SEN54_HUMAN
ID SEN54_HUMAN Reviewed; 526 AA.
AC Q7Z6J9; Q86WV3; Q86XE4; Q8N9H2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=tRNA-splicing endonuclease subunit Sen54;
DE AltName: Full=SEN54 homolog;
DE Short=HsSEN54;
DE AltName: Full=tRNA-intron endonuclease Sen54;
GN Name=TSEN54; Synonyms=SEN54;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASP-4.
RC TISSUE=Cerebellum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASP-4;
RP ASN-347 AND VAL-437.
RC TISSUE=Blood, and Uterus;
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 [4]
RP FUNCTION, AND COMPONENT OF A COMPLEX WITH SEN2; SEN15; 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, VARIANT [LARGE SCALE ANALYSIS]
RP ASP-4, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP INVOLVEMENT IN PCH5.
RX PubMed=21368912; DOI=10.1038/ejhg.2011.8;
RA Namavar Y., Chitayat D., Barth P.G., van Ruissen F., de Wissel M.B.,
RA Poll-The B.T., Silver R., Baas F.;
RT "TSEN54 mutations cause pontocerebellar hypoplasia type 5.";
RL Eur. J. Hum. Genet. 19:724-726(2011).
RN [9]
RP INVOLVEMENT IN PCH4.
RX PubMed=21824568; DOI=10.1016/j.pediatrneurol.2011.05.009;
RA Rudaks L.I., Moore L., Shand K.L., Wilkinson C., Barnett C.P.;
RT "Novel TSEN54 mutation causing pontocerebellar hypoplasia type 4.";
RL Pediatr. Neurol. 45:185-188(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, VARIANT [LARGE SCALE ANALYSIS]
RP ASP-4, AND IDENTIFICATION BY MASS 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-180 AND SER-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-316, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP VARIANT PCH2A SER-307, AND VARIANTS PCH4 PRO-93 AND SER-307.
RX PubMed=18711368; DOI=10.1038/ng.204;
RA Budde B.S., Namavar Y., Barth P.G., Poll-The B.T., Nuernberg G., Becker C.,
RA van Ruissen F., Weterman M.A.J., Fluiter K., te Beek E.T., Aronica E.,
RA van der Knaap M.S., Hoehne W., Toliat M.R., Crow Y.J., Steinling M.,
RA Voit T., Roelenso F., Brussel W., Brockmann K., Kyllerman M.,
RA Boltshauser E., Hammersen G., Willemsen M., Basel-Vanagaite L.,
RA Kraegeloh-Mann I., de Vries L.S., Sztriha L., Muntoni F., Ferrie C.D.,
RA Battini R., Hennekam R.C.M., Grillo E., Beemer F.A., Stoets L.M.E.,
RA Wollnik B., Nuernberg P., Baas F.;
RT "tRNA splicing endonuclease mutations cause pontocerebellar hypoplasia.";
RL Nat. Genet. 40:1113-1118(2008).
RN [14]
RP VARIANTS PCH2A ASP-119 AND SER-307.
RX PubMed=23307886; DOI=10.1177/0883073812470002;
RA Battini R., D'Arrigo S., Cassandrini D., Guzzetta A., Fiorillo C.,
RA Pantaleoni C., Romano A., Alfei E., Cioni G., Santorelli F.M.;
RT "Novel mutations in TSEN54 in pontocerebellar hypoplasia type 2.";
RL J. Child Neurol. 29:520-525(2014).
RN [15]
RP VARIANT VAL-85.
RX PubMed=24938831; DOI=10.3892/mmr.2014.2342;
RA Qian Y., Wang H., Jin T., Wang Y., Fang L., Chen Y., Chen L.;
RT "A familial late-onset hereditary ataxia mimicking pontocerebellar
RT hypoplasia caused by a novel TSEN54 mutation.";
RL Mol. Med. Report. 10:1423-1425(2014).
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. There
CC are no conserved sequences at the splice sites, but the intron is
CC invariably located at the same site in the gene, placing the splice
CC sites an invariant distance from the constant structural features of
CC the tRNA body. The tRNA splicing endonuclease is also involved in mRNA
CC processing via its association with pre-mRNA 3'-end processing factors,
CC establishing a link between pre-tRNA splicing and pre-mRNA 3'-end
CC formation, suggesting that the endonuclease subunits function in
CC multiple RNA-processing events. {ECO:0000269|PubMed:15109492}.
CC -!- SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of
CC TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA splicing endonuclease
CC complex also contains proteins of the pre-mRNA 3'-end processing
CC machinery such as CLP1, CPSF1, CPSF4 and CSTF2. Also belongs to a
CC complex containing isoform 2 of SEN2.
CC -!- INTERACTION:
CC Q7Z6J9; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2559824, EBI-10961624;
CC Q7Z6J9; Q92989: CLP1; NbExp=5; IntAct=EBI-2559824, EBI-2559831;
CC Q7Z6J9; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2559824, EBI-5916454;
CC Q7Z6J9; Q15306: IRF4; NbExp=3; IntAct=EBI-2559824, EBI-751345;
CC Q7Z6J9; Q15323: KRT31; NbExp=3; IntAct=EBI-2559824, EBI-948001;
CC Q7Z6J9; Q9UBR4-2: LHX3; NbExp=5; IntAct=EBI-2559824, EBI-12039345;
CC Q7Z6J9; Q969G2: LHX4; NbExp=3; IntAct=EBI-2559824, EBI-2865388;
CC Q7Z6J9; P25791-3: LMO2; NbExp=3; IntAct=EBI-2559824, EBI-11959475;
CC Q7Z6J9; Q96DV4: MRPL38; NbExp=3; IntAct=EBI-2559824, EBI-720441;
CC Q7Z6J9; P41227: NAA10; NbExp=3; IntAct=EBI-2559824, EBI-747693;
CC Q7Z6J9; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-2559824, EBI-10963850;
CC Q7Z6J9; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-2559824, EBI-10271199;
CC Q7Z6J9; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-2559824, EBI-726876;
CC Q7Z6J9; P36406: TRIM23; NbExp=3; IntAct=EBI-2559824, EBI-740098;
CC Q7Z6J9; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-2559824, EBI-11059915;
CC Q7Z6J9; Q8NCE0: TSEN2; NbExp=11; IntAct=EBI-2559824, EBI-2559818;
CC Q7Z6J9; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2559824, EBI-12030590;
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=Q7Z6J9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6J9-2; Sequence=VSP_010988, VSP_010989;
CC -!- DISEASE: Pontocerebellar hypoplasia 4 (PCH4) [MIM:225753]: A disorder
CC characterized by an abnormally small cerebellum and brainstem, severe
CC neonatal encephalopathy, microcephaly, myoclonus and muscular
CC hypertonia. There is a severe inferior olivary and pontine neuronal
CC loss and a diffuse white matter gliosis. {ECO:0000269|PubMed:18711368,
CC ECO:0000269|PubMed:21824568}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Pontocerebellar hypoplasia 2A (PCH2A) [MIM:277470]: A disorder
CC characterized by an abnormally small cerebellum and brainstem, and
CC progressive microcephaly from birth combined with extrapyramidal
CC dyskinesia. Severe chorea occurs and epilepsy is frequent. There are no
CC signs of spinal cord anterior horn cells degeneration.
CC {ECO:0000269|PubMed:18711368, ECO:0000269|PubMed:23307886}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Pontocerebellar hypoplasia 5 (PCH5) [MIM:610204]: A form of
CC pontocerebellar hypoplasia, a disorder characterized by structural
CC defects of the pons and cerebellum. Brain MRI shows an abnormally small
CC cerebellum and brainstem, decreased cerebral white matter, and a thin
CC corpus callosum. {ECO:0000269|PubMed:21368912}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SEN54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53643.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK094466; BAC04362.1; -; mRNA.
DR EMBL; BC047793; AAH47793.1; -; mRNA.
DR EMBL; AC100787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053643; AAH53643.1; ALT_INIT; mRNA.
DR CCDS; CCDS11724.1; -. [Q7Z6J9-1]
DR RefSeq; NP_997229.2; NM_207346.2. [Q7Z6J9-1]
DR AlphaFoldDB; Q7Z6J9; -.
DR BioGRID; 129721; 42.
DR CORUM; Q7Z6J9; -.
DR IntAct; Q7Z6J9; 22.
DR MINT; Q7Z6J9; -.
DR STRING; 9606.ENSP00000327487; -.
DR iPTMnet; Q7Z6J9; -.
DR PhosphoSitePlus; Q7Z6J9; -.
DR BioMuta; TSEN54; -.
DR DMDM; 296452961; -.
DR EPD; Q7Z6J9; -.
DR jPOST; Q7Z6J9; -.
DR MassIVE; Q7Z6J9; -.
DR MaxQB; Q7Z6J9; -.
DR PaxDb; Q7Z6J9; -.
DR PeptideAtlas; Q7Z6J9; -.
DR PRIDE; Q7Z6J9; -.
DR ProteomicsDB; 69429; -. [Q7Z6J9-1]
DR ProteomicsDB; 69430; -. [Q7Z6J9-2]
DR Antibodypedia; 32191; 58 antibodies from 19 providers.
DR DNASU; 283989; -.
DR Ensembl; ENST00000333213.11; ENSP00000327487.6; ENSG00000182173.14. [Q7Z6J9-1]
DR Ensembl; ENST00000679429.1; ENSP00000505403.1; ENSG00000182173.14. [Q7Z6J9-2]
DR GeneID; 283989; -.
DR KEGG; hsa:283989; -.
DR MANE-Select; ENST00000333213.11; ENSP00000327487.6; NM_207346.3; NP_997229.2.
DR UCSC; uc002jof.2; human. [Q7Z6J9-1]
DR CTD; 283989; -.
DR DisGeNET; 283989; -.
DR GeneCards; TSEN54; -.
DR GeneReviews; TSEN54; -.
DR HGNC; HGNC:27561; TSEN54.
DR HPA; ENSG00000182173; Low tissue specificity.
DR MalaCards; TSEN54; -.
DR MIM; 225753; phenotype.
DR MIM; 277470; phenotype.
DR MIM; 608755; gene.
DR MIM; 610204; phenotype.
DR neXtProt; NX_Q7Z6J9; -.
DR OpenTargets; ENSG00000182173; -.
DR Orphanet; 2524; Pontocerebellar hypoplasia type 2.
DR Orphanet; 166063; Pontocerebellar hypoplasia type 4.
DR PharmGKB; PA142670692; -.
DR VEuPathDB; HostDB:ENSG00000182173; -.
DR eggNOG; KOG4772; Eukaryota.
DR GeneTree; ENSGT00390000004214; -.
DR HOGENOM; CLU_033069_1_0_1; -.
DR InParanoid; Q7Z6J9; -.
DR OMA; AMVLQHI; -.
DR OrthoDB; 684082at2759; -.
DR PhylomeDB; Q7Z6J9; -.
DR TreeFam; TF314691; -.
DR BioCyc; MetaCyc:HS11953-MON; -.
DR BRENDA; 4.6.1.16; 2681.
DR PathwayCommons; Q7Z6J9; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; Q7Z6J9; -.
DR BioGRID-ORCS; 283989; 512 hits in 1091 CRISPR screens.
DR ChiTaRS; TSEN54; human.
DR GenomeRNAi; 283989; -.
DR Pharos; Q7Z6J9; Tbio.
DR PRO; PR:Q7Z6J9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q7Z6J9; protein.
DR Bgee; ENSG00000182173; Expressed in granulocyte and 169 other tissues.
DR ExpressionAtlas; Q7Z6J9; baseline and differential.
DR Genevisible; Q7Z6J9; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000214; C:tRNA-intron endonuclease complex; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IDA:UniProtKB.
DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central.
DR InterPro; IPR024337; tRNA_splic_suSen54.
DR InterPro; IPR024336; tRNA_splic_suSen54_N.
DR PANTHER; PTHR21027; PTHR21027; 1.
DR Pfam; PF12928; tRNA_int_end_N2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; Methylation;
KW mRNA processing; Neurodegeneration; Nucleus; Phosphoprotein;
KW Pontocerebellar hypoplasia; Reference proteome; tRNA processing.
FT CHAIN 1..526
FT /note="tRNA-splicing endonuclease subunit Sen54"
FT /id="PRO_0000194029"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 180
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 157..177
FT /note="VFSHLKRLGYVVRRFQPSSVL -> PPEEVGLCGSTIPTKLCPVPV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010988"
FT VAR_SEQ 178..526
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010989"
FT VARIANT 4
FT /note="E -> D (in dbSNP:rs7216673)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT /id="VAR_019459"
FT VARIANT 38
FT /note="H -> Q (in dbSNP:rs8079373)"
FT /id="VAR_019461"
FT VARIANT 85
FT /note="E -> V (found in familial late-onset hereditary
FT ataxia; unknown pathological significance;
FT dbSNP:rs1179247981)"
FT /evidence="ECO:0000269|PubMed:24938831"
FT /id="VAR_073350"
FT VARIANT 93
FT /note="S -> P (in PCH4; dbSNP:rs113994151)"
FT /evidence="ECO:0000269|PubMed:18711368"
FT /id="VAR_054812"
FT VARIANT 119
FT /note="Y -> D (in PCH2A)"
FT /evidence="ECO:0000269|PubMed:23307886"
FT /id="VAR_073351"
FT VARIANT 137
FT /note="I -> L (in dbSNP:rs11559205)"
FT /id="VAR_057721"
FT VARIANT 307
FT /note="A -> S (in PCH2A and PCH4; dbSNP:rs113994152)"
FT /evidence="ECO:0000269|PubMed:18711368,
FT ECO:0000269|PubMed:23307886"
FT /id="VAR_054813"
FT VARIANT 347
FT /note="K -> N (in dbSNP:rs9911502)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019462"
FT VARIANT 437
FT /note="A -> V (in dbSNP:rs8064529)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019463"
FT VARIANT 525
FT /note="G -> R (in dbSNP:rs11870627)"
FT /id="VAR_057722"
SQ SEQUENCE 526 AA; 58819 MW; 857D95C8F7C39461 CRC64;
MEPEPEPAAV EVPAGRVLSA RELFAARSRS QKLPQRSHGP KDFLPDGSAA QAERLRRCRE
ELWQLLAEQR VERLGSLVAA EWRPEEGFVE LKSPAGKFWQ TMGFSEQGRQ RLHPEEALYL
LECGSIHLFH QDLPLSIQEA YQLLLTDHTV TFLQYQVFSH LKRLGYVVRR FQPSSVLSPY
ERQLNLDASV QHLEDGDGKR KRSSSSPRSI NKKAKALDNS LQPKSLAASS PPPCSQPSQC
PEEKPQESSP MKGPGGPFQL LGSLGPSPGP AREGVGCSWE SGRAENGVTG AGKRRWNFEQ
ISFPNMASDS RHTLLRAPAP ELLPANVAGR ETDAESWCQK LNQRKEKLSR REREHHAEAA
QFQEDVNADP EVQRCSSWRE YKELLQRRQV QRSQRRAPHL WGQPVTPLLS PGQASSPAVV
LQHISVLQTT HLPDGGARLL EKSGGLEIIF DVYQADAVAT FRKNNPGKPY ARMCISGFDE
PVPDLCSLKR LSYQSGDVPL IFALVDHGDI SFYSFRDFTL PQDVGH
