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Protein

Pre-mRNA-processing-splicing factor 8

Gene

PRPF8

Organism
Homo sapiens (Human)
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.1 Publication1 Publication

GO - Molecular functioni

GO - Biological processi

  • cellular response to lipopolysaccharide Source: Ensembl
  • cellular response to tumor necrosis factor Source: Ensembl
  • mRNA processing Source: ProtInc
  • mRNA splicing, via spliceosome Source: UniProtKB
  • RNA splicing Source: UniProtKB
  • RNA splicing, via transesterification reactions Source: UniProtKB
  • spliceosomal tri-snRNP complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-processing-splicing factor 8
Alternative name(s):
220 kDa U5 snRNP-specific protein
PRP8 homolog
Splicing factor Prp8
p220
Gene namesi
Name:PRPF8
Synonyms:PRPC8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:17340. PRPF8.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • U5 snRNP Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 13 (RP13)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:600059
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0226262301P → T in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 PublicationCorresponds to variant rs121434239dbSNPEnsembl.1
Natural variantiVAR_0226272304F → L in RP13. 2 PublicationsCorresponds to variant rs121434240dbSNPEnsembl.1
Natural variantiVAR_0226282309H → P in RP13; no effect on interaction with SNRNP200 and EFTUD2. 2 PublicationsCorresponds to variant rs121434236dbSNPEnsembl.1
Natural variantiVAR_0226292309H → R in RP13; no effect on interaction with SNRNP200 and EFTUD2. 2 PublicationsCorresponds to variant rs121434236dbSNPEnsembl.1
Natural variantiVAR_0226302310R → G in RP13; reduces interaction with SNRNP200 and EFTUD2. 4 Publications1
Natural variantiVAR_0226312310R → K in RP13; reduces interaction with SNRNP200 and EFTUD2. 3 PublicationsCorresponds to variant rs121434238dbSNPEnsembl.1
Natural variantiVAR_0226322314F → L in RP13; reduces interaction with EFTUD2, but not with SNRNP200. 2 Publications1
Natural variantiVAR_0226332334Y → N in RP13. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1788V → D: Strongly reduced interaction with RNA. 1 Publication1
Mutagenesisi1789T → P: Strongly reduced interaction with RNA. 1 Publication1

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

DisGeNETi10594.
MalaCardsiPRPF8.
MIMi600059. phenotype.
OpenTargetsiENSG00000174231.
ENSG00000274442.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA33815.

Polymorphism and mutation databases

BioMutaiPRPF8.
DMDMi67460824.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000970402 – 2335Pre-mRNA-processing-splicing factor 8Add BLAST2334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei859PhosphoserineCombined sources1
Modified residuei1358PhosphoserineCombined sources1
Modified residuei1425N6,N6-dimethyllysineCombined sources1
Modified residuei1463N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ6P2Q9.
MaxQBiQ6P2Q9.
PaxDbiQ6P2Q9.
PeptideAtlasiQ6P2Q9.
PRIDEiQ6P2Q9.

PTM databases

iPTMnetiQ6P2Q9.
PhosphoSitePlusiQ6P2Q9.
SwissPalmiQ6P2Q9.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000174231.
CleanExiHS_PRPF8.
ExpressionAtlasiQ6P2Q9. baseline and differential.
GenevisibleiQ6P2Q9. HS.

Organism-specific databases

HPAiCAB009941.
CAB015457.

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.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAS2O759342EBI-538479,EBI-1050106
ECDO959052EBI-538479,EBI-2557598
EFTUD2Q150292EBI-538479,EBI-357897
GPKOWQ929172EBI-538479,EBI-746309
PCBP1Q153652EBI-538479,EBI-946095
PRPF19Q9UMS42EBI-538479,EBI-395746
SF3B2Q134353EBI-538479,EBI-749111
SF3B4Q154272EBI-538479,EBI-348469
SLU7O953912EBI-538479,EBI-750559
SNRNP40Q96DI73EBI-538479,EBI-538492
WDR83Q9BRX92EBI-538479,EBI-7705033
ZNF830Q96NB32EBI-538479,EBI-3920997

GO - Molecular functioni

  • K63-linked polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115842. 171 interactors.
DIPiDIP-29614N.
IntActiQ6P2Q9. 58 interactors.
MINTiMINT-1131724.
STRINGi9606.ENSP00000304350.

Structurei

Secondary structure

12335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1761 – 1763Combined sources3
Turni1765 – 1767Combined sources3
Helixi1768 – 1772Combined sources5
Beta strandi1773 – 1775Combined sources3
Beta strandi1777 – 1781Combined sources5
Beta strandi1785 – 1792Combined sources8
Beta strandi1794 – 1796Combined sources3
Beta strandi1798 – 1803Combined sources6
Beta strandi1805 – 1810Combined sources6
Turni1812 – 1814Combined sources3
Beta strandi1816 – 1822Combined sources7
Helixi1824 – 1827Combined sources4
Helixi1833 – 1851Combined sources19
Helixi1854 – 1856Combined sources3
Beta strandi1859 – 1865Combined sources7
Helixi1866 – 1868Combined sources3
Helixi1869 – 1875Combined sources7
Turni1876 – 1878Combined sources3
Beta strandi1883 – 1886Combined sources4
Helixi1893 – 1898Combined sources6
Helixi1900 – 1908Combined sources9
Beta strandi1913 – 1918Combined sources6
Turni1919 – 1922Combined sources4
Helixi1923 – 1925Combined sources3
Helixi1929 – 1945Combined sources17
Helixi1947 – 1953Combined sources7
Helixi1973 – 1989Combined sources17
Helixi1999 – 2001Combined sources3
Helixi2004 – 2012Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E9LX-ray1.95A1760-2016[»]
3ENBX-ray1.85A/B1769-1990[»]
3JCRelectron microscopy7.00A1-2335[»]
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[»]
ProteinModelPortaliQ6P2Q9.
SMRiQ6P2Q9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6P2Q9.

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 siteAdd BLAST366
Regioni1767 – 2020RNase H homology domainAdd BLAST254
Regioni2301 – 2335Required for interaction with EFTUD2 and SNRNP2001 PublicationAdd 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.
HOGENOMiHOG000184103.
HOVERGENiHBG052796.
InParanoidiQ6P2Q9.
KOiK12856.
OMAiRNQNEEF.
OrthoDBiEOG091G003B.
PhylomeDBiQ6P2Q9.
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.

Q6P2Q9-1 [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 ITEPHHIWPT 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 GQLPQHEYLK 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):273,600
Last modified:June 7, 2005 - v2
Checksum:iE823A15C60EA61C9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti184D → N in BAA22563 (Ref. 2) Curated1
Sequence conflicti492 – 493VG → GW in BAA22563 (Ref. 2) Curated2
Sequence conflicti604M → V in BAA22563 (Ref. 2) Curated1
Sequence conflicti806A → T in BAA22563 (Ref. 2) Curated1
Sequence conflicti997L → V in BAA22563 (Ref. 2) Curated1
Sequence conflicti1390A → S in BAA22563 (Ref. 2) Curated1
Sequence conflicti1867G → D in BAA22563 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02262268K → E.Corresponds to variant rs1043391dbSNPEnsembl.1
Natural variantiVAR_022623227R → H.1 PublicationCorresponds to variant rs11559304dbSNPEnsembl.1
Natural variantiVAR_022624874P → L.1 PublicationCorresponds to variant rs1043396dbSNPEnsembl.1
Natural variantiVAR_0226251293N → H.1 PublicationCorresponds to variant rs1043399dbSNPEnsembl.1
Natural variantiVAR_0226262301P → T in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 PublicationCorresponds to variant rs121434239dbSNPEnsembl.1
Natural variantiVAR_0226272304F → L in RP13. 2 PublicationsCorresponds to variant rs121434240dbSNPEnsembl.1
Natural variantiVAR_0226282309H → P in RP13; no effect on interaction with SNRNP200 and EFTUD2. 2 PublicationsCorresponds to variant rs121434236dbSNPEnsembl.1
Natural variantiVAR_0226292309H → R in RP13; no effect on interaction with SNRNP200 and EFTUD2. 2 PublicationsCorresponds to variant rs121434236dbSNPEnsembl.1
Natural variantiVAR_0226302310R → G in RP13; reduces interaction with SNRNP200 and EFTUD2. 4 Publications1
Natural variantiVAR_0226312310R → K in RP13; reduces interaction with SNRNP200 and EFTUD2. 3 PublicationsCorresponds to variant rs121434238dbSNPEnsembl.1
Natural variantiVAR_0226322314F → L in RP13; reduces interaction with EFTUD2, but not with SNRNP200. 2 Publications1
Natural variantiVAR_0226332334Y → N in RP13. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092565 mRNA. Translation: AAC61776.1.
AB007510 mRNA. Translation: BAA22563.1.
BC064370 mRNA. Translation: AAH64370.1.
CCDSiCCDS11010.1.
RefSeqiNP_006436.3. NM_006445.3.
UniGeneiHs.181368.

Genome annotation databases

EnsembliENST00000304992; ENSP00000304350; ENSG00000174231.
ENST00000572621; ENSP00000460348; ENSG00000174231.
ENST00000614672; ENSP00000479194; ENSG00000274442.
ENST00000634039; ENSP00000488611; ENSG00000274442.
GeneIDi10594.
KEGGihsa:10594.
UCSCiuc002fte.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092565 mRNA. Translation: AAC61776.1.
AB007510 mRNA. Translation: BAA22563.1.
BC064370 mRNA. Translation: AAH64370.1.
CCDSiCCDS11010.1.
RefSeqiNP_006436.3. NM_006445.3.
UniGeneiHs.181368.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E9LX-ray1.95A1760-2016[»]
3ENBX-ray1.85A/B1769-1990[»]
3JCRelectron microscopy7.00A1-2335[»]
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[»]
ProteinModelPortaliQ6P2Q9.
SMRiQ6P2Q9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115842. 171 interactors.
DIPiDIP-29614N.
IntActiQ6P2Q9. 58 interactors.
MINTiMINT-1131724.
STRINGi9606.ENSP00000304350.

PTM databases

iPTMnetiQ6P2Q9.
PhosphoSitePlusiQ6P2Q9.
SwissPalmiQ6P2Q9.

Polymorphism and mutation databases

BioMutaiPRPF8.
DMDMi67460824.

Proteomic databases

EPDiQ6P2Q9.
MaxQBiQ6P2Q9.
PaxDbiQ6P2Q9.
PeptideAtlasiQ6P2Q9.
PRIDEiQ6P2Q9.

Protocols and materials databases

DNASUi10594.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304992; ENSP00000304350; ENSG00000174231.
ENST00000572621; ENSP00000460348; ENSG00000174231.
ENST00000614672; ENSP00000479194; ENSG00000274442.
ENST00000634039; ENSP00000488611; ENSG00000274442.
GeneIDi10594.
KEGGihsa:10594.
UCSCiuc002fte.3. human.

Organism-specific databases

CTDi10594.
DisGeNETi10594.
GeneCardsiPRPF8.
GeneReviewsiPRPF8.
HGNCiHGNC:17340. PRPF8.
HPAiCAB009941.
CAB015457.
MalaCardsiPRPF8.
MIMi600059. phenotype.
607300. gene.
neXtProtiNX_Q6P2Q9.
OpenTargetsiENSG00000174231.
ENSG00000274442.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA33815.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1795. Eukaryota.
COG5178. LUCA.
GeneTreeiENSGT00390000015210.
HOGENOMiHOG000184103.
HOVERGENiHBG052796.
InParanoidiQ6P2Q9.
KOiK12856.
OMAiRNQNEEF.
OrthoDBiEOG091G003B.
PhylomeDBiQ6P2Q9.
TreeFamiTF105613.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiPRPF8. human.
EvolutionaryTraceiQ6P2Q9.
GeneWikiiPRPF8.
GenomeRNAii10594.
PROiQ6P2Q9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000174231.
CleanExiHS_PRPF8.
ExpressionAtlasiQ6P2Q9. baseline and differential.
GenevisibleiQ6P2Q9. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q6P2Q9
Secondary accession number(s): O14547, O75965
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 30, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.