIALLWAPRP FNLRSGRTRR ALDIPLVKNW YREHCPAGQP VKVRVSYQKL
460 470 480 490 500
LKYYVLNALK HRPPKAQKKR YLFRSFKATK FFQSTKLDWV EVGLQVCRQG
510 520 530 540 550
YNMLNLLIHR KNLNYLHLDY NFNLKPVKTL TTKERKKSRF GNAFHLCREV
560 570 580 590 600
LRLTKLVVDS HVQYRLGNVD AFQLADGLQY IFAHVGQLTG MYRYKYKLMR
610 620 630 640 650
QIRMCKDLKH LIYYRFNTGP VGKGPGCGFW AAGWRVWLFF MRGITPLLER
660 670 680 690 700
WLGNLLARQF EGRHSKGVAK TVTKQRVESH FDLELRAAVM HDILDMMPEG
710 720 730 740 750
IKQNKARTIL QHLSEAWRCW KANIPWKVPG LPTPIENMIL RYVKAKADWW
760 770 780 790 800
TNTAHYNRER IRRGATVDKT VCKKNLGRLT RLYLKAEQER QHNYLKDGPY
810 820 830 840 850
ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI LALERLKEAY
860 870 880 890 900
SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQRA FKEVGIEFMD
910 920 930 940 950
LYSHLVPVYD VEPLEKITDA YLDQYLWYEA DKRRLFPPWI KPADTEPPPL
960 970 980 990 1000
LVYKWCQGIN NLQDVWETSE GECNVMLESR FEKMYEKIDL TLLNRLLRLI
1010 1020 1030 1040 1050
VDHNIADYMT AKNNVVINYK DMNHTNSYGI IRGLQFASFI VQYYGLVMDL
1060 1070 1080 1090 1100
LVLGLHRASE MAGPPQMPND FLSFQDIATE AAHPIRLFCR YIDRIHIFFR
1110 1120 1130 1140 1150
FTADEARDLI QRYLTEHPDP NNENIVGYNN KKCWPRDARM RLMKHDVNLG
1160 1170 1180 1190 1200
RAVFWDIKNR LPRSVTTVQW ENSFVSVYSK DNPNLLFNMC GFECRILPKC
1210 1220 1230 1240 1250
RTSYEEFTHK DGVWNLQNEV TKERTAQCFL RVDDESMQRF HNRVRQILMA
1260 1270 1280 1290 1300
SGSTTFTKIV NKWNTALIGL MTYFREAVVN TQELLDLLVK CENKIQTRIK
1310 1320 1330 1340 1350
IGLNSKMPSR FPPVVFYTPK ELGGLGMLSM GHVLIPQSDL RWSKQTDVGI
1360 1370 1380 1390 1400
THFRSGMSHE EDQLIPNLYR YIQPWESEFI DSQRVWAEYA LKRQEAIAQN
1410 1420 1430 1440 1450
RRLTLEDLED SWDRGIPRIN TLFQKDRHTL AYDKGWRVRT DFKQYQVLKQ
1460 1470 1480 1490 1500
NPFWWTHQRH DGKLWNLNNY RTDMIQALGG VEGILEHTLF KGTYFPTWEG
1510 1520 1530 1540 1550
LFWEKASGFE ESMKWKKLTN AQRSGLNQIP NRRFTLWWSP TINRANVYVG
1560 1570 1580 1590 1600
FQVQLDLTGI FMHGKIPTLK ISLIQIFRAH LWQKIHESIV MDLCQVFDQE
1610 1620 1630 1640 1650
LDALEIETVQ KETIHPRKSY KMNSSCADIL LFASYKWNVS RPSLLADSKD
1660 1670 1680 1690 1700
VMDSTTTQKY WIDIQLRWGD YDSHDIERYA RAKFLDYTTD NMSIYPSPTG
1710 1720 1730 1740 1750
VLIAIDLAYN LHSAYGNWFP GSKPLIQQAM AKIMKANPAL YVLRERIRKG
1760 1770 1780 1790 1800
LQLYSSEPTE PYLSSQNYGE LFSNQIIWFV DDTNVYRVTI HKTFEGNLTT
1810 1820 1830 1840 1850
KPINGAIFIF NPRTGQLFLK IIHTSVWAGQ KRLGQLAKWK TAEEVAALIR
1860 1870 1880 1890 1900
SLPVEEQPKQ IIVTRKGMLD PLEVHLLDFP NIVIKGSELQ LPFQACLKVE
1910 1920 1930 1940 1950
KFGDLILKAT EPQMVLFNLY DDWLKTISSY TAFSRLILIL RALHVNNDRA
1960 1970 1980 1990 2000
KVILKPDKTT VTEPHHIWPT LTDEEWIKVE VQLKDLILAD YGKKNNVNVA
2010 2020 2030 2040 2050
SLTQSEIRDI ILGMEISAPS QQRQQIAEIE KQTKEQSQLT ATQTRTVNKH
2060 2070 2080 2090 2100
GDEIITSTTS NYETQTFSSK TEWRVRAISA ANLHLRTNHI YVSSDDIKET
2110 2120 2130 2140 2150
GYTYILPKNV LKKFICISDL RAQIAGYLYG VSPPDNPQVK EIRCIVMVPQ
2160 2170 2180 2190 2200
WGTHQTVHLP SQLPQHEYLK EMEPLGWIHT QPNESPQLSP QDVTTHAKIM
2210 2220 2230 2240 2250
ADNPSWDGEK TIIITCSFTP GSCTLTAYKL TPSGYEWGRQ NTDKGNNPKG
2260 2270 2280 2290 2300
YLPSHYERVQ MLLSDRFLGF FMVPAQSSWN YNFMGVRHDP NMKYELQLAN
2310 2320 2330
PKEFYHEVHR PSHFLNFALL QEGEVYSADR EDLYA
Length:2,335
Mass (Da):273,616
Last modified:November 24, 2009 - v2
Checksum:iC1A7A989B1AFB3B7
GO

Sequence cautioni

The sequence AAH54103 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti797D → V in BAB32671 (PubMed:11275560).Curated1
Sequence conflicti2191 – 2195QDVTT → THASA in AAH54103 (PubMed:15489334).Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047391 mRNA. Translation: BAB32671.1.
AL591496 Genomic DNA. Translation: CAI35387.1.
BC034648 mRNA. Translation: AAH34648.1.
BC054103 mRNA. Translation: AAH54103.1. Different initiation.
BC093481 mRNA. Translation: AAH93481.1.
AK041017 mRNA. Translation: BAC30783.1.
CCDSiCCDS25048.1.
RefSeqiNP_619600.2. NM_138659.2.
UniGeneiMm.3757.

Genome annotation databases

EnsembliENSMUST00000018449; ENSMUSP00000018449; ENSMUSG00000020850.
ENSMUST00000102510; ENSMUSP00000099568; ENSMUSG00000020850.
GeneIDi192159.
KEGGimmu:192159.
UCSCiuc007kdx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047391 mRNA. Translation: BAB32671.1.
AL591496 Genomic DNA. Translation: CAI35387.1.
BC034648 mRNA. Translation: AAH34648.1.
BC054103 mRNA. Translation: AAH54103.1. Different initiation.
BC093481 mRNA. Translation: AAH93481.1.
AK041017 mRNA. Translation: BAC30783.1.
CCDSiCCDS25048.1.
RefSeqiNP_619600.2. NM_138659.2.
UniGeneiMm.3757.

3D structure databases

ProteinModelPortaliQ99PV0.
SMRiQ99PV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228650. 55 interactors.
IntActiQ99PV0. 59 interactors.
MINTiMINT-1868113.
STRINGi10090.ENSMUSP00000018449.

PTM databases

iPTMnetiQ99PV0.
PhosphoSitePlusiQ99PV0.

Proteomic databases

EPDiQ99PV0.
MaxQBiQ99PV0.
PaxDbiQ99PV0.
PeptideAtlasiQ99PV0.
PRIDEiQ99PV0.

Protocols and materials databases

DNASUi192159.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018449; ENSMUSP00000018449; ENSMUSG00000020850.
ENSMUST00000102510; ENSMUSP00000099568; ENSMUSG00000020850.
GeneIDi192159.
KEGGimmu:192159.
UCSCiuc007kdx.1. mouse.

Organism-specific databases

CTDi10594.
MGIiMGI:2179381. Prpf8.

Phylogenomic databases

eggNOGiKOG1795. Eukaryota.
COG5178. LUCA.
GeneTreeiENSGT00390000015210.
HOVERGENiHBG052796.
InParanoidiQ99PV0.
KOiK12856.
OMAiRNQNEEF.
OrthoDBiEOG091G003B.
PhylomeDBiQ99PV0.
TreeFamiTF105613.

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.

Miscellaneous databases

ChiTaRSiPrpf8. mouse.
PROiQ99PV0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020850.
CleanExiMM_PRPF8.
ExpressionAtlasiQ99PV0. baseline and differential.
GenevisibleiQ99PV0. MM.

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. 1 hit.
PfamiPF01398. JAB. 1 hit.
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]
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_MOUSE
AccessioniPrimary (citable) accession number: Q99PV0
Secondary accession number(s): A5D6Q4
, Q5ND30, Q5ND31, Q7TQK2, Q8BRZ5, Q8K001
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: November 24, 2009
Last modified: November 30, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.