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Q9ESX5 (DKC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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):
Dyskerin
Nopp140-associated protein of 57 kDa
Nucleolar protein NAP57
Nucleolar protein family A member 4
snoRNP protein DKC1
Gene names
Name:Dkc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. Ref.4 Ref.5

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) By similarity. 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 By similarity.

Subcellular location

Nucleusnucleolus. NucleusCajal body. Note: Also localized to Cajal bodies (coiled bodies).

Tissue specificity

Ubiquitously expressed, with elevated levels in Purkinje cells, the olfactory bulb, and Leydig cells of the testis. Ref.1

Developmental stage

Expressed throughout development, particularly in developing epithelial tissues. Ref.1

Sequence similarities

Belongs to the pseudouridine synthase TruB family.

Contains 1 PUA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 509508H/ACA ribonucleoprotein complex subunit 4
PRO_0000121984

Regions

Domain297 – 37276PUA
Region2 – 2120Nucleolar localization By similarity
Region446 – 50964Nuclear and nucleolar localization By similarity
Compositional bias11 – 177Poly-Lys

Sites

Active site1251Nucleophile By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue4511Phosphoserine Ref.7 Ref.8 Ref.10
Modified residue4531Phosphoserine Ref.7 Ref.8 Ref.10
Modified residue4551Phosphoserine Ref.8 Ref.10
Modified residue4811Phosphoserine Ref.7
Modified residue5081Phosphoserine Ref.6 Ref.9 Ref.10

Experimental info

Mutagenesis3531A → V: Destabilization of TERC, impaired telomerase function, and reduced rRNA pseudouridylation and pre-rRNA processing. Ref.5
Mutagenesis4021G → E: Reduced rRNA pseudouridylation and pre-rRNA processing. Ref.5
Sequence conflict234 – 2418GLLLGVGG → CFVLGSGC in CAC04528. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9ESX5 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 17C50FDF48912A14

FASTA50957,402
        10         20         30         40         50         60 
MADAEVITFP KKHKKKKDRK PLQEDDVAEI QHAEEFLIKP ESKVAQLDTS QWPLLLKNFD 

        70         80         90        100        110        120 
KLNVRTAHYT PLPCGSNPLK 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 YGAKIMLPGL LRYEDGIEVN QEIVVITTKG EAICMAIALM TTAVISTCDH 

       370        380        390        400        410        420 
GIVAKIKRVI MERDTYPRKW GLGPKASQKK MMIKQGLLDK HGKPTDNTPA TWKQDYIDYS 

       430        440        450        460        470        480 
DSGKNTLVTE AVQAPQLAAE AVNVIKRKRD SESESDETPT VPQLKEKKKK KDKKPKTVLE 

       490        500 
SGGETGDGDN DTTKKKKKKK VKVVEEMSE 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: 129/Ola.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Colon.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Dyskeratosis congenita and cancer in mice deficient in ribosomal RNA modification."
Ruggero D., Grisendi S., Piazza F., Rego E., Mari F., Rao P.H., Cordon-Cardo C., Pandolfi P.P.
Science 299:259-262(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Mouse dyskerin mutations affect accumulation of telomerase RNA and small nucleolar RNA, telomerase activity, and ribosomal RNA processing."
Mochizuki Y., He J., Kulkarni S., Bessler M., Mason P.J.
Proc. Natl. Acad. Sci. U.S.A. 101:10756-10761(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ALA-353 AND GLY-402.
[6]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 AND SER-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453; SER-455 AND SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ250973 expand/collapse EMBL AC list , AJ250972, AJ250974, AJ250975, AJ250976, AJ250978, AJ250980, AJ250981, AJ250979, AJ250977 Genomic DNA. Translation: CAC04528.1.
AK136418 mRNA. Translation: BAE22970.1.
AL808110 Genomic DNA. Translation: CAM26485.1.
CCDSCCDS41029.1.
RefSeqNP_001025478.1. NM_001030307.2.
UniGeneMm.291062.

3D structure databases

ProteinModelPortalQ9ESX5.
SMRQ9ESX5. Positions 48-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid232777. 1 interaction.
IntActQ9ESX5. 3 interactions.
MINTMINT-1854010.

PTM databases

PhosphoSiteQ9ESX5.

Proteomic databases

MaxQBQ9ESX5.
PaxDbQ9ESX5.
PRIDEQ9ESX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033776; ENSMUSP00000033776; ENSMUSG00000031403.
GeneID245474.
KEGGmmu:245474.
UCSCuc009tpo.2. mouse.

Organism-specific databases

CTD1736.
MGIMGI:1861727. Dkc1.

Phylogenomic databases

eggNOGCOG0130.
GeneTreeENSGT00510000047092.
HOGENOMHOG000231224.
HOVERGENHBG081442.
InParanoidQ3UWE5.
KOK11131.
OMAHDKLPGG.
OrthoDBEOG7QC7W0.
TreeFamTF300354.

Gene expression databases

ArrayExpressQ9ESX5.
BgeeQ9ESX5.
GenevestigatorQ9ESX5.

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

NextBio386727.
PROQ9ESX5.
SOURCESearch...

Entry information

Entry nameDKC1_MOUSE
AccessionPrimary (citable) accession number: Q9ESX5
Secondary accession number(s): Q3UWE5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 110 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot