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Q9ESX5

- DKC1_MOUSE

UniProt

Q9ESX5 - DKC1_MOUSE

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Protein
H/ACA ribonucleoprotein complex subunit 4
Gene
Dkc1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

RNA uridine = RNA pseudouridine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei125 – 1251Nucleophile By similarity

GO - Molecular functioni

  1. RNA binding Source: MGI
  2. pseudouridine synthase activity Source: InterPro
  3. pseudouridylate synthase activity Source: MGI
  4. snoRNP binding Source: MGI
  5. telomerase activity Source: Ensembl

GO - Biological processi

  1. RNA processing Source: MGI
  2. rRNA modification Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Ribonucleoprotein

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Dkc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1861727. Dkc1.

Subcellular locationi

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

GO - Cellular componenti

  1. Cajal body Source: UniProtKB-SubCell
  2. nucleolus Source: MGI
  3. telomerase holoenzyme complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi353 – 3531A → V: Destabilization of TERC, impaired telomerase function, and reduced rRNA pseudouridylation and pre-rRNA processing. 1 Publication
Mutagenesisi402 – 4021G → E: Reduced rRNA pseudouridylation and pre-rRNA processing. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 509508H/ACA ribonucleoprotein complex subunit 4
PRO_0000121984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei451 – 4511Phosphoserine3 Publications
Modified residuei453 – 4531Phosphoserine3 Publications
Modified residuei455 – 4551Phosphoserine2 Publications
Modified residuei481 – 4811Phosphoserine1 Publication
Modified residuei508 – 5081Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9ESX5.
PaxDbiQ9ESX5.
PRIDEiQ9ESX5.

PTM databases

PhosphoSiteiQ9ESX5.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

ArrayExpressiQ9ESX5.
BgeeiQ9ESX5.
GenevestigatoriQ9ESX5.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi232777. 1 interaction.
IntActiQ9ESX5. 3 interactions.
MINTiMINT-1854010.

Structurei

3D structure databases

ProteinModelPortaliQ9ESX5.
SMRiQ9ESX5. Positions 48-408.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini297 – 37276PUA
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2120Nucleolar localization By similarity
Add
BLAST
Regioni446 – 50964Nuclear and nucleolar localization By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 177Poly-Lys

Sequence similaritiesi

Contains 1 PUA domain.

Phylogenomic databases

eggNOGiCOG0130.
GeneTreeiENSGT00510000047092.
HOGENOMiHOG000231224.
HOVERGENiHBG081442.
InParanoidiQ3UWE5.
KOiK11131.
OMAiHDKLPGG.
OrthoDBiEOG7QC7W0.
TreeFamiTF300354.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
InterProiIPR012960. 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]
PANTHERiPTHR23127. PTHR23127. 1 hit.
PfamiPF08068. DKCLD. 1 hit.
PF01472. PUA. 1 hit.
PF01509. TruB_N. 1 hit.
[Graphical view]
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00425. CBF5. 1 hit.
TIGR00451. unchar_dom_2. 1 hit.
PROSITEiPS50890. PUA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ESX5-1 [UniParc]FASTAAdd to Basket

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MADAEVITFP KKHKKKKDRK PLQEDDVAEI QHAEEFLIKP ESKVAQLDTS    50
QWPLLLKNFD KLNVRTAHYT PLPCGSNPLK REIGDYIRTG FINLDKPSNP 100
SSHEVVAWIR RILRVEKTGH SGTLDPKVTG CLIVCIERAT RLVKSQQSAG 150
KEYVGIVRLH NAIEGGTQLS RALETLTGAL FQRPPLIAAV KRQLRVRTIY 200
ESKMIEYDPE RRLGIFWVSC EAGTYIRTLC VHLGLLLGVG GQMQELRRVR 250
SGVMSEKDHM VTMHDVLDAQ WLYDNHKDES YLRRVVYPLE KLLTSHKRLV 300
MKDSAVNAIC YGAKIMLPGL LRYEDGIEVN QEIVVITTKG EAICMAIALM 350
TTAVISTCDH GIVAKIKRVI MERDTYPRKW GLGPKASQKK MMIKQGLLDK 400
HGKPTDNTPA TWKQDYIDYS DSGKNTLVTE AVQAPQLAAE AVNVIKRKRD 450
SESESDETPT VPQLKEKKKK KDKKPKTVLE SGGETGDGDN DTTKKKKKKK 500
VKVVEEMSE 509
Length:509
Mass (Da):57,402
Last modified:July 27, 2011 - v4
Checksum:i17C50FDF48912A14
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2418GLLLGVGG → CFVLGSGC in CAC04528. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ250973
, 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.
CCDSiCCDS41029.1.
RefSeqiNP_001025478.1. NM_001030307.2.
UniGeneiMm.291062.

Genome annotation databases

EnsembliENSMUST00000033776; ENSMUSP00000033776; ENSMUSG00000031403.
GeneIDi245474.
KEGGimmu:245474.
UCSCiuc009tpo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ250973
, 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 .
CCDSi CCDS41029.1.
RefSeqi NP_001025478.1. NM_001030307.2.
UniGenei Mm.291062.

3D structure databases

ProteinModelPortali Q9ESX5.
SMRi Q9ESX5. Positions 48-408.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 232777. 1 interaction.
IntActi Q9ESX5. 3 interactions.
MINTi MINT-1854010.

PTM databases

PhosphoSitei Q9ESX5.

Proteomic databases

MaxQBi Q9ESX5.
PaxDbi Q9ESX5.
PRIDEi Q9ESX5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033776 ; ENSMUSP00000033776 ; ENSMUSG00000031403 .
GeneIDi 245474.
KEGGi mmu:245474.
UCSCi uc009tpo.2. mouse.

Organism-specific databases

CTDi 1736.
MGIi MGI:1861727. Dkc1.

Phylogenomic databases

eggNOGi COG0130.
GeneTreei ENSGT00510000047092.
HOGENOMi HOG000231224.
HOVERGENi HBG081442.
InParanoidi Q3UWE5.
KOi K11131.
OMAi HDKLPGG.
OrthoDBi EOG7QC7W0.
TreeFami TF300354.

Miscellaneous databases

NextBioi 386727.
PROi Q9ESX5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ESX5.
Bgeei Q9ESX5.
Genevestigatori Q9ESX5.

Family and domain databases

Gene3Di 2.30.130.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR23127. PTHR23127. 1 hit.
Pfami PF08068. DKCLD. 1 hit.
PF01472. PUA. 1 hit.
PF01509. TruB_N. 1 hit.
[Graphical view ]
SMARTi SM00359. PUA. 1 hit.
[Graphical view ]
SUPFAMi SSF55120. SSF55120. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR00425. CBF5. 1 hit.
TIGR00451. unchar_dom_2. 1 hit.
PROSITEi PS50890. PUA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiDKC1_MOUSE
AccessioniPrimary (citable) accession number: Q9ESX5
Secondary accession number(s): Q3UWE5
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi