Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O60832

- DKC1_HUMAN

UniProt

O60832 - DKC1_HUMAN

Protein

H/ACA ribonucleoprotein complex subunit 4

Gene

DKC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 activityi

    RNA uridine = RNA pseudouridine.

    Sites

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

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. pseudouridine synthase activity Source: InterPro
    4. RNA binding Source: ProtInc
    5. telomerase activity Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. pseudouridine synthesis Source: InterPro
    3. RNA processing Source: ProtInc
    4. rRNA processing Source: ProtInc
    5. telomere maintenance Source: Reactome
    6. telomere maintenance via telomerase Source: Reactome

    Keywords - Molecular functioni

    Isomerase, Ribonucleoprotein

    Keywords - Biological processi

    Ribosome biogenesis, rRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_7974. Telomere Extension By Telomerase.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:DKC1
    Synonyms:NOLA4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2890. DKC1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. Cajal body Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleolus Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: LIFEdb
    6. telomerase holoenzyme complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Dyskeratosis congenita, X-linked (DKCX) [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.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21A → V in DKCX. 1 Publication
    Corresponds to variant rs121912303 [ dbSNP | Ensembl ].
    VAR_010076
    Natural varianti36 – 361F → V in DKCX. 1 Publication
    Corresponds to variant rs121912293 [ dbSNP | Ensembl ].
    VAR_006811
    Natural varianti37 – 371Missing in DKCX. 1 Publication
    VAR_006812
    Natural varianti39 – 391K → E in DKCX. 1 Publication
    Corresponds to variant rs121912296 [ dbSNP | Ensembl ].
    VAR_010077
    Natural varianti40 – 401P → R in DKCX. 1 Publication
    Corresponds to variant rs121912292 [ dbSNP | Ensembl ].
    VAR_006813
    Natural varianti41 – 411E → K in DKCX. 1 Publication
    Corresponds to variant rs121912302 [ dbSNP | Ensembl ].
    VAR_010078
    Natural varianti56 – 561L → S in DKCX; due to a 2 nucleotide inversion. 1 Publication
    Corresponds to variant rs121912287 [ dbSNP | Ensembl ].
    VAR_063821
    Natural varianti65 – 651R → T in DKCX. 1 Publication
    Corresponds to variant rs121912301 [ dbSNP | Ensembl ].
    VAR_010079
    Natural varianti66 – 661T → A in DKCX. 1 Publication
    Corresponds to variant rs121912297 [ dbSNP | Ensembl ].
    VAR_010080
    Natural varianti72 – 721L → F in DKCX. 1 Publication
    Corresponds to variant rs121912306 [ dbSNP | Ensembl ].
    VAR_063822
    Natural varianti72 – 721L → Y in DKCX; requires 2 nucleotide substitutions. 1 Publication
    Corresponds to variant rs121912294 [ dbSNP | Ensembl ].
    VAR_006814
    Natural varianti317 – 3171L → F in DKCX. 1 Publication
    Corresponds to variant rs121912290 [ dbSNP | Ensembl ].
    VAR_063823
    Natural varianti321 – 3211L → V in DKCX. 1 Publication
    Corresponds to variant rs2728726 [ dbSNP | Ensembl ].
    VAR_010081
    Natural varianti322 – 3221R → Q in DKCX. 1 Publication
    Corresponds to variant rs121912291 [ dbSNP | Ensembl ].
    VAR_063824
    Natural varianti350 – 3501M → I in DKCX. 1 Publication
    Corresponds to variant rs121912298 [ dbSNP | Ensembl ].
    VAR_010082
    Natural varianti350 – 3501M → T in DKCX. 1 Publication
    Corresponds to variant rs121912300 [ dbSNP | Ensembl ].
    VAR_010083
    Natural varianti353 – 3531A → V in DKCX and HHS. 2 Publications
    Corresponds to variant rs121912288 [ dbSNP | Ensembl ].
    VAR_009264
    Natural varianti402 – 4021G → E in DKCX. 1 Publication
    Corresponds to variant rs121912295 [ dbSNP | Ensembl ].
    VAR_006815
    Natural varianti402 – 4021G → R in DKCX. 1 Publication
    Corresponds to variant rs121912299 [ dbSNP | Ensembl ].
    VAR_010084
    Natural varianti409 – 4091P → L in DKCX. 1 Publication
    Corresponds to variant rs121912289 [ dbSNP | Ensembl ].
    VAR_063825
    Hoyeraal-Hreidarsson syndrome (HHS) [MIM:305000]: A clinically severe variant of dyskeratosis congenita that is characterized by multisystem involvement, early onset in utero, and often results in death in childhood. Affected individuals show intrauterine growth retardation, microcephaly, cerebellar hypoplasia, delayed development, and bone marrow failure resulting in immunodeficiency.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381I → T in HHS. 1 Publication
    Corresponds to variant rs28936072 [ dbSNP | Ensembl ].
    VAR_015674
    Natural varianti49 – 491T → M in HHS. 1 Publication
    Corresponds to variant rs121912304 [ dbSNP | Ensembl ].
    VAR_015675
    Natural varianti121 – 1211S → G in HHS. 1 Publication
    Corresponds to variant rs121912305 [ dbSNP | Ensembl ].
    VAR_015676
    Natural varianti353 – 3531A → V in DKCX and HHS. 2 Publications
    Corresponds to variant rs121912288 [ dbSNP | Ensembl ].
    VAR_009264

    Keywords - Diseasei

    Disease mutation, Dyskeratosis congenita

    Organism-specific databases

    MIMi305000. phenotype.
    Orphaneti1775. Dyskeratosis congenita.
    3322. Hoyeraal-Hreidarsson syndrome.
    PharmGKBiPA27344.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 514513H/ACA ribonucleoprotein complex subunit 4PRO_0000121983Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei21 – 211Phosphoserine6 Publications
    Modified residuei451 – 4511Phosphoserine2 Publications
    Modified residuei453 – 4531Phosphoserine2 Publications
    Modified residuei455 – 4551Phosphoserine1 Publication
    Modified residuei485 – 4851Phosphoserine4 Publications
    Modified residuei494 – 4941Phosphoserine5 Publications
    Modified residuei513 – 5131Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60832.
    PaxDbiO60832.
    PeptideAtlasiO60832.
    PRIDEiO60832.

    2D gel databases

    SWISS-2DPAGEO60832.

    PTM databases

    PhosphoSiteiO60832.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiO60832.
    BgeeiO60832.
    CleanExiHS_DKC1.
    GenevestigatoriO60832.

    Organism-specific databases

    HPAiHPA000166.
    HPA000447.
    HPA001022.

    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). 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.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HMBOX1Q6NT762EBI-713091,EBI-2549423
    NAF1Q96HR86EBI-713091,EBI-2515597
    RUVBL1Q9Y2658EBI-713091,EBI-353675

    Protein-protein interaction databases

    BioGridi108080. 46 interactions.
    DIPiDIP-40645N.
    IntActiO60832. 27 interactions.
    MINTiMINT-1379892.
    STRINGi9606.ENSP00000358563.

    Structurei

    3D structure databases

    ProteinModelPortaliO60832.
    SMRiO60832. Positions 35-408.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini296 – 37176PUAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 2120Nucleolar localizationAdd
    BLAST
    Regioni446 – 51469Nuclear and nucleolar localizationAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the pseudouridine synthase TruB family.Curated
    Contains 1 PUA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0130.
    HOGENOMiHOG000231224.
    HOVERGENiHBG081442.
    KOiK11131.
    OMAiHDKLPGG.
    PhylomeDBiO60832.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60832-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MADAEVIILP KKHKKKKERK SLPEEDVAEI QHAEEFLIKP ESKVAKLDTS    50
    QWPLLLKNFD KLNVRTTHYT PLACGSNPLK 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 YGAKIMLPGV LRYEDGIEVN QEIVVITTKG EAICMAIALM 350
    TTAVISTCDH GIVAKIKRVI MERDTYPRKW GLGPKASQKK LMIKQGLLDK 400
    HGKPTDSTPA TWKQEYVDYS ESAKKEVVAE VVKAPQVVAE AAKTAKRKRE 450
    SESESDETPP AAPQLIKKEK KKSKKDKKAK AGLESGAEPG DGDSDTTKKK 500
    KKKKKAKEVE LVSE 514
    Length:514
    Mass (Da):57,674
    Last modified:January 23, 2007 - v3
    Checksum:i12474DBEEFEB471C
    GO
    Isoform 3 (identifier: O60832-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         420-514: SESAKKEVVA...KAKEVELVSE → R

    Show »
    Length:420
    Mass (Da):47,603
    Checksum:iA14633849FB65A56
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371L → F in AAB94299. 1 PublicationCurated
    Sequence conflicti285 – 2851V → F in AAH09928. (PubMed:15489334)Curated
    Sequence conflicti446 – 4461K → KVSGMLSSVWN in CAB51168. (PubMed:10364516)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21A → V in DKCX. 1 Publication
    Corresponds to variant rs121912303 [ dbSNP | Ensembl ].
    VAR_010076
    Natural varianti36 – 361F → V in DKCX. 1 Publication
    Corresponds to variant rs121912293 [ dbSNP | Ensembl ].
    VAR_006811
    Natural varianti37 – 371Missing in DKCX. 1 Publication
    VAR_006812
    Natural varianti38 – 381I → T in HHS. 1 Publication
    Corresponds to variant rs28936072 [ dbSNP | Ensembl ].
    VAR_015674
    Natural varianti39 – 391K → E in DKCX. 1 Publication
    Corresponds to variant rs121912296 [ dbSNP | Ensembl ].
    VAR_010077
    Natural varianti40 – 401P → R in DKCX. 1 Publication
    Corresponds to variant rs121912292 [ dbSNP | Ensembl ].
    VAR_006813
    Natural varianti41 – 411E → K in DKCX. 1 Publication
    Corresponds to variant rs121912302 [ dbSNP | Ensembl ].
    VAR_010078
    Natural varianti49 – 491T → M in HHS. 1 Publication
    Corresponds to variant rs121912304 [ dbSNP | Ensembl ].
    VAR_015675
    Natural varianti56 – 561L → S in DKCX; due to a 2 nucleotide inversion. 1 Publication
    Corresponds to variant rs121912287 [ dbSNP | Ensembl ].
    VAR_063821
    Natural varianti65 – 651R → T in DKCX. 1 Publication
    Corresponds to variant rs121912301 [ dbSNP | Ensembl ].
    VAR_010079
    Natural varianti66 – 661T → A in DKCX. 1 Publication
    Corresponds to variant rs121912297 [ dbSNP | Ensembl ].
    VAR_010080
    Natural varianti72 – 721L → F in DKCX. 1 Publication
    Corresponds to variant rs121912306 [ dbSNP | Ensembl ].
    VAR_063822
    Natural varianti72 – 721L → Y in DKCX; requires 2 nucleotide substitutions. 1 Publication
    Corresponds to variant rs121912294 [ dbSNP | Ensembl ].
    VAR_006814
    Natural varianti121 – 1211S → G in HHS. 1 Publication
    Corresponds to variant rs121912305 [ dbSNP | Ensembl ].
    VAR_015676
    Natural varianti223 – 2231G → D.
    Corresponds to variant rs2728533 [ dbSNP | Ensembl ].
    VAR_022553
    Natural varianti317 – 3171L → F in DKCX. 1 Publication
    Corresponds to variant rs121912290 [ dbSNP | Ensembl ].
    VAR_063823
    Natural varianti321 – 3211L → V in DKCX. 1 Publication
    Corresponds to variant rs2728726 [ dbSNP | Ensembl ].
    VAR_010081
    Natural varianti322 – 3221R → Q in DKCX. 1 Publication
    Corresponds to variant rs121912291 [ dbSNP | Ensembl ].
    VAR_063824
    Natural varianti350 – 3501M → I in DKCX. 1 Publication
    Corresponds to variant rs121912298 [ dbSNP | Ensembl ].
    VAR_010082
    Natural varianti350 – 3501M → T in DKCX. 1 Publication
    Corresponds to variant rs121912300 [ dbSNP | Ensembl ].
    VAR_010083
    Natural varianti353 – 3531A → V in DKCX and HHS. 2 Publications
    Corresponds to variant rs121912288 [ dbSNP | Ensembl ].
    VAR_009264
    Natural varianti402 – 4021G → E in DKCX. 1 Publication
    Corresponds to variant rs121912295 [ dbSNP | Ensembl ].
    VAR_006815
    Natural varianti402 – 4021G → R in DKCX. 1 Publication
    Corresponds to variant rs121912299 [ dbSNP | Ensembl ].
    VAR_010084
    Natural varianti409 – 4091P → L in DKCX. 1 Publication
    Corresponds to variant rs121912289 [ dbSNP | Ensembl ].
    VAR_063825

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei420 – 51495SESAK…ELVSE → R in isoform 3. 1 PublicationVSP_042422Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14761.1. [O60832-1]
    RefSeqiNP_001135935.1. NM_001142463.2.
    NP_001275676.1. NM_001288747.1. [O60832-2]
    NP_001354.1. NM_001363.4. [O60832-1]
    UniGeneiHs.4747.

    Genome annotation databases

    EnsembliENST00000369550; ENSP00000358563; ENSG00000130826. [O60832-1]
    GeneIDi1736.
    KEGGihsa:1736.
    UCSCiuc004fmm.3. human. [O60832-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    DKC1base

    DKC1 mutation db

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14761.1. [O60832-1 ]
    RefSeqi NP_001135935.1. NM_001142463.2.
    NP_001275676.1. NM_001288747.1. [O60832-2 ]
    NP_001354.1. NM_001363.4. [O60832-1 ]
    UniGenei Hs.4747.

    3D structure databases

    ProteinModelPortali O60832.
    SMRi O60832. Positions 35-408.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108080. 46 interactions.
    DIPi DIP-40645N.
    IntActi O60832. 27 interactions.
    MINTi MINT-1379892.
    STRINGi 9606.ENSP00000358563.

    PTM databases

    PhosphoSitei O60832.

    2D gel databases

    SWISS-2DPAGE O60832.

    Proteomic databases

    MaxQBi O60832.
    PaxDbi O60832.
    PeptideAtlasi O60832.
    PRIDEi O60832.

    Protocols and materials databases

    DNASUi 1736.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369550 ; ENSP00000358563 ; ENSG00000130826 . [O60832-1 ]
    GeneIDi 1736.
    KEGGi hsa:1736.
    UCSCi uc004fmm.3. human. [O60832-1 ]

    Organism-specific databases

    CTDi 1736.
    GeneCardsi GC0XP153984.
    GeneReviewsi DKC1.
    HGNCi HGNC:2890. DKC1.
    HPAi HPA000166.
    HPA000447.
    HPA001022.
    MIMi 300126. gene.
    305000. phenotype.
    neXtProti NX_O60832.
    Orphaneti 1775. Dyskeratosis congenita.
    3322. Hoyeraal-Hreidarsson syndrome.
    PharmGKBi PA27344.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0130.
    HOGENOMi HOG000231224.
    HOVERGENi HBG081442.
    KOi K11131.
    OMAi HDKLPGG.
    PhylomeDBi O60832.
    TreeFami TF300354.

    Enzyme and pathway databases

    Reactomei REACT_7974. Telomere Extension By Telomerase.

    Miscellaneous databases

    ChiTaRSi DKC1. human.
    GeneWikii Dyskerin.
    GenomeRNAii 1736.
    NextBioi 7039.
    PROi O60832.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60832.
    Bgeei O60832.
    CleanExi HS_DKC1.
    Genevestigatori O60832.

    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

    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 DKCX 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 DKCX 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, IDENTIFICATION BY 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-485 AND SER-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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.
    26. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    27. "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.
    28. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "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.
    33. "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.
    34. "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 DKCX VAL-353 AND LEU-409.
    35. Cited for: VARIANT DKCX PHE-72.
    36. "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 DKCX SER-56.
    37. "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 DKCX PHE-317 AND GLN-322.

    Entry informationi

    Entry nameiDKC1_HUMAN
    AccessioniPrimary (citable) accession number: O60832
    Secondary accession number(s): F5BSB3
    , O43845, Q96G67, Q9Y505
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 164 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3