LOCUS       NM_000925               1507 bp    mRNA    linear   PRI 08-OCT-2024
DEFINITION  Homo sapiens pyruvate dehydrogenase E1 subunit beta (PDHB),
            transcript variant 1, mRNA; nuclear gene for mitochondrial product.
ACCESSION   NM_000925
VERSION     NM_000925.4
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 1507)
  AUTHORS   Wu,J., Wang,S., Liu,Y., Zhang,T., Wang,X. and Miao,C.
  TITLE     Integrated single-cell and bulk characterization of cuproptosis key
            regulator PDHB and association with tumor microenvironment
            infiltration in clear cell renal cell carcinoma
  JOURNAL   Front Immunol 14, 1132661 (2023)
   PUBMED   37350959
  REMARK    GeneRIF: Integrated single-cell and bulk characterization of
            cuproptosis key regulator PDHB and association with tumor
            microenvironment infiltration in clear cell renal cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (bases 1 to 1507)
  AUTHORS   Jiang,X., Ji,S., Yuan,F., Li,T., Cui,S., Wang,W., Ye,X., Wang,R.,
            Chen,Y. and Zhu,S.
  TITLE     Pyruvate dehydrogenase B regulates myogenic differentiation via the
            FoxP1-Arih2 axis
  JOURNAL   J Cachexia Sarcopenia Muscle 14 (1), 606-621 (2023)
   PUBMED   36564038
  REMARK    GeneRIF: Pyruvate dehydrogenase B regulates myogenic
            differentiation via the FoxP1-Arih2 axis.
REFERENCE   3  (bases 1 to 1507)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (bases 1 to 1507)
  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   5  (bases 1 to 1507)
  AUTHORS   Yonashiro,R., Eguchi,K., Wake,M., Takeda,N. and Nakayama,K.
  TITLE     Pyruvate Dehydrogenase PDH-E1beta Controls Tumor Progression by
            Altering the Metabolic Status of Cancer Cells
  JOURNAL   Cancer Res 78 (7), 1592-1603 (2018)
   PUBMED   29436427
  REMARK    GeneRIF: Building on evidence that PDH activity depends on the
            stability of a multi-protein PDH complex, the authors found that
            the PDH-E1beta subunit of the PDH complex is downregulated to
            inhibit PDH activity under conditions of prolonged hypoxia which
            establishs the specific mechanism through which PDH acts as an
            oncogenic factor by tuning glycolytic metabolism in cancer cells.
REFERENCE   6  (bases 1 to 1507)
  AUTHORS   Ganetzky,R., McCormick,E.M. and Falk,M.J.
  TITLE     Primary Pyruvate Dehydrogenase Complex Deficiency Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34138529
REFERENCE   7  (bases 1 to 1507)
  AUTHORS   Chun,K., Mackay,N., Willard,H.F. and Robinson,B.H.
  TITLE     Isolation, characterization and chromosomal localization of cDNA
            clones for the E1 beta subunit of the pyruvate dehydrogenase
            complex
  JOURNAL   Eur J Biochem 194 (2), 587-592 (1990)
   PUBMED   1702713
REFERENCE   8  (bases 1 to 1507)
  AUTHORS   Ho,L. and Patel,M.S.
  TITLE     Cloning and cDNA sequence of the beta-subunit component of human
            pyruvate dehydrogenase complex
  JOURNAL   Gene 86 (2), 297-302 (1990)
   PUBMED   2323578
REFERENCE   9  (bases 1 to 1507)
  AUTHORS   Olson,S., Song,B.J., Huh,T.L., Chi,Y.T., Veech,R.L. and
            McBride,O.W.
  TITLE     Three genes for enzymes of the pyruvate dehydrogenase complex map
            to human chromosomes 3, 7, and X
  JOURNAL   Am J Hum Genet 46 (2), 340-349 (1990)
   PUBMED   1967901
  REMARK    Erratum:[Am J Hum Genet 1990 Jun;46(6):1235]
REFERENCE   10 (bases 1 to 1507)
  AUTHORS   Muno,D., Kominami,E., Ishii,H., Usui,K., Saifuku,K., Sakakibara,Y.
            and Namihisa,T.
  TITLE     Isolation of tryptic fragment of antigen from mitochondrial inner
            membrane proteins reacting with antimitochondrial antibody in sera
            of patients with primary biliary cirrhosis
  JOURNAL   Hepatology 11 (1), 16-23 (1990)
   PUBMED   2295468
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135507.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2018 this sequence version replaced NM_000925.3.
            
            Summary: The pyruvate dehydrogenase (PDH) complex is a
            nuclear-encoded mitochondrial multienzyme complex that catalyzes
            the overall conversion of pyruvate to acetyl-CoA and carbon
            dioxide, and provides the primary link between glycolysis and the
            tricarboxylic acid (TCA) cycle. The PDH complex is composed of
            multiple copies of three enzymatic components: pyruvate
            dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
            lipoamide dehydrogenase (E3). The E1 enzyme is a heterotetramer of
            two alpha and two beta subunits. This gene encodes the E1 beta
            subunit. Mutations in this gene are associated with pyruvate
            dehydrogenase E1-beta deficiency. Alternatively spliced transcript
            variants have been found for this gene. [provided by RefSeq, Mar
            2012].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes the longest 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 :: AK225621.1, SRR5189658.106232.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2146411
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000302746.11/
                                                  ENSP00000307241.6
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-65                AC135507.2         135026-135090       c
            66-119              AC135507.2         134889-134942       c
            120-227             AC135507.2         133135-133242       c
            228-290             AC135507.2         132989-133051       c
            291-326             AC135507.2         132851-132886       c
            327-612             AC135507.2         131915-132200       c
            613-723             AC135507.2         131386-131496       c
            724-815             AC135507.2         130966-131057       c
            816-957             AC135507.2         129731-129872       c
            958-1507            AC135507.2         128888-129437       c
FEATURES             Location/Qualifiers
     source          1..1507
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     gene            1..1507
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /note="pyruvate dehydrogenase E1 subunit beta"
                     /db_xref="GeneID:5162"
                     /db_xref="HGNC:HGNC:8808"
                     /db_xref="MIM:179060"
     exon            1..65
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     CDS             24..1103
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /EC_number="1.2.4.1"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1; pyruvate dehydrogenase E1 component subunit
                     beta, mitochondrial; pyruvate dehydrogenase, E1 beta
                     polypeptide; pyruvate dehydrogenase (lipoamide) beta;
                     epididymis secretory sperm binding protein; pyruvate
                     dehydrogenase E1 beta subunit"
                     /codon_start=1
                     /product="pyruvate dehydrogenase E1 component subunit
                     beta, mitochondrial isoform 1 precursor"
                     /protein_id="NP_000916.2"
                     /db_xref="CCDS:CCDS2890.1"
                     /db_xref="GeneID:5162"
                     /db_xref="HGNC:HGNC:8808"
                     /db_xref="MIM:179060"
                     /translation="MAAVSGLVRRPLREVSGLLKRRFHWTAPAALQVTVRDAINQGMD
                     EELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMA
                     GLRPICEFMTFNFSMQAIDQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQ
                     CFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQS
                     KDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDM
                     ETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPY
                     AKILEDNSIPQVKDIIFAIKKTLNI"
     exon            66..119
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     exon            120..227
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     exon            228..290
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     exon            291..326
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     exon            327..612
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     exon            613..723
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     exon            724..815
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     exon            816..957
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     exon            958..1507
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1091..1096
                     /regulatory_class="polyA_signal_sequence"
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /note="hexamer: ATTAAA"
     polyA_site      1115
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /note="major polyA site"
     regulatory      1440..1445
                     /regulatory_class="polyA_signal_sequence"
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /note="hexamer: ATTAAA"
     polyA_site      1459
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
     regulatory      1486..1491
                     /regulatory_class="polyA_signal_sequence"
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /note="hexamer: AATAAA"
     polyA_site      1507
                     /gene="PDHB"
                     /gene_synonym="E1beta; PDHBD; PDHE1-B; PDHE1B; PHE1B"
                     /note="major polyA site"
ORIGIN      
        1 agcggataga ggacacgacc aagatggcgg cggtgtctgg cttggtgcgg agaccccttc
       61 gggaggtctc cgggctgctg aagaggcgct ttcactggac cgcgccggct gcgctgcagg
      121 tgacagttcg tgatgctata aatcagggta tggatgagga gctggaaaga gatgagaagg
      181 tatttctgct tggagaagaa gttgcccagt atgatggggc atacaaggtt agtcgagggc
      241 tgtggaagaa atatggagac aagaggatta ttgacactcc catatcagag atgggctttg
      301 ctggaattgc tgtaggtgca gctatggctg ggttgcggcc catttgtgaa tttatgacct
      361 tcaatttctc catgcaagcc attgaccagg ttataaactc agctgccaag acctactaca
      421 tgtctggtgg ccttcagcct gtgcctatag tcttcagagg gcccaatggt gcctcagcag
      481 gtgtagctgc ccagcactca cagtgctttg ctgcctggta tgggcactgc ccaggcttaa
      541 aggtggtcag tccctggaat tcagaggatg ctaaaggact tattaaatca gccattcggg
      601 ataacaatcc agtggtggtg ctagagaatg aattgatgta tggggttcct tttgaatttc
      661 ctccggaagc tcagtcaaaa gattttctga ttcctattgg aaaagccaaa atagaaaggc
      721 aaggaacaca tataactgtg gtttcccatt caagacctgt gggccactgc ttagaagctg
      781 cagcagtgct atctaaagaa ggagttgaat gtgaggtgat aaatatgcgt accattagac
      841 caatggacat ggaaaccata gaagccagtg tcatgaagac aaatcatctt gtaactgtgg
      901 aaggaggctg gccacagttt ggagtaggag ctgaaatctg tgccaggatc atggaaggtc
      961 ctgcgttcaa tttcctggat gctcctgctg ttcgtgtcac tggtgctgat gtccctatgc
     1021 cttatgcaaa gattctagag gacaactcta tacctcaggt caaagacatc atatttgcaa
     1081 taaagaaaac attaaatatt tagtttggac ttgaatatca agtcgttgaa atttatttga
     1141 aatacttgct ggcactgcac ctggatttgt actgcaagac ctgactattc ataacggaaa
     1201 acgatttcta aagcaacagc aggtattttt gtacagggaa gtttaaatgt gtttgtgtat
     1261 ggaaaactct ccactctcct cccctagatg ccatgcttcc ttttgtctgt tacggttgcc
     1321 atgttctttg aataacaaat tatataacat tttatcctct ctcaccacaa ggacaaagta
     1381 tggatgtggc agagtcctca tgaaagatgt atccaaacaa gataacttat atgtataaaa
     1441 ttaaagcata taatatacat ttactgttag tttgttttga taaggaataa aggaatttct
     1501 aacatga
//
