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Q6P2Q9

- PRP8_HUMAN

UniProt

Q6P2Q9 - PRP8_HUMAN

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
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. U5 snRNA binding Source: InterPro
    4. 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

    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. nuclear speck Source: UniProtKB-SubCell
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProt
    6. U5 snRNP Source: ProtInc

    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

    ArrayExpressiQ6P2Q9.
    BgeeiQ6P2Q9.
    CleanExiHS_PRPF8.
    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. 111 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.
    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

    MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK     50
    FGFVDAQKED MPPEHVRKII RDHGDMTNRK FRHDKRVYLG ALKYMPHAVL 100
    KLLENMPMPW EQIRDVPVLY HITGAISFVN EIPWVIEPVY ISQWGSMWIM 150
    MRREKRDRRH FKRMRFPPFD DEEPPLDYAD NILDVEPLEA IQLELDPEED 200
    APVLDWFYDH QPLRDSRKYV NGSTYQRWQF TLPMMSTLYR LANQLLTDLV 250
    DDNYFYLFDL KAFFTSKALN MAIPGGPKFE PLVRDINLQD EDWNEFNDIN 300
    KIIIRQPIRT EYKIAFPYLY NNLPHHVHLT WYHTPNVVFI KTEDPDLPAF 350
    YFDPLINPIS HRHSVKSQEP LPDDDEEFEL PEFVEPFLKD TPLYTDNTAN 400
    GIALLWAPRP FNLRSGRTRR ALDIPLVKNW YREHCPAGQP VKVRVSYQKL 450
    LKYYVLNALK HRPPKAQKKR YLFRSFKATK FFQSTKLDWV EVGLQVCRQG 500
    YNMLNLLIHR KNLNYLHLDY NFNLKPVKTL TTKERKKSRF GNAFHLCREV 550
    LRLTKLVVDS HVQYRLGNVD AFQLADGLQY IFAHVGQLTG MYRYKYKLMR 600
    QIRMCKDLKH LIYYRFNTGP VGKGPGCGFW AAGWRVWLFF MRGITPLLER 650
    WLGNLLARQF EGRHSKGVAK TVTKQRVESH FDLELRAAVM HDILDMMPEG 700
    IKQNKARTIL QHLSEAWRCW KANIPWKVPG LPTPIENMIL RYVKAKADWW 750
    TNTAHYNRER IRRGATVDKT VCKKNLGRLT RLYLKAEQER QHNYLKDGPY 800
    ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI LALERLKEAY 850
    SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQRA FKEVGIEFMD 900
    LYSHLVPVYD VEPLEKITDA YLDQYLWYEA DKRRLFPPWI KPADTEPPPL 950
    LVYKWCQGIN NLQDVWETSE GECNVMLESR FEKMYEKIDL TLLNRLLRLI 1000
    VDHNIADYMT AKNNVVINYK DMNHTNSYGI IRGLQFASFI VQYYGLVMDL 1050
    LVLGLHRASE MAGPPQMPND FLSFQDIATE AAHPIRLFCR YIDRIHIFFR 1100
    FTADEARDLI QRYLTEHPDP NNENIVGYNN KKCWPRDARM RLMKHDVNLG 1150
    RAVFWDIKNR LPRSVTTVQW ENSFVSVYSK DNPNLLFNMC GFECRILPKC 1200
    RTSYEEFTHK DGVWNLQNEV TKERTAQCFL RVDDESMQRF HNRVRQILMA 1250
    SGSTTFTKIV NKWNTALIGL MTYFREAVVN TQELLDLLVK CENKIQTRIK 1300
    IGLNSKMPSR FPPVVFYTPK ELGGLGMLSM GHVLIPQSDL RWSKQTDVGI 1350
    THFRSGMSHE EDQLIPNLYR YIQPWESEFI DSQRVWAEYA LKRQEAIAQN 1400
    RRLTLEDLED SWDRGIPRIN TLFQKDRHTL AYDKGWRVRT DFKQYQVLKQ 1450
    NPFWWTHQRH DGKLWNLNNY RTDMIQALGG VEGILEHTLF KGTYFPTWEG 1500
    LFWEKASGFE ESMKWKKLTN AQRSGLNQIP NRRFTLWWSP TINRANVYVG 1550
    FQVQLDLTGI FMHGKIPTLK ISLIQIFRAH LWQKIHESIV MDLCQVFDQE 1600
    LDALEIETVQ KETIHPRKSY KMNSSCADIL LFASYKWNVS RPSLLADSKD 1650
    VMDSTTTQKY WIDIQLRWGD YDSHDIERYA RAKFLDYTTD NMSIYPSPTG 1700
    VLIAIDLAYN LHSAYGNWFP GSKPLIQQAM AKIMKANPAL YVLRERIRKG 1750
    LQLYSSEPTE PYLSSQNYGE LFSNQIIWFV DDTNVYRVTI HKTFEGNLTT 1800
    KPINGAIFIF NPRTGQLFLK IIHTSVWAGQ KRLGQLAKWK TAEEVAALIR 1850
    SLPVEEQPKQ IIVTRKGMLD PLEVHLLDFP NIVIKGSELQ LPFQACLKVE 1900
    KFGDLILKAT EPQMVLFNLY DDWLKTISSY TAFSRLILIL RALHVNNDRA 1950
    KVILKPDKTT ITEPHHIWPT LTDEEWIKVE VQLKDLILAD YGKKNNVNVA 2000
    SLTQSEIRDI ILGMEISAPS QQRQQIAEIE KQTKEQSQLT ATQTRTVNKH 2050
    GDEIITSTTS NYETQTFSSK TEWRVRAISA ANLHLRTNHI YVSSDDIKET 2100
    GYTYILPKNV LKKFICISDL RAQIAGYLYG VSPPDNPQVK EIRCIVMVPQ 2150
    WGTHQTVHLP GQLPQHEYLK EMEPLGWIHT QPNESPQLSP QDVTTHAKIM 2200
    ADNPSWDGEK TIIITCSFTP GSCTLTAYKL TPSGYEWGRQ NTDKGNNPKG 2250
    YLPSHYERVQ MLLSDRFLGF FMVPAQSSWN YNFMGVRHDP NMKYELQLAN 2300
    PKEFYHEVHR PSHFLNFALL QEGEVYSADR EDLYA 2335
    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. 111 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.
    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

    ArrayExpressi Q6P2Q9.
    Bgeei Q6P2Q9.
    CleanExi HS_PRPF8.
    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

    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 1, 2014
    This is version 121 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

    Dasty 3