ID DKC1_MOUSE Reviewed; 509 AA. AC Q9ESX5; Q3UWE5; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 27-MAR-2024, entry version 174. DE RecName: Full=H/ACA ribonucleoprotein complex subunit DKC1; DE EC=5.4.99.- {ECO:0000250|UniProtKB:O60832}; DE AltName: Full=Dyskerin; DE AltName: Full=Nopp140-associated protein of 57 kDa; DE AltName: Full=Nucleolar protein NAP57; DE AltName: Full=Nucleolar protein family A member 4; DE AltName: Full=snoRNP protein DKC1; GN Name=Dkc1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=129/Ola; RX PubMed=10903840; DOI=10.1006/geno.2000.6227; RA Heiss N.S., Baechner D., Salowsky R., Kolb A., Kioschis P., Poustka A.; RT "Gene structure and expression of the mouse dyskeratosis congenita gene, RT dkc1."; RL Genomics 67:153-163(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Colon; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP FUNCTION. RX PubMed=12522253; DOI=10.1126/science.1079447; RA Ruggero D., Grisendi S., Piazza F., Rego E., Mari F., Rao P.H., RA Cordon-Cardo C., Pandolfi P.P.; RT "Dyskeratosis congenita and cancer in mice deficient in ribosomal RNA RT modification."; RL Science 299:259-262(2003). RN [5] RP FUNCTION, AND MUTAGENESIS OF ALA-353 AND GLY-402. RX PubMed=15240872; DOI=10.1073/pnas.0402560101; RA Mochizuki Y., He J., Kulkarni S., Bessler M., Mason P.J.; RT "Mouse dyskerin mutations affect accumulation of telomerase RNA and small RT nucleolar RNA, telomerase activity, and ribosomal RNA processing."; RL Proc. Natl. Acad. Sci. U.S.A. 101:10756-10761(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 AND SER-481, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 AND SER-455, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity RT chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453; SER-455 AND RP SER-508, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453; SER-455; RP THR-458; SER-481; THR-485 AND SER-508, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein CC (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA CC (PubMed:12522253, PubMed:15240872). This involves the isomerization of CC uridine such that the ribose is subsequently attached to C5, instead of CC the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') CC residues, which may serve to stabilize the conformation of rRNAs CC (PubMed:12522253, PubMed:15240872). Required for ribosome biogenesis CC and telomere maintenance (By similarity). Also required for correct CC processing or intranuclear trafficking of TERC, the RNA component of CC the telomerase reverse transcriptase (TERT) holoenzyme (By similarity). CC {ECO:0000250|UniProtKB:O60832, ECO:0000269|PubMed:12522253, CC ECO:0000269|PubMed:15240872}. CC -!- CATALYTIC ACTIVITY: CC Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA; CC Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731, CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; CC Evidence={ECO:0000250|UniProtKB:O60832}; CC -!- SUBUNIT: Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA CC snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3, CC and DKC1/NOLA4, which is presumed to be the catalytic subunit. The CC complex contains a stable core formed by binding of one or two NOP10- CC DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via CC DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which CC may target the specific site of modification within the RNA substrate. CC During assembly, the complex contains NAF1 instead of GAR1/NOLA1. The CC complex also interacts with TERC, which contains a 3'-terminal domain CC related to the box H/ACA snoRNAs. Specific interactions with snoRNAs or CC TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140. CC H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or CC SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is mediated by CC interaction between GAR1 and SMN1 or SMN2. The SMN complex may be CC required for correct assembly of the H/ACA snoRNP complex. Component of CC the telomerase holoenzyme complex composed of one molecule of TERT, one CC molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein CC complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA CC template component (TERC). The telomerase holoenzyme complex is CC associated with TEP1, SMG6/EST1A and POT1. Interacts with SHQ1; this CC interaction may lead to the stabilization of DKC1, from the time of its CC synthesis until its association with NOP10, NHP2, and NAF1 at the CC nascent H/ACA RNA (By similarity). Interacts with HMBOX1 (By CC similarity). Interacts with DHX36 (By similarity). CC {ECO:0000250|UniProtKB:O60832}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000250|UniProtKB:O60832}. Nucleus, Cajal body CC {ECO:0000250|UniProtKB:P40615}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with elevated levels in CC Purkinje cells, the olfactory bulb, and Leydig cells of the testis. CC {ECO:0000269|PubMed:10903840}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, particularly in CC developing epithelial tissues. {ECO:0000269|PubMed:10903840}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ250973; CAC04528.1; -; Genomic_DNA. DR EMBL; AJ250972; CAC04528.1; JOINED; Genomic_DNA. DR EMBL; AJ250974; CAC04528.1; JOINED; Genomic_DNA. DR EMBL; AJ250975; CAC04528.1; JOINED; Genomic_DNA. DR EMBL; AJ250976; CAC04528.1; JOINED; Genomic_DNA. DR EMBL; AJ250978; CAC04528.1; JOINED; Genomic_DNA. DR EMBL; AJ250980; CAC04528.1; JOINED; Genomic_DNA. DR EMBL; AJ250981; CAC04528.1; JOINED; Genomic_DNA. DR EMBL; AJ250979; CAC04528.1; JOINED; Genomic_DNA. DR EMBL; AJ250977; CAC04528.1; JOINED; Genomic_DNA. DR EMBL; AK136418; BAE22970.1; -; mRNA. DR EMBL; AL808110; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS41029.1; -. DR RefSeq; NP_001025478.1; NM_001030307.2. DR AlphaFoldDB; Q9ESX5; -. DR SMR; Q9ESX5; -. DR BioGRID; 232777; 19. DR ComplexPortal; CPX-1124; Telomerase holoenzyme complex. DR IntAct; Q9ESX5; 3. DR MINT; Q9ESX5; -. DR STRING; 10090.ENSMUSP00000033776; -. DR GlyGen; Q9ESX5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9ESX5; -. DR PhosphoSitePlus; Q9ESX5; -. DR SwissPalm; Q9ESX5; -. DR EPD; Q9ESX5; -. DR jPOST; Q9ESX5; -. DR MaxQB; Q9ESX5; -. DR PaxDb; 10090-ENSMUSP00000033776; -. DR PeptideAtlas; Q9ESX5; -. DR ProteomicsDB; 279717; -. DR Pumba; Q9ESX5; -. DR Antibodypedia; 418; 471 antibodies from 39 providers. DR Ensembl; ENSMUST00000033776.15; ENSMUSP00000033776.9; ENSMUSG00000031403.15. DR GeneID; 245474; -. DR KEGG; mmu:245474; -. DR UCSC; uc009tpo.2; mouse. DR AGR; MGI:1861727; -. DR CTD; 1736; -. DR MGI; MGI:1861727; Dkc1. DR VEuPathDB; HostDB:ENSMUSG00000031403; -. DR eggNOG; KOG2529; Eukaryota. DR GeneTree; ENSGT00510000047092; -. DR HOGENOM; CLU_032087_3_2_1; -. DR InParanoid; Q9ESX5; -. DR OMA; CIVRLHD; -. DR OrthoDB; 5472308at2759; -. DR PhylomeDB; Q9ESX5; -. DR TreeFam; TF300354; -. DR Reactome; R-MMU-171319; Telomere Extension By Telomerase. DR BioGRID-ORCS; 245474; 28 hits in 76 CRISPR screens. DR ChiTaRS; Dkc1; mouse. DR PRO; PR:Q9ESX5; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; Q9ESX5; Protein. DR Bgee; ENSMUSG00000031403; Expressed in manus and 244 other cell types or tissues. DR ExpressionAtlas; Q9ESX5; baseline and differential. DR GO; GO:0031429; C:box H/ACA snoRNP complex; ISO:MGI. DR GO; GO:0090661; C:box H/ACA telomerase RNP complex; ISO:MGI. DR GO; GO:0015030; C:Cajal body; IDA:MGI. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0005730; C:nucleolus; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0005697; C:telomerase holoenzyme complex; ISS:UniProtKB. DR GO; GO:0034513; F:box H/ACA snoRNA binding; ISO:MGI. DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; ISO:MGI. DR GO; GO:0003720; F:telomerase activity; ISO:MGI. DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI. DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IBA:GO_Central. DR GO; GO:0033979; P:box H/ACA RNA metabolic process; IMP:MGI. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; ISS:UniProtKB. DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:MGI. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; ISO:MGI. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:MGI. DR GO; GO:1904872; P:regulation of telomerase RNA localization to Cajal body; ISO:MGI. DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IMP:MGI. DR GO; GO:0090666; P:scaRNA localization to Cajal body; ISO:MGI. DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; ISO:MGI. DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0090669; P:telomerase RNA stabilization; ISO:MGI. DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB. DR CDD; cd02572; PseudoU_synth_hDyskerin; 1. DR CDD; cd21148; PUA_Cbf5; 1. DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1. DR Gene3D; 2.30.130.10; PUA domain; 1. DR InterPro; IPR012960; Dyskerin-like. DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf. DR InterPro; IPR002501; PsdUridine_synth_N. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR036974; PUA_sf. DR InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam. DR InterPro; IPR032819; TruB_C. DR InterPro; IPR004521; Uncharacterised_CHP00451. DR NCBIfam; TIGR00425; CBF5; 1. DR NCBIfam; TIGR00451; unchar_dom_2; 1. DR PANTHER; PTHR23127; CENTROMERE/MICROTUBULE BINDING PROTEIN CBF5; 1. DR PANTHER; PTHR23127:SF0; H_ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT DKC1; 1. DR Pfam; PF08068; DKCLD; 1. DR Pfam; PF01472; PUA; 1. DR Pfam; PF16198; TruB_C_2; 1. DR Pfam; PF01509; TruB_N; 1. DR SMART; SM01136; DKCLD; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF55120; Pseudouridine synthase; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. DR PROSITE; PS50890; PUA; 1. DR Genevisible; Q9ESX5; MM. PE 1: Evidence at protein level; KW Acetylation; Isomerase; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosome biogenesis; RNA-binding; KW rRNA processing; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:O60832" FT CHAIN 2..509 FT /note="H/ACA ribonucleoprotein complex subunit DKC1" FT /id="PRO_0000121984" FT DOMAIN 297..372 FT /note="PUA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..21 FT /note="Nucleolar localization" FT /evidence="ECO:0000250" FT REGION 446..509 FT /note="Nuclear and nucleolar localization" FT /evidence="ECO:0000250" FT REGION 447..509 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 447..466 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 125 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P60340" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:O60832" FT MOD_RES 387 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60832" FT MOD_RES 451 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 453 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 455 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18630941, FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079" FT MOD_RES 458 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 481 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 485 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 508 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O60832" FT CROSSLNK 39 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O60832" FT CROSSLNK 43 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O60832" FT CROSSLNK 191 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O60832" FT CROSSLNK 394 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O60832" FT CROSSLNK 413 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:O60832" FT CROSSLNK 413 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:O60832" FT CROSSLNK 424 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O60832" FT MUTAGEN 353 FT /note="A->V: Destabilization of TERC, impaired telomerase FT function, and reduced rRNA pseudouridylation and pre-rRNA FT processing." FT /evidence="ECO:0000269|PubMed:15240872" FT MUTAGEN 402 FT /note="G->E: Reduced rRNA pseudouridylation and pre-rRNA FT processing." FT /evidence="ECO:0000269|PubMed:15240872" FT CONFLICT 234..241 FT /note="GLLLGVGG -> CFVLGSGC (in Ref. 1; CAC04528)" FT /evidence="ECO:0000305" SQ SEQUENCE 509 AA; 57402 MW; 17C50FDF48912A14 CRC64; MADAEVITFP KKHKKKKDRK PLQEDDVAEI QHAEEFLIKP ESKVAQLDTS QWPLLLKNFD KLNVRTAHYT PLPCGSNPLK REIGDYIRTG FINLDKPSNP SSHEVVAWIR RILRVEKTGH SGTLDPKVTG CLIVCIERAT RLVKSQQSAG KEYVGIVRLH NAIEGGTQLS RALETLTGAL FQRPPLIAAV KRQLRVRTIY ESKMIEYDPE RRLGIFWVSC EAGTYIRTLC VHLGLLLGVG GQMQELRRVR SGVMSEKDHM VTMHDVLDAQ WLYDNHKDES YLRRVVYPLE KLLTSHKRLV MKDSAVNAIC YGAKIMLPGL LRYEDGIEVN QEIVVITTKG EAICMAIALM TTAVISTCDH GIVAKIKRVI MERDTYPRKW GLGPKASQKK MMIKQGLLDK HGKPTDNTPA TWKQDYIDYS DSGKNTLVTE AVQAPQLAAE AVNVIKRKRD SESESDETPT VPQLKEKKKK KDKKPKTVLE SGGETGDGDN DTTKKKKKKK VKVVEEMSE //