DYR_HUMAN - dbPTM
DYR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYR_HUMAN
UniProt AC P00374
Protein Name Dihydrofolate reductase
Gene Name DHFR
Organism Homo sapiens (Human).
Sequence Length 187
Subcellular Localization Mitochondrion . Cytoplasm .
Protein Description Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2..
Protein Sequence MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND
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
4Phosphorylation----MVGSLNCIVAV
----CCCCCCEEEEE		12.6624043423
4Ubiquitination----MVGSLNCIVAV
----CCCCCCEEEEE		12.66-
12UbiquitinationLNCIVAVSQNMGIGK
CCEEEEEECCCCCCC		13.19-
12PhosphorylationLNCIVAVSQNMGIGK
CCEEEEEECCCCCCC		13.1928102081
19UbiquitinationSQNMGIGKNGDLPWP
ECCCCCCCCCCCCCC		56.70-
29MethylationDLPWPPLRNEFRYFQ
CCCCCCCCCHHHHEE		46.54-
29UbiquitinationDLPWPPLRNEFRYFQ
CCCCCCCCCHHHHEE		46.54-
33MethylationPPLRNEFRYFQRMTT
CCCCCHHHHEEECCC		25.77-
39PhosphorylationFRYFQRMTTTSSVEG
HHHEEECCCCCCCCC		29.1620068231
47UbiquitinationTTSSVEGKQNLVIMG
CCCCCCCCEEEEECC		23.62-
47UbiquitinationTTSSVEGKQNLVIMG
CCCCCCCCEEEEECC		23.6221906983
55AcetylationQNLVIMGKKTWFSIP
EEEEECCEEEEEECC		29.6525953088
55UbiquitinationQNLVIMGKKTWFSIP
EEEEECCEEEEEECC		29.65-
56UbiquitinationNLVIMGKKTWFSIPE
EEEECCEEEEEECCC		45.30-
57UbiquitinationLVIMGKKTWFSIPEK
EEECCEEEEEECCCC		34.92-
64AcetylationTWFSIPEKNRPLKGR
EEEECCCCCCCCCCC		53.5625953088
64UbiquitinationTWFSIPEKNRPLKGR
EEEECCCCCCCCCCC		53.56-
69UbiquitinationPEKNRPLKGRINLVL
CCCCCCCCCCEEEEE		49.15-
71UbiquitinationKNRPLKGRINLVLSR
CCCCCCCCEEEEEEC		17.03-
77PhosphorylationGRINLVLSRELKEPP
CCEEEEEECCCCCCC		19.0724719451
81UbiquitinationLVLSRELKEPPQGAH
EEEECCCCCCCCCCH		64.52-
81UbiquitinationLVLSRELKEPPQGAH
EEEECCCCCCCCCCH		64.5221906983
81SumoylationLVLSRELKEPPQGAH
EEEECCCCCCCCCCH		64.52-
81SumoylationLVLSRELKEPPQGAH
EEEECCCCCCCCCCH		64.52-
93PhosphorylationGAHFLSRSLDDALKL
CCHHHCCCHHHHHHH		32.5420860994
99SumoylationRSLDDALKLTEQPEL
CCHHHHHHHHCCHHH		55.90-
99SumoylationRSLDDALKLTEQPEL
CCHHHHHHHHCCHHH		55.90-
99UbiquitinationRSLDDALKLTEQPEL
CCHHHHHHHHCCHHH		55.9021890473
104UbiquitinationALKLTEQPELANKVD
HHHHHCCHHHHCCCC		32.13-
106UbiquitinationKLTEQPELANKVDMV
HHHCCHHHHCCCCEE		8.95-
109UbiquitinationEQPELANKVDMVWIV
CCHHHHCCCCEEEEE		33.7221890473
122UbiquitinationIVGGSSVYKEAMNHP
EECCHHHHHHHHCCC		12.69-
122AcetylationIVGGSSVYKEAMNHP
EECCHHHHHHHHCCC		12.69-
123UbiquitinationVGGSSVYKEAMNHPG
ECCHHHHHHHHCCCC		36.52-
125UbiquitinationGSSVYKEAMNHPGHL
CHHHHHHHHCCCCHH		10.42-
127UbiquitinationSVYKEAMNHPGHLKL
HHHHHHHCCCCHHHH		45.29-
133UbiquitinationMNHPGHLKLFVTRIM
HCCCCHHHHHHHHHH		33.9221890473
133UbiquitinationMNHPGHLKLFVTRIM
HCCCCHHHHHHHHHH		33.9221890473
137PhosphorylationGHLKLFVTRIMQDFE
CHHHHHHHHHHHHHC		13.72-
145PhosphorylationRIMQDFESDTFFPEI
HHHHHHCCCCCCCCC		41.78-
156AcetylationFPEIDLEKYKLLPEY
CCCCCHHHHCCCCCC		55.7926051181
156UbiquitinationFPEIDLEKYKLLPEY
CCCCCHHHHCCCCCC		55.7921890473
156SumoylationFPEIDLEKYKLLPEY
CCCCCHHHHCCCCCC		55.79-
157PhosphorylationPEIDLEKYKLLPEYP
CCCCHHHHCCCCCCC		9.4822817900
158SumoylationEIDLEKYKLLPEYPG
CCCHHHHCCCCCCCC		55.40-
158UbiquitinationEIDLEKYKLLPEYPG
CCCHHHHCCCCCCCC		55.4021890473
158UbiquitinationEIDLEKYKLLPEYPG
CCCHHHHCCCCCCCC		55.4021890473
158SumoylationEIDLEKYKLLPEYPG
CCCHHHHCCCCCCCC		55.40-
163PhosphorylationKYKLLPEYPGVLSDV
HHCCCCCCCCCCCHH		11.8922817900
168PhosphorylationPEYPGVLSDVQEEKG
CCCCCCCCHHHHHHC		33.0726270265
174UbiquitinationLSDVQEEKGIKYKFE
CCHHHHHHCCEEEEE		66.2520639865
174SumoylationLSDVQEEKGIKYKFE
CCHHHHHHCCEEEEE		66.25-
174AcetylationLSDVQEEKGIKYKFE
CCHHHHHHCCEEEEE		66.2523954790
174SumoylationLSDVQEEKGIKYKFE
CCHHHHHHCCEEEEE		66.25-
177UbiquitinationVQEEKGIKYKFEVYE
HHHHHCCEEEEEEEE		51.56-
178PhosphorylationQEEKGIKYKFEVYEK
HHHHCCEEEEEEEEC		20.9929496907
179UbiquitinationEEKGIKYKFEVYEKN
HHHCCEEEEEEEECC		30.0121890473
179SumoylationEEKGIKYKFEVYEKN
HHHCCEEEEEEEECC		30.01-
179SumoylationEEKGIKYKFEVYEKN
HHHCCEEEEEEEECC		30.01-
183PhosphorylationIKYKFEVYEKND---
CEEEEEEEECCC---		17.6229496907
185UbiquitinationYKFEVYEKND-----
EEEEEEECCC-----		49.0521890473
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
145SPhosphorylationKinaseCK2A1P68400
PSP
168SPhosphorylationKinaseCK2A1P68400
PSP
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:18451149
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYR_HUMAN !!
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 DYR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CH60_HUMANHSPD1physical
8559246
MDM2_HUMANMDM2physical
18451149
P53_HUMANTP53physical
18451149
GKAP1_HUMANGKAP1physical
25416956
CDC73_HUMANCDC73genetic
27453043
CHK1_HUMANCHEK1genetic
27453043
WEE1_HUMANWEE1genetic
27453043
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613839Megaloblastic anemia due to dihydrofolate reductase deficiency (DHFRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00798Gentamicin
DB00563Methotrexate
DB00642Pemetrexed
DB06813Pralatrexate
DB01131Proguanil
DB00205Pyrimethamine
DB00440Trimethoprim
DB01157Trimetrexate
Regulatory Network of DYR_HUMAN

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Related Literatures of Post-Translational Modification

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