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O60832 (DKC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
H/ACA ribonucleoprotein complex subunit 4

EC=5.4.99.-
Alternative name(s):
CBF5 homolog
Dyskerin
Nopp140-associated protein of 57 kDa
Nucleolar protein NAP57
Nucleolar protein family A member 4
snoRNP protein DKC1
Gene names
Name:DKC1
Synonyms:NOLA4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1: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.

Isoform 3:Promotes cell to cell and cell to substratum adhesion, increases the cell proliferation rate and leads to cytokeratin hyper-expression (when overexpressed in HeLa cells).

Catalytic activity

RNA uridine = RNA pseudouridine.

Subunit structure

Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3, and DKC1/NOLA4, which is presumed to be the catalytic subunit. The complex contains a stable core formed by binding of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which may target the specific site of modification within the RNA substrate. During assembly, the complex contains NAF1 instead of GAR1/NOLA1. The complex also interacts with TERC, which contains a 3'-terminal domain related to the box H/ACA snoRNAs. Specific interactions with snoRNAs or TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140. H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is mediated by interaction between GAR1 and SMN1 or SMN2. The SMN complex may be required for correct assembly of the H/ACA snoRNP complex. Component of the telomerase holoenzyme complex at least composed of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). Interacts with SHQ1; this interaction may lead to the stabilization of DKC1, from the time of its synthesis until its association with NOP10, NHP2, and NAF1 at the nascent H/ACA RNA. Ref.12 Ref.16 Ref.18 Ref.25 Ref.27

Subcellular location

Isoform 1: Nucleusnucleolus. NucleusCajal body. Note: Also localized to Cajal bodies (coiled bodies). Ref.5 Ref.9 Ref.10 Ref.13

Isoform 3: Cytoplasm Ref.5 Ref.9 Ref.10 Ref.13.

Tissue specificity

Ubiquitously expressed. Ref.11

Involvement in disease

Dyskeratosis congenita, X-linked (DKCX) [MIM:305000]: A rare, progressive bone marrow failure syndrome characterized by the triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.34 Ref.35 Ref.36 Ref.37

Hoyeraal-Hreidarsson syndrome (HHS) [MIM:305000]: A clinically severe variant of dyskeratosis congenita that is characterized by multisystem involvement, early onset in utero, and often results in death in childhood. Affected individuals show intrauterine growth retardation, microcephaly, cerebellar hypoplasia, delayed development, and bone marrow failure resulting in immunodeficiency.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32 Ref.33

Sequence similarities

Belongs to the pseudouridine synthase TruB family.

Contains 1 PUA domain.

Ontologies

Keywords
   Biological processRibosome biogenesis
rRNA processing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Dyskeratosis congenita
   LigandRNA-binding
   Molecular functionIsomerase
Ribonucleoprotein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Traceable author statement Ref.1. Source: ProtInc

cell proliferation

Traceable author statement Ref.10. Source: ProtInc

pseudouridine synthesis

Inferred from electronic annotation. Source: InterPro

rRNA processing

Traceable author statement Ref.9. Source: ProtInc

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via telomerase

Traceable author statement. Source: Reactome

   Cellular_componentCajal body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: LIFEdb

telomerase holoenzyme complex

Inferred from direct assay PubMed 12135483. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.10. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

pseudouridine synthase activity

Inferred from electronic annotation. Source: InterPro

telomerase activity

Inferred from direct assay PubMed 12135483. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60832-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 3 (identifier: O60832-2)

The sequence of this isoform differs from the canonical sequence as follows:
     420-514: SESAKKEVVA...KAKEVELVSE → R

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 514513H/ACA ribonucleoprotein complex subunit 4
PRO_0000121983

Regions

Domain296 – 37176PUA
Region2 – 2120Nucleolar localization
Region446 – 51469Nuclear and nucleolar localization
Compositional bias11 – 177Poly-Lys

Sites

Active site1251Nucleophile By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.23 Ref.31
Modified residue211Phosphoserine Ref.15 Ref.20 Ref.21 Ref.26 Ref.28 Ref.30
Modified residue4511Phosphoserine Ref.28 Ref.30
Modified residue4531Phosphoserine Ref.28 Ref.30
Modified residue4551Phosphoserine Ref.30
Modified residue4851Phosphoserine Ref.21 Ref.26 Ref.28 Ref.30
Modified residue4941Phosphoserine Ref.17 Ref.21 Ref.26 Ref.28 Ref.30
Modified residue5131Phosphoserine Ref.15 Ref.24 Ref.28 Ref.30

Natural variations

Alternative sequence420 – 51495SESAK…ELVSE → R in isoform 3.
VSP_042422
Natural variant21A → V in DKCX. Ref.2
Corresponds to variant rs121912303 [ dbSNP | Ensembl ].
VAR_010076
Natural variant361F → V in DKCX. Ref.1
Corresponds to variant rs121912293 [ dbSNP | Ensembl ].
VAR_006811
Natural variant371Missing in DKCX. Ref.1
VAR_006812
Natural variant381I → T in HHS. Ref.33
Corresponds to variant rs28936072 [ dbSNP | Ensembl ].
VAR_015674
Natural variant391K → E in DKCX. Ref.2
Corresponds to variant rs121912296 [ dbSNP | Ensembl ].
VAR_010077
Natural variant401P → R in DKCX. Ref.1
Corresponds to variant rs121912292 [ dbSNP | Ensembl ].
VAR_006813
Natural variant411E → K in DKCX. Ref.2
Corresponds to variant rs121912302 [ dbSNP | Ensembl ].
VAR_010078
Natural variant491T → M in HHS. Ref.32
Corresponds to variant rs121912304 [ dbSNP | Ensembl ].
VAR_015675
Natural variant561L → S in DKCX; due to a 2 nucleotide inversion. Ref.36
Corresponds to variant rs121912287 [ dbSNP | Ensembl ].
VAR_063821
Natural variant651R → T in DKCX. Ref.2
Corresponds to variant rs121912301 [ dbSNP | Ensembl ].
VAR_010079
Natural variant661T → A in DKCX. Ref.2
Corresponds to variant rs121912297 [ dbSNP | Ensembl ].
VAR_010080
Natural variant721L → F in DKCX. Ref.35
Corresponds to variant rs121912306 [ dbSNP | Ensembl ].
VAR_063822
Natural variant721L → Y in DKCX; requires 2 nucleotide substitutions. Ref.1
Corresponds to variant rs121912294 [ dbSNP | Ensembl ].
VAR_006814
Natural variant1211S → G in HHS. Ref.32
Corresponds to variant rs121912305 [ dbSNP | Ensembl ].
VAR_015676
Natural variant2231G → D.
Corresponds to variant rs2728533 [ dbSNP | Ensembl ].
VAR_022553
Natural variant3171L → F in DKCX. Ref.37
Corresponds to variant rs121912290 [ dbSNP | Ensembl ].
VAR_063823
Natural variant3211L → V in DKCX. Ref.2
Corresponds to variant rs2728726 [ dbSNP | Ensembl ].
VAR_010081
Natural variant3221R → Q in DKCX. Ref.37
Corresponds to variant rs121912291 [ dbSNP | Ensembl ].
VAR_063824
Natural variant3501M → I in DKCX. Ref.2
Corresponds to variant rs121912298 [ dbSNP | Ensembl ].
VAR_010082
Natural variant3501M → T in DKCX. Ref.2
Corresponds to variant rs121912300 [ dbSNP | Ensembl ].
VAR_010083
Natural variant3531A → V in DKCX and HHS. Ref.2 Ref.34
Corresponds to variant rs121912288 [ dbSNP | Ensembl ].
VAR_009264
Natural variant4021G → E in DKCX. Ref.1
Corresponds to variant rs121912295 [ dbSNP | Ensembl ].
VAR_006815
Natural variant4021G → R in DKCX. Ref.2
Corresponds to variant rs121912299 [ dbSNP | Ensembl ].
VAR_010084
Natural variant4091P → L in DKCX. Ref.34
Corresponds to variant rs121912289 [ dbSNP | Ensembl ].
VAR_063825

Experimental info

Sequence conflict371L → F in AAB94299. Ref.4
Sequence conflict2851V → F in AAH09928. Ref.7
Sequence conflict4461K → KVSGMLSSVWN in CAB51168. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 12474DBEEFEB471C

FASTA51457,674
        10         20         30         40         50         60 
MADAEVIILP KKHKKKKERK SLPEEDVAEI QHAEEFLIKP ESKVAKLDTS QWPLLLKNFD 

        70         80         90        100        110        120 
KLNVRTTHYT PLACGSNPLK REIGDYIRTG FINLDKPSNP SSHEVVAWIR RILRVEKTGH 

       130        140        150        160        170        180 
SGTLDPKVTG CLIVCIERAT RLVKSQQSAG KEYVGIVRLH NAIEGGTQLS RALETLTGAL 

       190        200        210        220        230        240 
FQRPPLIAAV KRQLRVRTIY ESKMIEYDPE RRLGIFWVSC EAGTYIRTLC VHLGLLLGVG 

       250        260        270        280        290        300 
GQMQELRRVR SGVMSEKDHM VTMHDVLDAQ WLYDNHKDES YLRRVVYPLE KLLTSHKRLV 

       310        320        330        340        350        360 
MKDSAVNAIC YGAKIMLPGV LRYEDGIEVN QEIVVITTKG EAICMAIALM TTAVISTCDH 

       370        380        390        400        410        420 
GIVAKIKRVI MERDTYPRKW GLGPKASQKK LMIKQGLLDK HGKPTDSTPA TWKQEYVDYS 

       430        440        450        460        470        480 
ESAKKEVVAE VVKAPQVVAE AAKTAKRKRE SESESDETPP AAPQLIKKEK KKSKKDKKAK 

       490        500        510 
AGLESGAEPG DGDSDTTKKK KKKKKAKEVE LVSE 

« Hide

Isoform 3 [UniParc].

Checksum: A14633849FB65A56
Show »

FASTA42047,603

References

« Hide 'large scale' references
[1]"X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions."
Heiss N.S., Knight S.W., Vulliamy T.J., Klauck S.M., Wiemann S., Mason P.J., Poustka A., Dokal I.
Nat. Genet. 19:32-38(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS DKCX VAL-36; LEU-37 DEL; ARG-40; TYR-72 AND GLU-402.
[2]"X-linked dyskeratosis congenita is predominantly caused by missense mutations in the DKC1 gene."
Knight S.W., Heiss N.S., Vulliamy T.J., Greschner S., Stavrides G., Pai G.S., Lestringant G., Varma N., Mason P.J., Dokal I., Poustka A.
Am. J. Hum. Genet. 65:50-58(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS DKCX VAL-2; GLU-39; LYS-41; THR-65; ALA-66; VAL-321; ILE-350; THR-350; VAL-353 AND ARG-402.
[3]"Mapping and characterization of the X-linked dyskeratosis congenita (DKC) gene."
Hassock S., Vetrie D., Giannelli F.
Genomics 55:21-27(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[4]"A highly conserved nucleolar protein from human interacts with a HMG-like protein."
Jiang W., Clifford J., Koltin Y.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"A new human dyskerin isoform with cytoplasmic localization."
Angrisani A., Turano M., Paparo L., Di Mauro C., Furia M.
Biochim. Biophys. Acta 1810:1361-1368(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION.
[6]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[8]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11; 118-127; 159-191; 284-291; 303-322 AND 426-443, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Dyskerin localizes to the nucleolus and its mislocalization is unlikely to play a role in the pathogenesis of dyskeratosis congenita."
Heiss N.S., Girod A., Salowsky R., Wiemann S., Pepperkok R., Poustka A.
Hum. Mol. Genet. 8:2515-2524(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DOMAIN NUCLEOLAR LOCALIZATION.
[10]"A telomerase component is defective in the human disease dyskeratosis congenita."
Mitchell J.R., Wood E., Collins K.
Nature 402:551-555(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH TELOMERASE.
[11]"Gene structure and expression of the mouse dyskeratosis congenita gene, dkc1."
Heiss N.S., Baechner D., Salowsky R., Kolb A., Kioschis P., Poustka A.
Genomics 67:153-163(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"Human H/ACA small nucleolar RNPs and telomerase share evolutionarily conserved proteins NHP2 and NOP10."
Pogacic V., Dragon F., Filipowicz W.
Mol. Cell. Biol. 20:9028-9040(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NHP2.
[13]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins."
Wang C., Meier U.T.
EMBO J. 23:1857-1867(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Stepwise RNP assembly at the site of H/ACA RNA transcription in human cells."
Darzacq X., Kittur N., Roy S., Shav-Tal Y., Singer R.H., Meier U.T.
J. Cell Biol. 173:207-218(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAF1.
[17]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"hNaf1 is required for accumulation of human box H/ACA snoRNPs, scaRNPs, and telomerase."
Hoareau-Aveilla C., Bonoli M., Caizergues-Ferrer M., Henry Y.
RNA 12:832-840(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAF1.
[19]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[20]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-485 AND SER-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[23]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"SHQ1 is required prior to NAF1 for assembly of H/ACA small nucleolar and telomerase RNPs."
Grozdanov P.N., Roy S., Kittur N., Meier U.T.
RNA 15:1188-1197(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHQ1.
[26]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-485 AND SER-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[27]"A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis."
Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., Veenstra T.D., Terns M.P., Artandi S.E.
Science 323:644-648(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
[28]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-451; SER-453; SER-485; SER-494 AND SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-451; SER-453; SER-455; SER-485; SER-494 AND SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Unexplained aplastic anaemia, immunodeficiency, and cerebellar hypoplasia (Hoyeraal-Hreidarsson syndrome) due to mutations in the dyskeratosis congenita gene, DKC1."
Knight S.W., Heiss N.S., Vulliamy T.J., Aalfs C.M., McMahon C., Richmond P., Jones A., Hennekam R.C.M., Poustka A., Mason P.J., Dokal I.
Br. J. Haematol. 107:335-339(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHS MET-49 AND GLY-121.
[33]"A novel DKC1 mutation, severe combined immunodeficiency (T+B-NK-SCID) and bone marrow transplantation in an infant with Hoyeraal-Hreidarsson syndrome."
Cossu F., Vulliamy T.J., Marrone A., Badiali M., Cao A., Dokal I.
Br. J. Haematol. 119:765-768(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHS THR-38.
[34]"Identification of a novel mutation and a de novo mutation in DKC1 in two Chinese pedigrees with Dyskeratosis congenita."
Ding Y.G., Zhu T.S., Jiang W., Yang Y., Bu D.F., Tu P., Zhu X.J., Wang B.X.
J. Invest. Dermatol. 123:470-473(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DKCX VAL-353 AND LEU-409.
[35]"X-linked dyskeratosis congenita in Malaysia."
Hamidah A., Rashid R.A., Jamal R., Zhao M., Kanegane H.
Pediatr. Blood Cancer 50:432-432(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DKCX PHE-72.
[36]"Identification of a novel mutation in DKC1 in dyskeratosis congenita."
Kurnikova M., Shagina I., Khachatryan L., Schagina O., Maschan M., Shagin D.
Pediatr. Blood Cancer 52:135-137(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DKCX SER-56.
[37]"Novel mutations of the DKC1 gene in individuals affected with dyskeratosis congenita."
Rostamiani K., Klauck S.M., Heiss N., Poustka A., Khaleghi M., Rosales R., Metzenberg A.B.
Blood Cells Mol. Dis. 44:88-88(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DKCX PHE-317 AND GLN-322.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ224481 Genomic DNA. Translation: CAA11970.1.
AJ010395, AJ010396 Genomic DNA. Translation: CAB51168.1.
AF067008 mRNA. Translation: AAD11815.1.
AF067023 expand/collapse EMBL AC list , AF067009, AF067010, AF067011, AF067012, AF067013, AF067014, AF067015, AF067016, AF067017, AF067018, AF067019, AF067020, AF067021, AF067022 Genomic DNA. Translation: AAD20232.1.
U59151 mRNA. Translation: AAB94299.1.
JF279874 mRNA. Translation: ADX66370.1.
AC109993 Genomic DNA. No translation available.
BC009928 mRNA. Translation: AAH09928.1.
BC010015 mRNA. Translation: AAH10015.1.
RefSeqNP_001135935.1. NM_001142463.2.
NP_001275676.1. NM_001288747.1.
NP_001354.1. NM_001363.4.
UniGeneHs.4747.

3D structure databases

ProteinModelPortalO60832.
SMRO60832. Positions 35-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108080. 39 interactions.
DIPDIP-40645N.
IntActO60832. 27 interactions.
MINTMINT-1379892.
STRING9606.ENSP00000358563.

PTM databases

PhosphoSiteO60832.

2D gel databases

SWISS-2DPAGEO60832.

Proteomic databases

PaxDbO60832.
PeptideAtlasO60832.
PRIDEO60832.

Protocols and materials databases

DNASU1736.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369550; ENSP00000358563; ENSG00000130826. [O60832-1]
ENST00000596793; ENSP00000472996; ENSG00000268226. [O60832-1]
GeneID1736.
KEGGhsa:1736.
UCSCuc004fmm.3. human. [O60832-1]

Organism-specific databases

CTD1736.
GeneCardsGC0XP153984.
HGNCHGNC:2890. DKC1.
HPAHPA000166.
HPA000447.
HPA001022.
MIM300126. gene.
305000. phenotype.
neXtProtNX_O60832.
Orphanet1775. Dyskeratosis congenita.
3322. Hoyeraal-Hreidarsson syndrome.
PharmGKBPA27344.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0130.
HOGENOMHOG000231224.
HOVERGENHBG081442.
KOK11131.
OMAHDKLPGG.
PhylomeDBO60832.
TreeFamTF300354.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressO60832.
BgeeO60832.
CleanExHS_DKC1.
GenevestigatorO60832.

Family and domain databases

Gene3D2.30.130.10. 1 hit.
InterProIPR012960. Dyskerin-like.
IPR002501. PsdUridine_synth.
IPR020103. PsdUridine_synth_cat_dom.
IPR002478. PUA.
IPR015947. PUA-like_domain.
IPR004802. tRNA_PsdUridine_synth_B_fam.
IPR004521. Uncharacterised_CHP00451.
[Graphical view]
PANTHERPTHR23127. PTHR23127. 1 hit.
PfamPF08068. DKCLD. 1 hit.
PF01472. PUA. 1 hit.
PF01509. TruB_N. 1 hit.
[Graphical view]
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF55120. SSF55120. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR00425. CBF5. 1 hit.
TIGR00451. unchar_dom_2. 1 hit.
PROSITEPS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDKC1. human.
GeneWikiDyskerin.
GenomeRNAi1736.
NextBio7039.
PROO60832.
SOURCESearch...

Entry information

Entry nameDKC1_HUMAN
AccessionPrimary (citable) accession number: O60832
Secondary accession number(s): F5BSB3 expand/collapse secondary AC list , O43845, Q96G67, Q9Y505
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM