DKC1_MOUSE
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 03-AUG-2022, entry version 165.
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, Pancreas,
RC 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}. Note=Also localized to Cajal bodies
CC (coiled bodies). {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}.
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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 iPTMnet; Q9ESX5; -.
DR PhosphoSitePlus; Q9ESX5; -.
DR SwissPalm; Q9ESX5; -.
DR EPD; Q9ESX5; -.
DR jPOST; Q9ESX5; -.
DR MaxQB; Q9ESX5; -.
DR PaxDb; Q9ESX5; -.
DR PeptideAtlas; Q9ESX5; -.
DR PRIDE; Q9ESX5; -.
DR ProteomicsDB; 279717; -.
DR Antibodypedia; 418; 425 antibodies from 39 providers.
DR Ensembl; ENSMUST00000033776; ENSMUSP00000033776; ENSMUSG00000031403.
DR GeneID; 245474; -.
DR KEGG; mmu:245474; -.
DR UCSC; uc009tpo.2; mouse.
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; GPFKEDE; -.
DR OrthoDB; 1070373at2759; -.
DR PhylomeDB; Q9ESX5; -.
DR TreeFam; TF300354; -.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR BioGRID-ORCS; 245474; 28 hits in 72 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 241 other tissues.
DR ExpressionAtlas; Q9ESX5; baseline and differential.
DR Genevisible; Q9ESX5; MM.
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:0051973; P:positive regulation of telomerase activity; IMP: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 Gene3D; 2.30.130.10; -; 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 PANTHER; PTHR23127; PTHR23127; 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; SSF55120; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00425; CBF5; 1.
DR TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR PROSITE; PS50890; PUA; 1.
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
