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NOP10_HUMAN
ID   NOP10_HUMAN             Reviewed;          64 AA.
AC   Q9NPE3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=H/ACA ribonucleoprotein complex subunit 3;
DE   AltName: Full=Nucleolar protein 10;
DE   AltName: Full=Nucleolar protein family A member 3;
DE   AltName: Full=snoRNP protein NOP10;
GN   Name=NOP10; Synonyms=NOLA3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Toji S., Yano M., Tamai K.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=B-cell, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH GAR1; NHP2 AND DCK1.
RX   PubMed=11074001; DOI=10.1128/mcb.20.23.9028-9040.2000;
RA   Pogacic V., Dragon F., Filipowicz W.;
RT   "Human H/ACA small nucleolar RNPs and telomerase share evolutionarily
RT   conserved proteins NHP2 and NOP10.";
RL   Mol. Cell. Biol. 20:9028-9040(2000).
RN   [4]
RP   FUNCTION, AND CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
RX   PubMed=15044956; DOI=10.1038/sj.emboj.7600181;
RA   Wang C., Meier U.T.;
RT   "Architecture and assembly of mammalian H/ACA small nucleolar and
RT   telomerase ribonucleoproteins.";
RL   EMBO J. 23:1857-1867(2004).
RN   [5]
RP   INTERACTION WITH NAF1.
RX   PubMed=16601202; DOI=10.1261/rna.2344106;
RA   Hoareau-Aveilla C., Bonoli M., Caizergues-Ferrer M., Henry Y.;
RT   "hNaf1 is required for accumulation of human box H/ACA snoRNPs, scaRNPs,
RT   and telomerase.";
RL   RNA 12:832-840(2006).
RN   [6]
RP   IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
RX   PubMed=19179534; DOI=10.1126/science.1165357;
RA   Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M.,
RA   Veenstra T.D., Terns M.P., Artandi S.E.;
RT   "A human telomerase holoenzyme protein required for Cajal body localization
RT   and telomere synthesis.";
RL   Science 323:644-648(2009).
RN   [7]
RP   IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
RX   PubMed=20351177; DOI=10.1128/mcb.00151-10;
RA   Egan E.D., Collins K.;
RT   "Specificity and stoichiometry of subunit interactions in the human
RT   telomerase holoenzyme assembled in vivo.";
RL   Mol. Cell. Biol. 30:2775-2786(2010).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   STRUCTURE BY ELECTRON MICROSCOPY (7.7 ANGSTROMS) OF THE TELOMERASE
RP   HOLOENZYME COMPLEX.
RX   PubMed=29695869; DOI=10.1038/s41586-018-0062-x;
RA   Nguyen T.H.D., Tam J., Wu R.A., Greber B.J., Toso D., Nogales E.,
RA   Collins K.;
RT   "Cryo-EM structure of substrate-bound human telomerase holoenzyme.";
RL   Nature 557:190-195(2018).
RN   [11]
RP   VARIANT DKCB1 TRP-34.
RX   PubMed=17507419; DOI=10.1093/hmg/ddm111;
RA   Walne A.J., Vulliamy T., Marrone A., Beswick R., Kirwan M., Masunari Y.,
RA   Al-Qurashi F.-H., Aljurf M., Dokal I.;
RT   "Genetic heterogeneity in autosomal recessive dyskeratosis congenita with
RT   one subtype due to mutations in the telomerase-associated protein NOP10.";
RL   Hum. Mol. Genet. 16:1619-1629(2007).
CC   -!- FUNCTION: Required for ribosome biogenesis and telomere maintenance.
CC       Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP)
CC       complex, which catalyzes pseudouridylation of rRNA. This involves the
CC       isomerization of uridine such that the ribose is subsequently attached
CC       to C5, instead of the normal N1. Each rRNA can contain up to 100
CC       pseudouridine ('psi') residues, which may serve to stabilize the
CC       conformation of rRNAs. May also be required for correct processing or
CC       intranuclear trafficking of TERC, the RNA component of the telomerase
CC       reverse transcriptase (TERT) holoenzyme. {ECO:0000269|PubMed:15044956}.
CC   -!- SUBUNIT: Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA
CC       snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3,
CC       and DKC1/NOLA4, which is presumed to be the catalytic subunit
CC       (PubMed:11074001). The complex contains a stable core formed by binding
CC       of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds
CC       to this core via DKC1 (PubMed:11074001). The complex binds a box H/ACA
CC       small nucleolar RNA (snoRNA), which may target the specific site of
CC       modification within the RNA substrate (PubMed:16601202). During
CC       assembly, the complex contains NAF1 instead of GAR1/NOLA1
CC       (PubMed:11074001, PubMed:16601202). The complex also interacts with
CC       TERC, which contains a 3'-terminal domain related to the box H/ACA
CC       snoRNAs (PubMed:11074001, PubMed:16601202). Specific interactions with
CC       snoRNAs or TERC are mediated by GAR1 and NHP2 (PubMed:11074001,
CC       PubMed:16601202). Associates with NOLC1/NOPP140 (PubMed:11074001,
CC       PubMed:16601202). H/ACA snoRNPs interact with the SMN complex,
CC       consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4
CC       (PubMed:11074001, PubMed:16601202). This is mediated by interaction
CC       between GAR1 and SMN1 or SMN2 (PubMed:11074001, PubMed:16601202). The
CC       SMN complex may be required for correct assembly of the H/ACA snoRNP
CC       complex (PubMed:11074001, PubMed:16601202). Component of the telomerase
CC       holoenzyme complex composed of one molecule of TERT, one molecule of
CC       WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits
CC       DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component
CC       (TERC) (PubMed:19179534, PubMed:20351177, PubMed:29695869). The
CC       telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and
CC       POT1 (PubMed:19179534). {ECO:0000269|PubMed:11074001,
CC       ECO:0000269|PubMed:16601202, ECO:0000269|PubMed:19179534,
CC       ECO:0000269|PubMed:20351177, ECO:0000269|PubMed:29695869}.
CC   -!- INTERACTION:
CC       Q9NPE3; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-1642169, EBI-12011224;
CC       Q9NPE3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1642169, EBI-16439278;
CC       Q9NPE3; Q9NX24: NHP2; NbExp=11; IntAct=EBI-1642169, EBI-1050064;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11074001}.
CC       Nucleus, Cajal body {ECO:0000269|PubMed:11074001}. Note=Also localized
CC       to Cajal bodies (coiled bodies).
CC   -!- DISEASE: Dyskeratosis congenita, autosomal recessive, 1 (DKCB1)
CC       [MIM:224230]: A rare multisystem disorder caused by defective telomere
CC       maintenance. It is characterized by progressive bone marrow failure,
CC       and the clinical triad of reticulated skin hyperpigmentation, nail
CC       dystrophy, and mucosal leukoplakia. Common but variable features
CC       include premature graying, aplastic anemia, low platelets,
CC       osteoporosis, pulmonary fibrosis, and liver fibrosis among others.
CC       Early mortality is often associated with bone marrow failure,
CC       infections, fatal pulmonary complications, or malignancy.
CC       {ECO:0000269|PubMed:17507419}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the NOP10 family. {ECO:0000305}.
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DR   EMBL; AB043103; BAA96107.1; -; Genomic_DNA.
DR   EMBL; AB043104; BAA96133.1; -; mRNA.
DR   EMBL; BC008886; AAH08886.1; -; mRNA.
DR   EMBL; BC063023; AAH63023.1; -; mRNA.
DR   CCDS; CCDS10037.1; -.
DR   RefSeq; NP_061118.1; NM_018648.3.
DR   PDB; 7BGB; EM; 3.39 A; F/J=1-64.
DR   PDB; 7V9A; EM; 3.94 A; F/J=1-64.
DR   PDBsum; 7BGB; -.
DR   PDBsum; 7V9A; -.
DR   AlphaFoldDB; Q9NPE3; -.
DR   SMR; Q9NPE3; -.
DR   BioGRID; 120685; 89.
DR   ComplexPortal; CPX-265; Telomerase holoenzyme complex.
DR   CORUM; Q9NPE3; -.
DR   DIP; DIP-40092N; -.
DR   IntAct; Q9NPE3; 32.
DR   MINT; Q9NPE3; -.
DR   STRING; 9606.ENSP00000332198; -.
DR   GlyGen; Q9NPE3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NPE3; -.
DR   MetOSite; Q9NPE3; -.
DR   PhosphoSitePlus; Q9NPE3; -.
DR   BioMuta; NOP10; -.
DR   DMDM; 54036209; -.
DR   EPD; Q9NPE3; -.
DR   jPOST; Q9NPE3; -.
DR   MassIVE; Q9NPE3; -.
DR   MaxQB; Q9NPE3; -.
DR   PaxDb; Q9NPE3; -.
DR   PeptideAtlas; Q9NPE3; -.
DR   PRIDE; Q9NPE3; -.
DR   ProteomicsDB; 81979; -.
DR   TopDownProteomics; Q9NPE3; -.
DR   Antibodypedia; 41964; 61 antibodies from 16 providers.
DR   DNASU; 55505; -.
DR   Ensembl; ENST00000328848.6; ENSP00000332198.5; ENSG00000182117.6.
DR   GeneID; 55505; -.
DR   KEGG; hsa:55505; -.
DR   MANE-Select; ENST00000328848.6; ENSP00000332198.5; NM_018648.4; NP_061118.1.
DR   UCSC; uc001zie.2; human.
DR   CTD; 55505; -.
DR   DisGeNET; 55505; -.
DR   GeneCards; NOP10; -.
DR   GeneReviews; NOP10; -.
DR   HGNC; HGNC:14378; NOP10.
DR   HPA; ENSG00000182117; Low tissue specificity.
DR   MalaCards; NOP10; -.
DR   MIM; 224230; phenotype.
DR   MIM; 606471; gene.
DR   neXtProt; NX_Q9NPE3; -.
DR   OpenTargets; ENSG00000182117; -.
DR   Orphanet; 1775; Dyskeratosis congenita.
DR   PharmGKB; PA164723973; -.
DR   VEuPathDB; HostDB:ENSG00000182117; -.
DR   eggNOG; KOG3503; Eukaryota.
DR   GeneTree; ENSGT00390000012563; -.
DR   HOGENOM; CLU_184680_1_0_1; -.
DR   InParanoid; Q9NPE3; -.
DR   OMA; MYTLGPD; -.
DR   OrthoDB; 1628018at2759; -.
DR   PhylomeDB; Q9NPE3; -.
DR   TreeFam; TF300211; -.
DR   PathwayCommons; Q9NPE3; -.
DR   Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR   Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR   SignaLink; Q9NPE3; -.
DR   SIGNOR; Q9NPE3; -.
DR   BioGRID-ORCS; 55505; 677 hits in 1086 CRISPR screens.
DR   ChiTaRS; NOP10; human.
DR   GenomeRNAi; 55505; -.
DR   Pharos; Q9NPE3; Tbio.
DR   PRO; PR:Q9NPE3; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9NPE3; protein.
DR   Bgee; ENSG00000182117; Expressed in monocyte and 203 other tissues.
DR   ExpressionAtlas; Q9NPE3; baseline and differential.
DR   Genevisible; Q9NPE3; HS.
DR   GO; GO:0072589; C:box H/ACA scaRNP complex; TAS:BHF-UCL.
DR   GO; GO:0031429; C:box H/ACA snoRNP complex; IDA:BHF-UCL.
DR   GO; GO:0090661; C:box H/ACA telomerase RNP complex; IDA:BHF-UCL.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; TAS:UniProtKB.
DR   GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
DR   GO; GO:0034513; F:box H/ACA snoRNA binding; IPI:BHF-UCL.
DR   GO; GO:0003723; F:RNA binding; IPI:BHF-UCL.
DR   GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
DR   GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL.
DR   GO; GO:0001522; P:pseudouridine synthesis; NAS:UniProtKB.
DR   GO; GO:0031118; P:rRNA pseudouridine synthesis; IBA:GO_Central.
DR   GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IDA:UniProtKB.
DR   InterPro; IPR007264; H/ACA_rnp_Nop10.
DR   InterPro; IPR036756; H/ACA_rnp_Nop10_sf.
DR   PANTHER; PTHR13305; PTHR13305; 1.
DR   Pfam; PF04135; Nop10p; 1.
DR   SUPFAM; SSF144210; SSF144210; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disease variant; Dyskeratosis congenita; Nucleus;
KW   Reference proteome; Ribonucleoprotein; Ribosome biogenesis;
KW   rRNA processing.
FT   CHAIN           1..64
FT                   /note="H/ACA ribonucleoprotein complex subunit 3"
FT                   /id="PRO_0000149001"
FT   VARIANT         34
FT                   /note="R -> W (in DKCB1; dbSNP:rs121908092)"
FT                   /evidence="ECO:0000269|PubMed:17507419"
FT                   /id="VAR_043725"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:7BGB"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:7BGB"
FT   STRAND          13..20
FT                   /evidence="ECO:0007829|PDB:7BGB"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:7BGB"
FT   STRAND          28..31
FT                   /evidence="ECO:0007829|PDB:7BGB"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:7BGB"
SQ   SEQUENCE   64 AA;  7706 MW;  62E9BCFFB27036FA CRC64;
     MFLQYYLNEQ GDRVYTLKKF DPMGQQTCSA HPARFSPDDK YSRHRITIKK RFKVLMTQQP
     RPVL
 
 
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