PLPP_HUMAN - dbPTM
PLPP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLPP_HUMAN
UniProt AC Q96GD0
Protein Name Pyridoxal phosphate phosphatase
Gene Name PDXP
Organism Homo sapiens (Human).
Sequence Length 296
Subcellular Localization Cytoplasm, cytosol . Cytoplasm, cytoskeleton . Cell projection, ruffle membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, lamellipodium membrane
Peripheral membrane protein
Cytoplasmic side . Cell membrane
Peripheral membra
Protein Description Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. PNP > PMP' target='_blank'> [PubMed: 15580268 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]
Protein Sequence MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGLED
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
52UbiquitinationERLARAGKAALFVSN
HHHHHCCCCEEEEEC
29.51-
58PhosphorylationGKAALFVSNNSRRAR
CCCEEEEECCCCCCC
23.9829083192
61PhosphorylationALFVSNNSRRARPEL
EEEEECCCCCCCHHH
27.6529083192
128MethylationELRAAGLRLAGDPSA
HHHHHCCCCCCCCCC
22.90115486971
158AcetylationDEHFSFAKLREACAH
HHCCCHHHHHHHHHH
46.1725953088
176PhosphorylationPECLLVATDRDPWHP
CCCEEEEECCCCCCC
24.8820068231
190PhosphorylationPLSDGSRTPGTGSLA
CCCCCCCCCCCCCHH
27.9721406692
193PhosphorylationDGSRTPGTGSLAAAV
CCCCCCCCCCHHHHE
25.4621406692
195PhosphorylationSRTPGTGSLAAAVET
CCCCCCCCHHHHEEE
18.0521406692
202PhosphorylationSLAAAVETASGRQAL
CHHHHEEECCCCEEE
21.3721406692
204PhosphorylationAAAVETASGRQALVV
HHHEEECCCCEEEEE
41.7621406692
254PhosphorylationGHRCGMTTVLTLTGV
CCCCCCEEEEHHHCC
12.4822210691
257PhosphorylationCGMTTVLTLTGVSRL
CCCEEEEHHHCCCHH
20.2422210691

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PLPP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLPP_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PLPP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARRB1_HUMANARRB1physical
17500066

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLPP_HUMAN

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Related Literatures of Post-Translational Modification

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