TREA_SCHPO - dbPTM
TREA_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TREA_SCHPO
UniProt AC O42893
Protein Name Neutral trehalase
Gene Name ntp1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 735
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MPSKFSSKYVDTEAISNDDDNPFATAKSYYSKDTDLSTRVSAGRPRTLSTSMEASAAPTIPELKNLRRRGSLDEHKQPRKFLVDVDKTLNALLESEDTDRNMQITIEDTGPKVVSLGSASSGGYRLYELRGTYQLSNLLQELTLAKDYGRRYILLDERRLNENPVNRLSRLIKGTFWDALTRRIDASVLDVICRDTKDRSGSHVNRIYVPKAEQEMYEYYVRAAKERPYLNLQVEYLPEEITPEWVRDVNDKPGLLALAMEKYQDDEGNTHLRGVPFVVPGGRFNELYGWDSYFESLGLLVDDRVDLAKGMVENFIFEITYYGKILNANRTYYLLRSQPPFLTDMALRVYERIKNEEGSLDFLHRAFSATIKEYHTVWTATPRLDPKTGLSRYRPGGLGIPPETEASHFEHLLRPYMEKYHMTLEEFTHAYNYQQIHEPALDEYFVHDRAVRESGHDTTYRLEKVCADLATVDLNSLLYKYETDISHVILEYFDDKFVLPNGTIETSAIWDRRARARRAAMEKYLWSEADSMWYDYNTKLETKSTYESATAFWALWAGVATPRQAAKFVDVSLPKFEVAGGIVAGTKRSLGKVGLDNPSRQWDYPNGWSPQQILAWYGLIRYGYEEETRRLVYRWLYTITKSFVDFNGIVVEKYDLTRPVDPHRVEAEYGNQGVNIKGVAREGFGWVNASYEVGLTFCNSHMRRALGACTTPDVFFAGIKEESLPAFENLSIHKN
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
16PhosphorylationYVDTEAISNDDDNPF
CCCHHHCCCCCCCCC
41.0524763107
25PhosphorylationDDDNPFATAKSYYSK
CCCCCCHHCHHHCCC
34.6924763107
47PhosphorylationVSAGRPRTLSTSMEA
CCCCCCCCCCCCCCH
27.9528889911
49PhosphorylationAGRPRTLSTSMEASA
CCCCCCCCCCCCHHC
20.1628889911
50PhosphorylationGRPRTLSTSMEASAA
CCCCCCCCCCCHHCC
34.8928889911
51PhosphorylationRPRTLSTSMEASAAP
CCCCCCCCCCHHCCC
15.9628889911
55PhosphorylationLSTSMEASAAPTIPE
CCCCCCHHCCCCCHH
16.2025720772
59PhosphorylationMEASAAPTIPELKNL
CCHHCCCCCHHHHHH
44.4229996109
71PhosphorylationKNLRRRGSLDEHKQP
HHHHHCCCCCCCCCC
30.7329996109
120PhosphorylationVVSLGSASSGGYRLY
EEEECCCCCCCEEEE
31.0828889911
723PhosphorylationFAGIKEESLPAFENL
EECCCHHHCCHHHCC
40.5221712547
731PhosphorylationLPAFENLSIHKN---
CCHHHCCCCCCC---
33.9424763107

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 TREA_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TREA_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 TREA_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TREA_SCHPOntp1physical
12153582
TPP1_SCHPOtpp1physical
12153582
TPS1_SCHPOtps1physical
12153582
YE7A_SCHPOSPAC4A8.10genetic
22681890
CSN7_SCHPOcsn71genetic
22681890
ALP16_SCHPOalp16genetic
22681890
PFD5_SCHPObob1genetic
22681890
YM02_SCHPOSPAC212.02genetic
22681890
YJ03_SCHPOrhn1genetic
22681890
UAF30_SCHPOspp27genetic
22681890
POP2_SCHPOpop2genetic
22681890
ATF21_SCHPOatf21genetic
22681890
YGB8_SCHPOSPBC25B2.08genetic
22681890
YHEH_SCHPOSPBPB2B2.17cgenetic
22681890
HUS1_SCHPOhus1genetic
22681890
YD22_SCHPOSPAC56F8.02genetic
22681890
DAD2_SCHPOdad2genetic
22681890
PRS10_SCHPOrpt4genetic
22681890
PRZ1_SCHPOprz1genetic
22681890
SEC74_SCHPOsec74genetic
22681890
SGF29_SCHPOsgf29genetic
22681890

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-49; THR-50 ANDSER-51, AND MASS SPECTROMETRY.

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