H/ACA ribonucleoprotein complex subunit 4

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Reviewed, UniProtKB/Swiss-Prot O60832 (DKC1_HUMAN)

Last modified June 16, 2009. Version 108. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    H/ACA ribonucleoprotein complex subunit 4
    EC=5.4.99.-
Alternative name(s):
    Dyskerin
    Nucleolar protein family A member 4
    snoRNP protein DKC1
    Nopp140-associated protein of 57 kDa
    Nucleolar protein NAP57
    CBF5 homolog

Gene names

Name:	DKC1
Synonyms:	NOLA4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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General annotation (Comments)

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.
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, SIP1/GEMIN2, 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, WDR79/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). Ref.10 Ref.16 Ref.19
Subcellular location	Nucleus › nucleolus. Nucleus › Cajal body. Note: Also localized to Cajal bodies (coiled bodies). Ref.7 Ref.8 Ref.11
Tissue specificity	Ubiquitously expressed. Ref.9
Involvement in disease	Defects in DKC1 are a cause of dyskeratosis congenita X-linked recessive (XDKC) [MIM:305000]. XDKC is 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. Ref.1 Ref.2 Defects in DKC1 are the cause of Hoyeraal-Hreidarsson syndrome (HHS) [MIM:300240]. HHS is a multisystem disorder affecting males and is characterized by aplastic anemia, immunodeficiency, microcephaly, cerebellar hypoplasia, and growth retardation. Ref.29 Ref.30
Sequence similarities	Belongs to the pseudouridine synthase truB family. Contains 1 PUA domain.

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Ontologies

Keywords
Biological process	Ribosome biogenesis rRNA processing
Cellular component	Nucleus
Disease	Disease mutation Dyskeratosis congenita
Ligand	RNA-binding
Molecular function	Isomerase Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell proliferation Ref.8 Traceable author statement. Source: ProtInc pseudouridine synthesis Inferred from electronic annotation. Source: InterPro rRNA processing Ref.7 Traceable author statement. Source: ProtInc telomere maintenance via telomerase Ref.8 Traceable author statement. Source: ProtInc
Cellular component	Cajal body Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Ref.7 Inferred from direct assay. Source: HPA telomerase holoenzyme complex Inferred from direct assay. Source: UniProtKB
Molecular function	RNA binding Ref.8 Traceable author statement. Source: ProtInc protein binding Ref.16 Ref.19 Inferred from physical interaction. Source: UniProtKB pseudouridine synthase activity Inferred from electronic annotation. Source: InterPro telomerase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
RUVBL1	Q9Y265	2	EBI-713091,EBI-353675

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 514

513

H/ACA ribonucleoprotein complex subunit 4

PRO_0000121983

Regions

Domain

296 – 371

PUA

Region

2 – 21

Nucleolar localization

Region

446 – 514

Nuclear and nucleolar localization

Compositional bias

11 – 17

Poly-Lys

Sites

Active site

125

Nucleophile By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.6

Modified residue

Phosphoserine Ref.15 Ref.18 Ref.21 Ref.24 Ref.25

Modified residue

451

Phosphoserine Ref.15 Ref.25 Ref.20 Ref.22

Modified residue

453

Phosphoserine Ref.15 Ref.25 Ref.22 Ref.14

Modified residue

455

Phosphoserine Ref.15 Ref.25 Ref.20 Ref.14 Ref.23

Modified residue

458

Phosphothreonine Ref.15 Ref.25

Modified residue

485

Phosphoserine Ref.25

Modified residue

494

Phosphoserine Ref.25 Ref.13 Ref.17 Ref.26

Modified residue

513

Phosphoserine Ref.15 Ref.18 Ref.25 Ref.13 Ref.17

Natural variations

Natural variant

A → V in XDKC. Ref.2

VAR_010076

Natural variant

F → V in XDKC. Ref.1

VAR_006811

Natural variant

Missing in XDKC. Ref.1

VAR_006812

Natural variant

I → T in HHS. Ref.30

VAR_015674

Natural variant

K → E in XDKC. Ref.2

VAR_010077

Natural variant

P → R in XDKC. Ref.1

VAR_006813

Natural variant

E → K in XDKC. Ref.2

VAR_010078

Natural variant

T → M in HHS. Ref.29

VAR_015675

Natural variant

R → T in XDKC. Ref.2

VAR_010079

Natural variant

T → A in XDKC. Ref.2

VAR_010080

Natural variant

L → Y in XDKC; requires 2 nucleotide substitutions. Ref.1 Ref.2

VAR_006814

Natural variant

121

S → G in HHS. Ref.29

VAR_015676

Natural variant

223

G → D: dbSNP rs2728533.

VAR_022553

Natural variant

321

L → V in XDKC. Ref.2

VAR_010081

Natural variant

350

M → I in XDKC. Ref.2

VAR_010082

Natural variant

350

M → T in XDKC. Ref.2

VAR_010083

Natural variant

353

A → V in XDKC and HHS.

VAR_009264

Natural variant

402

G → E in XDKC. Ref.1 Ref.2

VAR_006815

Natural variant

402

G → R in XDKC. Ref.1 Ref.2

VAR_010084

Experimental info

Sequence conflict

L → F in AAB94299. Ref.4

Sequence conflict

285

V → F in AAH09928. Ref.5

Sequence conflict

446

K → KVSGMLSSVWN in CAB51168. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

O60832-1 [UniParc].

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

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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: 9590285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 10364516] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 9888995] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[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].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[6]	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.
[7]	"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: 10556300] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN NUCLEOLAR LOCALIZATION.
[8]	"A telomerase component is defective in the human disease dyskeratosis congenita." Mitchell J.R., Wood E., Collins K. Nature 402:551-555(1999) [PubMed: 10591218] [Abstract] Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH TELOMERASE.
[9]	"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: 10903840] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"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: 11074001] [Abstract] Cited for: INTERACTION WITH NHP2.
[11]	"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: 12429849] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins." Wang C., Meier U.T. EMBO J. 23:1857-1867(2004) [PubMed: 15044956] [Abstract] Cited for: CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
[13]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-513, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-455, MASS SPECTROMETRY.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-451; SER-453; SER-455; THR-458 AND SER-513, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 16618814] [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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-513, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-513, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"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: 16601202] [Abstract] Cited for: INTERACTION WITH NAF1.
[20]	"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: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-455, MASS SPECTROMETRY.
[21]	"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." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, MASS SPECTROMETRY. Tissue: Epithelium.
[22]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, MASS SPECTROMETRY.
[23]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, MASS SPECTROMETRY.
[24]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, MASS SPECTROMETRY.
[25]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-451; SER-453; SER-455; THR-458; SER-485; SER-494 AND SER-513, MASS SPECTROMETRY.
[26]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, MASS SPECTROMETRY. Tissue: Liver.
[27]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[28]	"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: 19179534] [Abstract] Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
[29]	"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: 10583221] [Abstract] Cited for: VARIANTS HHS MET-49 AND GLY-121.
[30]	"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: 12437656] [Abstract] Cited for: VARIANT HHS THR-38.
+	Additional computationally mapped references.

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Web resources

DKC1base

DKC1 mutation db

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

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Cross-references

Sequence databases
	AJ224481 Genomic DNA. Translation: CAA11970.1. AJ010395, AJ010396 Genomic DNA. Translation: CAB51168.1. AF067008 mRNA. Translation: AAD11815.1. AF067023 AF067022 Genomic DNA. Translation: AAD20232.1. U59151 mRNA. Translation: AAB94299.1. BC009928 mRNA. Translation: AAH09928.1. BC010015 mRNA. Translation: AAH10015.1.
IPI	IPI00221394.
RefSeq	NP_001354.1.
UniGene	Hs.4747
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O60832. 11 interactions.
PTM databases
PhosphoSite	O60832.
2-D gel databases
SWISS-2DPAGE	O60832.
Proteomic databases
PeptideAtlas	O60832.
PRIDE	O60832.
Genome annotation databases
Ensembl	ENSG00000130826. Homo sapiens. [Contig view]
GeneID	1736.
KEGG	hsa:1736.
NMPDR	fig\|9606.3.peg.33669.
Organism-specific databases
GeneCards	GC0XP153554.
H-InvDB	HIX0017164.
HGNC	HGNC:2890. DKC1.
HPA	HPA000166. HPA000447.
MIM	300126. gene. 300240. phenotype. 305000. phenotype.
Orphanet	1775. Dyskeratosis congenita. 3322. Progressive pancytopenia - immunodeficiency - cerebellar hypoplasia.
PharmGKB	PA27344.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O60832.
HOVERGEN	O60832.
Enzyme and pathway databases
Pathway_Interaction_DB	telomerasepathway. Regulation of Telomerase.
Gene expression databases
ArrayExpress	O60832.
Bgee	O60832.
CleanEx	HS_DKC1.
GermOnline	ENSG00000130826. Homo sapiens.
Family and domain databases
InterPro	IPR004802. Cbf5_synth. IPR012960. DKCLD. IPR002478. PUA. IPR002501. tRNA_psdUrid_synth_B_N. IPR004521. Unchar_dom_2. [Graphical view]
Pfam	PF08068. DKCLD. 1 hit. PF01472. PUA. 1 hit. PF01509. TruB_N. 1 hit. [Graphical view]
SMART	SM00359. PUA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00425. CBF5. 1 hit. TIGR00451. unchar_dom_2. 1 hit.
PROSITE	PS50890. PUA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	7039.
SOURCE	Search...

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Entry information

Entry name

DKC1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents