LOCUS       NM_001004                462 bp    mRNA    linear   PRI 27-APR-2025
DEFINITION  Homo sapiens ribosomal protein lateral stalk subunit P2 (RPLP2),
            mRNA.
ACCESSION   NM_001004
VERSION     NM_001004.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 462)
  AUTHORS   Horbowicz-Drozdzal,P., Kamel,K., Kmiecik,S., Borkiewicz,L.,
            Tumer,N.E., Shaw,P.C., Tchorzewski,M. and Grela,P.
  TITLE     Phosphorylation of the conserved C-terminal domain of ribosomal
            P-proteins impairs the mode of interaction with plant toxins
  JOURNAL   FEBS Lett 595 (17), 2221-2236 (2021)
   PUBMED   34328639
  REMARK    GeneRIF: Phosphorylation of the conserved C-terminal domain of
            ribosomal P-proteins impairs the mode of interaction with plant
            toxins.
REFERENCE   2  (bases 1 to 462)
  AUTHORS   Cai,Z., Wu,Y., Zhang,F. and Wu,H.
  TITLE     A three-gene signature and clinical outcome in pediatric acute
            myeloid leukemia
  JOURNAL   Clin Transl Oncol 23 (4), 866-873 (2021)
   PUBMED   32862280
  REMARK    GeneRIF: A three-gene signature and clinical outcome in pediatric
            acute myeloid leukemia.
REFERENCE   3  (bases 1 to 462)
  AUTHORS   Campos,R.K., Wijeratne,H.R.S., Shah,P., Garcia-Blanco,M.A. and
            Bradrick,S.S.
  TITLE     Ribosomal stalk proteins RPLP1 and RPLP2 promote biogenesis of
            flaviviral and cellular multi-pass transmembrane proteins
  JOURNAL   Nucleic Acids Res 48 (17), 9872-9885 (2020)
   PUBMED   32890404
  REMARK    GeneRIF: Ribosomal stalk proteins RPLP1 and RPLP2 promote
            biogenesis of flaviviral and cellular multi-pass transmembrane
            proteins.
REFERENCE   4  (bases 1 to 462)
  AUTHORS   Jiang,D., Izumi,K., Ueda,T., Oshima,K., Nakashima,T. and Kimura,M.
  TITLE     Functional characterization of archaeal homologs of human nuclear
            RNase P proteins Rpp21 and Rpp29 provides insights into the
            molecular basis of their cooperativity in catalysis
  JOURNAL   Biochem Biophys Res Commun 482 (1), 68-74 (2017)
   PUBMED   27810361
  REMARK    GeneRIF: Collectively, the present results suggest that PhoRpp21
            binds the loop between P11 and P12 helices through overall
            positively charged clusters on the surface of the complex and
            serves as a scaffold for PhoRpp29 to optimize structural
            conformation of its N-terminal helix (alpha2) in PhoRpp21, as well
            as C-terminal residues in PhoRpp29, for RNase P activity.
REFERENCE   5  (bases 1 to 462)
  AUTHORS   Artero-Castro,A., Perez-Alea,M., Feliciano,A., Leal,J.A.,
            Genestar,M., Castellvi,J., Peg,V., Ramon Y Cajal,S. and
            Lleonart,M.E.
  TITLE     Disruption of the ribosomal P complex leads to stress-induced
            autophagy
  JOURNAL   Autophagy 11 (9), 1499-1519 (2015)
   PUBMED   26176264
  REMARK    GeneRIF: absence of RPLP0, RPLP1, or RPLP2 resulted in reactive
            oxygen species (ROS) accumulation and MAPK1/ERK2 signaling pathway
            activation.
REFERENCE   6  (bases 1 to 462)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   7  (bases 1 to 462)
  AUTHORS   Matoba,R., Okubo,K., Hori,N., Fukushima,A. and Matsubara,K.
  TITLE     The addition of 5'-coding information to a 3'-directed cDNA library
            improves analysis of gene expression
  JOURNAL   Gene 146 (2), 199-207 (1994)
   PUBMED   8076819
REFERENCE   8  (bases 1 to 462)
  AUTHORS   Hochstrasser,D.F., Frutiger,S., Paquet,N., Bairoch,A., Ravier,F.,
            Pasquali,C., Sanchez,J.C., Tissot,J.D., Bjellqvist,B., Vargas,R. et
            al.
  TITLE     Human liver protein map: a reference database established by
            microsequencing and gel comparison
  JOURNAL   Electrophoresis 13 (12), 992-1001 (1992)
   PUBMED   1286669
REFERENCE   9  (bases 1 to 462)
  AUTHORS   Sharp,M.G., Adams,S.M., Elvin,P., Walker,R.A., Brammar,W.J. and
            Varley,J.M.
  TITLE     A sequence previously identified as metastasis-related encodes an
            acidic ribosomal phosphoprotein, P2
  JOURNAL   Br J Cancer 61 (1), 83-88 (1990)
   PUBMED   2153399
REFERENCE   10 (bases 1 to 462)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol Cell Biol 7 (11), 4065-4074 (1987)
   PUBMED   3323886
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC005354.1 and BC007573.1.
            
            On Nov 22, 2018 this sequence version replaced NM_001004.3.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            phosphoprotein that is a component of the 60S subunit. The protein,
            which is a functional equivalent of the E. coli L7/L12 ribosomal
            protein, belongs to the L12P family of ribosomal proteins. It plays
            an important role in the elongation step of protein synthesis.
            Unlike most ribosomal proteins, which are basic, the encoded
            protein is acidic. Its C-terminal end is nearly identical to the
            C-terminal ends of the ribosomal phosphoproteins P0 and P1. The P2
            protein can interact with P0 and P1 to form a pentameric complex
            consisting of P1 and P2 dimers, and a P0 monomer. The protein is
            located in the cytoplasm. As is typical for genes encoding
            ribosomal proteins, there are multiple processed pseudogenes of
            this gene dispersed through the genome. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB152601.1, DB577310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321153.9/ ENSP00000322419.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-461               BC005354.1         3-463
            462-462             BC007573.1         438-438
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     gene            1..462
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /note="ribosomal protein lateral stalk subunit P2"
                     /db_xref="GeneID:6181"
                     /db_xref="HGNC:HGNC:10377"
                     /db_xref="MIM:180530"
     exon            1..73
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /inference="alignment:Splign:2.1.0"
     exon            74..197
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /inference="alignment:Splign:2.1.0"
     CDS             75..422
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /note="60S acidic ribosomal protein P2; acidic ribosomal
                     phosphoprotein P2; renal carcinoma antigen NY-REN-44;
                     ribosomal protein, large, P2"
                     /codon_start=1
                     /product="large ribosomal subunit protein P2"
                     /protein_id="NP_000995.1"
                     /db_xref="CCDS:CCDS7717.1"
                     /db_xref="GeneID:6181"
                     /db_xref="HGNC:HGNC:10377"
                     /db_xref="MIM:180530"
                     /translation="MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVIS
                     ELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEES
                     EESDDDMGFGLFD"
     exon            198..246
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /inference="alignment:Splign:2.1.0"
     exon            247..345
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /inference="alignment:Splign:2.1.0"
     exon            346..462
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /inference="alignment:Splign:2.1.0"
     regulatory      440..445
                     /regulatory_class="polyA_signal_sequence"
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /note="hexamer: AATAAA"
     polyA_site      462
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /note="major polyA site"
ORIGIN      
        1 ccttttcctc cctgtcgcca ccgaggtcgc acgcgtgaga cttctccgcc gcctccgccg
       61 cagacgccgc cgcgatgcgc tacgtcgcct cctacctgct ggctgcccta gggggcaact
      121 cctcccccag cgccaaggac atcaagaaga tcttggacag cgtgggtatc gaggcggacg
      181 acgaccggct caacaaggtt atcagtgagc tgaatggaaa aaacattgaa gacgtcattg
      241 cccagggtat tggcaagctt gccagtgtac ctgctggtgg ggctgtagcc gtctctgctg
      301 ccccaggctc tgcagcccct gctgctggtt ctgcccctgc tgcagcagag gagaagaaag
      361 atgagaagaa ggaggagtct gaagagtcag atgatgacat gggatttggc ctttttgatt
      421 aaattcctgc tcccctgcaa ataaagcctt tttacacatc tc
//
