IPI3_YEAST - dbPTM
IPI3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPI3_YEAST
UniProt AC P53877
Protein Name Pre-rRNA-processing protein IPI3
Gene Name IPI3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 555
Subcellular Localization Nucleus .
Protein Description Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA..
Protein Sequence MDEQVIFTTNTSGTIASVHSFEQINLRQCSTQSRNSCVQVGNKYLFIAQAQKALINVYNLSGSFKRESVEQRLPLPEILKCLEVVENDGVQYDRIQGVNHNLPDFNLPYLLLGSTESGKLYIWELNSGILLNVKPMAHYQSITKIKSILNGKYIITSGNDSRVIIWQTVDLVSASNDDPKPLCILHDHTLPVTDFQVSSSQGKFLSCTDTKLFTVSQDATIRCYDLSLIGSKKKQKANENDVSIGKTPVLLATFTTPYSIKSIVLDPADRACYIGTAEGCFSLNLFYKLKGNAIVNLLQSAGVNTVQKGRVFSLVQRNSLTGGENEDLDALYAMGQLVCENVLNSNVSCLEISMDGTLLLIGDTEGKVSIAEIYSKQIIRTIQTLTTSQDSVGEVTNLLTNPYRLERGNLLFEGESKGKQPSNNNGHNFMKIPNLQRVIFDGKNKGHLHDIWYQIGEPEAETDPNLALPLNDFNAYLEQVKTQESIFSHIGKVSSNVKVIDNKIDATSSLDSNAAKDEEITELKTNIEALTHAYKELRDMHEKLYEEHQQMLDKQ
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
65AcetylationYNLSGSFKRESVEQR
HCCCCCCCCCCHHHH		57.8824489116
206PhosphorylationSSQGKFLSCTDTKLF
CCCCCEEEECCCEEE		20.3627017623
247PhosphorylationNDVSIGKTPVLLATF
CCCCCCCCCEEEEEE		17.2622369663
253PhosphorylationKTPVLLATFTTPYSI
CCCEEEEEECCCCCC		22.8322369663
255PhosphorylationPVLLATFTTPYSIKS
CEEEEEECCCCCCEE		23.6222369663
256PhosphorylationVLLATFTTPYSIKSI
EEEEEECCCCCCEEE		18.9522369663
258PhosphorylationLATFTTPYSIKSIVL
EEEECCCCCCEEEEE		22.4222369663
259PhosphorylationATFTTPYSIKSIVLD
EEECCCCCCEEEEEC		25.4122369663
313PhosphorylationVQKGRVFSLVQRNSL
HHCCCEEEEEECCCC		25.4429688323
381PhosphorylationYSKQIIRTIQTLTTS
HHHHHHHHHHHHCCC		13.6630377154
384PhosphorylationQIIRTIQTLTTSQDS
HHHHHHHHHCCCCCC		23.4030377154
386PhosphorylationIRTIQTLTTSQDSVG
HHHHHHHCCCCCCHH		27.9930377154
388PhosphorylationTIQTLTTSQDSVGEV
HHHHHCCCCCCHHHH		27.1028889911
391PhosphorylationTLTTSQDSVGEVTNL
HHCCCCCCHHHHHHH		25.1227017623
492UbiquitinationSIFSHIGKVSSNVKV
HHHHHHCCCCCCEEE		38.0424961812
503AcetylationNVKVIDNKIDATSSL
CEEEECCCCCCCCCC		37.9124489116
509PhosphorylationNKIDATSSLDSNAAK
CCCCCCCCCCCCCCC		31.6621551504
512PhosphorylationDATSSLDSNAAKDEE
CCCCCCCCCCCCHHH		33.3921551504
531PhosphorylationKTNIEALTHAYKELR
HHHHHHHHHHHHHHH		16.1121551504
534PhosphorylationIEALTHAYKELRDMH
HHHHHHHHHHHHHHH		9.4421551504
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 IPI3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPI3_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 IPI3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATG17_YEASTATG17physical
11805837
H4_YEASTHHF1physical
11805837
RIX1_YEASTRIX1physical
12374754
RIX1_YEASTRIX1physical
15260980
SDA1_YEASTSDA1physical
12374754
SDA1_YEASTSDA1physical
15260980
MDN1_YEASTMDN1physical
15260980
NOG1_YEASTNOG1physical
15260980
RIX1_YEASTRIX1physical
16429126
NLE1_YEASTRSA4physical
16429126
ATG17_YEASTATG17physical
11283351
NAB3_YEASTNAB3physical
18467557
ALG5_YEASTALG5physical
18467557
MCM2_YEASTMCM2physical
22421151
ORC1_YEASTORC1physical
22421151
ORC3_YEASTORC3physical
22421151
ORC2_YEASTORC2physical
22421151
CDC6_YEASTCDC6physical
22421151
CDT1_YEASTTAH11physical
22421151
MCM4_YEASTMCM4physical
22421151
NOC3_YEASTNOC3physical
22421151
YAP6_YEASTYAP6physical
22875988
SHE9_YEASTSHE9physical
22875988
TSC11_YEASTTSC11physical
22875988
SP105_YEASTSPC105physical
22875988
ATG1_YEASTATG1physical
22875988
SKN7_YEASTSKN7physical
22875988
RE107_YEASTREC107physical
22875988
LHS1_YEASTLHS1physical
22875988
DID2_YEASTDID2physical
22875988
SNF7_YEASTSNF7physical
22875988
BUL2_YEASTBUL2physical
22875988
NST1_YEASTNST1physical
22875988
CNM67_YEASTCNM67physical
22875988
RLF2_YEASTRLF2physical
22875988
CDC37_YEASTCDC37genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
AXL1_YEASTAXL1genetic
27708008
DPOD_YEASTPOL3genetic
27708008
RRP42_YEASTRRP42genetic
27708008
FAL1_YEASTFAL1genetic
27708008
RRP1_YEASTRRP1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
GPI11_YEASTGPI11genetic
27708008
SDA1_YEASTSDA1genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
GRC3_YEASTGRC3genetic
27708008
NEP1_YEASTEMG1genetic
27708008
NIP7_YEASTNIP7genetic
27708008
TF2B_YEASTSUA7genetic
27708008
RPN7_YEASTRPN7genetic
27708008
ECM8_YEASTECM8genetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
THRC_YEASTTHR4genetic
27708008
VAM6_YEASTVAM6genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
MAF1_YEASTMAF1genetic
27708008
GLU2B_YEASTGTB1genetic
27708008
CP56_YEASTDIT2genetic
27708008
PUF6_YEASTPUF6genetic
27708008
RIM15_YEASTRIM15genetic
27708008
YFD4_YEASTYFL034Wgenetic
27708008
XRN1_YEASTXRN1genetic
27708008
SNG1_YEASTSNG1genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
VPS53_YEASTVPS53genetic
27708008
MET5_YEASTMET5genetic
27708008
LHS1_YEASTLHS1genetic
27708008
CTK1_YEASTCTK1genetic
27708008
SRR1L_YEASTBER1genetic
27708008
GBLP_YEASTASC1genetic
27708008
CTL1_YEASTCTL1genetic
27708008
PUR1_YEASTADE4genetic
27708008
MSN1_YEASTMSN1genetic
27708008
PEX27_YEASTPEX27genetic
27708008
CAF20_YEASTCAF20genetic
27708008
PDE2_YEASTPDE2genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
MDL2_YEASTMDL2genetic
27708008
THP3_YEASTTHP3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IPI3_YEAST

loading...

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-388, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory