Q8TCT1 (PHOP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 67.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Phosphoethanolamine/phosphocholine phosphatase EC=3.1.3.75 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 267 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). Involved in the generation of inorganic phosphate for bone mineralization. |
| Catalytic activity | O-phosphoethanolamine + H2O = ethanolamine + phosphate. Ref.4 Phosphocholine + H2O = choline + phosphate. Ref.4 |
| Cofactor | Magnesium. Ref.4 |
| Tissue specificity | Expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix, but not in MG-63 cell line, which do not mineralize. Ref.5 |
| Sequence similarities | Belongs to the HAD-like hydrolase superfamily. PHOSPHO family. |
| Biophysicochemical properties | Kinetic parameters: KM=3 µM for PEA Ref.4 KM=11.4 µM for PCho pH dependence: Optimum pH is 6.7. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Mineral balance |
| Coding sequence diversity | Alternative splicing |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | regulation of bone mineralization Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphocholine phosphatase activityInferred from electronic annotation. Source: EC phosphoethanolamine phosphatase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q8TCT1-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q8TCT1-2) Also known as: PHOSPHO1-3a; The sequence of this isoform differs from the canonical sequence as follows: 1-15: MSGCFPVSGLRCLSR → MCQRLWPANQPLPGGLLPRPLSLAPSSSSSCCSPPCSQ |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 267 | 267 | Phosphoethanolamine/phosphocholine phosphatase | PRO_0000068829 | |||||
Sites | |||||||||
| Active site | 32 | 1 | Nucleophile Probable | ||||||
| Active site | 34 | 1 | Proton donor By similarity | ||||||
| Metal binding | 32 | 1 | Magnesium Probable | ||||||
| Metal binding | 34 | 1 | Magnesium By similarity | ||||||
| Metal binding | 203 | 1 | Magnesium Probable | ||||||
| Binding site | 43 | 1 | Substrate Probable | ||||||
| Binding site | 123 | 1 | Substrate Probable | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 15 | 15 | MSGCF…RCLSR → MCQRLWPANQPLPGGLLPRP LSLAPSSSSSCCSPPCSQ in isoform 2. | VSP_040624 | |||||
Experimental info | |||||||||
| Mutagenesis | 32 | 1 | D → N: Abolishes phosphatase activity. Ref.7 | ||||||
| Mutagenesis | 43 | 1 | D → N: Strongly reduces reactivity toward PEA and PCho substrates. Abolishes phosphatase activity; when associated with N-123. Ref.7 | ||||||
| Mutagenesis | 123 | 1 | D → N: Strongly reduces reactivity toward PEA and PCho substrates. Abolishes phosphatase activity; when associated with N-43. Ref.7 | ||||||
| Mutagenesis | 203 | 1 | D → S: Abolishes phosphatase activity. Ref.7 | ||||||
Sequences
| ||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Chromosomal localization of the chicken and mammalian orthologues of the orphan phosphatase PHOSPHO1 gene." Houston B., Paton I.R., Burt D.W., Farquharson C. Anim. Genet. 33:451-454(2002) [PubMed: 12464021] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [2] | "Identification of a novel splice variant of the haloacid dehalogenase: PHOSPHO1." Roberts S.J., Owen H.C., Farquharson C. Biochem. Biophys. Res. Commun. 371:872-876(2008) [PubMed: 18471996] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon. |
| [4] | "Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities." Roberts S.J., Stewart A.J., Sadler P.J., Farquharson C. Biochem. J. 382:59-65(2004) [PubMed: 15175005] [Abstract] Cited for: ENZYME ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. |
| [5] | "PHOSPHO1 -- a novel phosphatase specifically expressed at sites of mineralisation in bone and cartilage." Houston B., Stewart A.J., Farquharson C. Bone 34:629-637(2004) [PubMed: 15050893] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [6] | "Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily." Stewart A.J., Schmid R., Blindauer C.A., Paisey S.J., Farquharson C. Protein Eng. 16:889-895(2003) [PubMed: 14983068] [Abstract] Cited for: SIMILARITY TO HAD-LIKE HYDROLASE SUPERFAMILY. |
| [7] | "Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2." Roberts S.J., Stewart A.J., Schmid R., Blindauer C.A., Bond S.R., Sadler P.J., Farquharson C. Biochim. Biophys. Acta 1752:73-82(2005) [PubMed: 16054448] [Abstract] Cited for: MUTAGENESIS OF ASP-32; ASP-43; ASP-123 AND ASP-203. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ457189 mRNA. Translation: CAD29803.1. BC117187 mRNA. Translation: AAI17188.1. |
| IPI | IPI00152434. IPI00916923. |
| RefSeq | NP_001137276.1. NM_001143804.1. NP_848595.1. NM_178500.3. |
| UniGene | Hs.405607. |
3D structure databases | |
| ProteinModelPortal | Q8TCT1. |
| SMR | Q8TCT1. Positions 167-267. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8TCT1. |
PTM databases | |
| PhosphoSite | Q8TCT1. |
Polymorphism databases | |
| DMDM | 74715842. |
Proteomic databases | |
| PRIDE | Q8TCT1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000310544; ENSP00000311925; ENSG00000173868. |
| GeneID | 162466. |
| KEGG | hsa:162466. |
| UCSC | uc002ior.1. human. |
Organism-specific databases | |
| CTD | 162466. |
| GeneCards | GC17M047300. |
| H-InvDB | HIX0039112. |
| HGNC | HGNC:16815. PHOSPHO1. |
| neXtProt | NX_Q8TCT1. |
| PharmGKB | PA33276. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG13707. |
| GeneTree | ENSGT00390000007741. |
| HOVERGEN | HBG080058. |
| InParanoid | Q8TCT1. |
| OrthoDB | EOG4S4PH0. |
| PhylomeDB | Q8TCT1. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.75. 2681. |
Gene expression databases | |
| ArrayExpress | Q8TCT1. |
| Bgee | Q8TCT1. |
| CleanEx | HS_PHOSPHO1. |
| Genevestigator | Q8TCT1. |
| GermOnline | ENSG00000173868. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR023214. HAD-like_dom. IPR006383. HAD-SF_hydro_IB_PSP-like. IPR016965. Pase_PHOSPHO-typ. IPR006384. PyrdxlP_Pase-rel. [Graphical view] |
| Gene3D | G3DSA:3.40.50.1000. HAD-like_dom. 2 hits. |
| KO | K06124. |
| Pfam | PF06888. Put_Phosphatase. 1 hit. [Graphical view] |
| PIRSF | PIRSF031051. PyrdxlP_Pase_PHOSPHO2. 1 hit. |
| SUPFAM | SSF56784. HAD-like_dom. 1 hit. |
| TIGRFAMs | TIGR01489. DKMTPPase-SF. 1 hit. TIGR01488. HAD-SF-IB. 1 hit. |
| ProtoNet | Search... |
Other | |
| DrugBank | DB00122. Choline. |
| NextBio | 88177. |
Entry information
| Entry name | PHOP1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8TCT1 Secondary accession number(s): Q17RU6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| SIMILARITY comments Index of protein domains and families |

Clusters with