MTH1_YEAST - dbPTM
MTH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTH1_YEAST
UniProt AC P35198
Protein Name Protein MTH1
Gene Name MTH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 433
Subcellular Localization
Protein Description
Protein Sequence MFVSPPPATSKNQVLQRRPLESTNSNHGFASSLQAIPENTMSGSDNASFQSLPLSMSSSQSTTSSRRENFVNAPPEYTDRARDEIKKRLLASSPSRRSHHSSSMHSASRRSSVAESGSLLSDNASSYQSSIFSAPSTVHTQLTNDSSFSEFPNHKLITRVSLDEALPKTFYDMYSPDILLADPSNILCNGRPKFTKRELLDWDLNDIRSLLIVEKLRPEWGNQLPEVITVGDNMPQFRLQLLPLYSSDETIIATLVHSDLYMEANLDYEFKLTSAKYTVATARKRHEHITGRNEAVMNLSKPEWRNIIENYLLNIAVEAQCRFDFKQRCSEYKKWKLQQSNLKRPDMPPPSIIPRKNSTETKSLLKKALLKNIQLKNPNNNLDELMMRSSAATNQQGKNKVSLSKEEKATIWSQCQAQVYQRLGLDWQPDSVS
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
92PhosphorylationIKKRLLASSPSRRSH
HHHHHHHCCCCHHCC
42.6328889911
93PhosphorylationKKRLLASSPSRRSHH
HHHHHHCCCCHHCCC
22.6828889911
108PhosphorylationSSSMHSASRRSSVAE
CHHCCCHHHHHCHHH
31.1028889911
168UbiquitinationSLDEALPKTFYDMYS
EHHHHCCHHHHHCCC
52.7123749301
271UbiquitinationANLDYEFKLTSAKYT
ECCCEEEEECCCEEE
38.6322817900
276UbiquitinationEFKLTSAKYTVATAR
EEEECCCEEEHHHHH
41.0223749301
301UbiquitinationEAVMNLSKPEWRNII
HHHHHCCCHHHHHHH
50.5523749301

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
-KUbiquitinationE3 ubiquitin ligaseGRR1P24814
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTH1_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 MTH1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RGT1_YEASTRGT1physical
14508605
RGT2_YEASTRGT2physical
10632886
SNF3_YEASTSNF3physical
10632886
SNF3_YEASTSNF3physical
10373505
GRR1_YEASTGRR1physical
15456873
HXT1_YEASTHXT1genetic
8366037
HXT1_YEASTHXT1genetic
8002563
HXT2_YEASTHXT2genetic
8002563
HXT3_YEASTHXT3genetic
8366037
HXT3_YEASTHXT3genetic
8002563
HXT4_YEASTHXT4genetic
8366037
STD1_YEASTSTD1genetic
19720826
AGP1_YEASTAGP1genetic
20093466
GET3_YEASTGET3genetic
20093466
VPS41_YEASTVPS41genetic
20093466
MED5_YEASTNUT1genetic
20093466
YG3A_YEASTYGR130Cgenetic
20093466
STP2_YEASTSTP2genetic
20093466
VPS29_YEASTVPS29genetic
20093466
FMC1_YEASTFMC1genetic
20093466
CTK3_YEASTCTK3genetic
20093466
RCN2_YEASTRCN2genetic
20093466
YP264_YEASTYPL264Cgenetic
20093466
STD1_YEASTSTD1genetic
9725828
STD1_YEASTSTD1genetic
20959818
SUM1_YEASTSUM1genetic
20959818
URE2_YEASTURE2genetic
20959818
SPT3_YEASTSPT3genetic
20959818
STB5_YEASTSTB5genetic
20959818
UPC2_YEASTUPC2genetic
20959818
GAT1_YEASTGAT1genetic
20959818
VHS1_YEASTVHS1genetic
21127252
STD1_YEASTSTD1genetic
23234240
HXT2_YEASTHXT2genetic
23234240
TUP1_YEASTTUP1genetic
23468525
KAPA_YEASTTPK1genetic
23468525
PP4R3_YEASTPSY2physical
24277933
PP4C_YEASTPPH3physical
24277933
STD1_YEASTSTD1genetic
26431967
STD1_YEASTSTD1genetic
25541485
MRM2_YEASTMRM2genetic
27708008
MED5_YEASTNUT1genetic
27708008
YG3A_YEASTYGR130Cgenetic
27708008
VPS29_YEASTVPS29genetic
27708008
TOK1_YEASTTOK1genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
CTK3_YEASTCTK3genetic
27708008
RCN2_YEASTRCN2genetic
27708008
CWC27_YEASTCWC27genetic
27708008
ELP3_YEASTELP3genetic
27708008
MED1_YEASTMED1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTH1_YEAST

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Related Literatures of Post-Translational Modification

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