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Protein

Phosphomannomutase 1

Gene

PMM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.1 Publication

Catalytic activityi

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

Cofactori

Mg2+1 Publication

Enzyme regulationi

IMP, a metabolite whose concentration is elevated in anoxia, inhibits phosphomannomutase and phosphoglucomutase activities and strongly enhances glucose-1,6-bisphosphatase activity.By similarity

Kineticsi

  1. KM=54 µM for alpha-D-mannose 1-phosphate1 Publication
  2. KM=7.5 µM for alpha-D-glucose 1-phosphate1 Publication

    Pathwayi: GDP-alpha-D-mannose biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Mannose-6-phosphate isomerase (MPI), Mannose-6-phosphate isomerase (MPI), Mannose-6-phosphate isomerase (MPI), Mannose-6-phosphate isomerase (MPI), Mannose-6-phosphate isomerase
    2. Phosphomannomutase, Phosphomannomutase, Phosphomannomutase (PMM2), Phosphomannomutase, Phosphomannomutase, Phosphomannomutase (PMM2), Phosphomannomutase (PMM2), Phosphomannomutase (PMM2), Phosphomannomutase, Phosphomannomutase (PMM2), Phosphomannomutase, Phosphomannomutase (PMM2), Phosphomannomutase (PMM2), Phosphomannomutase (PMM1), Phosphomannomutase 1 (PMM1), Phosphomannomutase (PMM2), Phosphomannomutase (PMM2), Phosphomannomutase 2 (PMM2)
    This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate, the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei19Nucleophile1 Publication1
    Metal bindingi19Magnesium1
    Active sitei21Proton donor/acceptorSequence analysis1
    Metal bindingi21Magnesium; via carbonyl oxygen1
    Binding sitei28Substrate1
    Binding sitei132Substrate1
    Binding sitei143Substrate1
    Binding sitei150Substrate1
    Binding sitei186Substrate; via amide nitrogen1
    Binding sitei188Substrate1
    Binding sitei190Substrate1
    Metal bindingi218Magnesium1

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • phosphomannomutase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciZFISH:HS02079-MONOMER.
    BRENDAi5.4.2.8. 2681.
    ReactomeiR-HSA-446205. Synthesis of GDP-mannose.
    UniPathwayiUPA00126; UER00424.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphomannomutase 1 (EC:5.4.2.8)
    Short name:
    PMM 1
    Alternative name(s):
    PMMH-22
    Gene namesi
    Name:PMM1
    Synonyms:PMMH22
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:9114. PMM1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    DisGeNETi5372.
    OpenTargetsiENSG00000100417.
    PharmGKBiPA33440.

    Polymorphism and mutation databases

    BioMutaiPMM1.
    DMDMi2499519.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00001996922 – 262Phosphomannomutase 1Add BLAST261

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1
    Modified residuei242PhosphoserineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ92871.
    MaxQBiQ92871.
    PaxDbiQ92871.
    PeptideAtlasiQ92871.
    PRIDEiQ92871.

    PTM databases

    DEPODiQ92871.
    iPTMnetiQ92871.
    PhosphoSitePlusiQ92871.

    Expressioni

    Tissue specificityi

    Strong expression in liver, heart, brain, and pancreas; lower expression in skeletal muscle.

    Gene expression databases

    BgeeiENSG00000100417.
    CleanExiHS_PMM1.
    ExpressionAtlasiQ92871. baseline and differential.
    GenevisibleiQ92871. HS.

    Organism-specific databases

    HPAiHPA030712.
    HPA056509.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAB6AP203404EBI-746784,EBI-1052826

    Protein-protein interaction databases

    BioGridi111385. 13 interactors.
    IntActiQ92871. 6 interactors.
    MINTiMINT-1482037.
    STRINGi9606.ENSP00000216259.

    Structurei

    Secondary structure

    1262
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi14 – 21Combined sources8
    Turni22 – 24Combined sources3
    Helixi33 – 42Combined sources10
    Turni43 – 45Combined sources3
    Beta strandi46 – 51Combined sources6
    Helixi56 – 63Combined sources8
    Turni66 – 68Combined sources3
    Helixi69 – 72Combined sources4
    Beta strandi74 – 78Combined sources5
    Helixi79 – 81Combined sources3
    Beta strandi83 – 86Combined sources4
    Beta strandi89 – 91Combined sources3
    Helixi96 – 100Combined sources5
    Helixi102 – 117Combined sources16
    Beta strandi128 – 131Combined sources4
    Beta strandi136 – 138Combined sources3
    Helixi147 – 160Combined sources14
    Helixi162 – 173Combined sources12
    Turni174 – 176Combined sources3
    Beta strandi179 – 182Combined sources4
    Beta strandi185 – 187Combined sources3
    Beta strandi189 – 193Combined sources5
    Helixi198 – 201Combined sources4
    Helixi202 – 205Combined sources4
    Turni206 – 209Combined sources4
    Beta strandi211 – 218Combined sources8
    Helixi227 – 231Combined sources5
    Beta strandi235 – 239Combined sources5
    Helixi243 – 254Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2FUCX-ray2.10A1-262[»]
    2FUEX-ray1.75A1-262[»]
    ProteinModelPortaliQ92871.
    SMRiQ92871.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92871.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic PMM family.Curated

    Phylogenomic databases

    eggNOGiKOG3189. Eukaryota.
    COG0561. LUCA.
    GeneTreeiENSGT00390000002918.
    HOGENOMiHOG000181843.
    HOVERGENiHBG009971.
    InParanoidiQ92871.
    KOiK17497.
    OMAiNDYEIYD.
    OrthoDBiEOG091G0J2S.
    PhylomeDBiQ92871.
    TreeFamiTF300874.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR005002. PMM.
    [Graphical view]
    PANTHERiPTHR10466. PTHR10466. 1 hit.
    PfamiPF03332. PMM. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q92871-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV
    60 70 80 90 100
    VGGSDYCKIA EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL
    110 120 130 140 150
    GEELLQDLIN FCLSYMALLR LPKKRGTFIE FRNGMLNISP IGRSCTLEER
    160 170 180 190 200
    IEFSELDKKE KIREKFVEAL KTEFAGKGLR FSRGGMISFD VFPEGWDKRY
    210 220 230 240 250
    CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV VSPQDTVQRC
    260
    REIFFPETAH EA
    Length:262
    Mass (Da):29,747
    Last modified:November 1, 1997 - v2
    Checksum:i1FBA7BFC9C3BB0BB
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti11K → R in AAC51117 (PubMed:9070917).Curated1
    Sequence conflicti169A → D in AAC51117 (PubMed:9070917).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U62526 mRNA. Translation: AAC51117.1.
    D87810 mRNA. Translation: BAA13460.1.
    U86070 mRNA. Translation: AAC00023.1.
    CR456544 mRNA. Translation: CAG30430.1.
    AK289368 mRNA. Translation: BAF82057.1.
    AK316580 mRNA. Translation: BAG38168.1.
    AL023553 Genomic DNA. Translation: CAB46025.1.
    CH471095 Genomic DNA. Translation: EAW60443.1.
    BC010855 mRNA. Translation: AAH10855.1.
    BC016818 mRNA. Translation: AAH16818.1.
    CCDSiCCDS14020.1.
    RefSeqiNP_002667.2. NM_002676.2.
    UniGeneiHs.75835.

    Genome annotation databases

    EnsembliENST00000216259; ENSP00000216259; ENSG00000100417.
    GeneIDi5372.
    KEGGihsa:5372.
    UCSCiuc003bal.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U62526 mRNA. Translation: AAC51117.1.
    D87810 mRNA. Translation: BAA13460.1.
    U86070 mRNA. Translation: AAC00023.1.
    CR456544 mRNA. Translation: CAG30430.1.
    AK289368 mRNA. Translation: BAF82057.1.
    AK316580 mRNA. Translation: BAG38168.1.
    AL023553 Genomic DNA. Translation: CAB46025.1.
    CH471095 Genomic DNA. Translation: EAW60443.1.
    BC010855 mRNA. Translation: AAH10855.1.
    BC016818 mRNA. Translation: AAH16818.1.
    CCDSiCCDS14020.1.
    RefSeqiNP_002667.2. NM_002676.2.
    UniGeneiHs.75835.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2FUCX-ray2.10A1-262[»]
    2FUEX-ray1.75A1-262[»]
    ProteinModelPortaliQ92871.
    SMRiQ92871.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111385. 13 interactors.
    IntActiQ92871. 6 interactors.
    MINTiMINT-1482037.
    STRINGi9606.ENSP00000216259.

    PTM databases

    DEPODiQ92871.
    iPTMnetiQ92871.
    PhosphoSitePlusiQ92871.

    Polymorphism and mutation databases

    BioMutaiPMM1.
    DMDMi2499519.

    Proteomic databases

    EPDiQ92871.
    MaxQBiQ92871.
    PaxDbiQ92871.
    PeptideAtlasiQ92871.
    PRIDEiQ92871.

    Protocols and materials databases

    DNASUi5372.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000216259; ENSP00000216259; ENSG00000100417.
    GeneIDi5372.
    KEGGihsa:5372.
    UCSCiuc003bal.3. human.

    Organism-specific databases

    CTDi5372.
    DisGeNETi5372.
    GeneCardsiPMM1.
    HGNCiHGNC:9114. PMM1.
    HPAiHPA030712.
    HPA056509.
    MIMi601786. gene.
    neXtProtiNX_Q92871.
    OpenTargetsiENSG00000100417.
    PharmGKBiPA33440.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3189. Eukaryota.
    COG0561. LUCA.
    GeneTreeiENSGT00390000002918.
    HOGENOMiHOG000181843.
    HOVERGENiHBG009971.
    InParanoidiQ92871.
    KOiK17497.
    OMAiNDYEIYD.
    OrthoDBiEOG091G0J2S.
    PhylomeDBiQ92871.
    TreeFamiTF300874.

    Enzyme and pathway databases

    UniPathwayiUPA00126; UER00424.
    BioCyciZFISH:HS02079-MONOMER.
    BRENDAi5.4.2.8. 2681.
    ReactomeiR-HSA-446205. Synthesis of GDP-mannose.

    Miscellaneous databases

    EvolutionaryTraceiQ92871.
    GeneWikiiPMM1.
    GenomeRNAii5372.
    PROiQ92871.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000100417.
    CleanExiHS_PMM1.
    ExpressionAtlasiQ92871. baseline and differential.
    GenevisibleiQ92871. HS.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR005002. PMM.
    [Graphical view]
    PANTHERiPTHR10466. PTHR10466. 1 hit.
    PfamiPF03332. PMM. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPMM1_HUMAN
    AccessioniPrimary (citable) accession number: Q92871
    Secondary accession number(s): A8K003, Q92586
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: November 30, 2016
    This is version 157 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.