LOCUS       NP_005024                439 aa            linear   PRI 21-SEP-2024
DEFINITION  exosome complex component RRP45 isoform 2 [Homo sapiens].
ACCESSION   NP_005024
VERSION     NP_005024.2
DBSOURCE    REFSEQ: accession NM_005033.3
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  (residues 1 to 439)
  AUTHORS   Quttina,M., Waiters,K.D., Khan,A.F., Karami,S., Peidl,A.S.,
            Babajide,M.F., Pennington,J., Merchant,F.A. and Bawa-Khalfe,T.
  TITLE     Exosc9 Initiates SUMO-Dependent lncRNA TERRA Degradation to Impact
            Telomeric Integrity in Endocrine Therapy Insensitive Hormone
            Receptor-Positive Breast Cancer
  JOURNAL   Cells 12 (20), 2495 (2023)
   PUBMED   37887339
  REMARK    GeneRIF: Exosc9 Initiates SUMO-Dependent lncRNA TERRA Degradation
            to Impact Telomeric Integrity in Endocrine Therapy Insensitive
            Hormone Receptor-Positive Breast Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Sakamoto,M., Iwama,K., Sekiguchi,F., Mashimo,H., Kumada,S.,
            Ishigaki,K., Okamoto,N., Behnam,M., Ghadami,M., Koshimizu,E.,
            Miyatake,S., Mitsuhashi,S., Mizuguchi,T., Takata,A., Saitsu,H.,
            Miyake,N. and Matsumoto,N.
  TITLE     Novel EXOSC9 variants cause pontocerebellar hypoplasia type 1D with
            spinal motor neuronopathy and cerebellar atrophy
  JOURNAL   J Hum Genet 66 (4), 401-407 (2021)
   PUBMED   33040083
  REMARK    GeneRIF: Novel EXOSC9 variants cause pontocerebellar hypoplasia
            type 1D with spinal motor neuronopathy and cerebellar atrophy.
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Yoshino,S., Matsui,Y., Fukui,Y., Seki,M., Yamaguchi,K.,
            Kanamori,A., Saitoh,Y., Shimamura,T., Suzuki,Y., Furukawa,Y.,
            Kaneko,S., Seiki,M., Murakami,Y., Inoue,J.I. and Sakamoto,T.
  TITLE     EXOSC9 depletion attenuates P-body formation, stress resistance,
            and tumorigenicity of cancer cells
  JOURNAL   Sci Rep 10 (1), 9275 (2020)
   PUBMED   32518284
  REMARK    GeneRIF: EXOSC9 depletion attenuates P-body formation, stress
            resistance, and tumorigenicity of cancer cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Bizzari,S., Hamzeh,A.R., Mohamed,M., Al-Ali,M.T. and Bastaki,F.
  TITLE     Expanded PCH1D phenotype linked to EXOSC9 mutation
  JOURNAL   Eur J Med Genet 63 (1), 103622 (2020)
   PUBMED   30690203
  REMARK    GeneRIF: Expanded PCH1D phenotype linked to EXOSC9 mutation.
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Mukherjee,D., Gao,M., O'Connor,J.P., Raijmakers,R., Pruijn,G.,
            Lutz,C.S. and Wilusz,J.
  TITLE     The mammalian exosome mediates the efficient degradation of mRNAs
            that contain AU-rich elements
  JOURNAL   EMBO J 21 (1-2), 165-174 (2002)
   PUBMED   11782436
  REMARK    GeneRIF: The mammalian exosome mediates the efficient degradation
            of mRNAs that contain AU-rich elements, possibly by direct binding
            of PM/Scl-75 to these RNA regions.
REFERENCE   7  (residues 1 to 439)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   8  (residues 1 to 439)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   9  (residues 1 to 439)
  AUTHORS   Allmang,C., Petfalski,E., Podtelejnikov,A., Mann,M., Tollervey,D.
            and Mitchell,P.
  TITLE     The yeast exosome and human PM-Scl are related complexes of 3' -->
            5' exonucleases
  JOURNAL   Genes Dev 13 (16), 2148-2158 (1999)
   PUBMED   10465791
REFERENCE   10 (residues 1 to 439)
  AUTHORS   Alderuccio,F., Chan,E.K. and Tan,E.M.
  TITLE     Molecular characterization of an autoantigen of PM-Scl in the
            polymyositis/scleroderma overlap syndrome: a unique and complete
            human cDNA encoding an apparent 75-kD acidic protein of the
            nucleolar complex
  JOURNAL   J Exp Med 173 (4), 941-952 (1991)
   PUBMED   2007859
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079341.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 18, 2005 this sequence version replaced NP_005024.1.
            
            Summary: This gene encodes a component of the human exosome, a
            exoribonuclease complex which processes and degrades RNA in the
            nucleus and cytoplasm. This component may play a role in mRNA
            degradation and the polymyositis/scleroderma autoantigen complex.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            3' coding region, compared to variant 1. This results in a shorter
            protein (isoform 2), compared to isoform 1.
            
            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 :: SRR3476690.898416.1,
                                           SRR3476690.624888.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000243498.10/ ENSP00000243498.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q27"
     Protein         1..439
                     /product="exosome complex component RRP45 isoform 2"
                     /EC_number="3.1.13.-"
                     /note="polymyositis/scleroderma autoantigen 1, 75kDa;
                     exosome complex exonuclease RRP45; exosome complex
                     component RRP45; PMSCL autoantigen, 75kD; P75
                     polymyositis-scleroderma overlap syndrome associated
                     autoantigen; autoantigen PM/Scl 1"
                     /calculated_mol_wt=48818
     Region          1..268
                     /region_name="ARE binding.
                     /evidence=ECO:0000269|PubMed:16912217"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06265.3)"
     Region          6..264
                     /region_name="RNase_PH_RRP45"
                     /note="RRP45 subunit of eukaryotic exosome; cd11368"
                     /db_xref="CDD:206773"
     Site            order(7..9,12..13,17,20,22)
                     /site_type="other"
                     /note="Rrp40 interface [polypeptide binding]"
                     /db_xref="CDD:206773"
     Site            order(41,43,58,60..62,77,79,84,101,104,108,130,135,140,
                     158..160,190,231..242,247,251)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:206773"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     Site            297
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     Region          335..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06265.3)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     Region          391..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06265.3)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06265.3)"
     CDS             1..439
                     /gene="EXOSC9"
                     /gene_synonym="p5; p6; PCH1D; PM/Scl-75; PMSCL1; RRP45;
                     Rrp45p"
                     /coded_by="NM_005033.3:103..1422"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3722.2"
                     /db_xref="GeneID:5393"
                     /db_xref="HGNC:HGNC:9137"
                     /db_xref="MIM:606180"
ORIGIN      
        1 mketplsnce rrfllraiee kkrldgrqty dyrnirisfg tdygccivel gktrvlgqvs
       61 celvspklnr ategilffnl elsqmaapaf epgrqsdllv klnrlmercl rnskcidtes
      121 lcvvagekvw qirvdlhlln hdgniidaas iaaivalchf rrpdvsvqgd evtlytpeer
      181 dpvplsihhm picvsfaffq qgtyllvdpn ereervmdgl lviamnkhre ictiqssggi
      241 mllkdqvlrc skiagvkvae itelilkale ndqkvrkegg kfgfaesian qritafkmek
      301 apidtsdvee kaeeiiaeae ppsevvstpv lwtpgtaqig egvenswgdl edsekeddeg
      361 ggdqaiildg ikmdtgvevs digsqdapii lsdseeeemi ilepdknpkk irtqttsakq
      421 ekapskkpvk rrkkkraan
//
