Search Results
Overview
| Uniprot ID | A0A024R1I3 |
|---|---|
| Protein Name | Chronophin |
| Gene Name | PDXP |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 213 | RQALVVGKPSPYMFE |
Function
Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism. Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine
Protein Sequence
10
MARCERLRGA
20
ALRDVLGRAQ
30
GVLFDCDGVL
40
WNGERAVPGA
50
PELLERLARA
60
GKAALFVSNN
70
SRRARPELAL
80
RFARLGFGGL
90
RAEQLFSSAL
100
CAARLLRQRL
110
PGPPDAPGAV
120
FVLGGEGLRA
130
ELRAAGLRLA
140
GDPSAGDGAA
150
PRVRAVLVGY
160
DEHFSFAKLR
170
EACAHLRDPE
180
CLLVATDRDP
190
WHPLSDGSRT
200
PGTGSLAAAV
210
ETASGRQALV
220
VGKPSPYMFE
230
CITENFSIDP
240
ARTLMVGDRL
250
ETDILFGHRC
260
GMTTVLTLTG
270
VSRLEEAQAY
280
LAAGQHDLVP
290
HYYVESIADL
TEGLED
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005911 | cell-cell junction |
| Cellular Component | GO:0005856 | cytoskeleton |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0031258 | lamellipodium membrane |
| Cellular Component | GO:0098794 | postsynapse |
| Cellular Component | GO:0032587 | ruffle membrane |
| Molecular Function | GO:0000287 | magnesium ion binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0004722 | protein serine/threonine phosphatase activity |
| Molecular Function | GO:0033883 | pyridoxal phosphatase activity |
| Biological Process | GO:0032361 | pyridoxal phosphate catabolic process |
| Biological Process | GO:0099159 | regulation of modification of postsynaptic structure |
Reference
PMID: N/A