IMDH2_YEAST - dbPTM
IMDH2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IMDH2_YEAST
UniProt AC P38697
Protein Name Inosine-5'-monophosphate dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_03156}
Gene Name IMD2 {ECO:0000255|HAMAP-Rule:MF_03156}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 523
Subcellular Localization Cytoplasm .
Protein Description Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. In contrast to the other IMPDH alleles IMD3 and IMD4, the enzymatic activity of IMD2 seems to be intrinsically drug resistant..
Protein Sequence MAAIRDYKTALDFTKSLPRPDGLSVQELMDSKIRGGLTYNDFLILPGLVDFASSEVSLQTKLTRNITLNIPLVSSPMDTVTESEMATFMALLGGIGFIHHNCTPEDQADMVRRVKNYENGFINNPIVISPTTTVGEAKSMKEKYGFAGFPVTTDGKRNAKLVGVITSRDIQFVEDNSLLVQDVMTKNPVTGAQGITLSEGNEILKKIKKGRLLVVDEKGNLVSMLSRTDLMKNQNYPLASKSANTKQLLCGASIGTMDADKERLRLLVKAGLDVVILDSSQGNSIFELNMLKWVKESFPGLEVIAGNVVTREQAANLIAAGADGLRIGMGTGSICITQEVMACGRPQGTAVYNVCEFANQFGVPCMADGGVQNIGHITKALALGSSTVMMGGMLAGTTESPGEYFYQDGKRLKAYRGMGSIDAMQKTGTKGNASTSRYFSESDSVLVAQGVSGAVVDKGSIKKFIPYLYNGLQHSCQDIGCRSLTLLKNNVQRGKVRFEFRTASAQLEGGVHNLHSYEKRLHN
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
8AcetylationMAAIRDYKTALDFTK
CCCCCCHHHHHHHHH		31.4524489116
15AcetylationKTALDFTKSLPRPDG
HHHHHHHHCCCCCCC		50.4124489116
16PhosphorylationTALDFTKSLPRPDGL
HHHHHHHCCCCCCCC		40.3121440633
32AcetylationVQELMDSKIRGGLTY
HHHHHHCCCCCCCCH		31.9624489116
129PhosphorylationINNPIVISPTTTVGE
CCCCEEECCCCCHHC		12.8025752575
138AcetylationTTTVGEAKSMKEKYG
CCCHHCHHHHHHHHC		46.9424489116
143AcetylationEAKSMKEKYGFAGFP
CHHHHHHHHCCCCCC		45.1924489116
198PhosphorylationGAQGITLSEGNEILK
CCCCEECCCCHHHHH		34.5028152593
205SuccinylationSEGNEILKKIKKGRL
CCCHHHHHHHHCCCE		59.1023954790
205UbiquitinationSEGNEILKKIKKGRL
CCCHHHHHHHHCCCE		59.1023749301
205AcetylationSEGNEILKKIKKGRL
CCCHHHHHHHHCCCE		59.1024489116
218AcetylationRLLVVDEKGNLVSML
CEEEECCCCCEEEEE		48.9424489116
232AcetylationLSRTDLMKNQNYPLA
EHHHHHHHCCCCCCC		63.7824489116
385PhosphorylationTKALALGSSTVMMGG
HHHHHHCCCEEEECC		24.5619823750
386PhosphorylationKALALGSSTVMMGGM
HHHHHCCCEEEECCC		24.1919823750
397PhosphorylationMGGMLAGTTESPGEY
ECCCCCCCCCCCCCC		23.0628889911
415PhosphorylationDGKRLKAYRGMGSID
CCCCCCCCCCCCHHH		13.2027017623
420PhosphorylationKAYRGMGSIDAMQKT
CCCCCCCHHHHHHHH		14.3822369663
427PhosphorylationSIDAMQKTGTKGNAS
HHHHHHHHCCCCCCC		32.9423749301
438PhosphorylationGNASTSRYFSESDSV
CCCCCCCEECCCCEE		15.9527017623
440PhosphorylationASTSRYFSESDSVLV
CCCCCEECCCCEEEE		27.5328889911
442PhosphorylationTSRYFSESDSVLVAQ
CCCEECCCCEEEEEC		33.7130377154
444PhosphorylationRYFSESDSVLVAQGV
CEECCCCEEEEECCC		26.9930377154
458UbiquitinationVSGAVVDKGSIKKFI
CCCEEECHHHHHHHH		42.8422817900
462UbiquitinationVVDKGSIKKFIPYLY
EECHHHHHHHHHHHH		43.2422817900
463UbiquitinationVDKGSIKKFIPYLYN
ECHHHHHHHHHHHHH		47.0222817900
485PhosphorylationDIGCRSLTLLKNNVQ
HHCCHHHEEHHCCCC		31.1522369663
488AcetylationCRSLTLLKNNVQRGK
CHHHEEHHCCCCCCC		49.9825381059
502PhosphorylationKVRFEFRTASAQLEG
CEEEEEECCEEEECC		30.2224961812
504PhosphorylationRFEFRTASAQLEGGV
EEEEECCEEEECCCC		18.8828889911
516PhosphorylationGGVHNLHSYEKRLHN
CCCCCHHCHHHHHCC		37.8528889911
517PhosphorylationGVHNLHSYEKRLHN-
CCCCHHCHHHHHCC-		18.0930377154
519AcetylationHNLHSYEKRLHN---
CCHHCHHHHHCC---		52.6124489116
519UbiquitinationHNLHSYEKRLHN---
CCHHCHHHHHCC---		52.6123749301
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 IMDH2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMDH2_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 IMDH2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMDH3_YEASTIMD3genetic
12746440
IMDH4_YEASTIMD4genetic
12746440
PDX3_YEASTPDX3genetic
21623372
SER33_YEASTSER33genetic
21623372
MHT1_YEASTMHT1genetic
21623372
PCD1_YEASTPCD1genetic
21623372
DPP1_YEASTDPP1genetic
21623372
SUR2_YEASTSUR2genetic
21623372
ARO10_YEASTARO10genetic
21623372
COQ3_YEASTCOQ3genetic
21623372
QCR8_YEASTQCR8genetic
21623372
PUR4_YEASTADE6genetic
21623372
ALDH2_YEASTALD2genetic
21623372
ATPA_YEASTATP1genetic
21623372
HXKB_YEASTHXK2genetic
21623372
AK_YEASTHOM3genetic
21623372
TPS2_YEASTTPS2genetic
21623372
ELO2_YEASTELO2genetic
21623372
PPT2_YEASTPPT2genetic
21623372
MCM1_YEASTMCM1genetic
27708008
TF2B_YEASTSUA7genetic
27708008
VPS41_YEASTVPS41genetic
27708008
SAC1_YEASTSAC1genetic
27708008
MKT1_YEASTMKT1genetic
27708008
INO4_YEASTINO4genetic
27708008
BUD21_YEASTBUD21genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
MCE1_YEASTCEG1genetic
27708008
MOB1_YEASTMOB1genetic
27708008
DPB11_YEASTDPB11genetic
27708008
NSE5_YEASTNSE5genetic
27708008
PRP24_YEASTPRP24genetic
27708008
GPI12_YEASTGPI12genetic
27708008
TYSY_YEASTCDC21genetic
27708008
THIL_YEASTERG10genetic
27708008
SNF5_YEASTSNF5genetic
27708008
XRN1_YEASTXRN1genetic
27708008
IME1_YEASTIME1genetic
27708008
MSC1_YEASTMSC1genetic
27708008
PEX12_YEASTPEX12genetic
27708008
YHM2_YEASTYHM2genetic
27708008
SCS7_YEASTSCS7genetic
27708008
RTG1_YEASTRTG1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IMDH2_YEAST

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Related Literatures of Post-Translational Modification

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