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Q6P2Q9 (PRP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

Names and origin

Protein namesRecommended name:
Pre-mRNA-processing-splicing factor 8
Alternative name(s):
220 kDa U5 snRNP-specific protein
PRP8 homolog
Splicing factor Prp8
p220
Gene names
Name:PRPF8
Synonyms:PRPC8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 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.

Subunit structure

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, NHP2L1, 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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.34

Subcellular location

Nucleus speckle By similarity.

Tissue specificity

Widely expressed. Ref.1

Domain

The MPN (JAB/Mov34) domain has structural similarity with deubiquitinating enzymes, but lacks the residues that would bind the catalytic metal ion By similarity. Ref.28

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. Ref.28

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. Ref.28

Contains a region with structural similarity to RNase H, but lacks RNase H activity By similarity. Ref.28

Involvement in disease

Retinitis pigmentosa 13 (RP13) [MIM:600059]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.30 Ref.31 Ref.32 Ref.33 Ref.34

Sequence similarities

Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Retinitis pigmentosa
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement Ref.12. Source: UniProtKB

RNA splicing, via transesterification reactions

Traceable author statement Ref.12. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

mRNA processing

Traceable author statement Ref.12. Source: ProtInc

mRNA splicing, via spliceosome

Inferred by curator PubMed 11991638. Source: UniProtKB

   Cellular_componentU5 snRNP

Traceable author statement Ref.12. Source: ProtInc

catalytic step 2 spliceosome

Inferred from direct assay PubMed 11991638. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 22720776. Source: UniProt

   Molecular_functionU5 snRNA binding

Inferred from electronic annotation. Source: InterPro

U6 snRNA binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18951082. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 23352334Pre-mRNA-processing-splicing factor 8
PRO_0000097040

Regions

Domain2099 – 2233135MPN
Region812 – 1303492Reverse transcriptase homology domain
Region1304 – 1577274Linker
Region1513 – 152614Important for branch point selection By similarity
Region1581 – 1752172Restriction endonuclease homology domain
Region1669 – 2034366Involved in interaction with pre-mRNA 5' splice site
Region1767 – 2020254RNase H homology domain
Region2301 – 233535Required for interaction with EFTUD2 and SNRNP200

Amino acid modifications

Modified residue21N-acetylalanine Ref.4 Ref.23 Ref.27
Modified residue8591Phosphoserine Ref.25
Modified residue14631N6-acetyllysine Ref.24

Natural variations

Natural variant681K → E.
Corresponds to variant rs1043391 [ dbSNP | Ensembl ].
VAR_022622
Natural variant2271R → H. Ref.3
Corresponds to variant rs11559304 [ dbSNP | Ensembl ].
VAR_022623
Natural variant8741P → L. Ref.2
Corresponds to variant rs1043396 [ dbSNP | Ensembl ].
VAR_022624
Natural variant12931N → H. Ref.2
Corresponds to variant rs1043399 [ dbSNP | Ensembl ].
VAR_022625
Natural variant23011P → T in RP13; no effect on interaction with SNRNP200 and EFTUD2. Ref.30
VAR_022626
Natural variant23041F → L in RP13. Ref.30 Ref.34
VAR_022627
Natural variant23091H → P in RP13; no effect on interaction with SNRNP200 and EFTUD2. Ref.30 Ref.34
VAR_022628
Natural variant23091H → R in RP13; no effect on interaction with SNRNP200 and EFTUD2. Ref.30 Ref.34
VAR_022629
Natural variant23101R → G in RP13; reduces interaction with SNRNP200 and EFTUD2. Ref.30 Ref.31 Ref.33 Ref.34
VAR_022630
Natural variant23101R → K in RP13; reduces interaction with SNRNP200 and EFTUD2. Ref.30 Ref.32 Ref.34
VAR_022631
Natural variant23141F → L in RP13; reduces interaction with EFTUD2, but not with SNRNP200. Ref.30 Ref.34
VAR_022632
Natural variant23341Y → N in RP13. Ref.31
VAR_022633

Experimental info

Mutagenesis17881V → D: Strongly reduced interaction with RNA. Ref.29
Mutagenesis17891T → P: Strongly reduced interaction with RNA. Ref.29
Sequence conflict1841D → N in BAA22563. Ref.2
Sequence conflict492 – 4932VG → GW in BAA22563. Ref.2
Sequence conflict6041M → V in BAA22563. Ref.2
Sequence conflict8061A → T in BAA22563. Ref.2
Sequence conflict9971L → V in BAA22563. Ref.2
Sequence conflict13901A → S in BAA22563. Ref.2
Sequence conflict18671G → D in BAA22563. Ref.2

Secondary structure

.................................................... 2335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6P2Q9 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: E823A15C60EA61C9

FASTA2,335273,600
        10         20         30         40         50         60 
MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED 

        70         80         90        100        110        120 
MPPEHVRKII RDHGDMTNRK FRHDKRVYLG ALKYMPHAVL KLLENMPMPW EQIRDVPVLY 

       130        140        150        160        170        180 
HITGAISFVN EIPWVIEPVY ISQWGSMWIM MRREKRDRRH FKRMRFPPFD DEEPPLDYAD 

       190        200        210        220        230        240 
NILDVEPLEA IQLELDPEED APVLDWFYDH QPLRDSRKYV NGSTYQRWQF TLPMMSTLYR 

       250        260        270        280        290        300 
LANQLLTDLV DDNYFYLFDL KAFFTSKALN MAIPGGPKFE PLVRDINLQD EDWNEFNDIN 

       310        320        330        340        350        360 
KIIIRQPIRT EYKIAFPYLY NNLPHHVHLT WYHTPNVVFI KTEDPDLPAF YFDPLINPIS 

       370        380        390        400        410        420 
HRHSVKSQEP LPDDDEEFEL PEFVEPFLKD TPLYTDNTAN GIALLWAPRP FNLRSGRTRR 

       430        440        450        460        470        480 
ALDIPLVKNW YREHCPAGQP VKVRVSYQKL LKYYVLNALK HRPPKAQKKR YLFRSFKATK 

       490        500        510        520        530        540 
FFQSTKLDWV EVGLQVCRQG YNMLNLLIHR KNLNYLHLDY NFNLKPVKTL TTKERKKSRF 

       550        560        570        580        590        600 
GNAFHLCREV LRLTKLVVDS HVQYRLGNVD AFQLADGLQY IFAHVGQLTG MYRYKYKLMR 

       610        620        630        640        650        660 
QIRMCKDLKH LIYYRFNTGP VGKGPGCGFW AAGWRVWLFF MRGITPLLER WLGNLLARQF 

       670        680        690        700        710        720 
EGRHSKGVAK TVTKQRVESH FDLELRAAVM HDILDMMPEG IKQNKARTIL QHLSEAWRCW 

       730        740        750        760        770        780 
KANIPWKVPG LPTPIENMIL RYVKAKADWW TNTAHYNRER IRRGATVDKT VCKKNLGRLT 

       790        800        810        820        830        840 
RLYLKAEQER QHNYLKDGPY ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI 

       850        860        870        880        890        900 
LALERLKEAY SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQRA FKEVGIEFMD 

       910        920        930        940        950        960 
LYSHLVPVYD VEPLEKITDA YLDQYLWYEA DKRRLFPPWI KPADTEPPPL LVYKWCQGIN 

       970        980        990       1000       1010       1020 
NLQDVWETSE GECNVMLESR FEKMYEKIDL TLLNRLLRLI VDHNIADYMT AKNNVVINYK 

      1030       1040       1050       1060       1070       1080 
DMNHTNSYGI IRGLQFASFI VQYYGLVMDL LVLGLHRASE MAGPPQMPND FLSFQDIATE 

      1090       1100       1110       1120       1130       1140 
AAHPIRLFCR YIDRIHIFFR FTADEARDLI QRYLTEHPDP NNENIVGYNN KKCWPRDARM 

      1150       1160       1170       1180       1190       1200 
RLMKHDVNLG RAVFWDIKNR LPRSVTTVQW ENSFVSVYSK DNPNLLFNMC GFECRILPKC 

      1210       1220       1230       1240       1250       1260 
RTSYEEFTHK DGVWNLQNEV TKERTAQCFL RVDDESMQRF HNRVRQILMA SGSTTFTKIV 

      1270       1280       1290       1300       1310       1320 
NKWNTALIGL MTYFREAVVN TQELLDLLVK CENKIQTRIK IGLNSKMPSR FPPVVFYTPK 

      1330       1340       1350       1360       1370       1380 
ELGGLGMLSM GHVLIPQSDL RWSKQTDVGI THFRSGMSHE EDQLIPNLYR YIQPWESEFI 

      1390       1400       1410       1420       1430       1440 
DSQRVWAEYA LKRQEAIAQN RRLTLEDLED SWDRGIPRIN TLFQKDRHTL AYDKGWRVRT 

      1450       1460       1470       1480       1490       1500 
DFKQYQVLKQ NPFWWTHQRH DGKLWNLNNY RTDMIQALGG VEGILEHTLF KGTYFPTWEG 

      1510       1520       1530       1540       1550       1560 
LFWEKASGFE ESMKWKKLTN AQRSGLNQIP NRRFTLWWSP TINRANVYVG FQVQLDLTGI 

      1570       1580       1590       1600       1610       1620 
FMHGKIPTLK ISLIQIFRAH LWQKIHESIV MDLCQVFDQE LDALEIETVQ KETIHPRKSY 

      1630       1640       1650       1660       1670       1680 
KMNSSCADIL LFASYKWNVS RPSLLADSKD VMDSTTTQKY WIDIQLRWGD YDSHDIERYA 

      1690       1700       1710       1720       1730       1740 
RAKFLDYTTD NMSIYPSPTG VLIAIDLAYN LHSAYGNWFP GSKPLIQQAM AKIMKANPAL 

      1750       1760       1770       1780       1790       1800 
YVLRERIRKG LQLYSSEPTE PYLSSQNYGE LFSNQIIWFV DDTNVYRVTI HKTFEGNLTT 

      1810       1820       1830       1840       1850       1860 
KPINGAIFIF NPRTGQLFLK IIHTSVWAGQ KRLGQLAKWK TAEEVAALIR SLPVEEQPKQ 

      1870       1880       1890       1900       1910       1920 
IIVTRKGMLD PLEVHLLDFP NIVIKGSELQ LPFQACLKVE KFGDLILKAT EPQMVLFNLY 

      1930       1940       1950       1960       1970       1980 
DDWLKTISSY TAFSRLILIL RALHVNNDRA KVILKPDKTT ITEPHHIWPT LTDEEWIKVE 

      1990       2000       2010       2020       2030       2040 
VQLKDLILAD YGKKNNVNVA SLTQSEIRDI ILGMEISAPS QQRQQIAEIE KQTKEQSQLT 

      2050       2060       2070       2080       2090       2100 
ATQTRTVNKH GDEIITSTTS NYETQTFSSK TEWRVRAISA ANLHLRTNHI YVSSDDIKET 

      2110       2120       2130       2140       2150       2160 
GYTYILPKNV LKKFICISDL RAQIAGYLYG VSPPDNPQVK EIRCIVMVPQ WGTHQTVHLP 

      2170       2180       2190       2200       2210       2220 
GQLPQHEYLK EMEPLGWIHT QPNESPQLSP QDVTTHAKIM ADNPSWDGEK TIIITCSFTP 

      2230       2240       2250       2260       2270       2280 
GSCTLTAYKL TPSGYEWGRQ NTDKGNNPKG YLPSHYERVQ MLLSDRFLGF FMVPAQSSWN 

      2290       2300       2310       2320       2330 
YNFMGVRHDP NMKYELQLAN PKEFYHEVHR PSHFLNFALL QEGEVYSADR EDLYA 

« Hide

References

« Hide 'large scale' references
[1]"The human Prp8 protein is a component of both U2- and U12-dependent spliceosomes."
Luo H.R., Moreau G.A., Levin N., Moore M.J.
RNA 5:893-908(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION IN U2- AND U12-DEPENDENT SPLICEOSOME COMPLEXES.
[2]"Human homologue of Saccharomyces cerevisiae PRP8, pre-mRNA splicing factor."
Shimada Y., Fujiwara T., Kawai A., Shimizu F., Okuno S., Ozaki K., Takeda S., Watanabe T., Nagata M., Takahashi E.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS 68-GLU; LEU-874 AND HIS-1293.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-227.
Tissue: Testis.
[4]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-8; 51-58; 218-227; 268-278; 421-428; 453-460; 556-565; 610-623; 643-650; 677-702; 747-758; 822-833; 838-845; 988-995; 999-1032; 1113-1131; 1142-1158; 1225-1231; 1246-1258; 1311-1320; 1345-1354; 1371-1392; 1450-1459; 1464-1491; 1524-1532; 1571-1578; 1642-1649; 1668-1678; 1724-1732; 1736-1744; 1814-1831; 1841-1859; 1902-1908; 1926-1935; 1995-2031; 2035-2045; 2050-2070; 2087-2108; 2114-2121; 2199-2210; 2230-2239; 2250-2266 AND 2288-2302, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[5]"Conservation between yeast and man of a protein associated with U5 small nuclear ribonucleoprotein."
Anderson G.J., Bach M., Luehrmann R., Beggs J.D.
Nature 342:819-821(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN U5 SNRNP COMPLEX.
[6]"20S small nuclear ribonucleoprotein U5 shows a surprisingly complex protein composition."
Bach M., Winkelmann G., Luehrmann R.
Proc. Natl. Acad. Sci. U.S.A. 86:6038-6042(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN U5 SNRNP COMPLEX.
[7]"The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome."
Pinto A.L., Steitz J.A.
Proc. Natl. Acad. Sci. U.S.A. 86:8742-8746(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN U5 SNRNP; U5/4/6 SNRNP AND SPLICEOSOME COMPLEXES.
[8]"A mammalian protein of 220 kDa binds pre-mRNAs in the spliceosome: a potential homologue of the yeast PRP8 protein."
Garcia-Blanco M.A., Anderson G.J., Beggs J., Sharp P.A.
Proc. Natl. Acad. Sci. U.S.A. 87:3082-3086(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SPLICEOSOME COMPLEX, INTERACTION WITH PRE-MRNA.
[9]"Domain analysis of human U5 RNA. Cap trimethylation, protein binding, and spliceosome assembly."
Hinz M., Moore M.J., Bindereif A.
J. Biol. Chem. 271:19001-19007(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN U5 SNRNP COMPLEX, INTERACTION WITH U5 SNRNA.
[10]"The canonical GU dinucleotide at the 5' splice site is recognized by p220 of the U5 snRNP within the spliceosome."
Reyes J.L., Kois P., Konforti B.B., Konarska M.M.
RNA 2:213-225(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRE-MRNA.
[11]"Evidence that U5 snRNP recognizes the 3' splice site for catalytic step II in mammals."
Chiara M.D., Palandjian L., Feld Kramer R., Reed R.
EMBO J. 16:4746-4759(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SPLICEOSOME COMPLEX, INTERACTION WITH PRE-MRNA.
[12]"The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein."
Achsel T., Ahrens K., Brahms H., Teigelkamp S., Luehrmann R.
Mol. Cell. Biol. 18:6756-6766(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN U5 SNRP COMPLEX, INTERACTION WITH SNRP116 AND SNRNP40.
[13]"The C-terminal region of hPrp8 interacts with the conserved GU dinucleotide at the 5' splice site."
Reyes J.L., Gustafson E.H., Luo H.R., Moore M.J., Konarska M.M.
RNA 5:167-179(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRE-MRNA.
[14]"Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions."
Le Hir H., Moore M.J., Maquat L.E.
Genes Dev. 14:1098-1108(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH SRRM1.
[15]"A general approach for identification of RNA-protein cross-linking sites within native human spliceosomal small nuclear ribonucleoproteins (snRNPs). Analysis of RNA-protein contacts in native U1 and U4/U6.U5 snRNPs."
Urlaub H., Hartmuth K., Kostka S., Grelle G., Luehrmann R.
J. Biol. Chem. 275:41458-41468(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH U5 SNRNA.
[16]"Functional recognition of 5' splice site by U4/U6.U5 tri-snRNP defines a novel ATP-dependent step in early spliceosome assembly."
Maroney P.A., Romfo C.M., Nilsen T.W.
Mol. Cell 6:317-328(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRE-MRNA, IDENTIFICATION IN U5/4/6 SNRNP COMPLEX.
[17]"Human U4/U6.U5 and U4atac/U6atac.U5 tri-snRNPs exhibit similar protein compositions."
Schneider C., Will C.L., Makarova O.V., Makarov E.M., Luehrmann R.
Mol. Cell. Biol. 22:3219-3229(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN U12-DEPENDENT SPLICEOSOME.
[18]"Prp8 protein: at the heart of the spliceosome."
Grainger R.J., Beggs J.D.
RNA 11:533-557(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[19]"The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[20]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[21]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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 (1.95 ANGSTROMS) OF 1760-2016, DOMAIN, LACK OF METAL-BINDING.
[29]"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: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1769-1990, IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING, MUTAGENESIS OF VAL-1788 AND THR-1789, LACK OF METAL-BINDING SITE.
[30]"Mutations in the pre-mRNA splicing factor gene PRPC8 in autosomal dominant retinitis pigmentosa (RP13)."
McKie A.B., McHale J.C., Keen T.J., Tarttelin E.E., Goliath R., van Lith-Verhoeven J.J., Greenberg J., Ramesar R.S., Hoyng C.B., Cremers F.P., Mackey D.A., Bhattacharya S.S., Bird A.C., Markham A.F., Inglehearn C.F.
Hum. Mol. Genet. 10:1555-1562(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP13 THR-2301; LEU-2304; ARG-2309; PRO-2309; GLY-2310; LYS-2310 AND LEU-2314.
[31]"Novel mutations in the PRPC8 gene, encoding a pre-mRNA splicing factor in patients with autosomal dominant retinitis pigmentosa."
De Erkenez A.C., Berson E.L., Dryja T.P.
Invest. Ophthalmol. Vis. Sci. 43:ARVO E-Abstract 791(2002)
Cited for: VARIANTS RP13 GLY-2310 AND ASN-2334.
[32]"Clinical characterization, linkage analysis, and PRPC8 mutation analysis of a family with autosomal dominant retinitis pigmentosa type 13 (RP13)."
van Lith-Verhoeven J.J., van der Velde-Visser S.D., Sohocki M.M., Deutman A.F., Brink H.M., Cremers F.P., Hoyng C.B.
Ophthalmic Genet. 23:1-12(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP13 LYS-2310.
[33]"Mutations in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and PRPF31 in Spanish families with autosomal dominant retinitis pigmentosa."
Martinez-Gimeno M., Gamundi M.J., Hernan I., Maseras M., Milla E., Ayuso C., Garcia-Sandoval B., Beneyto M., Vilela C., Baiget M., Antinolo G., Carballo M.
Invest. Ophthalmol. Vis. Sci. 44:2171-2177(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP13 GLY-2310.
[34]"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: CHARACTERIZATION OF VARIANTS RP13 LEU-2304; PRO-2309; ARG-2309; GLY-2310; LYS-2310 AND LEU-2314, INTERACTION WITH EFTUD2 AND SNRNP200.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF092565 mRNA. Translation: AAC61776.1.
AB007510 mRNA. Translation: BAA22563.1.
BC064370 mRNA. Translation: AAH64370.1.
CCDSCCDS11010.1.
RefSeqNP_006436.3. NM_006445.3.
UniGeneHs.181368.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E9LX-ray1.95A1760-2016[»]
3ENBX-ray1.85A/B1769-1990[»]
3LRUX-ray1.85A/B1831-1990[»]
4JK7X-ray1.40A/B1769-1990[»]
4JK8X-ray1.15A/B1769-1990[»]
4JK9X-ray1.50A/B1769-1990[»]
4JKAX-ray1.32A/B1769-1990[»]
4JKBX-ray1.30A/B1769-1990[»]
4JKCX-ray1.50A/B1769-1990[»]
4JKDX-ray1.55A/B1769-1990[»]
4JKEX-ray1.65A/B1769-1990[»]
4JKFX-ray1.95A/B1769-1990[»]
4JKGX-ray1.80A/B1769-1990[»]
4JKHX-ray1.80A/B1769-1990[»]
4KITX-ray3.60C2064-2335[»]
ProteinModelPortalQ6P2Q9.
SMRQ6P2Q9. Positions 1760-2335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115842. 111 interactions.
DIPDIP-29614N.
IntActQ6P2Q9. 42 interactions.
MINTMINT-1131724.
STRING9606.ENSP00000304350.

PTM databases

PhosphoSiteQ6P2Q9.

Polymorphism databases

DMDM67460824.

Proteomic databases

MaxQBQ6P2Q9.
PaxDbQ6P2Q9.
PeptideAtlasQ6P2Q9.
PRIDEQ6P2Q9.

Protocols and materials databases

DNASU10594.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304992; ENSP00000304350; ENSG00000174231.
ENST00000572621; ENSP00000460348; ENSG00000174231.
GeneID10594.
KEGGhsa:10594.
UCSCuc002fte.3. human.

Organism-specific databases

CTD10594.
GeneCardsGC17M001553.
GeneReviewsPRPF8.
HGNCHGNC:17340. PRPF8.
HPACAB009941.
CAB015457.
MIM600059. phenotype.
607300. gene.
neXtProtNX_Q6P2Q9.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA33815.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5178.
HOGENOMHOG000184103.
HOVERGENHBG052796.
InParanoidQ6P2Q9.
KOK12856.
OMAPPGWGAS.
OrthoDBEOG7034G0.
PhylomeDBQ6P2Q9.
TreeFamTF105613.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ6P2Q9.
BgeeQ6P2Q9.
CleanExHS_PRPF8.
GenevestigatorQ6P2Q9.

Family and domain databases

InterProIPR000555. 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]
PANTHERPTHR11140. PTHR11140. 1 hit.
PfamPF01398. 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]
ProDomPD149576. Pre-mRNA-splicing_factor-8. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 2 hits.
ProtoNetSearch...

Other

ChiTaRSPRPF8. human.
EvolutionaryTraceQ6P2Q9.
GeneWikiPRPF8.
GenomeRNAi10594.
NextBio40233.
PROQ6P2Q9.
SOURCESearch...

Entry information

Entry namePRP8_HUMAN
AccessionPrimary (citable) accession number: Q6P2Q9
Secondary accession number(s): O14547, O75965
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM