H3BPH4 · H3BPH4_HUMAN
- ProteinPhosphomannomutase
- GenePMM2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids142 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Catalytic activity
- alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
Cofactor
Pathway
Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 3 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 3 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 5 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 5 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 12 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 114 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 125 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 132 | alpha-D-mannose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | metal ion binding | |
Molecular Function | phosphomannomutase activity | |
Biological Process | GDP-mannose biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphomannomutase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionH3BPH4
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
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The viewer provides 205 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusFragment
- Length142
- Mass (Da)16,334
- Last updated2012-04-18 v1
- ChecksumA450D931404CC343
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: X |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC012173 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC022167 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |