IPT1_YEAST - dbPTM
IPT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPT1_YEAST
UniProt AC P38954
Protein Name Inositolphosphotransferase 1
Gene Name IPT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 527
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Catalyzes the addition of a phosphorylinositol group onto mannosyl phosphorylinositol ceramide to form mannosyl diphosphorylinositol ceramide..
Protein Sequence MNVIFSLASFVKNMYNASLNQRNLISLPFNFMLNFAPVFIWLSIFKRAGLIPIRLRPDIHSKFAFFADQFLFGDYWHELTVQLPDNTSKLFFWSFISSSAFLLVFLICIPFAIWYYIYYIKHVNYNLLEWFANIFHYPCKRKQRPIQKRFRTIFIPFALPLFTFVILNIDHFFAYQSDANFTKTKDLLAWFSYVILHLTAPILTAVYLYVFQPPGTLKCFSFALGLQNIAGVLTHLLVPMASPWFTHLYGIDDTEHVNYTQEGFAAGLIRVDSHLGTHLNTKGFHMSPIVFGAVPSLHSAIAFQCFLFLVSRSTSLKHRFSNAGGFTMHNNDSSTFKLSEEDSEDEGDNSIPPTIGPNDLEMEPLGTVEPVDISNERSSSPSSSFTVSSNERSTGGGDGSIINSNGNKKPLQFVHLYDEDTNFTNKWIFKIVNDGFIPKFWAILYIILQWWATMYLDHHYRFDLFVGVLYAMTSFIIINWFVLQPKVLKKWIHIRLGDKVDTRNEARTFGMRVFCGTKMEWFFDPLA
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
15PhosphorylationASFVKNMYNASLNQR
HHHHHHHHHCCCCCC		19.5728132839
192PhosphorylationKDLLAWFSYVILHLT
HHHHHHHHHHHHHHH		14.0528889911
193PhosphorylationDLLAWFSYVILHLTA
HHHHHHHHHHHHHHH		5.0928889911
199PhosphorylationSYVILHLTAPILTAV
HHHHHHHHHHHHHHH		21.4628889911
204PhosphorylationHLTAPILTAVYLYVF
HHHHHHHHHHHHHHC		18.1328889911
207PhosphorylationAPILTAVYLYVFQPP
HHHHHHHHHHHCCCC		7.0028889911
209PhosphorylationILTAVYLYVFQPPGT
HHHHHHHHHCCCCCC		4.9828889911
333PhosphorylationFTMHNNDSSTFKLSE
EEEECCCCCCEECCC		33.1419779198
334PhosphorylationTMHNNDSSTFKLSEE
EEECCCCCCEECCCC		40.5019779198
335PhosphorylationMHNNDSSTFKLSEED
EECCCCCCEECCCCC		28.8328889911
378PhosphorylationVDISNERSSSPSSSF
EECCCCCCCCCCCCE		29.0522369663
379PhosphorylationDISNERSSSPSSSFT
ECCCCCCCCCCCCEE		53.1122369663
380PhosphorylationISNERSSSPSSSFTV
CCCCCCCCCCCCEEE		30.0122369663
382PhosphorylationNERSSSPSSSFTVSS
CCCCCCCCCCEEEEC		40.3322369663
383PhosphorylationERSSSPSSSFTVSSN
CCCCCCCCCEEEECC		32.6222369663
384PhosphorylationRSSSPSSSFTVSSNE
CCCCCCCCEEEECCC		29.3122369663
386PhosphorylationSSPSSSFTVSSNERS
CCCCCCEEEECCCCC		22.7922369663
388PhosphorylationPSSSFTVSSNERSTG
CCCCEEEECCCCCCC		25.1222369663
389PhosphorylationSSSFTVSSNERSTGG
CCCEEEECCCCCCCC		38.0722369663
393PhosphorylationTVSSNERSTGGGDGS
EEECCCCCCCCCCCC		25.8117563356
394PhosphorylationVSSNERSTGGGDGSI
EECCCCCCCCCCCCE		46.1717563356
400PhosphorylationSTGGGDGSIINSNGN
CCCCCCCCEECCCCC		25.6529136822
404PhosphorylationGDGSIINSNGNKKPL
CCCCEECCCCCCCCE		35.3917563356
409UbiquitinationINSNGNKKPLQFVHL
ECCCCCCCCEEEEEE		55.7623749301
499UbiquitinationIHIRLGDKVDTRNEA
HHEECCCCCCCHHHH		39.9623749301
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 IPT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPT1_YEAST !!
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 IPT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPS1_YEASTTPS1genetic
19269370
BEM1_YEASTBEM1genetic
19269370
BMH2_YEASTBMH2genetic
19269370
ISC1_YEASTISC1genetic
19269370
GET1_YEASTGET1genetic
19269370
RPA34_YEASTRPA34genetic
19269370
MNN11_YEASTMNN11genetic
19269370
CANB_YEASTCNB1genetic
19269370
SAC1_YEASTSAC1genetic
19269370
SKN1_YEASTSKN1genetic
20030721
TPS1_YEASTTPS1genetic
20093466
SGF29_YEASTSGF29genetic
20093466
RNH2B_YEASTRNH202genetic
20093466
VPS74_YEASTVPS74genetic
20093466
YOR1_YEASTYOR1genetic
20093466
NEM1_YEASTNEM1genetic
20093466
GPI7_YEASTLAS21genetic
20093466
PEP8_YEASTPEP8genetic
20093466
GEF1_YEASTGEF1genetic
20093466
SAC1_YEASTSAC1genetic
20093466
RSSA2_YEASTRPS0Bgenetic
20093466
NKP2_YEASTNKP2genetic
20093466
VRP1_YEASTVRP1genetic
20093466
SCS7_YEASTSCS7genetic
20093466
APP1_YEASTAPP1genetic
20093466
ZRG17_YEASTZRG17genetic
20093466
VAM10_YEASTVAM10genetic
20093466
NEW1_YEASTNEW1genetic
20093466
NACB1_YEASTEGD1genetic
20093466
AGE1_YEASTAGE1genetic
20979339
RV161_YEASTRVS161genetic
20526336
RV167_YEASTRVS167genetic
20526336
ISC1_YEASTISC1genetic
20526336
SAC1_YEASTSAC1genetic
20526336
MON2_YEASTMON2genetic
20526336
TOR2_YEASTTOR2genetic
20526336
CSG2_YEASTCSG2genetic
21623372
LCB5_YEASTLCB5genetic
21623372
COX7_YEASTCOX7genetic
21623372
ATPO_YEASTATP5genetic
21623372
PABC_YEASTABZ2genetic
21623372
ERG2_YEASTERG2genetic
21623372
6PGD1_YEASTGND1genetic
21623372
ELO3_YEASTELO3genetic
23891562
SUR1_YEASTSUR1genetic
23891562
ERG7_YEASTERG7genetic
23891562
LCB1_YEASTLCB1genetic
25040056
VRP1_YEASTVRP1genetic
27708008
ATC3_YEASTDRS2genetic
27708008
TPS1_YEASTTPS1genetic
27708008
SGF29_YEASTSGF29genetic
27708008
VPS74_YEASTVPS74genetic
27708008
SHE9_YEASTSHE9genetic
27708008
YOR1_YEASTYOR1genetic
27708008
NEM1_YEASTNEM1genetic
27708008
GEF1_YEASTGEF1genetic
27708008
IXR1_YEASTIXR1genetic
27708008
SAC1_YEASTSAC1genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IPT1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; THR-394 ANDSER-404, AND MASS SPECTROMETRY.

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