NHP2_MOUSE
ID NHP2_MOUSE Reviewed; 153 AA.
AC Q9CRB2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
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. The
CC complex contains a stable core formed by binding of one or two NOP10-
CC DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via
CC DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which
CC may target the specific site of modification within the RNA substrate.
CC During assembly, the complex contains NAF1 instead of GAR1/NOLA1. The
CC complex also interacts with TERC, which contains a 3'-terminal domain
CC related to the box H/ACA snoRNAs. Specific interactions with snoRNAs or
CC TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140.
CC H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or
CC SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is mediated by
CC interaction between GAR1 and SMN1 or SMN2. The SMN complex may be
CC required for correct assembly of the H/ACA snoRNP complex. Component of
CC the 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). The telomerase holoenzyme complex is
CC associated with TEP1, SMG6/EST1A and POT1.
CC {ECO:0000250|UniProtKB:Q9NX24}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, Cajal
CC body {ECO:0000250}. Note=Also localized to Cajal bodies (coiled
CC bodies). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK007340; BAB24973.1; -; mRNA.
DR EMBL; AK008766; BAB25882.1; -; mRNA.
DR EMBL; AK019134; BAB31561.1; -; mRNA.
DR EMBL; BC024944; AAH24944.1; -; mRNA.
DR CCDS; CCDS24655.1; -.
DR RefSeq; NP_080907.1; NM_026631.3.
DR AlphaFoldDB; Q9CRB2; -.
DR SMR; Q9CRB2; -.
DR BioGRID; 206642; 4.
DR ComplexPortal; CPX-1124; Telomerase holoenzyme complex.
DR CORUM; Q9CRB2; -.
DR IntAct; Q9CRB2; 2.
DR MINT; Q9CRB2; -.
DR STRING; 10090.ENSMUSP00000120014; -.
DR iPTMnet; Q9CRB2; -.
DR PhosphoSitePlus; Q9CRB2; -.
DR EPD; Q9CRB2; -.
DR MaxQB; Q9CRB2; -.
DR PaxDb; Q9CRB2; -.
DR PeptideAtlas; Q9CRB2; -.
DR PRIDE; Q9CRB2; -.
DR ProteomicsDB; 252835; -.
DR Antibodypedia; 46084; 106 antibodies from 24 providers.
DR DNASU; 52530; -.
DR Ensembl; ENSMUST00000127405; ENSMUSP00000120014; ENSMUSG00000001056.
DR GeneID; 52530; -.
DR KEGG; mmu:52530; -.
DR UCSC; uc007iuc.1; mouse.
DR CTD; 55651; -.
DR MGI; MGI:1098547; Nhp2.
DR VEuPathDB; HostDB:ENSMUSG00000001056; -.
DR eggNOG; KOG3167; Eukaryota.
DR GeneTree; ENSGT00550000074939; -.
DR HOGENOM; CLU_084513_1_0_1; -.
DR InParanoid; Q9CRB2; -.
DR OMA; IDVYSHI; -.
DR OrthoDB; 1538526at2759; -.
DR PhylomeDB; Q9CRB2; -.
DR TreeFam; TF105839; -.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR BioGRID-ORCS; 52530; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Nhp2; mouse.
DR PRO; PR:Q9CRB2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CRB2; protein.
DR Bgee; ENSMUSG00000001056; Expressed in primitive streak and 266 other tissues.
DR Genevisible; Q9CRB2; MM.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; ISO:MGI.
DR GO; GO:0090661; C:box H/ACA telomerase RNP complex; ISO:MGI.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI.
DR GO; GO:0034511; F:U3 snoRNA binding; ISO:MGI.
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:0031118; P:rRNA pseudouridine synthesis; ISS:UniProtKB.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; ISO:MGI.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS: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 Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing;
KW Ubl conjugation.
FT CHAIN 1..153
FT /note="H/ACA ribonucleoprotein complex subunit 2"
FT /id="PRO_0000136765"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX24"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NX24"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NX24"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NX24"
SQ SEQUENCE 153 AA; 17247 MW; 0696C52CC7AFBF10 CRC64;
MTKVKAAPEE SEAQAEGCSE ERTYKELLVN LNPIAQPLAS RRLTRKLYKC IKKAVKQKQI
RRGVKEVQKF VNKGEKGIMV LAGDTLPIEV YCHLPVLCED QNLPYVYIPS KTDLGAATGS
KRPTCVIMVK PHEEYQETYD KCLEEVQALP TPL
