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Q6P2Q9

- PRP8_HUMAN

UniProt

Q6P2Q9 - PRP8_HUMAN

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Protein

Pre-mRNA-processing-splicing factor 8

Gene

PRPF8

Organism
Homo sapiens (Human)
Status
Reviewed - 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.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. U5 snRNA binding Source: InterPro
  3. U6 snRNA binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA processing Source: ProtInc
  3. mRNA splicing, via spliceosome Source: UniProtKB
  4. RNA splicing Source: UniProtKB
  5. RNA splicing, via transesterification reactions Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major 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
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:17340. PRPF8.

Subcellular locationi

Nucleus speckle By similarity

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. membrane Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. U5 snRNP Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2301 – 23011P → T in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 Publication
VAR_022626
Natural varianti2304 – 23041F → L in RP13. 1 Publication
VAR_022627
Natural varianti2309 – 23091H → P in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 Publication
VAR_022628
Natural varianti2309 – 23091H → R in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 Publication
VAR_022629
Natural varianti2310 – 23101R → G in RP13; reduces interaction with SNRNP200 and EFTUD2. 3 Publications
VAR_022630
Natural varianti2310 – 23101R → K in RP13; reduces interaction with SNRNP200 and EFTUD2. 2 Publications
VAR_022631
Natural varianti2314 – 23141F → L in RP13; reduces interaction with EFTUD2, but not with SNRNP200. 1 Publication
VAR_022632
Natural varianti2334 – 23341Y → N in RP13. 1 Publication
VAR_022633

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1788 – 17881V → D: Strongly reduced interaction with RNA. 1 Publication
Mutagenesisi1789 – 17891T → P: Strongly reduced interaction with RNA. 1 Publication

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi600059. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA33815.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 23352334Pre-mRNA-processing-splicing factor 8PRO_0000097040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei859 – 8591Phosphoserine1 Publication
Modified residuei1463 – 14631N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ6P2Q9.
PaxDbiQ6P2Q9.
PeptideAtlasiQ6P2Q9.
PRIDEiQ6P2Q9.

PTM databases

PhosphoSiteiQ6P2Q9.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ6P2Q9.
CleanExiHS_PRPF8.
ExpressionAtlasiQ6P2Q9. baseline and differential.
GenevestigatoriQ6P2Q9.

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, 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 SNRNP200.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAS2O759342EBI-538479,EBI-1050106
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

Protein-protein interaction databases

BioGridi115842. 119 interactions.
DIPiDIP-29614N.
IntActiQ6P2Q9. 42 interactions.
MINTiMINT-1131724.
STRINGi9606.ENSP00000304350.

Structurei

Secondary structure

1
2335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1761 – 17633
Turni1765 – 17673
Helixi1768 – 17725
Beta strandi1773 – 17753
Beta strandi1777 – 17815
Beta strandi1785 – 17928
Beta strandi1794 – 17963
Beta strandi1798 – 18036
Beta strandi1805 – 18106
Turni1812 – 18143
Beta strandi1816 – 18227
Helixi1824 – 18274
Helixi1833 – 185119
Helixi1854 – 18563
Beta strandi1859 – 18657
Helixi1866 – 18683
Helixi1869 – 18757
Turni1876 – 18783
Beta strandi1883 – 18864
Helixi1893 – 18986
Helixi1900 – 19089
Beta strandi1913 – 19186
Turni1919 – 19224
Helixi1923 – 19253
Helixi1929 – 194517
Helixi1947 – 19537
Helixi1973 – 198917
Helixi1999 – 20013
Helixi2004 – 20129

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ6P2Q9.
SMRiQ6P2Q9. Positions 1760-2335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6P2Q9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2099 – 2233135MPNAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni812 – 1303492Reverse transcriptase homology domainAdd
BLAST
Regioni1304 – 1577274LinkerAdd
BLAST
Regioni1513 – 152614Important for branch point selectionBy similarityAdd
BLAST
Regioni1581 – 1752172Restriction endonuclease homology domainAdd
BLAST
Regioni1669 – 2034366Involved in interaction with pre-mRNA 5' splice siteAdd
BLAST
Regioni1767 – 2020254RNase H homology domainAdd
BLAST
Regioni2301 – 233535Required for interaction with EFTUD2 and SNRNP200Add
BLAST

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

eggNOGiCOG5178.
GeneTreeiENSGT00390000015210.
HOGENOMiHOG000184103.
HOVERGENiHBG052796.
InParanoidiQ6P2Q9.
KOiK12856.
OMAiPPGWGAS.
OrthoDBiEOG7034G0.
PhylomeDBiQ6P2Q9.
TreeFamiTF105613.

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841D → N in BAA22563. 1 PublicationCurated
Sequence conflicti492 – 4932VG → GW in BAA22563. 1 PublicationCurated
Sequence conflicti604 – 6041M → V in BAA22563. 1 PublicationCurated
Sequence conflicti806 – 8061A → T in BAA22563. 1 PublicationCurated
Sequence conflicti997 – 9971L → V in BAA22563. 1 PublicationCurated
Sequence conflicti1390 – 13901A → S in BAA22563. 1 PublicationCurated
Sequence conflicti1867 – 18671G → D in BAA22563. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681K → E.
Corresponds to variant rs1043391 [ dbSNP | Ensembl ].
VAR_022622
Natural varianti227 – 2271R → H.1 Publication
Corresponds to variant rs11559304 [ dbSNP | Ensembl ].
VAR_022623
Natural varianti874 – 8741P → L.1 Publication
Corresponds to variant rs1043396 [ dbSNP | Ensembl ].
VAR_022624
Natural varianti1293 – 12931N → H.1 Publication
Corresponds to variant rs1043399 [ dbSNP | Ensembl ].
VAR_022625
Natural varianti2301 – 23011P → T in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 Publication
VAR_022626
Natural varianti2304 – 23041F → L in RP13. 1 Publication
VAR_022627
Natural varianti2309 – 23091H → P in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 Publication
VAR_022628
Natural varianti2309 – 23091H → R in RP13; no effect on interaction with SNRNP200 and EFTUD2. 1 Publication
VAR_022629
Natural varianti2310 – 23101R → G in RP13; reduces interaction with SNRNP200 and EFTUD2. 3 Publications
VAR_022630
Natural varianti2310 – 23101R → K in RP13; reduces interaction with SNRNP200 and EFTUD2. 2 Publications
VAR_022631
Natural varianti2314 – 23141F → L in RP13; reduces interaction with EFTUD2, but not with SNRNP200. 1 Publication
VAR_022632
Natural varianti2334 – 23341Y → N in RP13. 1 Publication
VAR_022633

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi10594.
KEGGihsa:10594.
UCSCiuc002fte.3. human.

Polymorphism databases

DMDMi67460824.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF092565 mRNA. Translation: AAC61776.1 .
AB007510 mRNA. Translation: BAA22563.1 .
BC064370 mRNA. Translation: AAH64370.1 .
CCDSi CCDS11010.1.
RefSeqi NP_006436.3. NM_006445.3.
UniGenei Hs.181368.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4JK7 X-ray 1.40 A/B 1769-1990 [» ]
4JK8 X-ray 1.15 A/B 1769-1990 [» ]
4JK9 X-ray 1.50 A/B 1769-1990 [» ]
4JKA X-ray 1.32 A/B 1769-1990 [» ]
4JKB X-ray 1.30 A/B 1769-1990 [» ]
4JKC X-ray 1.50 A/B 1769-1990 [» ]
4JKD X-ray 1.55 A/B 1769-1990 [» ]
4JKE X-ray 1.65 A/B 1769-1990 [» ]
4JKF X-ray 1.95 A/B 1769-1990 [» ]
4JKG X-ray 1.80 A/B 1769-1990 [» ]
4JKH X-ray 1.80 A/B 1769-1990 [» ]
4KIT X-ray 3.60 C 2064-2335 [» ]
ProteinModelPortali Q6P2Q9.
SMRi Q6P2Q9. Positions 1760-2335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115842. 119 interactions.
DIPi DIP-29614N.
IntActi Q6P2Q9. 42 interactions.
MINTi MINT-1131724.
STRINGi 9606.ENSP00000304350.

PTM databases

PhosphoSitei Q6P2Q9.

Polymorphism databases

DMDMi 67460824.

Proteomic databases

MaxQBi Q6P2Q9.
PaxDbi Q6P2Q9.
PeptideAtlasi Q6P2Q9.
PRIDEi Q6P2Q9.

Protocols and materials databases

DNASUi 10594.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304992 ; ENSP00000304350 ; ENSG00000174231 .
ENST00000572621 ; ENSP00000460348 ; ENSG00000174231 .
GeneIDi 10594.
KEGGi hsa:10594.
UCSCi uc002fte.3. human.

Organism-specific databases

CTDi 10594.
GeneCardsi GC17M001553.
GeneReviewsi PRPF8.
HGNCi HGNC:17340. PRPF8.
HPAi CAB009941.
CAB015457.
MIMi 600059. phenotype.
607300. gene.
neXtProti NX_Q6P2Q9.
Orphaneti 791. Retinitis pigmentosa.
PharmGKBi PA33815.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5178.
GeneTreei ENSGT00390000015210.
HOGENOMi HOG000184103.
HOVERGENi HBG052796.
InParanoidi Q6P2Q9.
KOi K12856.
OMAi PPGWGAS.
OrthoDBi EOG7034G0.
PhylomeDBi Q6P2Q9.
TreeFami TF105613.

Enzyme and pathway databases

Reactomei REACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi PRPF8. human.
EvolutionaryTracei Q6P2Q9.
GeneWikii PRPF8.
GenomeRNAii 10594.
NextBioi 40233.
PROi Q6P2Q9.
SOURCEi Search...

Gene expression databases

Bgeei Q6P2Q9.
CleanExi HS_PRPF8.
ExpressionAtlasi Q6P2Q9. baseline and differential.
Genevestigatori Q6P2Q9.

Family and domain databases

InterProi IPR000555. 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 ]
PANTHERi PTHR11140. PTHR11140. 1 hit.
Pfami PF01398. 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 ]
ProDomi PD149576. Pre-mRNA-splicing_factor-8. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00232. JAB_MPN. 1 hit.
[Graphical view ]
SUPFAMi SSF53098. SSF53098. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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
    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. 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. 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. 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. 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.

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: October 29, 2014
This is version 122 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

External Data

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