EMI2_YEAST - dbPTM
EMI2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EMI2_YEAST
UniProt AC Q04409
Protein Name Putative glucokinase-2
Gene Name EMI2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 500
Subcellular Localization Cytoplasm .
Protein Description Putative glucokinase involved in phosphorylation of aldohexoses and glucose uptake (By similarity). Involved in sporulation. Required for the full activation of the early meiotic inducer IME1..
Protein Sequence MSFENLHKVNAEALEDAVVEICSSLQVDAAKLDELTAYFIECMEKGLNNTSVGEEKTVDKGLPMIPTYVTSLPNGTERGVLLAADLGGTHFRVCSVTLNGDGTFDMQQLKSKIPEEYLNDKDVTSEELFSYLGRRTRAFVRKHHPELLKSTGENIKPLKMGFTFSYPVDQTSLSSGTLIRWTKSFKIEDTVGKDVVRLYQEQLDIQGLSMINVVALTNDTVGTFLSHCYTSGSRPSSAGEISEPVIGCIFGTGTNGCYMEDIENIKKLPDELRTRLLHEGKTQMCINIEWGSFDNELKHLSATKYDIDIDQKFSPNPGYHLFEKRISGMYLGELLRNILVDLHARGLILGQYRNYDQLPHRLKTPFQLCSEVLSRIEIDDSTNLRETELSFLQSLRLPTTFEERKAIQNLVRSITRRSAYLAAVPIAAILIKTNALNKRYHGEVEIGFDGYVIEYYPGFRSMLRHALALSPIGTEGERKIHLRLAKDGSGVGAALCALVA
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
2Acetylation------MSFENLHKV
------CCCCCHHHC		41.07-
2Phosphorylation------MSFENLHKV
------CCCCCHHHC		41.0722369663
60AcetylationGEEKTVDKGLPMIPT
CCCCCCCCCCCCCCE		58.9924489116
110AcetylationTFDMQQLKSKIPEEY
CCCHHHHHHHCCHHH		45.4224489116
111PhosphorylationFDMQQLKSKIPEEYL
CCHHHHHHHCCHHHH		44.3922369663
117PhosphorylationKSKIPEEYLNDKDVT
HHHCCHHHHCCCCCC		14.7822369663
156UbiquitinationKSTGENIKPLKMGFT
HHCCCCCCCCEEEEE		56.7423749301
184PhosphorylationTLIRWTKSFKIEDTV
CEEEEECCEEEECCC		25.1322369663
186AcetylationIRWTKSFKIEDTVGK
EEEECCEEEECCCCH		52.8824489116
190PhosphorylationKSFKIEDTVGKDVVR
CCEEEECCCCHHHHH		20.5422369663
324AcetylationPGYHLFEKRISGMYL
CCCCHHHHHHHCHHH		47.9324489116
381PhosphorylationSRIEIDDSTNLRETE
HCCCCCCCCCCCHHH		18.5628889911
382PhosphorylationRIEIDDSTNLRETEL
CCCCCCCCCCCHHHH		45.3127214570
387PhosphorylationDSTNLRETELSFLQS
CCCCCCHHHHHHHHH		35.4719779198
470PhosphorylationLRHALALSPIGTEGE
HHHHHHHCCCCCCCC		14.63-
489PhosphorylationLRLAKDGSGVGAALC
EEECCCCCCHHHHHH		40.2030377154
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 EMI2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EMI2_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 EMI2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HXKG_YEASTGLK1genetic
18408719
LTE1_YEASTLTE1genetic
20093466
SHE1_YEASTSHE1genetic
20093466
YD199_YEASTYDL199Cgenetic
20093466
PMT5_YEASTPMT5genetic
20093466
THI3_YEASTTHI3genetic
20093466
SPO71_YEASTSPO71genetic
20093466
SAC3_YEASTSAC3genetic
20093466
HSP42_YEASTHSP42genetic
20093466
AHA1_YEASTAHA1genetic
20093466
CYPD_YEASTCPR5genetic
20093466
HIM1_YEASTHIM1genetic
20093466
MCM21_YEASTMCM21genetic
20093466
YFT2_YEASTYFT2genetic
20093466
VPS74_YEASTVPS74genetic
20093466
LSM6_YEASTLSM6genetic
20093466
ECM32_YEASTECM32genetic
20093466
DCV1_YEASTDCV1genetic
20093466
ROG3_YEASTROG3genetic
20093466
SCY1_YEASTSCY1genetic
20093466
MPC1_YEASTMPC1genetic
20093466
ERV14_YEASTERV14genetic
20093466
ORM1_YEASTORM1genetic
20093466
DBF2_YEASTDBF2genetic
20093466
YG34_YEASTYGR122Wgenetic
20093466
BGL2_YEASTBGL2genetic
20093466
YG5X_YEASTYGR283Cgenetic
20093466
RL8A_YEASTRPL8Agenetic
20093466
YIC4_YEASTYIL024Cgenetic
20093466
CBPS_YEASTCPS1genetic
20093466
RS21B_YEASTRPS21Bgenetic
20093466
PYR1_YEASTURA2genetic
20093466
LSM1_YEASTLSM1genetic
20093466
ASF1_YEASTASF1genetic
20093466
PTK2_YEASTPTK2genetic
20093466
MOG1_YEASTMOG1genetic
20093466
PYRD_YEASTURA1genetic
20093466
APC9_YEASTAPC9genetic
20093466
PFD6_YEASTYKE2genetic
20093466
CTF3_YEASTCTF3genetic
20093466
PYRC_YEASTURA4genetic
20093466
SST2_YEASTSST2genetic
20093466
PML39_YEASTPML39genetic
20093466
PYRE_YEASTURA5genetic
20093466
NU188_YEASTNUP188genetic
20093466
GAT2_YEASTGAT2genetic
20093466
LSM7_YEASTLSM7genetic
20093466
HRB1_YEASTHRB1genetic
20093466
ATG3_YEASTATG3genetic
20093466
VAM3_YEASTVAM3genetic
20093466
AIM44_YEASTAIM44genetic
20093466
CTF19_YEASTCTF19genetic
20093466
MED1_YEASTMED1genetic
20093466
CG22_YEASTCLB2genetic
20093466
LTE1_YEASTLTE1genetic
20065090
BNS1_YEASTBNS1genetic
20065090
SPO12_YEASTSPO12genetic
20065090
SLK19_YEASTSLK19genetic
20065090
DBF2_YEASTDBF2genetic
20065090
MOB1_YEASTMOB1genetic
20065090
BOS1_YEASTBOS1genetic
27708008
CND2_YEASTBRN1genetic
27708008
MAK5_YEASTMAK5genetic
27708008
APC11_YEASTAPC11genetic
27708008
RPB1_YEASTRPO21genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
CDC12_YEASTCDC12genetic
27708008
MET30_YEASTMET30genetic
27708008
NU159_YEASTNUP159genetic
27708008
MCM10_YEASTMCM10genetic
27708008
ARP4_YEASTARP4genetic
27708008
KTHY_YEASTCDC8genetic
27708008
SMC4_YEASTSMC4genetic
27708008
TYSY_YEASTCDC21genetic
27708008
PROF_YEASTPFY1genetic
27708008
RPA1_YEASTRPA190genetic
27708008
MOT1_YEASTMOT1genetic
27708008
NAB3_YEASTNAB3genetic
27708008
RPN7_YEASTRPN7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EMI2_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-381 AND THR-382, ANDMASS SPECTROMETRY.

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