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O35621

- PMM1_MOUSE

UniProt

O35621 - PMM1_MOUSE

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Protein

Phosphomannomutase 1

Gene

Pmm1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Magnesium.By similarity

Enzyme regulationi

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

Kineticsi

  1. KM=17 µM for glucose-1,6-bisphosphate in the presence of 1 µM IMP1 Publication
  2. KM=40 µM for glucose-1,6-bisphosphate in the presence of 20 µM IMP1 Publication

Vmax=2.1 µmol/min/mg enzyme with glucose-1,6-bisphosphate as substrate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei19 – 191NucleophileBy similarity
Metal bindingi19 – 191MagnesiumBy similarity
Active sitei21 – 211Proton donor/acceptorSequence Analysis
Metal bindingi21 – 211Magnesium; via carbonyl oxygenBy similarity
Binding sitei28 – 281SubstrateBy similarity
Binding sitei132 – 1321SubstrateBy similarity
Binding sitei143 – 1431SubstrateBy similarity
Binding sitei150 – 1501SubstrateBy similarity
Binding sitei186 – 1861Substrate; via amide nitrogenBy similarity
Binding sitei188 – 1881SubstrateBy similarity
Binding sitei190 – 1901SubstrateBy similarity
Metal bindingi218 – 2181MagnesiumBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphomannomutase activity Source: UniProtKB

GO - Biological processi

  1. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  2. mannose biosynthetic process Source: InterPro
  3. mannose metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198715. Synthesis of GDP-mannose.
UniPathwayiUPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase 1 (EC:5.4.2.8)
Short name:
PMM 1
Gene namesi
Name:Pmm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1353418. Pmm1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. neuronal cell body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile and develop normally.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 262261Phosphomannomutase 1PRO_0000199693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO35621.
PaxDbiO35621.
PRIDEiO35621.

PTM databases

PhosphoSiteiO35621.

Expressioni

Tissue specificityi

Present in brain, where it is restricted to neuronal cell bodies. Present at lower levels in pancreas, liver, lung, gonads, uterus, adrenal glands and pituitary (at protein level). Undetectable in intestine.1 Publication

Developmental stagei

Highly expressed at E17 in most organs (at protein level).1 Publication

Gene expression databases

BgeeiO35621.
CleanExiMM_PMM1.
ExpressionAtlasiO35621. baseline and differential.
GenevestigatoriO35621.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO35621.
SMRiO35621. Positions 13-258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic PMM family.Curated

Phylogenomic databases

eggNOGiCOG0561.
HOGENOMiHOG000181843.
HOVERGENiHBG009971.
InParanoidiO35621.
KOiK17497.
OMAiNDYEIYD.
OrthoDBiEOG773XH0.
PhylomeDBiO35621.
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.

O35621 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVAVEGARR KERILCLFDV DGTLTPARQK IDPEVSAFLQ KLRSRVQIGV
60 70 80 90 100
VGGSDYSKIA EQLGEGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL
110 120 130 140 150
GEELLQDLIN FCLSYMALLR LPKKRGTFIE FRNGMLNVSP IGRSCTLEER
160 170 180 190 200
IEFSELDKKE KIREKFVEAL KTEFAGKGLR FSRGGMISFD VFPEGWDKRY
210 220 230 240 250
CLDSLDEDSF DIIHFFGNET SPGGNDFEIY ADPRTVGHSV VSPQDTVQRC
260
RELFFPETAH EA
Length:262
Mass (Da):29,775
Last modified:January 1, 1998 - v1
Checksum:i2967154C0FF292B0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF007267 mRNA. Translation: AAB62943.1.
CCDSiCCDS27678.1.
RefSeqiNP_038900.1. NM_013872.4.
UniGeneiMm.18939.

Genome annotation databases

EnsembliENSMUST00000023112; ENSMUSP00000023112; ENSMUSG00000022474.
GeneIDi29858.
KEGGimmu:29858.
UCSCiuc007wxt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF007267 mRNA. Translation: AAB62943.1 .
CCDSi CCDS27678.1.
RefSeqi NP_038900.1. NM_013872.4.
UniGenei Mm.18939.

3D structure databases

ProteinModelPortali O35621.
SMRi O35621. Positions 13-258.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei O35621.

Proteomic databases

MaxQBi O35621.
PaxDbi O35621.
PRIDEi O35621.

Protocols and materials databases

DNASUi 29858.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023112 ; ENSMUSP00000023112 ; ENSMUSG00000022474 .
GeneIDi 29858.
KEGGi mmu:29858.
UCSCi uc007wxt.2. mouse.

Organism-specific databases

CTDi 5372.
MGIi MGI:1353418. Pmm1.

Phylogenomic databases

eggNOGi COG0561.
HOGENOMi HOG000181843.
HOVERGENi HBG009971.
InParanoidi O35621.
KOi K17497.
OMAi NDYEIYD.
OrthoDBi EOG773XH0.
PhylomeDBi O35621.
TreeFami TF300874.

Enzyme and pathway databases

UniPathwayi UPA00126 ; UER00424 .
Reactomei REACT_198715. Synthesis of GDP-mannose.

Miscellaneous databases

ChiTaRSi PMM1. mouse.
NextBioi 307058.
PROi O35621.
SOURCEi Search...

Gene expression databases

Bgeei O35621.
CleanExi MM_PMM1.
ExpressionAtlasi O35621. baseline and differential.
Genevestigatori O35621.

Family and domain databases

Gene3Di 3.40.50.1000. 2 hits.
InterProi IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view ]
PANTHERi PTHR10466. PTHR10466. 1 hit.
Pfami PF03332. PMM. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01484. HAD-SF-IIB. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Janoueix-Lerosey I., Goud B.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The normal phenotype of Pmm1-deficient mice suggests that Pmm1 is not essential for normal mouse development."
    Cromphout K., Vleugels W., Heykants L., Schollen E., Keldermans L., Sciot R., D'Hooge R., De Deyn P.P., von Figura K., Hartmann D., Korner C., Matthijs G.
    Mol. Cell. Biol. 26:5621-5635(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  3. "Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-bisphosphatase."
    Veiga-da-Cunha M., Vleugels W., Maliekal P., Matthijs G., Van Schaftingen E.
    J. Biol. Chem. 283:33988-33993(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiPMM1_MOUSE
AccessioniPrimary (citable) accession number: O35621
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3