O60832 (DKC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.24 Ref.26
Subcellular location	Isoform 1: Nucleus › nucleolus. Nucleus › Cajal 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 recessive (XDKC) [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.32 Ref.33 Ref.34 Ref.35 Hoyeraal-Hreidarsson syndrome (HHS) [MIM:300240]: A multisystem disorder affecting males and characterized by aplastic anemia, immunodeficiency, microcephaly, cerebellar hypoplasia, and growth retardation. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.30 Ref.31
Sequence similarities	Belongs to the pseudouridine synthase TruB family. Contains 1 PUA domain.

Ontologies

Keywords
Biological process	Ribosome biogenesis rRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Dyskeratosis congenita
Ligand	RNA-binding
Molecular function	Isomerase Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 via telomerase Traceable author statement. Source: Reactome
Cellular_component	Cajal 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 telomerase holoenzyme complex Inferred from direct assay PubMed 12135483. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.10. Source: ProtInc pseudouridine synthase activity Inferred from electronic annotation. Source: InterPro telomerase activity Inferred from direct assay PubMed 12135483. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RUVBL1	Q9Y265	5	EBI-713091,EBI-353675

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 514	513	H/ACA ribonucleoprotein complex subunit 4		PRO_0000121983
Regions
	Domain	296 – 371	76	PUA
	Region	2 – 21	20	Nucleolar localization
	Region	446 – 514	69	Nuclear and nucleolar localization
	Compositional bias	11 – 17	7	Poly-Lys
Sites
	Active site	125	1	Nucleophile By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8
	Modified residue	21	1	Phosphoserine Ref.15 Ref.20 Ref.21 Ref.25 Ref.27 Ref.29
	Modified residue	451	1	Phosphoserine Ref.27 Ref.29
	Modified residue	453	1	Phosphoserine Ref.27 Ref.29
	Modified residue	455	1	Phosphoserine Ref.29
	Modified residue	458	1	Phosphothreonine By similarity
	Modified residue	485	1	Phosphoserine Ref.21 Ref.25 Ref.27 Ref.29
	Modified residue	494	1	Phosphoserine Ref.17 Ref.21 Ref.25 Ref.27 Ref.29
	Modified residue	513	1	Phosphoserine Ref.15 Ref.23 Ref.27 Ref.29
Natural variations
	Alternative sequence	420 – 514	95	SESAK…ELVSE → R in isoform 3.		VSP_042422
	Natural variant	2	1	A → V in XDKC. Ref.2 Corresponds to variant rs121912303 [ dbSNP | Ensembl ].		VAR_010076
	Natural variant	36	1	F → V in XDKC. Ref.1 Corresponds to variant rs121912293 [ dbSNP | Ensembl ].		VAR_006811
	Natural variant	37	1	Missing in XDKC. Ref.1		VAR_006812
	Natural variant	38	1	I → T in HHS. Ref.31 Corresponds to variant rs28936072 [ dbSNP | Ensembl ].		VAR_015674
	Natural variant	39	1	K → E in XDKC. Ref.2 Corresponds to variant rs121912296 [ dbSNP | Ensembl ].		VAR_010077
	Natural variant	40	1	P → R in XDKC. Ref.1 Corresponds to variant rs121912292 [ dbSNP | Ensembl ].		VAR_006813
	Natural variant	41	1	E → K in XDKC. Ref.2 Corresponds to variant rs121912302 [ dbSNP | Ensembl ].		VAR_010078
	Natural variant	49	1	T → M in HHS. Ref.30 Corresponds to variant rs121912304 [ dbSNP | Ensembl ].		VAR_015675
	Natural variant	56	1	L → S in XDKC; due to a 2 nucleotide inversion. Ref.34 Corresponds to variant rs121912287 [ dbSNP | Ensembl ].		VAR_063821
	Natural variant	65	1	R → T in XDKC. Ref.2 Corresponds to variant rs121912301 [ dbSNP | Ensembl ].		VAR_010079
	Natural variant	66	1	T → A in XDKC. Ref.2 Corresponds to variant rs121912297 [ dbSNP | Ensembl ].		VAR_010080
	Natural variant	72	1	L → F in XDKC. Ref.33 Corresponds to variant rs121912306 [ dbSNP | Ensembl ].		VAR_063822
	Natural variant	72	1	L → Y in XDKC; requires 2 nucleotide substitutions. Ref.1 Corresponds to variant rs121912294 [ dbSNP | Ensembl ].		VAR_006814
	Natural variant	121	1	S → G in HHS. Ref.30 Corresponds to variant rs121912305 [ dbSNP | Ensembl ].		VAR_015676
	Natural variant	223	1	G → D. Corresponds to variant rs2728533 [ dbSNP | Ensembl ].		VAR_022553
	Natural variant	317	1	L → F in XDKC. Ref.35 Corresponds to variant rs121912290 [ dbSNP | Ensembl ].		VAR_063823
	Natural variant	321	1	L → V in XDKC. Ref.2 Corresponds to variant rs2728726 [ dbSNP | Ensembl ].		VAR_010081
	Natural variant	322	1	R → Q in XDKC. Ref.35 Corresponds to variant rs121912291 [ dbSNP | Ensembl ].		VAR_063824
	Natural variant	350	1	M → I in XDKC. Ref.2 Corresponds to variant rs121912298 [ dbSNP | Ensembl ].		VAR_010082
	Natural variant	350	1	M → T in XDKC. Ref.2 Corresponds to variant rs121912300 [ dbSNP | Ensembl ].		VAR_010083
	Natural variant	353	1	A → V in XDKC and HHS. Ref.2 Ref.32 Corresponds to variant rs121912288 [ dbSNP | Ensembl ].		VAR_009264
	Natural variant	402	1	G → E in XDKC. Ref.1 Corresponds to variant rs121912295 [ dbSNP | Ensembl ].		VAR_006815
	Natural variant	402	1	G → R in XDKC. Ref.2 Corresponds to variant rs121912299 [ dbSNP | Ensembl ].		VAR_010084
	Natural variant	409	1	P → L in XDKC. Ref.32 Corresponds to variant rs121912289 [ dbSNP | Ensembl ].		VAR_063825
Experimental info
	Sequence conflict	37	1	L → F in AAB94299. Ref.4
	Sequence conflict	285	1	V → F in AAH09928. Ref.7
	Sequence conflict	446	1	K → KVSGMLSSVWN in CAB51168. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 12474DBEEFEB471C	FASTA	514	57,674
	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
	Isoform 3 [UniParc]. Checksum: A14633849FB65A56	FASTA	420	47,603
	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 TWKQEYVDYR

References

	« Hide 'large scale' referencesShow '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 XDKC 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 XDKC 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. , 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, 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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, MASS SPECTROMETRY.
[24]	"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.
[25]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"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.
[27]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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].
[29]	"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, MASS SPECTROMETRY.
[30]	"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.
[31]	"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.
[32]	"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 XDKC VAL-353 AND LEU-409.
[33]	"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 XDKC PHE-72.
[34]	"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 XDKC SER-56.
[35]	"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 XDKC PHE-317 AND GLN-322.
+	Additional computationally mapped references.

Web resources

DKC1base

DKC1 mutation db

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

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 , 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.
IPI	IPI00221394.
RefSeq	NP_001354.1. NM_001363.3.
UniGene	Hs.4747.
3D structure databases
ProteinModelPortal	O60832.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60832. 16 interactions.
MINT	MINT-1379892.
STRING	9606.ENSP00000358563.
PTM databases
PhosphoSite	O60832.
2D gel databases
SWISS-2DPAGE	O60832.
Proteomic databases
PaxDb	O60832.
PeptideAtlas	O60832.
PRIDE	O60832.
Protocols and materials databases
DNASU	1736.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369550; ENSP00000358563; ENSG00000130826. ENST00000596793; ENSP00000472996; ENSG00000268226.
GeneID	1736.
KEGG	hsa:1736.
UCSC	uc004fmm.3. human.
Organism-specific databases
CTD	1736.
GeneCards	GC0XP153984.
HGNC	HGNC:2890. DKC1.
HPA	HPA000166. HPA000447.
MIM	300126. gene. 300240. phenotype. 305000. phenotype.
neXtProt	NX_O60832.
Orphanet	1775. Dyskeratosis congenita. 3322. Hoyeraal-Hreidarsson syndrome.
PharmGKB	PA27344.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0130.
HOGENOM	HOG000231224.
HOVERGEN	HBG081442.
KO	K11131.
OMA	TIHESKL.
OrthoDB	EOG4NS3BP.
PhylomeDB	O60832.
Enzyme and pathway databases
Pathway_Interaction_DB	telomerasepathway. Regulation of Telomerase.
Reactome	REACT_115566. Cell Cycle.
Gene expression databases
ArrayExpress	O60832.
Bgee	O60832.
CleanEx	HS_DKC1.
Genevestigator	O60832.
GermOnline	ENSG00000130826. Homo sapiens.
Family and domain databases
InterPro	IPR012960. 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]
PANTHER	PTHR23127. PTHR23127. 1 hit.
Pfam	PF08068. DKCLD. 1 hit. PF01472. PUA. 1 hit. PF01509. TruB_N. 1 hit. [Graphical view]
SMART	SM00359. PUA. 1 hit. [Graphical view]
SUPFAM	SSF55120. PsdUridine_synth_cat_dom. 1 hit. SSF88697. PUA-like. 1 hit.
TIGRFAMs	TIGR00425. CBF5. 1 hit. TIGR00451. unchar_dom_2. 1 hit.
PROSITE	PS50890. PUA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DKC1. human.
GenomeRNAi	1736.
NextBio	7039.
SOURCE	Search...

Entry information

Entry name

DKC1_HUMAN

Accession

Primary (citable) accession number: O60832
Secondary accession number(s): F5BSB3 , O43845, Q96G67, Q9Y505

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 149 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.