DMA1_YEAST - dbPTM
DMA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DMA1_YEAST
UniProt AC P38823
Protein Name E3 ubiquitin-protein ligase DMA1 {ECO:0000305|PubMed:18202552}
Gene Name DMA1 {ECO:0000303|PubMed:15146058}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 416
Subcellular Localization Cytoplasm .
Protein Description E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjonction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugationg enzymes. [PubMed: 18202552 Involved in nutritional control of the cell cycle]
Protein Sequence MSTNTVPSSPPNQTPPAASGIATSHDHTKFNNPIRLPISISLTINDTPNNNSNNNSVSNGLGILPSRTATSLVVANNGSANGNVGATAAAAATVETNTAPAVNTTKSIRHFIYPPNQVNQTEFSLDIHLPPNTSLPERIDQSTLKRRMDKHGLFSIRLTPFIDTSSTSVANQGLFFDPIIRTAGAGSQIIIGRYTERVREAISKIPDQYHPVVFKSKVISRTHGCFKVDDQGNWFLKDVKSSSGTFLNHQRLSSASTTSKDYLLHDGDIIQLGMDFRGGTEEIYRCVKMKIELNKSWKLKANAFNKEALSRIKNLQKLTTGLEQEDCSICLNKIKPCQAIFISPCAHSWHFHCVRRLVIMNYPQFMCPNCRTNCDLETTLESESESEFENEDEDEPDIEMDIDMEINNNLGVRLVD
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
2Phosphorylation------MSTNTVPSS
------CCCCCCCCC		30.3022369663
3Phosphorylation-----MSTNTVPSSP
-----CCCCCCCCCC		33.3422369663
5Phosphorylation---MSTNTVPSSPPN
---CCCCCCCCCCCC		33.6022369663
8PhosphorylationMSTNTVPSSPPNQTP
CCCCCCCCCCCCCCC		51.6622369663
9PhosphorylationSTNTVPSSPPNQTPP
CCCCCCCCCCCCCCC		38.0022369663
14PhosphorylationPSSPPNQTPPAASGI
CCCCCCCCCCCCCCC		37.5722369663
19PhosphorylationNQTPPAASGIATSHD
CCCCCCCCCCCCCCC		32.6022369663
23PhosphorylationPAASGIATSHDHTKF
CCCCCCCCCCCCCCC		25.3622369663
24PhosphorylationAASGIATSHDHTKFN
CCCCCCCCCCCCCCC		20.2122369663
28PhosphorylationIATSHDHTKFNNPIR
CCCCCCCCCCCCCCC		43.3122369663
106UbiquitinationAPAVNTTKSIRHFIY
CCCCCCCCEEEEEEC		41.6723749301
150UbiquitinationTLKRRMDKHGLFSIR
HHHHHHHHCCCCEEE		30.1718202552
204UbiquitinationRVREAISKIPDQYHP
HHHHHHHCCCCCCCC		52.7418202552
217UbiquitinationHPVVFKSKVISRTHG
CCEEEECEEEEECCC		44.1518202552
237UbiquitinationDQGNWFLKDVKSSSG
CCCCEEEEEECCCCC		51.5118202552
237AcetylationDQGNWFLKDVKSSSG
CCCCEEEEEECCCCC		51.5124489116
240UbiquitinationNWFLKDVKSSSGTFL
CEEEEEECCCCCCCC		55.5418202552
260UbiquitinationSSASTTSKDYLLHDG
CCCCCCCCCEECCCC		48.5818202552
296PhosphorylationMKIELNKSWKLKANA
EEEEECCCCCCCCCC		28.5028889911
300UbiquitinationLNKSWKLKANAFNKE
ECCCCCCCCCCCCHH		35.5518202552
306UbiquitinationLKANAFNKEALSRIK
CCCCCCCHHHHHHHH		37.6023749301
313UbiquitinationKEALSRIKNLQKLTT
HHHHHHHHHHHHHHH		50.9618202552
317UbiquitinationSRIKNLQKLTTGLEQ
HHHHHHHHHHHCCCH		51.4723749301
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 DMA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
150Kubiquitylation

18202552
204Kubiquitylation

18202552
204Kubiquitylation

18202552
217Kubiquitylation

18202552
237Kubiquitylation

18202552
237Kubiquitylation

18202552
240Kubiquitylation

18202552
260Kubiquitylation

18202552
300Kubiquitylation

18202552
306Kubiquitylation

18202552
306Kubiquitylation

18202552
306Kubiquitylation

18202552
313Kubiquitylation

18202552
317Kubiquitylation

18202552
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 DMA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKP2_YEASTSKP2physical
11805837
DMA2_YEASTDMA2physical
11805837
YEF1_YEASTYEF1physical
10688190
CD123_YEASTCDC123physical
10688190
CD123_YEASTCDC123physical
15319434
DBP3_YEASTDBP3physical
14660704
IF2G_YEASTGCD11physical
14660704
JIP5_YEASTJIP5physical
14660704
MKT1_YEASTMKT1physical
14660704
SEC16_YEASTSEC16physical
14660704
YL21B_YEASTYLR410W-Bphysical
14660704
YF21B_YEASTYFL002W-Aphysical
14660704
YG22B_YEASTYFL002W-Aphysical
14660704
YD22B_YEASTYDR210W-Bphysical
14660704
YD21B_YEASTYDR034C-Dphysical
14660704
YC21B_YEASTYCL019Wphysical
14660704
YO11A_YEASTYOL103W-Aphysical
14660704
YL14A_YEASTYLR256W-Aphysical
14660704
YJ11A_YEASTYLR227W-Aphysical
14660704
YL13A_YEASTYLR227W-Aphysical
14660704
YM12A_YEASTYLR227W-Aphysical
14660704
YD15A_YEASTYLR157C-Aphysical
14660704
YE11A_YEASTYLR157C-Aphysical
14660704
YL12A_YEASTYLR157C-Aphysical
14660704
YP11A_YEASTYLR157C-Aphysical
14660704
YJ12A_YEASTYJR028Wphysical
14660704
ESC2_YEASTESC2genetic
17314980
GET2_YEASTGET2genetic
17314980
INP52_YEASTINP52genetic
19269370
DMA2_YEASTDMA2genetic
20351217
CD123_YEASTCDC123genetic
15319434
DMA2_YEASTDMA2genetic
21562220
HSL1_YEASTHSL1genetic
21562220
2ABA_YEASTCDC55genetic
21562220
SWE1_YEASTSWE1genetic
21562220
MPIP_YEASTMIH1genetic
21562220
BNI5_YEASTBNI5genetic
21562220
PP2C1_YEASTPTC1genetic
21127252
IRE1_YEASTIRE1genetic
21127252
KSP1_YEASTKSP1genetic
21127252
2A5D_YEASTRTS1genetic
22570619
SWE1_YEASTSWE1genetic
22570619
KIN4_YEASTKIN4genetic
22570619
ELM1_YEASTELM1genetic
22570619
BNI4_YEASTBNI4genetic
22570619
DMA2_YEASTDMA2genetic
23264631
PCL1_YEASTPCL1physical
23264631
CYK3_YEASTCYK3genetic
23966170
DMA2_YEASTDMA2genetic
23966170
POG1_YEASTPOG1genetic
25073408
DMA1_YEASTDMA1physical
18202552
UBC4_YEASTUBC4physical
18202552
UBC13_YEASTUBC13physical
18202552
DMA2_YEASTDMA2physical
18202552
VAC17_YEASTVAC17physical
24636257
COM1_YEASTSAE2physical
25762720
BNI1_YEASTBNI1genetic
27449057
BNI1_YEASTBNI1physical
27449057
BNR1_YEASTBNR1physical
27449057
DMA2_YEASTDMA2genetic
27449057
GIC1_YEASTGIC1genetic
27449057
GIC2_YEASTGIC2genetic
27449057
RHO1_YEASTRHO1genetic
26179915
KPC1_YEASTPKC1genetic
26179915
SYP1_YEASTSYP1genetic
26179915
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DMA1_YEAST

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Yeast Chfr homologs retard cell cycle at G1 and G2/M via Ubc4 andUbc13/Mms2-dependent ubiquitination.";
Loring G.L., Christensen K.C., Gerber S.A., Brenner C.;
Cell Cycle 7:96-105(2008).
Cited for: FUNCTION, MASS SPECTROMETRY, AND UBIQUITINATION AT LYS-150; LYS-204;LYS-217; LYS-237; LYS-240; LYS-260; LYS-300; LYS-306; LYS-313 ANDLYS-317.

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