PIK1_SCHPO - dbPTM
PIK1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIK1_SCHPO
UniProt AC Q10366
Protein Name Phosphatidylinositol 4-kinase pik1
Gene Name pik1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 851
Subcellular Localization Golgi apparatus . Nucleus.
Protein Description Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate. PIK1 is part of a nuclear phosphoinositide cycle and could control cytokinesis through the actin cytoskeleton (By similarity)..
Protein Sequence MPSSNSGNELLLRFFESAHFTSQLCVAYLSRYPNNIGIHHFLCEKLATFPYEEIEFFIPQLIHLVLNKDSESVALEEFIISQCEQNTQCALITFWYLQAHMVDLGLQPHSSCFKICKRLYNRIQILVFMSSSSLIQSQQKISENVTPALILSGIMLGGVCVPELLKKAGPIAIAQGRKAPRQDPDESDVDVLRRLSTEPRYSLDVLRSSLNNSIVEQHSEVSLRLKAPELTRTHSYQSSATLSIDEQRRVLRSNYFQQEIQFLFALQDISIRLIIVPRQARLSSLRAELALLNNNLPADVNIPLLRSYHKEVSHKIVRIDPKEATILNSAERVPYLIMVEVLSGELSFEPQSKKNKAKVQKIVSHKNQRKRWFDLTDVDPYTNLQDSTDNDISESESEGGDLSMSPLIKGLVPDTLSLSKSFSSFGNVSLQVPSSHRDTDVVLLSGRHSDSDGNGALKRSKIYASEITARMRAAATMLSQLDAEGSRRPKAETERIKNSIILDMQRLEEERLNEPSIYPVSVDISCAEDLRFGKETQKAERKGDRDDPSAATFQEDWYAKKERIRKSSPYGHYPNWDLVSVIVKTGADLRQETFACQLIYAFQRVWLECKEKVWVRRMKILVTGDNSGLIETITNAISVHSIKKNLTKQLREAELAQGKIAGKNVVTLKDYFIKQFGDPNSSRYRQAQTNFLQSLVAYSIISYLLQLKDRHNGNVLIDSEGHIIHIDFGFLLTNTPGNVGFESAPFKLTADYLEILDDRFDEYRSLMKAAFKSVRKNADQIILLVEVMQNNSTMPCFRAGENTSAQLLQRFQLQLGDKECDDFVDLLIQKANCSVWTRLYDLFQNITNGIY
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
187PhosphorylationPRQDPDESDVDVLRR
CCCCCCCCHHHHHHH
25720772
196PhosphorylationVDVLRRLSTEPRYSL
HHHHHHHCCCCCHHH
25720772
197PhosphorylationDVLRRLSTEPRYSLD
HHHHHHCCCCCHHHH
29996109
201PhosphorylationRLSTEPRYSLDVLRS
HHCCCCCHHHHHHHH
29996109
202PhosphorylationLSTEPRYSLDVLRSS
HCCCCCHHHHHHHHH
28889911
219PhosphorylationNSIVEQHSEVSLRLK
CHHHHHCCCEEEEEC
28889911
222PhosphorylationVEQHSEVSLRLKAPE
HHHCCCEEEEECCCC
28889911
235PhosphorylationPELTRTHSYQSSATL
CCCCCCEEECCCCEE
28889911
236PhosphorylationELTRTHSYQSSATLS
CCCCCEEECCCCEEE
28889911
241PhosphorylationHSYQSSATLSIDEQR
EEECCCCEEEHHHHH
25720772
415PhosphorylationIKGLVPDTLSLSKSF
HCCCCCCCEECCCCC
25720772
421PhosphorylationDTLSLSKSFSSFGNV
CCEECCCCCCCCCCE
29996109
423PhosphorylationLSLSKSFSSFGNVSL
EECCCCCCCCCCEEE
29996109
424PhosphorylationSLSKSFSSFGNVSLQ
ECCCCCCCCCCEEEE
29996109
429PhosphorylationFSSFGNVSLQVPSSH
CCCCCCEEEECCCCC
25720772
445PhosphorylationDTDVVLLSGRHSDSD
CCCEEEEECCCCCCC
29996109
449PhosphorylationVLLSGRHSDSDGNGA
EEEECCCCCCCCCCC
29996109
451PhosphorylationLSGRHSDSDGNGALK
EECCCCCCCCCCCCC
25720772

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 PIK1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIK1_SCHPO !!

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 PIK1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MLR4_SCHPOcdc4physical
11087749
POT1_SCHPOpot1genetic
29410177

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIK1_SCHPO

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Related Literatures of Post-Translational Modification

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