Q6P2Q9 (PRP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Central component of the spliceosome, which may play a role in aligning the pre-mRNA 5'- and 3'-exons for ligation. Interacts with U5 snRNA, and with pre-mRNA 5'-splice sites in B spliceosomes and 3'-splice sites in C spliceosomes.
Subunit structure	Part of the U5 snRNP complex, and of U5.4/6 and U5.U4atac/U6atac snRNP complexes in U2- and U12-dependent spliceosomes, respectively. Found in a mRNA splicing-dependent exon junction complex (EJC) with SRRM1. Interacts with U5 snRNP proteins SNRP116 and WDR57/SPF38. Interacts with EFTUD2 and SNRNP200. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.31
Subcellular location	Nucleus speckle By similarity.
Tissue specificity	Widely expressed. Ref.1
Domain	The MPN domain has structural similarity with viral ribonucleases and RNase H, but unlike RNases, it does not bind any metal ions. Ref.25
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.19 Ref.20 Ref.21
Involvement in disease	Defects in PRPF8 are the cause of retinitis pigmentosa type 13 (RP13) [MIM:600059]. RP leads to degeneration of retinal photoreceptor cells. 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. RP13 inheritance is autosomal dominant. Ref.27 Ref.28 Ref.29 Ref.30 Ref.31
Sequence similarities	Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Polymorphism
Disease	Disease mutation Retinitis pigmentosa
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Inferred by curator. Source: UniProtKB
Cellular component	U5 snRNP Traceable author statement. Source: ProtInc catalytic step 2 spliceosome Inferred from direct assay. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.12. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EFTUD2	Q15029	2	EBI-538479,EBI-357897
SNRNP40	Q96DI7	3	EBI-538479,EBI-538492

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 2335

2334

Pre-mRNA-processing-splicing factor 8

PRO_0000097040

Regions

Domain

2099 – 2233

135

MPN

Region

1669 – 2034

366

Involved in interaction with pre-mRNA 5' splice site

Region

2301 – 2335

35

Required for interaction with EFTUD2 and SNRNP200

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.4 Ref.22

Modified residue

1318

1

Phosphothreonine By similarity

Modified residue

1463

1

N6-acetyllysine Ref.23

Modified residue

1539

1

Phosphoserine Ref.20

Modified residue

2042

1

Phosphothreonine Ref.19

Modified residue

2064

1

Phosphothreonine Ref.19

Modified residue

2079

1

Phosphoserine Ref.21

Natural variations

Natural variant

68

1

K → E.
Corresponds to variant rs1043391 [ dbSNP | Ensembl ].

VAR_022622

Natural variant

227

1

R → H. Ref.3
Corresponds to variant rs11559304 [ dbSNP | Ensembl ].

VAR_022623

Natural variant

874

1

P → L. Ref.28
Corresponds to variant rs1043396 [ dbSNP | Ensembl ].

VAR_022624

Natural variant

1293

1

N → H. Ref.28
Corresponds to variant rs1043399 [ dbSNP | Ensembl ].

VAR_022625

Natural variant

2301

1

P → T in RP13; no effect on interaction with SNRNP200 and EFTUD2. Ref.27

VAR_022626

Natural variant

2304

1

F → L in RP13. Ref.27 Ref.31

VAR_022627

Natural variant

2309

1

H → P in RP13; no effect on interaction with SNRNP200 and EFTUD2. Ref.27 Ref.31

VAR_022628

Natural variant

2309

1

H → R in RP13; no effect on interaction with SNRNP200 and EFTUD2. Ref.27 Ref.31

VAR_022629

Natural variant

2310

1

R → G in RP13; reduces interaction with SNRNP200 and EFTUD2. Ref.27 Ref.28 Ref.30 Ref.31

VAR_022630

Natural variant

2310

1

R → K in RP13; reduces interaction with SNRNP200 and EFTUD2. Ref.27 Ref.29 Ref.31

VAR_022631

Natural variant

2314

1

F → L in RP13; reduces interaction with EFTUD2, but not with SNRNP200. Ref.27 Ref.31

VAR_022632

Natural variant

2334

1

Y → N in RP13. Ref.28

VAR_022633

Experimental info

Mutagenesis

1788

1

V → D: Strongly reduced interaction with RNA. Ref.26

Mutagenesis

1789

1

T → P: Strongly reduced interaction with RNA. Ref.26

Sequence conflict

184

1

D → N in BAA22563. Ref.2

Sequence conflict

492 – 493

2

VG → GW in BAA22563. Ref.2

Sequence conflict

604

1

M → V in BAA22563. Ref.2

Sequence conflict

806

1

A → T in BAA22563. Ref.2

Sequence conflict

997

1

L → V in BAA22563. Ref.2

Sequence conflict

1390

1

A → S in BAA22563. Ref.2

Sequence conflict

1867

1

G → D in BAA22563. Ref.2

Secondary structure

1

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2335

Helix Strand Turn

Details...

Beta strand

1773 – 1775

3

Beta strand

1777 – 1781

5

Beta strand

1785 – 1792

8

Beta strand

1798 – 1803

6

Beta strand

1807 – 1810

4

Beta strand

1817 – 1821

5

Helix

1824 – 1826

3

Helix

1836 – 1851

16

Helix

1854 – 1856

3

Beta strand

1859 – 1864

6

Helix

1869 – 1875

7

Turn

1876 – 1878

3

Beta strand

1883 – 1885

3

Helix

1893 – 1898

6

Helix

1905 – 1908

4

Beta strand

1913 – 1917

5

Turn

1919 – 1922

4

Helix

1923 – 1925

3

Helix

1929 – 1945

17

Helix

1947 – 1953

7

Helix

1973 – 1988

16

Sequences

	Sequence		Length	Mass (Da)
	Q6P2Q9 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: E823A15C60EA61C9	FASTA	2,335	273,600
	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

References

	« Hide 'large scale' referencesShow '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: 10411133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION IN U2- AND U12-DEPENDENT SPLICEOSOME COMPLEXES.
[2]	"Human homologue of Saccharomyces serevisiae 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: 15489334] [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, 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: 2532307] [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: 2527369] [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: 2479028] [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: 2139226] [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: 8702566] [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: 8608445] [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: 9303319] [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: 9774689] [Abstract] Cited for: IDENTIFICATION IN U5 SNRP COMPLEX, INTERACTION WITH SNRP116 AND WDR57.
[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: 10024169] [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: 10809668] [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: 11006293] [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: 10983979] [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: 11971955] [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: 15840809] [Abstract] Cited for: REVIEW.
[19]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2042 AND THR-2064, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1539, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2079, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1463, MASS SPECTROMETRY.
[24]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]	"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: 18843295] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1760-2016, DOMAIN, LACK OF METAL-BINDING.
[26]	"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: 18836455] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1769-1990, MASS SPECTROMETRY, RNA-BINDING, MUTAGENESIS OF VAL-1788 AND THR-1789, LACK OF METAL-BINDING SITE.
[27]	"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: 11468273] [Abstract] Cited for: VARIANTS RP13 THR-2301; LEU-2304; ARG-2309; PRO-2309; GLY-2310; LYS-2310 AND LEU-2314.
[28]	"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.
[29]	"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: 11910553] [Abstract] Cited for: VARIANT RP13 LYS-2310.
[30]	"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: 12714658] [Abstract] Cited for: VARIANT RP13 GLY-2310.
[31]	"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: 17317632] [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.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF092565 mRNA. Translation: AAC61776.1.
AB007510 mRNA. Translation: BAA22563.1.
BC064370 mRNA. Translation: AAH64370.1.

IPI

IPI00007928.

RefSeq

NP_006436.3. NM_006445.3.

UniGene

Hs.181368.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3E9L	X-ray	1.95	A	1760-2016	[»]
3ENB	X-ray	1.85	A/B	1769-1990	[»]
3LRU	X-ray	1.85	A/B	1831-1990	[»]

ProteinModelPortal

Q6P2Q9.

SMR

Q6P2Q9. Positions 1760-2016, 2069-2314.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29614N.

IntAct

Q6P2Q9. 18 interactions.

MINT

MINT-1131724.

STRING

Q6P2Q9.

PTM databases

PhosphoSite

Q6P2Q9.

Polymorphism databases

DMDM

67460824.

Proteomic databases

PeptideAtlas

Q6P2Q9.

PRIDE

Q6P2Q9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000304992; ENSP00000304350; ENSG00000174231.

GeneID

10594.

KEGG

hsa:10594.

UCSC

uc002fte.1. human.

Organism-specific databases

CTD

10594.

GeneCards

GC17M001553.

H-InvDB

HIX0202447.

HGNC

HGNC:17340. PRPF8.

HPA

CAB009941.
CAB015457.

MIM

600059. phenotype.
607300. gene.

neXtProt

NX_Q6P2Q9.

Orphanet

791. Retinitis pigmentosa.

PharmGKB

PA33815.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06439.

GeneTree

ENSGT00390000015210.

HOGENOM

HBG398200.

HOVERGEN

HBG052796.

InParanoid

Q6P2Q9.

OMA

VITCSFT.

OrthoDB

EOG45HRWF.

PhylomeDB

Q6P2Q9.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q6P2Q9.

Bgee

Q6P2Q9.

CleanEx

HS_PRPF8.

Genevestigator

Q6P2Q9.

GermOnline

ENSG00000174231. Homo sapiens.

Family and domain databases

InterPro

IPR000555. 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]

KO

K12856.

Pfam

PF01398. Mov34. 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]

ProDom

PD149576. Pre-mRNA-splicing_factor-8. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00232. JAB_MPN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

40233.

SOURCE

Search...

Entry information

Entry name

PRP8_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.