DRE2_YEAST - dbPTM
DRE2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DRE2_YEAST
UniProt AC P36152
Protein Name Fe-S cluster assembly protein DRE2 {ECO:0000255|HAMAP-Rule:MF_03115}
Gene Name DRE2 {ECO:0000255|HAMAP-Rule:MF_03115}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 348
Subcellular Localization Cytoplasm . Mitochondrion intermembrane space .
Protein Description Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2. Has anti-apoptotic effects in the cell. Involved in negative control of H(2)O(2)-induced cell death..
Protein Sequence MSQYKTGLLLIHPAVTTTPELVENTKAQAASKKVKFVDQFLINKLNDGSITLENAKYETVHYLTPEAQTDIKFPKKLISVLADSLKPNGSLIGLSDIYKVDALINGFEIINEPDYCWIKMDSSKLNQTVSIPLKKKKTNNTKLQSGSKLPTFKKASSSTSNLPSFKKADHSRQPIVKETDSFKPPSFKMTTEPKVYRVVDDLIEDSDDDDFSSDSSKAQYFDQVDTSDDSIEEEELIDEDGSGKSMITMITCGKSKTKKKKACKDCTCGMKEQEENEINDIRSQQDKVVKFTEDELTEIDFTIDGKKVGGCGSCSLGDAFRCSGCPYLGLPAFKPGQPINLDSISDDL
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
5Ubiquitination---MSQYKTGLLLIH
---CCCCCCEEEEEC		28.6017644757
26AcetylationPELVENTKAQAASKK
HHHHHCHHHHHHHCC		50.5124489116
26UbiquitinationPELVENTKAQAASKK
HHHHHCHHHHHHHCC		50.5117644757
33AcetylationKAQAASKKVKFVDQF
HHHHHHCCCCEEEHH		48.4324489116
35AcetylationQAASKKVKFVDQFLI
HHHHCCCCEEEHHHH		48.8524489116
35UbiquitinationQAASKKVKFVDQFLI
HHHHCCCCEEEHHHH		48.8515699485
44UbiquitinationVDQFLINKLNDGSIT
EEHHHHHHHCCCCEE		41.4915699485
49PhosphorylationINKLNDGSITLENAK
HHHHCCCCEEEECCE		18.4422369663
51PhosphorylationKLNDGSITLENAKYE
HHCCCCEEEECCEEE		29.7122369663
72AcetylationPEAQTDIKFPKKLIS
HHHHCCCCCCHHHHH		59.4324489116
130PhosphorylationSKLNQTVSIPLKKKK
HHCCCEEEEECCCCC		23.1321551504
148AcetylationTKLQSGSKLPTFKKA
CCCCCCCCCCCCCCC		63.1125381059
153UbiquitinationGSKLPTFKKASSSTS
CCCCCCCCCCCCCCC		50.3217644757
154UbiquitinationSKLPTFKKASSSTSN
CCCCCCCCCCCCCCC		49.6717644757
156PhosphorylationLPTFKKASSSTSNLP
CCCCCCCCCCCCCCC		33.4322369663
157PhosphorylationPTFKKASSSTSNLPS
CCCCCCCCCCCCCCC		42.3622369663
158PhosphorylationTFKKASSSTSNLPSF
CCCCCCCCCCCCCCH		33.1022369663
159PhosphorylationFKKASSSTSNLPSFK
CCCCCCCCCCCCCHH		24.4722369663
160PhosphorylationKKASSSTSNLPSFKK
CCCCCCCCCCCCHHC		38.0122369663
164PhosphorylationSSTSNLPSFKKADHS
CCCCCCCCHHCCCCC		53.5219823750
166UbiquitinationTSNLPSFKKADHSRQ
CCCCCCHHCCCCCCC		51.9217644757
167UbiquitinationSNLPSFKKADHSRQP
CCCCCHHCCCCCCCC		57.9717644757
179PhosphorylationRQPIVKETDSFKPPS
CCCCCCCCCCCCCCC		31.0919823750
181PhosphorylationPIVKETDSFKPPSFK
CCCCCCCCCCCCCCC		42.4619823750
183AcetylationVKETDSFKPPSFKMT
CCCCCCCCCCCCCCC		61.0324489116
183UbiquitinationVKETDSFKPPSFKMT
CCCCCCCCCCCCCCC		61.0322817900
186PhosphorylationTDSFKPPSFKMTTEP
CCCCCCCCCCCCCCC		46.1319823750
188AcetylationSFKPPSFKMTTEPKV
CCCCCCCCCCCCCCE		39.4125381059
188UbiquitinationSFKPPSFKMTTEPKV
CCCCCCCCCCCCCCE		39.4123749301
206PhosphorylationVDDLIEDSDDDDFSS
HHHHHCCCCCCCCCC		30.1022369663
212PhosphorylationDSDDDDFSSDSSKAQ
CCCCCCCCCCCHHHH		39.9822369663
213PhosphorylationSDDDDFSSDSSKAQY
CCCCCCCCCCHHHHH		41.3220377248
215PhosphorylationDDDFSSDSSKAQYFD
CCCCCCCCHHHHHHE		35.3722369663
216PhosphorylationDDFSSDSSKAQYFDQ
CCCCCCCHHHHHHEE		36.6820377248
220PhosphorylationSDSSKAQYFDQVDTS
CCCHHHHHHEECCCC		17.6219795423
226PhosphorylationQYFDQVDTSDDSIEE
HHHEECCCCCCCCCH		34.8919823750
227PhosphorylationYFDQVDTSDDSIEEE
HHEECCCCCCCCCHH		34.6519795423
230PhosphorylationQVDTSDDSIEEEELI
ECCCCCCCCCHHHHC		36.5719795423
245PhosphorylationDEDGSGKSMITMITC
CCCCCCCEEEEEEEC		20.9522369663
248PhosphorylationGSGKSMITMITCGKS
CCCCEEEEEEECCCC		8.2228889911
251PhosphorylationKSMITMITCGKSKTK
CEEEEEEECCCCCCC		12.3721440633
264AcetylationTKKKKACKDCTCGMK
CCCCCCCCCCCCCCH		61.7825381059
267PhosphorylationKKACKDCTCGMKEQE
CCCCCCCCCCCHHHH		23.4128889911
271UbiquitinationKDCTCGMKEQEENEI
CCCCCCCHHHHHHHH		41.3423749301
283PhosphorylationNEINDIRSQQDKVVK
HHHHHHHHHHHHEEE		32.3122369663
297PhosphorylationKFTEDELTEIDFTID
ECCHHHCEEEEEEEC		28.9324961812
306UbiquitinationIDFTIDGKKVGGCGS
EEEEECCEEECCCCC		40.3017644757
307UbiquitinationDFTIDGKKVGGCGSC
EEEECCEEECCCCCC		52.2017644757
345PhosphorylationPINLDSISDDL----
CCCHHHCCCCC----		29.0821440633
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 DRE2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DRE2_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 DRE2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPOD_YEASTPOL3genetic
12759774
SYSC_YEASTSES1physical
16554755
NDOR1_YEASTTAH18physical
16554755
NDOR1_YEASTTAH18physical
18467557
MRS3_YEASTMRS3genetic
18625724
MRS4_YEASTMRS4genetic
18625724
NDOR1_YEASTTAH18physical
19194512
UBI4P_YEASTUBI4physical
20694217
CFD1_YEASTCFD1physical
20802492
NBP35_YEASTNBP35physical
20802492
NAR1_YEASTNAR1physical
20802492
AFT1_YEASTAFT1genetic
24733891
AFT2_YEASTAFT2genetic
24733891
DUN1_YEASTDUN1genetic
24733891
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DRE2_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-158; SER-186 ANDSER-206, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158 AND SER-186, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND MASSSPECTROMETRY.

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