SEN15_HUMAN
ID SEN15_HUMAN Reviewed; 171 AA.
AC Q8WW01; B4DKP0; Q9BZQ5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=tRNA-splicing endonuclease subunit Sen15;
DE AltName: Full=SEN15 homolog;
DE Short=HsSEN15;
DE AltName: Full=tRNA-intron endonuclease Sen15;
GN Name=TSEN15; Synonyms=C1orf19, SEN15;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA Carpten J.D.;
RT "Cloning and characterization of 13 novel transcripts and the human RGS8
RT gene from the 1q25 region encompassing the hereditary prostate cancer
RT (HPC1) locus.";
RL Genomics 73:211-222(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND COMPONENT OF A COMPLEX WITH SEN2;
RP SEN54; SEN34 AND CLP1.
RX PubMed=15109492; DOI=10.1016/s0092-8674(04)00342-3;
RA Paushkin S.V., Patel M., Furia B.S., Peltz S.W., Trotta C.R.;
RT "Identification of a human endonuclease complex reveals a link between tRNA
RT splicing and pre-mRNA 3' end formation.";
RL Cell 117:311-321(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-168, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP INVOLVEMENT IN PCH2F, AND VARIANT PCH2F GLY-76.
RX PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015;
RA Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S.,
RA Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A.,
RA Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S.,
RA Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F., Alshahwan S.A.,
RA Seidahmed M.Z., Alhadid A.A., Aldhalaan H., Alqallaf F., Kurdi W.,
RA Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N.,
RA Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S.,
RA Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F.,
RA Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R.,
RA Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.;
RT "Accelerating novel candidate gene discovery in neurogenetic disorders via
RT whole-exome sequencing of prescreened multiplex consanguineous families.";
RL Cell Rep. 10:148-161(2015).
RN [10]
RP STRUCTURE BY NMR OF 36-157, AND HOMODIMERIZATION.
RX PubMed=17166513; DOI=10.1016/j.jmb.2006.11.024;
RA Song J., Markley J.L.;
RT "Three-dimensional structure determined for a subunit of human tRNA
RT splicing endonuclease (Sen15) reveals a novel dimeric fold.";
RL J. Mol. Biol. 366:155-164(2007).
RN [11]
RP VARIANTS PCH2F GLY-76; TYR-116 AND CYS-152, CHARACTERIZATION OF VARIANTS
RP PCH2F GLY-76; TYR-116 AND CYS-152, AND FUNCTION.
RX PubMed=27392077; DOI=10.1016/j.ajhg.2016.05.023;
RA Breuss M.W., Sultan T., James K.N., Rosti R.O., Scott E., Musaev D.,
RA Furia B., Reis A., Sticht H., Al-Owain M., Alkuraya F.S., Reuter M.S.,
RA Abou Jamra R., Trotta C.R., Gleeson J.G.;
RT "Autosomal-recessive mutations in the tRNA splicing endonuclease subunit
RT TSEN15 cause pontocerebellar hypoplasia and progressive microcephaly.";
RL Am. J. Hum. Genet. 99:228-235(2016).
CC -!- FUNCTION: Non-catalytic subunit of the tRNA-splicing endonuclease
CC complex, a complex responsible for identification and cleavage of the
CC splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice
CC sites to release the intron. The products are an intron and two tRNA
CC half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini
CC (PubMed:15109492, PubMed:27392077). There are no conserved sequences at
CC the splice sites, but the intron is invariably located at the same site
CC in the gene, placing the splice sites an invariant distance from the
CC constant structural features of the tRNA body. The tRNA splicing
CC endonuclease is also involved in mRNA processing via its association
CC with pre-mRNA 3'-end processing factors, establishing a link between
CC pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the
CC endonuclease subunits function in multiple RNA-processing events
CC (PubMed:15109492). {ECO:0000269|PubMed:15109492,
CC ECO:0000269|PubMed:27392077}.
CC -!- SUBUNIT: Homodimer (PubMed:17166513). tRNA splicing endonuclease is a
CC heterotetramer composed of TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA
CC splicing endonuclease complex also contains proteins of the Pre-mRNA 3'
CC end processing machinery, such as CLP1, CPSF1, CPSF4 and CSTF2.
CC {ECO:0000269|PubMed:17166513}.
CC -!- INTERACTION:
CC Q8WW01; Q9BQI0-4: AIF1L; NbExp=3; IntAct=EBI-372432, EBI-12351549;
CC Q8WW01; Q03989: ARID5A; NbExp=3; IntAct=EBI-372432, EBI-948603;
CC Q8WW01; Q8WXK4-2: ASB12; NbExp=3; IntAct=EBI-372432, EBI-18394052;
CC Q8WW01; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-372432, EBI-742054;
CC Q8WW01; Q9NQM4: DNAAF6; NbExp=3; IntAct=EBI-372432, EBI-10239299;
CC Q8WW01; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-372432, EBI-744099;
CC Q8WW01; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-372432, EBI-739467;
CC Q8WW01; O75031: HSF2BP; NbExp=3; IntAct=EBI-372432, EBI-7116203;
CC Q8WW01; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-372432, EBI-747204;
CC Q8WW01; Q0VD86: INCA1; NbExp=3; IntAct=EBI-372432, EBI-6509505;
CC Q8WW01; P25791-3: LMO2; NbExp=3; IntAct=EBI-372432, EBI-11959475;
CC Q8WW01; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-372432, EBI-473196;
CC Q8WW01; A8MW99: MEI4; NbExp=3; IntAct=EBI-372432, EBI-19944212;
CC Q8WW01; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-372432, EBI-2548751;
CC Q8WW01; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-372432, EBI-10302990;
CC Q8WW01; Q8TCD6: PHOSPHO2; NbExp=5; IntAct=EBI-372432, EBI-2861380;
CC Q8WW01; Q6P1J6-2: PLB1; NbExp=3; IntAct=EBI-372432, EBI-10694821;
CC Q8WW01; P62487: POLR2G; NbExp=3; IntAct=EBI-372432, EBI-347928;
CC Q8WW01; P78424: POU6F2; NbExp=3; IntAct=EBI-372432, EBI-12029004;
CC Q8WW01; Q04864-2: REL; NbExp=3; IntAct=EBI-372432, EBI-10829018;
CC Q8WW01; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-372432, EBI-745958;
CC Q8WW01; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-372432, EBI-11139477;
CC Q8WW01; Q08117-2: TLE5; NbExp=3; IntAct=EBI-372432, EBI-11741437;
CC Q8WW01; Q96PF2: TSSK2; NbExp=3; IntAct=EBI-372432, EBI-852089;
CC Q8WW01; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-372432, EBI-11975223;
CC Q8WW01; Q96NC0: ZMAT2; NbExp=5; IntAct=EBI-372432, EBI-2682299;
CC Q8WW01; Q86TJ5: ZNF554; NbExp=3; IntAct=EBI-372432, EBI-19137100;
CC Q8WW01; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-372432, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus, nucleolus
CC {ECO:0000305}. Note=May be transiently localized in the nucleolus.
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WW01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WW01-2; Sequence=VSP_042723;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis and
CC uterus. {ECO:0000269|PubMed:11318611}.
CC -!- DISEASE: Pontocerebellar hypoplasia 2F (PCH2F) [MIM:617026]: A
CC neurodevelopmental disorder characterized by progressive microcephaly,
CC cognitive and motor delay, poor or absent speech, seizures, and
CC spasticity. PCH2F inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:25558065, ECO:0000269|PubMed:27392077}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SEN15 family. {ECO:0000305}.
CC -!- CAUTION: Although only weakly related to the S.cerevisiae SEN15
CC protein, it probably displays the same function within the tRNA
CC splicing endonuclease complex. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG60614.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF288394; AAG60614.1; ALT_INIT; mRNA.
DR EMBL; AK296655; BAG59252.1; -; mRNA.
DR EMBL; AL157943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91174.1; -; Genomic_DNA.
DR EMBL; BC022030; AAH22030.1; -; mRNA.
DR CCDS; CCDS1361.1; -. [Q8WW01-1]
DR CCDS; CCDS44286.1; -. [Q8WW01-2]
DR RefSeq; NP_001120866.1; NM_001127394.3. [Q8WW01-2]
DR RefSeq; NP_001287693.1; NM_001300764.1.
DR RefSeq; NP_001287695.1; NM_001300766.1.
DR RefSeq; NP_443197.1; NM_052965.3. [Q8WW01-1]
DR PDB; 2GW6; NMR; -; A/B=36-157.
DR PDB; 6Z9U; X-ray; 2.10 A; B/D=23-170.
DR PDBsum; 2GW6; -.
DR PDBsum; 6Z9U; -.
DR AlphaFoldDB; Q8WW01; -.
DR BMRB; Q8WW01; -.
DR SMR; Q8WW01; -.
DR BioGRID; 125513; 59.
DR CORUM; Q8WW01; -.
DR IntAct; Q8WW01; 41.
DR MINT; Q8WW01; -.
DR STRING; 9606.ENSP00000355299; -.
DR GlyGen; Q8WW01; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WW01; -.
DR PhosphoSitePlus; Q8WW01; -.
DR BioMuta; TSEN15; -.
DR DMDM; 50401628; -.
DR EPD; Q8WW01; -.
DR jPOST; Q8WW01; -.
DR MassIVE; Q8WW01; -.
DR MaxQB; Q8WW01; -.
DR PaxDb; Q8WW01; -.
DR PeptideAtlas; Q8WW01; -.
DR PRIDE; Q8WW01; -.
DR ProteomicsDB; 74840; -. [Q8WW01-1]
DR ProteomicsDB; 74841; -. [Q8WW01-2]
DR Antibodypedia; 34450; 111 antibodies from 17 providers.
DR DNASU; 116461; -.
DR Ensembl; ENST00000423085.7; ENSP00000402002.2; ENSG00000198860.14. [Q8WW01-2]
DR Ensembl; ENST00000645668.2; ENSP00000493902.2; ENSG00000198860.14. [Q8WW01-1]
DR GeneID; 116461; -.
DR KEGG; hsa:116461; -.
DR MANE-Select; ENST00000645668.2; ENSP00000493902.2; NM_052965.4; NP_443197.1.
DR UCSC; uc001gqt.5; human. [Q8WW01-1]
DR CTD; 116461; -.
DR DisGeNET; 116461; -.
DR GeneCards; TSEN15; -.
DR HGNC; HGNC:16791; TSEN15.
DR HPA; ENSG00000198860; Low tissue specificity.
DR MalaCards; TSEN15; -.
DR MIM; 608756; gene.
DR MIM; 617026; phenotype.
DR neXtProt; NX_Q8WW01; -.
DR OpenTargets; ENSG00000198860; -.
DR Orphanet; 2524; Pontocerebellar hypoplasia type 2.
DR PharmGKB; PA162407135; -.
DR VEuPathDB; HostDB:ENSG00000198860; -.
DR eggNOG; ENOG502S21U; Eukaryota.
DR GeneTree; ENSGT00390000014781; -.
DR HOGENOM; CLU_130469_1_0_1; -.
DR InParanoid; Q8WW01; -.
DR OMA; HKSIRHV; -.
DR OrthoDB; 1522443at2759; -.
DR PhylomeDB; Q8WW01; -.
DR TreeFam; TF336144; -.
DR BioCyc; MetaCyc:HS13020-MON; -.
DR BRENDA; 4.6.1.16; 2681.
DR PathwayCommons; Q8WW01; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; Q8WW01; -.
DR BioGRID-ORCS; 116461; 42 hits in 1035 CRISPR screens.
DR ChiTaRS; TSEN15; human.
DR EvolutionaryTrace; Q8WW01; -.
DR GeneWiki; C1orf19; -.
DR GenomeRNAi; 116461; -.
DR Pharos; Q8WW01; Tbio.
DR PRO; PR:Q8WW01; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8WW01; protein.
DR Bgee; ENSG00000198860; Expressed in left ventricle myocardium and 181 other tissues.
DR ExpressionAtlas; Q8WW01; baseline and differential.
DR Genevisible; Q8WW01; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:InterPro.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR018593; tRNA-endonuc_su_Sen15.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf.
DR Pfam; PF09631; Sen15; 1.
DR SUPFAM; SSF53032; SSF53032; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disease variant; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; tRNA processing.
FT CHAIN 1..171
FT /note="tRNA-splicing endonuclease subunit Sen15"
FT /id="PRO_0000194023"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 120..171
FT /note="REILKASRKLQGDPDLPMSFTLAIVESDSTIVYYKLTDGFMLPDPQNISLRR
FT -> FLLEDDIHVS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042723"
FT VARIANT 19
FT /note="G -> D (in dbSNP:rs2274432)"
FT /id="VAR_019457"
FT VARIANT 59
FT /note="Q -> H (in dbSNP:rs1046934)"
FT /id="VAR_019458"
FT VARIANT 76
FT /note="W -> G (in PCH2F; Almost complete loss of tRNA-
FT intron endonuclease activity in vitro; may affect protein
FT levels; dbSNP:rs730882223)"
FT /evidence="ECO:0000269|PubMed:25558065,
FT ECO:0000269|PubMed:27392077"
FT /id="VAR_077061"
FT VARIANT 116
FT /note="H -> Y (in PCH2F; Almost complete loss of tRNA-
FT intron endonuclease activity in vitro; dbSNP:rs879253780)"
FT /evidence="ECO:0000269|PubMed:27392077"
FT /id="VAR_077062"
FT VARIANT 152
FT /note="Y -> C (in PCH2F; Almost complete loss of tRNA-
FT intron endonuclease activity in vitro; may affect protein
FT levels; dbSNP:rs879253779)"
FT /evidence="ECO:0000269|PubMed:27392077"
FT /id="VAR_077063"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:6Z9U"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2GW6"
FT HELIX 57..72
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:6Z9U"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2GW6"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6Z9U"
SQ SEQUENCE 171 AA; 18641 MW; E728BF39A89DD1FB CRC64;
MEERGDSEPT PGCSGLGPGG VRGFGDGGGA PSWAPEDAWM GTHPKYLEMM ELDIGDATQV
YVAFLVYLDL MESKSWHEVN CVGLPELQLI CLVGTEIEGE GLQTVVPTPI TASLSHNRIR
EILKASRKLQ GDPDLPMSFT LAIVESDSTI VYYKLTDGFM LPDPQNISLR R
