PRP18_HUMAN
ID PRP18_HUMAN Reviewed; 342 AA.
AC Q99633; Q5T9P9; Q9BUI9;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Pre-mRNA-splicing factor 18;
DE AltName: Full=PRP18 homolog;
DE Short=hPRP18;
GN Name=PRPF18; Synonyms=HPRP18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH PRPF4 AND THE
RP SPLICEOSOME.
RC TISSUE=Cervix carcinoma;
RX PubMed=9000057; DOI=10.1101/gad.11.1.139;
RA Horowitz D.S., Krainer A.R.;
RT "A human protein required for the second step of pre-mRNA splicing is
RT functionally related to a yeast splicing factor.";
RL Genes Dev. 11:139-151(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH PPIH.
RX PubMed=11823439; DOI=10.1093/emboj/21.3.470;
RA Horowitz D.S., Lee E.J., Mabon S.A., Misteli T.;
RT "A cyclophilin functions in pre-mRNA splicing.";
RL EMBO J. 21:470-480(2002).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP STRUCTURE BY NMR OF 60-122.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of splicing factor motif in pre-mRNA splicing factor 18
RT (HPRP18).";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Participates in the second step of pre-mRNA splicing.
CC {ECO:0000269|PubMed:9000057}.
CC -!- SUBUNIT: Heterodimer with PPIH. Interacts with PRPF4 and with the
CC spliceosome. Part of a complex containing U4/U6 snRNPs.
CC {ECO:0000269|PubMed:11823439, ECO:0000269|PubMed:9000057}.
CC -!- INTERACTION:
CC Q99633; O95994: AGR2; NbExp=3; IntAct=EBI-2798416, EBI-712648;
CC Q99633; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-2798416, EBI-11522760;
CC Q99633; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-2798416, EBI-746752;
CC Q99633; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-2798416, EBI-297683;
CC Q99633; Q9H1I8: ASCC2; NbExp=3; IntAct=EBI-2798416, EBI-711197;
CC Q99633; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-2798416, EBI-742722;
CC Q99633; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-2798416, EBI-11975051;
CC Q99633; Q9H2G9: BLZF1; NbExp=5; IntAct=EBI-2798416, EBI-2548012;
CC Q99633; A2RRN7: CADPS; NbExp=3; IntAct=EBI-2798416, EBI-10179719;
CC Q99633; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-2798416, EBI-739580;
CC Q99633; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-2798416, EBI-3866279;
CC Q99633; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-2798416, EBI-11530605;
CC Q99633; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-2798416, EBI-11524851;
CC Q99633; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-2798416, EBI-10171570;
CC Q99633; Q8NCX0-3: CCDC150; NbExp=3; IntAct=EBI-2798416, EBI-12235840;
CC Q99633; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2798416, EBI-10961624;
CC Q99633; P24863: CCNC; NbExp=3; IntAct=EBI-2798416, EBI-395261;
CC Q99633; Q01850: CDR2; NbExp=3; IntAct=EBI-2798416, EBI-1181367;
CC Q99633; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2798416, EBI-739624;
CC Q99633; Q96S65: CSRNP1; NbExp=3; IntAct=EBI-2798416, EBI-4311573;
CC Q99633; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-2798416, EBI-742054;
CC Q99633; Q92997: DVL3; NbExp=3; IntAct=EBI-2798416, EBI-739789;
CC Q99633; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-2798416, EBI-2349927;
CC Q99633; Q96CN4: EVI5L; NbExp=3; IntAct=EBI-2798416, EBI-749523;
CC Q99633; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-2798416, EBI-10220102;
CC Q99633; O15287: FANCG; NbExp=3; IntAct=EBI-2798416, EBI-81610;
CC Q99633; Q86UX7-2: FERMT3; NbExp=3; IntAct=EBI-2798416, EBI-12915620;
CC Q99633; A1L4K1: FSD2; NbExp=3; IntAct=EBI-2798416, EBI-5661036;
CC Q99633; P51114-2: FXR1; NbExp=3; IntAct=EBI-2798416, EBI-11022345;
CC Q99633; O95995: GAS8; NbExp=3; IntAct=EBI-2798416, EBI-1052570;
CC Q99633; Q96CN9: GCC1; NbExp=3; IntAct=EBI-2798416, EBI-746252;
CC Q99633; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-2798416, EBI-2548508;
CC Q99633; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2798416, EBI-618309;
CC Q99633; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2798416, EBI-5916454;
CC Q99633; Q86WP2: GPBP1; NbExp=3; IntAct=EBI-2798416, EBI-2349758;
CC Q99633; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-2798416, EBI-717919;
CC Q99633; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-2798416, EBI-2549423;
CC Q99633; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-2798416, EBI-10961706;
CC Q99633; O75031: HSF2BP; NbExp=3; IntAct=EBI-2798416, EBI-7116203;
CC Q99633; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-2798416, EBI-81279;
CC Q99633; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-2798416, EBI-11522367;
CC Q99633; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-2798416, EBI-747204;
CC Q99633; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-2798416, EBI-2556193;
CC Q99633; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-2798416, EBI-11954971;
CC Q99633; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2798416, EBI-14069005;
CC Q99633; Q15323: KRT31; NbExp=3; IntAct=EBI-2798416, EBI-948001;
CC Q99633; O76011: KRT34; NbExp=3; IntAct=EBI-2798416, EBI-1047093;
CC Q99633; Q92764: KRT35; NbExp=3; IntAct=EBI-2798416, EBI-1058674;
CC Q99633; Q6A163: KRT39; NbExp=3; IntAct=EBI-2798416, EBI-11958242;
CC Q99633; Q6A162: KRT40; NbExp=3; IntAct=EBI-2798416, EBI-10171697;
CC Q99633; O95751: LDOC1; NbExp=3; IntAct=EBI-2798416, EBI-740738;
CC Q99633; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-2798416, EBI-1216080;
CC Q99633; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2798416, EBI-741037;
CC Q99633; P23508: MCC; NbExp=3; IntAct=EBI-2798416, EBI-307531;
CC Q99633; Q99750: MDFI; NbExp=3; IntAct=EBI-2798416, EBI-724076;
CC Q99633; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2798416, EBI-16439278;
CC Q99633; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2798416, EBI-11522433;
CC Q99633; Q96RE7: NACC1; NbExp=3; IntAct=EBI-2798416, EBI-7950997;
CC Q99633; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-2798416, EBI-10172876;
CC Q99633; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-2798416, EBI-1051317;
CC Q99633; O76083-2: PDE9A; NbExp=3; IntAct=EBI-2798416, EBI-11524542;
CC Q99633; Q99471: PFDN5; NbExp=3; IntAct=EBI-2798416, EBI-357275;
CC Q99633; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2798416, EBI-14066006;
CC Q99633; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2798416, EBI-79165;
CC Q99633; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-2798416, EBI-949255;
CC Q99633; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-2798416, EBI-302345;
CC Q99633; O43447: PPIH; NbExp=7; IntAct=EBI-2798416, EBI-1055615;
CC Q99633; P31321: PRKAR1B; NbExp=3; IntAct=EBI-2798416, EBI-2805516;
CC Q99633; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-2798416, EBI-726876;
CC Q99633; P0DPB3-4: SCHIP1; NbExp=3; IntAct=EBI-2798416, EBI-11962426;
CC Q99633; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-2798416, EBI-748601;
CC Q99633; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2798416, EBI-5235340;
CC Q99633; O75558: STX11; NbExp=3; IntAct=EBI-2798416, EBI-714135;
CC Q99633; Q12933: TRAF2; NbExp=3; IntAct=EBI-2798416, EBI-355744;
CC Q99633; P36406: TRIM23; NbExp=3; IntAct=EBI-2798416, EBI-740098;
CC Q99633; P14373: TRIM27; NbExp=3; IntAct=EBI-2798416, EBI-719493;
CC Q99633; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2798416, EBI-2130429;
CC Q99633; Q99598: TSNAX; NbExp=3; IntAct=EBI-2798416, EBI-742638;
CC Q99633; Q2TAA8: TSNAXIP1; NbExp=3; IntAct=EBI-2798416, EBI-6872498;
CC Q99633; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-2798416, EBI-9090990;
CC Q99633; Q6PKC3: TXNDC11; NbExp=3; IntAct=EBI-2798416, EBI-749812;
CC Q99633; Q5T124-6: UBXN11; NbExp=3; IntAct=EBI-2798416, EBI-11524408;
CC Q99633; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-2798416, EBI-11035148;
CC Q99633; Q9UID6: ZNF639; NbExp=5; IntAct=EBI-2798416, EBI-947476;
CC Q99633; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2798416, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Note=Colocalizes
CC with spliceosomal snRNPs. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99633-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99633-2; Sequence=VSP_008327, VSP_008328;
CC -!- SIMILARITY: Belongs to the PRP18 family. {ECO:0000305}.
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DR EMBL; U51990; AAB41490.1; -; mRNA.
DR EMBL; AL157392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86281.1; -; Genomic_DNA.
DR EMBL; BC000794; AAH00794.1; -; mRNA.
DR EMBL; BC002572; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS7100.1; -. [Q99633-1]
DR RefSeq; NP_003666.1; NM_003675.3. [Q99633-1]
DR PDB; 2DK4; NMR; -; A=60-122.
DR PDBsum; 2DK4; -.
DR AlphaFoldDB; Q99633; -.
DR BMRB; Q99633; -.
DR SMR; Q99633; -.
DR BioGRID; 114129; 91.
DR CORUM; Q99633; -.
DR IntAct; Q99633; 90.
DR MINT; Q99633; -.
DR STRING; 9606.ENSP00000367835; -.
DR iPTMnet; Q99633; -.
DR MetOSite; Q99633; -.
DR PhosphoSitePlus; Q99633; -.
DR BioMuta; PRPF18; -.
DR DMDM; 37082244; -.
DR EPD; Q99633; -.
DR jPOST; Q99633; -.
DR MassIVE; Q99633; -.
DR MaxQB; Q99633; -.
DR PaxDb; Q99633; -.
DR PeptideAtlas; Q99633; -.
DR PRIDE; Q99633; -.
DR ProteomicsDB; 78369; -. [Q99633-1]
DR ProteomicsDB; 78370; -. [Q99633-2]
DR Antibodypedia; 35190; 121 antibodies from 23 providers.
DR DNASU; 8559; -.
DR Ensembl; ENST00000378572.8; ENSP00000367835.3; ENSG00000165630.14. [Q99633-1]
DR GeneID; 8559; -.
DR KEGG; hsa:8559; -.
DR MANE-Select; ENST00000378572.8; ENSP00000367835.3; NM_003675.4; NP_003666.1.
DR UCSC; uc001imp.4; human. [Q99633-1]
DR CTD; 8559; -.
DR DisGeNET; 8559; -.
DR GeneCards; PRPF18; -.
DR HGNC; HGNC:17351; PRPF18.
DR HPA; ENSG00000165630; Low tissue specificity.
DR MIM; 604993; gene.
DR neXtProt; NX_Q99633; -.
DR OpenTargets; ENSG00000165630; -.
DR PharmGKB; PA38449; -.
DR VEuPathDB; HostDB:ENSG00000165630; -.
DR eggNOG; KOG2808; Eukaryota.
DR GeneTree; ENSGT00390000015073; -.
DR HOGENOM; CLU_039675_0_1_1; -.
DR InParanoid; Q99633; -.
DR OMA; SFAQVRW; -.
DR OrthoDB; 1485522at2759; -.
DR PhylomeDB; Q99633; -.
DR TreeFam; TF315049; -.
DR PathwayCommons; Q99633; -.
DR SignaLink; Q99633; -.
DR BioGRID-ORCS; 8559; 473 hits in 1071 CRISPR screens.
DR ChiTaRS; PRPF18; human.
DR EvolutionaryTrace; Q99633; -.
DR GenomeRNAi; 8559; -.
DR Pharos; Q99633; Tbio.
DR PRO; PR:Q99633; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q99633; protein.
DR Bgee; ENSG00000165630; Expressed in calcaneal tendon and 104 other tissues.
DR ExpressionAtlas; Q99633; baseline and differential.
DR Genevisible; Q99633; HS.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005681; C:spliceosomal complex; TAS:ProtInc.
DR GO; GO:0071021; C:U2-type post-spliceosomal complex; IBA:GO_Central.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR Gene3D; 4.10.280.110; -; 1.
DR IDEAL; IID00678; -.
DR InterPro; IPR004098; Prp18.
DR InterPro; IPR014906; PRP4-like.
DR InterPro; IPR036285; PRP4-like_sf.
DR InterPro; IPR039979; PRPF18.
DR PANTHER; PTHR13007; PTHR13007; 1.
DR Pfam; PF02840; Prp18; 1.
DR Pfam; PF08799; PRP4; 1.
DR SMART; SM00500; SFM; 1.
DR SUPFAM; SSF158230; SSF158230; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Spliceosome.
FT CHAIN 1..342
FT /note="Pre-mRNA-splicing factor 18"
FT /id="PRO_0000058582"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 22..259
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008327"
FT VAR_SEQ 286..342
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008328"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2DK4"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:2DK4"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:2DK4"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2DK4"
SQ SEQUENCE 342 AA; 39860 MW; 269D79E1E733CF6D CRC64;
MDILKSEILR KRQLVEDRNL LVENKKYFKR SELAKKEEEA YFERCGYKIQ PKEEDQKPLT
SSNPVLELEL AEEKLPMTLS RQEVIRRLRE RGEPIRLFGE TDYDAFQRLR KIEILTPEVN
KGLRNDLKAA LDKIDQQYLN EIVGGQEPGE EDTQNDLKVH EENTTIEELE ALGESLGKGD
DHKDMDIITK FLKFLLGVWA KELNAREDYV KRSVQGKLNS ATQKQTESYL RPLFRKLRKR
NLPADIKESI TDIIKFMLQR EYVKANDAYL QMAIGNAPWP IGVTMVGIHA RTGREKIFSK
HVAHVLNDET QRKYIQGLKR LMTICQKHFP TDPSKCVEYN AL
