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NHP2_PONAB
ID   NHP2_PONAB              Reviewed;         153 AA.
AC   Q5RC65;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CR858415; CAH90644.1; -; mRNA.
DR   RefSeq; NP_001125348.1; NM_001131876.2.
DR   AlphaFoldDB; Q5RC65; -.
DR   SMR; Q5RC65; -.
DR   STRING; 9601.ENSPPYP00000018020; -.
DR   Ensembl; ENSPPYT00000061991; ENSPPYP00000030089; ENSPPYG00000038546.
DR   GeneID; 100172250; -.
DR   KEGG; pon:100172250; -.
DR   CTD; 55651; -.
DR   eggNOG; KOG3167; Eukaryota.
DR   GeneTree; ENSGT00550000074939; -.
DR   HOGENOM; CLU_084513_1_0_1; -.
DR   InParanoid; Q5RC65; -.
DR   OMA; IDVYSHI; -.
DR   OrthoDB; 1538526at2759; -.
DR   TreeFam; TF105839; -.
DR   Proteomes; UP000001595; Chromosome 5.
DR   GO; GO:0031429; C:box H/ACA snoRNP complex; IEA:Ensembl.
DR   GO; GO:0090661; C:box H/ACA telomerase RNP complex; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0070034; F:telomerase RNA binding; IEA:Ensembl.
DR   GO; GO:0031118; P:rRNA pseudouridine synthesis; ISS:UniProtKB.
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   2: Evidence at transcript 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_0000136764"
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;  17187 MW;  7658FDFF89744178 CRC64;
     MTKIKADPDG PEAQAEACSG ERTYQELLVN QNPIAQPLAS RRLTRKLYKC IKKAVKQKQI
     RRGVKEVQKF VNKGEKGIMV LAGDTLPIEV YCHLPVMCED RNLPYVYIPS KTDLGAAAGS
     KRPTCVIMVK PHDEYQEAYD ECLEEVQSLP LPL
 
 
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