ID   D6RC52_HUMAN            Unreviewed;       132 AA.
AC   D6RC52;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=H/ACA ribonucleoprotein complex subunit 2 {ECO:0000256|RuleBase:RU366039};
DE   Flags: Fragment;
GN   Name=NHP2 {ECO:0000313|Ensembl:ENSP00000423849.1};
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 {ECO:0000313|Ensembl:ENSP00000423849.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000423849.1, ECO:0000313|Proteomes:UP000005640}
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   [2] {ECO:0007829|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3] {ECO:0007829|PubMed:21269460}
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., Burckstummer 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   [4] {ECO:0007829|PubMed:22814378}
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   [5] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [6] {ECO:0007829|PubMed:25218447}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447;
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   [7] {ECO:0007829|PubMed:25114211}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211;
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   [8] {ECO:0007829|PubMed:25772364}
RP   IDENTIFICATION BY MASS 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   [9] {ECO:0007829|PubMed:25755297}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.O114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson 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   [10] {ECO:0007829|PubMed:28112733}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733;
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   [11] {ECO:0000313|Ensembl:ENSP00000423849.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Common component of the spliceosome and rRNA processing
CC       machinery. {ECO:0000256|RuleBase:RU366039}.
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.
CC       {ECO:0000256|RuleBase:RU366039}.
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:0000256|RuleBase:RU366039}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU366039}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC       {ECO:0000256|ARBA:ARBA00007337, ECO:0000256|RuleBase:RU366039}.
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; AC136632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; D6RC52; -.
DR   SMR; D6RC52; -.
DR   MassIVE; D6RC52; -.
DR   MaxQB; D6RC52; -.
DR   PeptideAtlas; D6RC52; -.
DR   ProteomicsDB; 13825; -.
DR   Antibodypedia; 46084; 130 antibodies from 25 providers.
DR   Ensembl; ENST00000511078.1; ENSP00000423849.1; ENSG00000145912.10.
DR   UCSC; uc063kjr.1; human.
DR   HGNC; HGNC:14377; NHP2.
DR   VEuPathDB; HostDB:ENSG00000145912; -.
DR   GeneTree; ENSGT00550000074939; -.
DR   ChiTaRS; NHP2; human.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000145912; Expressed in esophagus squamous epithelium and 203 other cell types or tissues.
DR   ExpressionAtlas; D6RC52; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR   InterPro; IPR018492; Ribosomal_eL8/Nhp2.
DR   Pfam; PF01248; Ribosomal_L7Ae; 1.
DR   PRINTS; PR00881; L7ARS6FAMILY.
DR   PRINTS; PR00883; NUCLEARHMG.
DR   SUPFAM; SSF55315; L30e-like; 1.
PE   1: Evidence at protein level;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366039};
KW   Proteomics identification {ECO:0007829|EPD:D6RC52,
KW   ECO:0007829|MaxQB:D6RC52};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU366039};
KW   RNA-binding {ECO:0000256|RuleBase:RU366039}.
FT   DOMAIN          46..111
FT                   /note="Ribosomal protein eL8/eL30/eS12/Gadd45"
FT                   /evidence="ECO:0000259|Pfam:PF01248"
FT   NON_TER         132
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000423849.1"
SQ   SEQUENCE   132 AA;  15018 MW;  3F0F4EE41A1A18BD CRC64;
     MTKIKADPDG PEAQAEACSG ERTYQELLVN QNPIAQPLAS RRLTRKLYKC IKKAVKQKQI
     RRGVKEVQKF VNKGEKGIMV LAGDTLPIEV YCHLPVMCED RNLPYVYIPS KTVRSTWPPD
     LAQHWGVWDS LP
//