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Pre-mRNA-processing factor 6 (Androgen receptor N-terminal domain-transactivating protein 1) (ANT-1) (PRP6 homolog) (U5 snRNP-associated 102 kDa protein) (U5-102 kDa protein)

 PRP6_HUMAN              Reviewed;         941 AA.
O94906; B2RAR5; B3KMC6; O95109; Q5VXS5; Q9H3Z1; Q9H4T9; Q9H4U8;
Q9NTE6;
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
07-NOV-2018, entry version 187.
RecName: Full=Pre-mRNA-processing factor 6;
AltName: Full=Androgen receptor N-terminal domain-transactivating protein 1;
Short=ANT-1;
AltName: Full=PRP6 homolog;
AltName: Full=U5 snRNP-associated 102 kDa protein;
Short=U5-102 kDa protein;
Name=PRPF6; Synonyms=C20orf14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 138-147;
300-309; 352-359; 776-784 AND 891-898, AND SUBCELLULAR LOCATION.
TISSUE=Cervix carcinoma;
PubMed=10561546; DOI=10.1016/S0167-4838(99)00203-4;
Nishikimi A., Mukai J., Kioka N., Yamada M.;
"A novel mammalian nuclear protein similar to Schizosaccharomyces
pombe Prp1p/Zer1p and Saccharomyces cerevisiae Prp6p pre-mRNA splicing
factors.";
Biochim. Biophys. Acta 1435:147-152(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 324-334;
395-408; 755-768; 871-883 AND 917-924, AND INTERACTION WITH U5 AND
U4/U6 SNRNPS.
TISSUE=Cervix carcinoma;
PubMed=10788320; DOI=10.1006/jmbi.2000.3685;
Makarov E.M., Makarova O.V., Achsel T., Luehrmann R.;
"The human homologue of the yeast splicing factor Prp6p contains
multiple TPR elements and is stably associated with the U5 snRNP via
protein-protein interactions.";
J. Mol. Biol. 298:567-575(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH ARAF1.
TISSUE=Cervix carcinoma;
PubMed=10848612; DOI=10.1128/MCB.20.13.4870-4878.2000;
Yuryev A., Ono M., Goff S.A., Macaluso F., Wennogle L.P.;
"Isoform-specific localization of A-RAF in mitochondria.";
Mol. Cell. Biol. 20:4870-4878(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Teratocarcinoma, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 402-941.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
FUNCTION, INTERACTION WITH AR AND NR3C1, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=12039962; DOI=10.1074/jbc.M203811200;
Zhao Y., Goto K., Saitoh M., Yanase T., Nomura M., Okabe T.,
Takayanagi R., Nawata H.;
"Activation function-1 domain of androgen receptor contributes to the
interaction between subnuclear splicing factor compartment and nuclear
receptor compartment. Identification of the p102 U5 small nuclear
ribonucleoprotein particle-binding protein as a coactivator for the
receptor.";
J. Biol. Chem. 277:30031-30039(2002).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[10]
SUBUNIT.
PubMed=16723661; DOI=10.1261/rna.55406;
Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
"The network of protein-protein interactions within the human U4/U6.U5
tri-snRNP.";
RNA 12:1418-1430(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266; THR-275 AND
SER-279, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266; THR-275 AND
SER-279, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND THR-266, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-266, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17] {ECO:0000244|PDB:3JCR}
STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBUNIT,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=26912367; DOI=10.1126/science.aad2085;
Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T.,
Urlaub H., Luhrmann R., Stark H.;
"Molecular architecture of the human U4/U6.U5 tri-snRNP.";
Science 351:1416-1420(2016).
[18] {ECO:0000244|PDB:5O9Z}
STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
"Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
Activation.";
Cell 170:701-713(2017).
[19]
VARIANT RP60 TRP-729, CHARACTERIZATION OF VARIANT RP60 TRP-729,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21549338; DOI=10.1016/j.ajhg.2011.04.008;
Tanackovic G., Ransijn A., Ayuso C., Harper S., Berson E.L.,
Rivolta C.;
"A missense mutation in PRPF6 causes impairment of pre-mRNA splicing
and autosomal-dominant retinitis pigmentosa.";
Am. J. Hum. Genet. 88:643-649(2011).
[20]
VARIANT SER-477.
PubMed=22235333; DOI=10.1371/journal.pone.0029729;
Velinov M., Dolzhanskaya N., Gonzalez M., Powell E., Konidari I.,
Hulme W., Staropoli J.F., Xin W., Wen G.Y., Barone R., Coppel S.H.,
Sims K., Brown W.T., Zuchner S.;
"Mutations in the gene DNAJC5 cause autosomal dominant Kufs disease in
a proportion of cases: study of the Parry family and 8 other
families.";
PLoS ONE 7:E29729-E29729(2012).
-!- FUNCTION: Involved in pre-mRNA splicing as component of the U4/U6-
U5 tri-snRNP complex, one of the building blocks of the
spliceosome (PubMed:28781166, PubMed:21549338). Enhances
dihydrotestosterone-induced transactivation activity of AR, as
well as dexamethasone-induced transactivation activity of NR3C1,
but does not affect estrogen-induced transactivation.
{ECO:0000269|PubMed:12039962, ECO:0000269|PubMed:21549338,
ECO:0000269|PubMed:28781166}.
-!- SUBUNIT: Identified in the spliceosome B complex
(PubMed:28781166). Identified in the spliceosome C complex
(PubMed:11991638). Associates with the U5 snRNP particle
(PubMed:10788320). 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, LSm proteins LSm2-8 and Sm
proteins (PubMed:16723661, PubMed:26912367, PubMed:28781166).
Interacts with ARAF1 (PubMed:10848612). Interacts with AR and
NR3C1, but not ESR1, independently of the presence of hormones
(PubMed:12039962). {ECO:0000269|PubMed:10788320,
ECO:0000269|PubMed:10848612, ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:12039962, ECO:0000269|PubMed:16723661,
ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.
-!- INTERACTION:
P10398:ARAF; NbExp=4; IntAct=EBI-536755, EBI-365961;
O95400:CD2BP2; NbExp=5; IntAct=EBI-536755, EBI-768015;
Q13123:IK; NbExp=2; IntAct=EBI-536755, EBI-713456;
Q8WWY3:PRPF31; NbExp=2; IntAct=EBI-536755, EBI-1567797;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:10561546, ECO:0000269|PubMed:26912367,
ECO:0000269|PubMed:28781166}. Nucleus speckle
{ECO:0000269|PubMed:21549338}. Note=Localized in splicing
speckles. {ECO:0000269|PubMed:21549338}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O94906-1; Sequence=Displayed;
Name=2;
IsoId=O94906-2; Sequence=VSP_041857;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:12039962}.
-!- DISEASE: Retinitis pigmentosa 60 (RP60) [MIM:613983]: 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. {ECO:0000269|PubMed:21549338}. Note=The disease
may be caused by mutations affecting the gene represented in this
entry. Cells from RP60 patients show intron retention for pre-mRNA
bearing specific splicing signals.
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EMBL; AB019219; BAA37140.1; -; mRNA.
EMBL; AF221842; AAF66128.1; -; mRNA.
EMBL; AF026031; AAD01798.1; -; mRNA.
EMBL; AK001554; BAG50938.1; -; mRNA.
EMBL; AK314310; BAG36962.1; -; mRNA.
EMBL; AL118506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001666; AAH01666.1; -; mRNA.
EMBL; AL137320; CAB70695.1; -; mRNA.
CCDS; CCDS13550.1; -. [O94906-1]
PIR; T46386; T46386.
RefSeq; NP_036601.2; NM_012469.3. [O94906-1]
UniGene; Hs.31334; -.
PDB; 3JCR; EM; 7.00 A; G=1-941.
PDB; 5O9Z; EM; 4.50 A; G=1-941.
PDBsum; 3JCR; -.
PDBsum; 5O9Z; -.
ProteinModelPortal; O94906; -.
SMR; O94906; -.
BioGrid; 117298; 120.
CORUM; O94906; -.
DIP; DIP-29006N; -.
IntAct; O94906; 50.
MINT; O94906; -.
STRING; 9606.ENSP00000266079; -.
MoonDB; O94906; Predicted.
iPTMnet; O94906; -.
PhosphoSitePlus; O94906; -.
SwissPalm; O94906; -.
BioMuta; PRPF6; -.
EPD; O94906; -.
MaxQB; O94906; -.
PaxDb; O94906; -.
PeptideAtlas; O94906; -.
PRIDE; O94906; -.
ProteomicsDB; 50541; -.
ProteomicsDB; 50542; -. [O94906-2]
Ensembl; ENST00000266079; ENSP00000266079; ENSG00000101161. [O94906-1]
GeneID; 24148; -.
KEGG; hsa:24148; -.
UCSC; uc002yho.4; human. [O94906-1]
CTD; 24148; -.
DisGeNET; 24148; -.
EuPathDB; HostDB:ENSG00000101161.7; -.
GeneCards; PRPF6; -.
GeneReviews; PRPF6; -.
HGNC; HGNC:15860; PRPF6.
HPA; HPA047106; -.
MalaCards; PRPF6; -.
MIM; 613979; gene.
MIM; 613983; phenotype.
neXtProt; NX_O94906; -.
OpenTargets; ENSG00000101161; -.
Orphanet; 791; Retinitis pigmentosa.
PharmGKB; PA25682; -.
eggNOG; KOG0495; Eukaryota.
eggNOG; ENOG410XRKD; LUCA.
GeneTree; ENSGT00550000075016; -.
HOVERGEN; HBG023330; -.
InParanoid; O94906; -.
KO; K12855; -.
OMA; LIMRGCE; -.
OrthoDB; EOG091G01F5; -.
PhylomeDB; O94906; -.
TreeFam; TF105743; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
SignaLink; O94906; -.
ChiTaRS; PRPF6; human.
GeneWiki; PRPF6; -.
GenomeRNAi; 24148; -.
PRO; PR:O94906; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101161; Expressed in 227 organ(s), highest expression level in tendon of biceps brachii.
CleanEx; HS_PRPF6; -.
Genevisible; O94906; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB.
GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:BHF-UCL.
GO; GO:0005682; C:U5 snRNP; IDA:BHF-UCL.
GO; GO:0050681; F:androgen receptor binding; IPI:MGI.
GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0003713; F:transcription coactivator activity; IGI:MGI.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0006403; P:RNA localization; IMP:MGI.
GO; GO:0008380; P:RNA splicing; NAS:UniProtKB.
GO; GO:0000375; P:RNA splicing, via transesterification reactions; NAS:UniProtKB.
GO; GO:0000245; P:spliceosomal complex assembly; NAS:UniProtKB.
GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IMP:BHF-UCL.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR003107; HAT.
InterPro; IPR010491; PRP1_N.
InterPro; IPR027108; Prp6/Prp1/STA1.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR11246:SF1; PTHR11246:SF1; 1.
Pfam; PF06424; PRP1_N; 1.
Pfam; PF13181; TPR_8; 1.
SMART; SM00386; HAT; 13.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Retinitis pigmentosa; Spliceosome.
CHAIN 1 941 Pre-mRNA-processing factor 6.
/FTId=PRO_0000205759.
REPEAT 384 416 HAT 1.
REPEAT 418 444 HAT 2.
REPEAT 445 476 HAT 3.
REPEAT 554 586 HAT 4.
REPEAT 588 620 HAT 5.
REPEAT 622 654 HAT 6.
REPEAT 689 721 HAT 7.
REPEAT 723 755 HAT 8.
REPEAT 855 887 HAT 9.
COMPBIAS 67 72 Poly-Asp.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 180 180 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 266 266 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 275 275 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 637 676 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041857.
VARIANT 477 477 N -> S (very rare variant found in a
family with neuronal ceroid
lipofuscinosis carrying a causative
mutation in DNAJC5; uncertain role as a
disease phenotype modifier).
{ECO:0000269|PubMed:22235333}.
/FTId=VAR_069766.
VARIANT 729 729 R -> W (in RP60; impaired function in
pre-mRNA splicing; mislocalized in Cajal
bodies; partial loss of localization in
splicing speckles; dbSNP:rs387907100).
{ECO:0000269|PubMed:21549338}.
/FTId=VAR_065768.
CONFLICT 20 20 G -> W (in Ref. 3; AAD01798).
{ECO:0000305}.
CONFLICT 223 223 P -> R (in Ref. 3; AAD01798).
{ECO:0000305}.
CONFLICT 284 284 H -> R (in Ref. 4; BAG50938).
{ECO:0000305}.
CONFLICT 421 421 I -> T (in Ref. 4; BAG36962).
{ECO:0000305}.
SEQUENCE 941 AA; 106925 MW; 91C2F1ADCA439BE9 CRC64;
MNKKKKPFLG MPAPLGYVPG LGRGATGFTT RSDIGPARDA NDPVDDRHAP PGKRTVGDQM
KKNQAADDDD EDLNDTNYDE FNGYAGSLFS SGPYEKDDEE ADAIYAALDK RMDERRKERR
EQREKEEIEK YRMERPKIQQ QFSDLKRKLA EVTEEEWLSI PEVGDARNKR QRNPRYEKLT
PVPDSFFAKH LQTGENHTSV DPRQTQFGGL NTPYPGGLNT PYPGGMTPGL MTPGTGELDM
RKIGQARNTL MDMRLSQVSD SVSGQTVVDP KGYLTDLNSM IPTHGGDIND IKKARLLLKS
VRETNPHHPP AWIASARLEE VTGKLQVARN LIMKGTEMCP KSEDVWLEAA RLQPGDTAKA
VVAQAVRHLP QSVRIYIRAA ELETDIRAKK RVLRKALEHV PNSVRLWKAA VELEEPEDAR
IMLSRAVECC PTSVELWLAL ARLETYENAR KVLNKARENI PTDRHIWITA AKLEEANGNT
QMVEKIIDRA ITSLRANGVE INREQWIQDA EECDRAGSVA TCQAVMRAVI GIGIEEEDRK
HTWMEDADSC VAHNALECAR AIYAYALQVF PSKKSVWLRA AYFEKNHGTR ESLEALLQRA
VAHCPKAEVL WLMGAKSKWL AGDVPAARSI LALAFQANPN SEEIWLAAVK LESENDEYER
ARRLLAKARS SAPTARVFMK SVKLEWVQDN IRAAQDLCEE ALRHYEDFPK LWMMKGQIEE
QKEMMEKARE AYNQGLKKCP HSTPLWLLLS RLEEKIGQLT RARAILEKSR LKNPKNPGLW
LESVRLEYRA GLKNIANTLM AKALQECPNS GILWSEAIFL EARPQRRTKS VDALKKCEHD
PHVLLAVAKL FWSQRKITKA REWFHRTVKI DSDLGDAWAF FYKFELQHGT EEQQEEVRKR
CESAEPRHGE LWCAVSKDIA NWQKKIGDIL RLVAGRIKNT F


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