LOCUS       NM_002676               1242 bp    mRNA    linear   PRI 05-APR-2024
DEFINITION  Homo sapiens phosphomannomutase 1 (PMM1), mRNA.
ACCESSION   NM_002676
VERSION     NM_002676.3
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  (bases 1 to 1242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (bases 1 to 1242)
  AUTHORS   Ji,T., Zhang,C., Zheng,L., Dunaway-Mariano,D. and Allen,K.N.
  TITLE     Structural Basis of the Molecular Switch between Phosphatase and
            Mutase Functions of Human Phosphomannomutase 1 under Ischemic
            Conditions
  JOURNAL   Biochemistry 57 (25), 3480-3492 (2018)
   PUBMED   29695157
  REMARK    GeneRIF: The 1.93 A resolution structure of PMM1 complexed with
            inosine monophosphate (IMP) was determined. The structure reveals
            IMP bound at the substrate recruitment site, thus inhibiting the
            mutase activity while simultaneously activating a phosphatase
            activity (IMP Kact = 1.5 muM) resulting from the hydrolysis of the
            phospho-enzyme.
REFERENCE   3  (bases 1 to 1242)
  AUTHORS   Citro,V., Cimmaruta,C., Liguori,L., Viscido,G., Cubellis,M.V. and
            Andreotti,G.
  TITLE     A mutant of phosphomannomutase1 retains full enzymatic activity,
            but is not activated by IMP: Possible implications for the disease
            PMM2-CDG
  JOURNAL   PLoS One 12 (12), e0189629 (2017)
   PUBMED   29261720
  REMARK    GeneRIF: a triple mutant of phospomannomutase1 that retains mutase
            and phosphatase activity, but is unable to bind inosine
            monophosphate, was characterized.
            Publication Status: Online-Only
REFERENCE   4  (bases 1 to 1242)
  AUTHORS   Veiga-da-Cunha,M., Vleugels,W., Maliekal,P., Matthijs,G. and Van
            Schaftingen,E.
  TITLE     Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive
            glucose-1,6-bisphosphatase
  JOURNAL   J Biol Chem 283 (49), 33988-33993 (2008)
   PUBMED   18927083
  REMARK    GeneRIF: PMM1 is responsible for the degradation of Glc-1,6-P(2) in
            brain
REFERENCE   5  (bases 1 to 1242)
  AUTHORS   Romanowski,T., Sikorska,K. and Bielawski,K.P.
  TITLE     GUS and PMM1 as suitable reference genes for gene expression
            analysis in the liver tissue of patients with chronic hepatitis
  JOURNAL   Med Sci Monit 14 (7), BR147-BR152 (2008)
   PUBMED   18591914
  REMARK    GeneRIF: The genes GUS and PMM1 are recommended for normalization
            purposes in gene expression studies of liver tissue from patients
            with chronic hepatitis.
REFERENCE   6  (bases 1 to 1242)
  AUTHORS   Collet,J.F., Stroobant,V., Pirard,M., Delpierre,G. and Van
            Schaftingen,E.
  TITLE     A new class of phosphotransferases phosphorylated on an aspartate
            residue in an amino-terminal DXDX(T/V) motif
  JOURNAL   J Biol Chem 273 (23), 14107-14112 (1998)
   PUBMED   9603909
REFERENCE   7  (bases 1 to 1242)
  AUTHORS   Hansen,S.H., Frank,S.R. and Casanova,J.E.
  TITLE     Cloning and characterization of human phosphomannomutase, a
            mammalian homologue of yeast SEC53
  JOURNAL   Glycobiology 7 (6), 829-834 (1997)
   PUBMED   9376685
REFERENCE   8  (bases 1 to 1242)
  AUTHORS   Pirard,M., Collet,J.F., Matthijs,G. and Van Schaftingen,E.
  TITLE     Comparison of PMM1 with the phosphomannomutases expressed in rat
            liver and in human cells
  JOURNAL   FEBS Lett 411 (2-3), 251-254 (1997)
   PUBMED   9271215
REFERENCE   9  (bases 1 to 1242)
  AUTHORS   Matthijs,G., Schollen,E., Pirard,M., Budarf,M.L., Van
            Schaftingen,E. and Cassiman,J.J.
  TITLE     PMM (PMM1), the human homologue of SEC53 or yeast
            phosphomannomutase, is localized on chromosome 22q13
  JOURNAL   Genomics 40 (1), 41-47 (1997)
   PUBMED   9070917
REFERENCE   10 (bases 1 to 1242)
  AUTHORS   Wada,Y. and Sakamoto,M.
  TITLE     Isolation of the human phosphomannomutase gene (PMM1) and
            assignment to chromosome 22q13
  JOURNAL   Genomics 39 (3), 416-417 (1997)
   PUBMED   9119384
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC016818.1 and BC010855.2.
            
            On Nov 23, 2018 this sequence version replaced NM_002676.2.
            
            Summary: Phosphomannomutase catalyzes the conversion between
            D-mannose 6-phosphate and D-mannose 1-phosphate which is a
            substrate for GDP-mannose synthesis. GDP-mannose is used for
            synthesis of dolichol-phosphate-mannose, which is essential for
            N-linked glycosylation and thus the secretion of several
            glycoproteins as well as for the synthesis of
            glycosyl-phosphatidyl-inositol (GPI) anchored proteins. [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 :: SRR5189652.38470.1,
                                           SRR5189667.210396.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216259.8/ ENSP00000216259.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-20                BC016818.1         32-51
            21-1242             BC010855.2         1-1222
FEATURES             Location/Qualifiers
     source          1..1242
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     gene            1..1242
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /note="phosphomannomutase 1"
                     /db_xref="GeneID:5372"
                     /db_xref="HGNC:HGNC:9114"
                     /db_xref="MIM:601786"
     exon            1..122
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /inference="alignment:Splign:2.1.0"
     CDS             36..824
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /EC_number="5.4.2.8"
                     /note="brain glucose-1,6-bisphosphatase"
                     /codon_start=1
                     /product="phosphomannomutase 1"
                     /protein_id="NP_002667.2"
                     /db_xref="CCDS:CCDS14020.1"
                     /db_xref="GeneID:5372"
                     /db_xref="HGNC:HGNC:9114"
                     /db_xref="MIM:601786"
                     /translation="MAVTAQAARRKERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRS
                     RVQIGVVGGSDYCKIAEQLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGE
                     ELLQDLINFCLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKE
                     KIREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQDSFDTIHFFGN
                     ETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFPETAHEA"
     exon            123..240
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /inference="alignment:Splign:2.1.0"
     exon            241..317
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /inference="alignment:Splign:2.1.0"
     exon            318..409
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /inference="alignment:Splign:2.1.0"
     exon            410..509
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /inference="alignment:Splign:2.1.0"
     exon            510..585
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /inference="alignment:Splign:2.1.0"
     exon            586..701
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /inference="alignment:Splign:2.1.0"
     exon            702..1242
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1223..1228
                     /regulatory_class="polyA_signal_sequence"
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /note="hexamer: ATTAAA"
     polyA_site      1242
                     /gene="PMM1"
                     /gene_synonym="PMM 1; PMMH-22; Sec53"
                     /note="major polyA site"
ORIGIN      
        1 cttcgggact ccgccccgcg cgcggacctg cagccatggc agtcaccgcc caggcagccc
       61 gcaggaagga gcgcgtcctc tgcctgtttg acgtggacgg gaccctcacg ccggctcgcc
      121 agaaaattga ccctgaggtg gccgccttcc tgcagaagct acgaagtaga gtgcagatcg
      181 gtgtggtggg cggctctgac tactgtaaga tcgctgagca gctgggtgac ggggatgaag
      241 tcattgagaa gtttgattat gtgtttgccg agaacgggac ggtgcagtat aagcacggac
      301 gactgctctc caagcagacc atccagaacc acctggggga ggagctgctg caggacttga
      361 tcaacttctg cctcagctac atggccctgc tcaggctgcc caagaagcgt ggaaccttca
      421 tcgagttccg gaatggcatg ctgaacatct cgcccatcgg ccggagctgc accctggagg
      481 agaggatcga gttctccgaa ctggacaaga aagagaagat ccgggagaag ttcgtggaag
      541 ccctgaaaac agagtttgct ggcaaagggc tgaggttctc tcgaggaggc atgatcagct
      601 ttgacgtctt ccccgagggc tgggacaagc gctactgcct ggatagcctg gaccaggaca
      661 gcttcgacac catccacttc tttgggaacg agactagccc tggtgggaac gactttgaga
      721 tctttgccga cccccggact gttggccaca gcgtggtgtc tcctcaggac acggtgcagc
      781 gatgccggga gattttcttc ccagagacag ctcatgaggc gtgaccgggg cccacatctg
      841 tgtgtcgtga cttctgaaga gtttggccta ggcctaaaga gaggtcctgg tgttggatag
      901 atgccagggc ccctcctctg gcccaggacg cctgctgcaa gcccacccag atggggccag
      961 agtctgtgtg gacaaccgtc cccagccagt ctgctcctag tggcactggc ttcgtcctcc
     1021 cagggcccag agtgttcccc atgctccacc tggtggccca ggccacagct gctgcttgta
     1081 tttcggtaca gaagaggttt ctttctgcac caggaggagg cgtgctcaag tatcggtacg
     1141 agatctagcc tgccctgcct gcctgccctg ggcgatgagg tacggtgggg aaggtgccta
     1201 ttttagagaa ctttgtcaca gtattaaagt tcccagaaca aa
//
