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P40615 (DKC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Synonyms:Nap57
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 telomere maintenance; necessary for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme By similarity. Also required for ribosome biogenesis. 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. Ref.4

Catalytic activity

RNA uridine = RNA pseudouridine.

Subunit structure

May interact with TERC, which contains a 3'-terminal domain related to the box H/ACA snoRNAs. May interact with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. 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. 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. Specific interactions with snoRNAs or TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140. 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. Ref.1 Ref.4

Subcellular location

Nucleusnucleolus. NucleusCajal body. Note: Also localized to Cajal bodies (coiled bodies). Ref.1 Ref.4

Sequence similarities

Belongs to the pseudouridine synthase TruB family.

Contains 1 PUA domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LOC100360065D3ZMP64EBI-5746997,EBI-8792072
NAF1Q96HR83EBI-5746997,EBI-2515597From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 509508H/ACA ribonucleoprotein complex subunit 4
PRO_0000121985

Regions

Domain297 – 37276PUA
Region2 – 2221Nucleolar localization By similarity
Region447 – 50963Nuclear and nucleolar localization By similarity
Compositional bias12 – 187Poly-Lys

Sites

Active site1261Nucleophile By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue4521Phosphoserine By similarity
Modified residue4541Phosphoserine By similarity
Modified residue5081Phosphoserine By similarity

Experimental info

Sequence conflict459 – 50850ATPTT…AEELS → RRPLPRP AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40615 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 038862EBBF2A1E2F

FASTA50956,615
        10         20         30         40         50         60 
MADAEAAMTF PKKHKKKKER KPLPEADVAE IQHAEDFLIK PESKAAQLDT SQWPLLLKNF 

        70         80         90        100        110        120 
DRLNVRTTHY TPIPCGSNPL KREIGEYVRT GFINLDKPSN PSSHEVVAWI RRILRVEKTG 

       130        140        150        160        170        180 
HSGTLDPKVT GCLIVCIERA TRLVKSQQSA GKEYVGVVRL HNAIEGTAQL SRALETLTGA 

       190        200        210        220        230        240 
LFQRPPLIAA VKRQLRVRTI YESRVVEYDP ERRLGVFWVS CEAGTYIRTL CVHLGLLLGV 

       250        260        270        280        290        300 
GGQMQELRRV RSGVVGERDH MVTMHDVLDA QYLYDHHRDE SYLRRVVFPL EKLLTSHKRL 

       310        320        330        340        350        360 
VMKDSAVNAI CYGAKIMLPG LLRYEDGIEV NQEVVVITTK GEAVCVAIAL MTTAVISTCD 

       370        380        390        400        410        420 
HGVVAKIKRV IMERDTYPRK WGLGPKASQK KQLIKQGLLD KHGRPTDGTP ASWTRDYVDY 

       430        440        450        460        470        480 
SDSSKKATAA EATPGPGVTA DAASIVKRKR DSDSDADEAT PTTTPRVKKE KKKKKEKADG 

       490        500 
GEEAAEDGDG DATRKKKKKK ARAAEELSG 

« Hide

References

« Hide 'large scale' references
[1]"NAP57, a mammalian nucleolar protein with a putative homolog in yeast and bacteria."
Meier U., Blobel G.
J. Cell Biol. 127:1505-1514(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-43; 83-96 AND 98-119, SUBCELLULAR LOCATION, INTERACTION WITH NOLC1.
Tissue: Liver.
[2]Meier U.
Submitted (DEC-1997) to UniProtKB
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]"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].
Tissue: Prostate.
[4]"Immunopurified small nucleolar ribonucleoprotein particles pseudouridylate rRNA independently of their association with phosphorylated Nopp140."
Wang C., Query C.C., Meier U.T.
Mol. Cell. Biol. 22:8457-8466(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GAR1; NHP2; NOP10 AND NOLC1, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z34922 mRNA. Translation: CAA84402.1.
BC099832 mRNA. Translation: AAH99832.1.
PIRA55163.
RefSeqNP_596910.1. NM_133419.1.
UniGeneRn.4223.

3D structure databases

ProteinModelPortalP40615.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP40615. 5 interactions.

PTM databases

PhosphoSiteP40615.

Proteomic databases

PRIDEP40615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID170944.
KEGGrno:170944.

Organism-specific databases

CTD1736.
RGD621780. Dkc1.

Phylogenomic databases

HOVERGENHBG081442.
KOK11131.
PhylomeDBP40615.

Gene expression databases

GenevestigatorP40615.

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

NextBio621465.
PROP40615.

Entry information

Entry nameDKC1_RAT
AccessionPrimary (citable) accession number: P40615
Secondary accession number(s): Q499M9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 107 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