SYJ1_SCHPO - dbPTM
SYJ1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYJ1_SCHPO
UniProt AC O43001
Protein Name Inositol-1,4,5-trisphosphate 5-phosphatase 1
Gene Name syj1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1076
Subcellular Localization Cytoplasm . Localizes at the cell tip and the barrier septum.
Protein Description Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Involved in distinct membrane trafficking and signal transduction pathways. Highly active against a range of soluble and lipid inositol phosphates. Active in dephosphorylating the 5-position of Ins(1,4,5)P3 and Ins(1,3,4,5)P4 and to a lesser extent Ins(1,4,5,6)P4. The enzyme is also active against PI(4,5)P2 presented in sonicated vesicles and Triton mixed micelles, and somewhat less active against PI(3,5)P2 in unilamellar vesicles. Activity against PI(3,5)P2 drops sharply when this substrate is presented in mixed micelles. Also hydrolyzes PIP3 to produce PI(3,4)P2..
Protein Sequence MQCLLREKPRSLALVNKDHALMFHSVPQNKNSLSVCVAEFTALSEKPLEGFRKISSHRIYGTLGLIELEGSNFLCVISGASEVARVRDKERVFRIMEVCFYSVNRSNWDHIRQENYSPDIPDGYDTDTQGYDSYKYAAEPFSSLRKLLTNGSFYFSLDFDITTRLQLRTSQTMTEPQYDSMHTQFMWNEFMLRQLIKFRSHLNGDEKSALDGCRFFTCAIRGFASTEQFKLGIQTIRLSLISRLSSLRAGTRFLSRGVDDDGNVANFVETETILDSSKYCVSYCQVRGSIPIFWEQEGVQMFGQKIDITRSLEATRAAFEKHFTSLIEEYGPVHIINLLGTGSGERSLSERLRQHIQLSPEKDLIHLTEFDYHSQIRSFEDANKIRPMIYSDAETFGFYFENNEGQSIVVQDGVFRTNCLDCLDRTNVIQNLVSRVFLEQVMIYTRQNAGYDFWQVHSTIWANNGDALARIYTGTGALKSSFTRKGKLSIAGALNDLSKSVGRMYINNFQDKGRQETIDLLLGRLIDQHPVILYDPIHEYVNHELRKRENEFSEHKNVKIFVASYNLNGCSATTKLENWLFPENTPLADIYVVGFQEIVQLTPQQVISADPAKRREWESCVKRLLNGKCTSGPGYVQLRSGQLVGTALMIFCKESCLPSIKNVEGTVKKTGLGGVSGNKGAVAIRFDYEDTGLCFITSHLAAGYTNYDERDHDYRTIASGLRFRRGRSIFNHDYVVWFGDFNYRISLTYEEVVPCIAQGKLSYLFEYDQLNKQMLTGKVFPFFSELPITFPPTYKFDIGTDIYDTSDKHRVPAWTDRILYRGELVPHSYQSVPLYYSDHRPIYATYEANIVKVDREKKKILFEELYNQRKQEVRDASQTSYTLIDIAGSVAGKPNLIPHLPANGVDKIKQPSSERSKWWFDDGLPAKSIAAPPGPEYRLNPSRPINPFEPTAEPDWISNTKQSFDKKSSLIDSIPALSPAPSSLARSSVSSQRSSTSIIPIKPNKPTKPDHLVAPRVKPLLPPRSGSSSSGVPAPNLTPVNVPPTPPPRKSSASQRSGDLLASSPEESSISWKPLV
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
126PhosphorylationDIPDGYDTDTQGYDS
CCCCCCCCCCCCCCH
32.2527738172
489PhosphorylationFTRKGKLSIAGALND
CCCCCCEEHHHHHHH
17.5524763107
963PhosphorylationWISNTKQSFDKKSSL
HHHCCCCCCCCCCCH
36.6529996109
1045PhosphorylationTPVNVPPTPPPRKSS
CCCCCCCCCCCCCCC
42.2127738172
1051PhosphorylationPTPPPRKSSASQRSG
CCCCCCCCCCCHHCC
32.2024763107
1052PhosphorylationTPPPRKSSASQRSGD
CCCCCCCCCCHHCCC
34.6724763107
1057PhosphorylationKSSASQRSGDLLASS
CCCCCHHCCCCCCCC
29.0829996109
1063PhosphorylationRSGDLLASSPEESSI
HCCCCCCCCCCCCCC
46.5324763107
1064PhosphorylationSGDLLASSPEESSIS
CCCCCCCCCCCCCCC
30.6229996109
1068PhosphorylationLASSPEESSISWKPL
CCCCCCCCCCCCCCC
31.1729996109
1069PhosphorylationASSPEESSISWKPLV
CCCCCCCCCCCCCCC
24.7525720772

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 SYJ1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYJ1_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 SYJ1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PYP1_SCHPOpyp1genetic
18931302
CDS1_SCHPOcds1genetic
18818364
HCS1_SCHPOSPCC737.07cgenetic
18818364
MLH1_SCHPOmlh1genetic
22681890
YG58_SCHPOSPBC56F2.08cgenetic
22681890
HRP3_SCHPOhrp3genetic
22681890
YIQ9_SCHPOSPAC824.09cgenetic
22681890
YK98_SCHPOwhi2genetic
22681890
YI35_SCHPOtoe1genetic
22681890
COQ5_SCHPOcoq5genetic
22681890
CTBL1_SCHPOSPAC1952.06cgenetic
22681890
MGR2_SCHPOmgr2genetic
22681890
YAN8_SCHPOSPAC3H1.08cgenetic
22681890
YMR1_SCHPOymr1genetic
22681890
YE8A_SCHPOSPAC9G1.10cgenetic
22681890
PYRD_SCHPOura3genetic
22681890
YFY7_SCHPOSPAC9.07cgenetic
22681890
TRM6_SCHPOgcd10genetic
22681890
ARV1_SCHPOarv1genetic
22681890
MID1_SCHPOmid1genetic
22681890
DIP1_SCHPOdip1genetic
22681890
DOP1_SCHPOSPAPB21F2.02genetic
22681890
OPA3_SCHPOSPBC1703.11genetic
22681890
MAM3_SCHPOmam3genetic
22681890
YK18_SCHPOSPAPB1A10.08genetic
22681890
LYS12_SCHPOlys12genetic
22681890

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYJ1_SCHPO

loading...

Related Literatures of Post-Translational Modification

TOP