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Identification
HMDB Protein ID HMDBP01675
Secondary Accession Numbers
  • 7012
Name H/ACA ribonucleoprotein complex subunit 4
Synonyms
  1. CBF5 homolog
  2. Dyskerin
  3. Nopp140-associated protein of 57 kDa
  4. Nucleolar protein NAP57
  5. Nucleolar protein family A member 4
  6. snoRNP protein DKC1
Gene Name DKC1
Protein Type Enzyme
Biological Properties
General Function Involved in RNA processing
Specific Function Required for ribosome biogenesis and telomere maintenance. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. Also required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
catalytic activity
nucleic acid binding
isomerase activity
pseudouridine synthase activity
intramolecular transferase activity
rna binding
Process
rna metabolic process
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
rna processing
rna modification
pseudouridine synthesis
Cellular Location
  1. Nucleus
  2. Nucleus
  3. nucleolus
  4. Cajal body
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs DKC1
Gene Sequence
>1545 bp
ATGGCGGATGCGGAAGTAATTATTTTGCCAAAGAAACATAAGAAGAAAAAGGAGCGGAAG
TCATTGCCAGAAGAAGATGTAGCCGAAATACAACACGCTGAAGAATTTCTTATCAAACCT
GAATCCAAAGTTGCTAAGTTGGACACGTCTCAGTGGCCCCTTTTGCTAAAGAATTTTGAT
AAGCTGAATGTAAGGACAACACACTATACACCTCTTGCATGTGGTTCAAATCCTCTGAAG
AGAGAGATTGGGGACTATATCAGGACAGGTTTCATTAATCTTGACAAGCCCTCTAACCCC
TCTTCCCATGAGGTGGTAGCCTGGATTCGACGGATACTTCGGGTGGAGAAGACAGGGCAC
AGTGGTACTCTGGATCCCAAGGTGACTGGTTGTTTAATCGTGTGCATAGAACGAGCCACT
CGCTTGGTGAAGTCACAACAGAGTGCAGGCAAAGAGTATGTGGGGATTGTCCGGCTGCAC
AATGCTATTGAAGGGGGGACCCAGCTTTCTAGGGCCCTAGAAACTCTGACAGGTGCCTTA
TTCCAGCGACCCCCACTTATTGCTGCAGTAAAGAGGCAGCTCCGAGTGAGGACCATCTAC
GAGAGCAAAATGATTGAATACGATCCTGAAAGAAGATTAGGAATCTTTTGGGTGAGTTGT
GAGGCTGGCACCTACATTCGGACATTATGTGTGCACCTTGGTTTGTTATTGGGAGTTGGT
GGTCAGATGCAGGAGCTTCGGAGGGTTCGTTCTGGAGTCATGAGTGAAAAGGACCACATG
GTGACAATGCATGATGTGCTTGATGCTCAGTGGCTGTATGATAACCACAAGGATGAGAGT
TACCTGCGGCGAGTTGTTTACCCTTTGGAAAAGCTGTTGACATCTCATAAACGGCTGGTT
ATGAAAGACAGTGCAGTAAATGCCATCTGCTATGGGGCCAAGATTATGCTTCCAGGTGTT
CTTCGATATGAGGACGGCATTGAGGTCAATCAGGAGATTGTGGTTATCACCACCAAAGGA
GAAGCAATCTGCATGGCTATTGCATTAATGACCACAGCGGTCATCTCTACCTGCGACCAT
GGTATAGTAGCCAAGATCAAGAGAGTGATCATGGAGAGAGACACTTACCCTCGGAAGTGG
GGTTTAGGTCCAAAGGCAAGTCAGAAGAAGCTGATGATCAAGCAGGGCCTTCTGGACAAG
CATGGGAAGCCCACAGACAGCACACCTGCCACCTGGAAGCAGGAGTATGTTGACTACAGT
GAGTCTGCCAAAAAAGAGGTGGTTGCTGAAGTGGTAAAAGCCCCGCAGGTAGTTGCCGAA
GCAGCAAAAACTGCGAAGCGGAAGCGAGAGAGTGAGAGTGAAAGTGACGAGACTCCTCCA
GCAGCTCCTCAGTTGATCAAGAAGGAAAAGAAGAAGAGTAAGAAGGACAAGAAGGCCAAA
GCTGGTCTGGAGAGCGGGGCCGAGCCTGGAGATGGGGACAGTGATACCACCAAGAAGAAG
AAGAAGAAGAAGAAAGCAAAAGAGGTAGAATTGGTTTCTGAGTAG
Protein Properties
Number of Residues 514
Molecular Weight 57673.7
Theoretical pI 10.02
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>H/ACA ribonucleoprotein complex subunit 4
MADAEVIILPKKHKKKKERKSLPEEDVAEIQHAEEFLIKPESKVAKLDTSQWPLLLKNFD
KLNVRTTHYTPLACGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGH
SGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGAL
FQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVG
GQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLV
MKDSAVNAICYGAKIMLPGVLRYEDGIEVNQEIVVITTKGEAICMAIALMTTAVISTCDH
GIVAKIKRVIMERDTYPRKWGLGPKASQKKLMIKQGLLDKHGKPTDSTPATWKQEYVDYS
ESAKKEVVAEVVKAPQVVAEAAKTAKRKRESESESDETPPAAPQLIKKEKKKSKKDKKAK
AGLESGAEPGDGDSDTTKKKKKKKKAKEVELVSE
GenBank ID Protein 3873221
UniProtKB/Swiss-Prot ID O60832
UniProtKB/Swiss-Prot Entry Name DKC1_HUMAN
PDB IDs Not Available
GenBank Gene ID AF067008
GeneCard ID DKC1
GenAtlas ID DKC1
HGNC ID HGNC:2890
References
General References
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  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
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  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  8. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  9. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  11. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  12. Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [PubMed:17487921 ]
  13. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  14. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. doi: 10.1002/pmic.200700884. [PubMed:18318008 ]
  15. Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed:16083285 ]
  16. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. doi: 10.1021/ac801708p. [PubMed:19007248 ]
  17. Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ: Functional proteomic analysis of human nucleolus. Mol Biol Cell. 2002 Nov;13(11):4100-9. [PubMed:12429849 ]
  18. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed:16565220 ]
  19. Heiss NS, Knight SW, Vulliamy TJ, Klauck SM, Wiemann S, Mason PJ, Poustka A, Dokal I: X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions. Nat Genet. 1998 May;19(1):32-8. [PubMed:9590285 ]
  20. Knight SW, Heiss NS, Vulliamy TJ, Greschner S, Stavrides G, Pai GS, Lestringant G, Varma N, Mason PJ, Dokal I, Poustka A: X-linked dyskeratosis congenita is predominantly caused by missense mutations in the DKC1 gene. Am J Hum Genet. 1999 Jul;65(1):50-8. [PubMed:10364516 ]
  21. Hassock S, Vetrie D, Giannelli F: Mapping and characterization of the X-linked dyskeratosis congenita (DKC) gene. Genomics. 1999 Jan 1;55(1):21-7. [PubMed:9888995 ]
  22. Heiss NS, Girod A, Salowsky R, Wiemann S, Pepperkok R, Poustka A: Dyskerin localizes to the nucleolus and its mislocalization is unlikely to play a role in the pathogenesis of dyskeratosis congenita. Hum Mol Genet. 1999 Dec;8(13):2515-24. [PubMed:10556300 ]
  23. Mitchell JR, Wood E, Collins K: A telomerase component is defective in the human disease dyskeratosis congenita. Nature. 1999 Dec 2;402(6761):551-5. [PubMed:10591218 ]
  24. Heiss NS, Bachner D, Salowsky R, Kolb A, Kioschis P, Poustka A: Gene structure and expression of the mouse dyskeratosis congenita gene, dkc1. Genomics. 2000 Jul 15;67(2):153-63. [PubMed:10903840 ]
  25. Pogacic V, Dragon F, Filipowicz W: Human H/ACA small nucleolar RNPs and telomerase share evolutionarily conserved proteins NHP2 and NOP10. Mol Cell Biol. 2000 Dec;20(23):9028-40. [PubMed:11074001 ]
  26. Wang C, Meier UT: Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins. EMBO J. 2004 Apr 21;23(8):1857-67. Epub 2004 Mar 25. [PubMed:15044956 ]
  27. Darzacq X, Kittur N, Roy S, Shav-Tal Y, Singer RH, Meier UT: Stepwise RNP assembly at the site of H/ACA RNA transcription in human cells. J Cell Biol. 2006 Apr 24;173(2):207-18. Epub 2006 Apr 17. [PubMed:16618814 ]
  28. Hoareau-Aveilla C, Bonoli M, Caizergues-Ferrer M, Henry Y: hNaf1 is required for accumulation of human box H/ACA snoRNPs, scaRNPs, and telomerase. RNA. 2006 May;12(5):832-40. Epub 2006 Apr 6. [PubMed:16601202 ]
  29. Venteicher AS, Abreu EB, Meng Z, McCann KE, Terns RM, Veenstra TD, Terns MP, Artandi SE: A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis. Science. 2009 Jan 30;323(5914):644-8. doi: 10.1126/science.1165357. [PubMed:19179534 ]
  30. Knight SW, Heiss NS, Vulliamy TJ, Aalfs CM, McMahon C, Richmond P, Jones A, Hennekam RC, Poustka A, Mason PJ, Dokal I: Unexplained aplastic anaemia, immunodeficiency, and cerebellar hypoplasia (Hoyeraal-Hreidarsson syndrome) due to mutations in the dyskeratosis congenita gene, DKC1. Br J Haematol. 1999 Nov;107(2):335-9. [PubMed:10583221 ]
  31. Cossu F, Vulliamy TJ, Marrone A, Badiali M, Cao A, Dokal I: A novel DKC1 mutation, severe combined immunodeficiency (T+B-NK- SCID) and bone marrow transplantation in an infant with Hoyeraal-Hreidarsson syndrome. Br J Haematol. 2002 Dec;119(3):765-8. [PubMed:12437656 ]