NHP2_HUMAN
ID NHP2_HUMAN Reviewed; 153 AA.
AC Q9NX24; A6NKY8; Q9P095;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit 2;
DE AltName: Full=Nucleolar protein family A member 2;
DE AltName: Full=snoRNP protein NHP2;
GN Name=NHP2; Synonyms=NOLA2; ORFNames=HSPC286;
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 [MRNA], INTERACTION WITH GAR1; SMALL NUCLEOLAR RNAS AND
RP TERC, AND SUBCELLULAR LOCATION.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12020816; DOI=10.1016/s0167-4781(02)00240-3;
RA Kang H.S., Jung H.M., Jun D., Huh T.L., Kim Y.H.;
RT "Expression of the human homologue of the small nucleolar RNA-binding
RT protein NHP2 gene during monocytic differentiation of U937 cells.";
RL Biochim. Biophys. Acta 1575:31-39(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and Placenta;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=11790298; DOI=10.1016/s0960-9822(01)00650-9;
RA Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H.,
RA Mann M., Lamond A.I.;
RT "Directed proteomic analysis of the human nucleolus.";
RL Curr. Biol. 12:1-11(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [10]
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 [11]
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 [12]
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 [13]
RP SUMOYLATION AT LYS-5.
RX PubMed=20797632; DOI=10.1016/j.molcel.2010.07.025;
RA Westman B.J., Verheggen C., Hutten S., Lam Y.W., Bertrand E., Lamond A.I.;
RT "A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates
RT the function of Nop5/Nop58.";
RL Mol. Cell 39:618-631(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-5, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
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 [24]
RP VARIANTS DKCB2 MET-126 AND HIS-139, AND VARIANT THR-118.
RX PubMed=18523010; DOI=10.1073/pnas.0800042105;
RA Vulliamy T., Beswick R., Kirwan M., Marrone A., Digweed M., Walne A.,
RA Dokal I.;
RT "Mutations in the telomerase component NHP2 cause the premature ageing
RT syndrome dyskeratosis congenita.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8073-8078(2008).
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:11074001). During
CC assembly, the complex contains NAF1 instead of GAR1/NOLA1
CC (PubMed:11074001). The complex also interacts with TERC, which contains
CC a 3'-terminal domain related to the box H/ACA snoRNAs
CC (PubMed:11074001). Specific interactions with snoRNAs or TERC are
CC mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140
CC (PubMed:11074001). H/ACA snoRNPs interact with the SMN complex,
CC consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This
CC is mediated by interaction between GAR1 and SMN1 or SMN2
CC (PubMed:11074001). The SMN complex may be required for correct assembly
CC of the H/ACA snoRNP complex (PubMed:11074001). Component of the
CC telomerase holoenzyme complex composed of one molecule of TERT, one
CC molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein
CC complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA
CC template component (TERC) (PubMed:19179534, PubMed:20351177,
CC PubMed:29695869). The telomerase holoenzyme complex is associated with
CC TEP1, SMG6/EST1A and POT1 (PubMed:19179534).
CC {ECO:0000269|PubMed:11074001, ECO:0000269|PubMed:19179534,
CC ECO:0000269|PubMed:20351177, ECO:0000269|PubMed:29695869}.
CC -!- INTERACTION:
CC Q9NX24; P42858: HTT; NbExp=3; IntAct=EBI-1050064, EBI-466029;
CC Q9NX24; Q9NPE3: NOP10; NbExp=11; IntAct=EBI-1050064, EBI-1642169;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, Cajal body.
CC Note=Also localized to Cajal bodies (coiled bodies).
CC -!- TISSUE SPECIFICITY: Expressed in brain, colon, heart, kidney, ovary,
CC pancreas, placenta, prostate, skeletal muscle, small intestine, spleen,
CC testis and thymus. Also expressed at lower levels in the liver.
CC {ECO:0000269|PubMed:12020816}.
CC -!- DEVELOPMENTAL STAGE: Transcript peaks at G1/S transition.
CC {ECO:0000269|PubMed:12020816}.
CC -!- DISEASE: Dyskeratosis congenita, autosomal recessive, 2 (DKCB2)
CC [MIM:613987]: 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:18523010}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28964.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ293309; CAC08452.1; -; mRNA.
DR EMBL; AF401219; AAL02175.1; -; mRNA.
DR EMBL; AF161404; AAF28964.1; ALT_FRAME; mRNA.
DR EMBL; AK000486; BAA91198.1; -; mRNA.
DR EMBL; CR457238; CAG33519.1; -; mRNA.
DR EMBL; AC136632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000009; AAH00009.1; -; mRNA.
DR EMBL; BC006387; AAH06387.1; -; mRNA.
DR CCDS; CCDS4432.1; -.
DR RefSeq; NP_001030005.1; NM_001034833.1.
DR RefSeq; NP_060308.1; NM_017838.3.
DR PDB; 7BGB; EM; 3.39 A; E/I=1-153.
DR PDB; 7V9A; EM; 3.94 A; E/I=1-153.
DR PDBsum; 7BGB; -.
DR PDBsum; 7V9A; -.
DR AlphaFoldDB; Q9NX24; -.
DR SMR; Q9NX24; -.
DR BioGRID; 120783; 114.
DR ComplexPortal; CPX-265; Telomerase holoenzyme complex.
DR CORUM; Q9NX24; -.
DR IntAct; Q9NX24; 29.
DR MINT; Q9NX24; -.
DR STRING; 9606.ENSP00000274606; -.
DR GlyGen; Q9NX24; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NX24; -.
DR PhosphoSitePlus; Q9NX24; -.
DR SwissPalm; Q9NX24; -.
DR BioMuta; NHP2; -.
DR DMDM; 68565945; -.
DR SWISS-2DPAGE; Q9NX24; -.
DR EPD; Q9NX24; -.
DR jPOST; Q9NX24; -.
DR MassIVE; Q9NX24; -.
DR MaxQB; Q9NX24; -.
DR PaxDb; Q9NX24; -.
DR PeptideAtlas; Q9NX24; -.
DR PRIDE; Q9NX24; -.
DR ProteomicsDB; 83025; -.
DR Antibodypedia; 46084; 106 antibodies from 24 providers.
DR DNASU; 55651; -.
DR Ensembl; ENST00000274606.8; ENSP00000274606.4; ENSG00000145912.9.
DR GeneID; 55651; -.
DR KEGG; hsa:55651; -.
DR MANE-Select; ENST00000274606.8; ENSP00000274606.4; NM_017838.4; NP_060308.1.
DR UCSC; uc003mir.4; human.
DR CTD; 55651; -.
DR DisGeNET; 55651; -.
DR GeneCards; NHP2; -.
DR GeneReviews; NHP2; -.
DR HGNC; HGNC:14377; NHP2.
DR HPA; ENSG00000145912; Low tissue specificity.
DR MalaCards; NHP2; -.
DR MIM; 606470; gene.
DR MIM; 613987; phenotype.
DR neXtProt; NX_Q9NX24; -.
DR OpenTargets; ENSG00000145912; -.
DR Orphanet; 1775; Dyskeratosis congenita.
DR PharmGKB; PA164723898; -.
DR VEuPathDB; HostDB:ENSG00000145912; -.
DR eggNOG; KOG3167; Eukaryota.
DR GeneTree; ENSGT00550000074939; -.
DR HOGENOM; CLU_084513_1_0_1; -.
DR InParanoid; Q9NX24; -.
DR OMA; IDVYSHI; -.
DR OrthoDB; 1538526at2759; -.
DR PhylomeDB; Q9NX24; -.
DR TreeFam; TF105839; -.
DR PathwayCommons; Q9NX24; -.
DR Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR SignaLink; Q9NX24; -.
DR SIGNOR; Q9NX24; -.
DR BioGRID-ORCS; 55651; 725 hits in 1048 CRISPR screens.
DR ChiTaRS; NHP2; human.
DR GeneWiki; NOLA2; -.
DR GenomeRNAi; 55651; -.
DR Pharos; Q9NX24; Tbio.
DR PRO; PR:Q9NX24; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NX24; protein.
DR Bgee; ENSG00000145912; Expressed in esophagus squamous epithelium and 201 other tissues.
DR ExpressionAtlas; Q9NX24; baseline and differential.
DR Genevisible; Q9NX24; 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:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; ISS: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:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IPI:BHF-UCL.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
DR GO; GO:0034511; F:U3 snoRNA binding; IEA:Ensembl.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; ISS:UniProtKB.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IEA:Ensembl.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:UniProtKB.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00883; NUCLEARHMG.
DR SUPFAM; SSF55315; SSF55315; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Dyskeratosis congenita; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1..153
FT /note="H/ACA ribonucleoprotein complex subunit 2"
FT /id="PRO_0000136763"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VARIANT 118
FT /note="A -> T (in dbSNP:rs139588879)"
FT /evidence="ECO:0000269|PubMed:18523010"
FT /id="VAR_065870"
FT VARIANT 126
FT /note="V -> M (in DKCB2; dbSNP:rs121908090)"
FT /evidence="ECO:0000269|PubMed:18523010"
FT /id="VAR_065871"
FT VARIANT 139
FT /note="Y -> H (in DKCB2; dbSNP:rs121908089)"
FT /evidence="ECO:0000269|PubMed:18523010"
FT /id="VAR_065872"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:7BGB"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:7BGB"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:7BGB"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:7BGB"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:7BGB"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:7BGB"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:7BGB"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:7BGB"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7BGB"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:7BGB"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:7BGB"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:7BGB"
SQ SEQUENCE 153 AA; 17201 MW; 7658FDFF88AF3178 CRC64;
MTKIKADPDG PEAQAEACSG ERTYQELLVN QNPIAQPLAS RRLTRKLYKC IKKAVKQKQI
RRGVKEVQKF VNKGEKGIMV LAGDTLPIEV YCHLPVMCED RNLPYVYIPS KTDLGAAAGS
KRPTCVIMVK PHEEYQEAYD ECLEEVQSLP LPL
