SLD2_YEAST - dbPTM
SLD2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLD2_YEAST
UniProt AC P34252
Protein Name DNA replication regulator SLD2
Gene Name SLD2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 453
Subcellular Localization Nucleus.
Protein Description Has a role in the initiation of DNA replication. Required at S-phase checkpoint. Also required for the proper activation of RAD53 in response to DNA damage and replication blocks..
Protein Sequence MYSFELDKLKIELKTWEHDFIDKNKREPTRDDIKSLRTVRQMYKQYSTLKKKQSLQRQKVDTQESVELPAHKKDHDEVVEIGPTPQVYGKAISIFDMNLSPIKPIYMTFTNNIDVNNDNSKTISNESSPRKTILLKSSPADRTLVAEPISSVKRQLNFQMLNASSTRTPTSSPCKNRNGKLVEIKKCSPTINPPLESGKPSGYYGPNSPLKLDEENIHLNISLNSSTKRRLQIAYPSLQKTPSKDQADISTSFSPSPLIRRPLTKSLIELAREHTEIVKEFGVLQEEDIEEEEEGEEGENGYDEKNHEDDFGLEDELIRPKVVKDIFQEDDDNDDSQAREDTFIRKRPKRRKVIRRLRDNDPETETAGFERDVHKELVKLKRRKVAEFLGSTSQISDTEFEHDPEASSGVVSSEQKPTAKRKGRKKYNLVSNNFRRLKLPKKNRFSNGRWGRR
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
3Phosphorylation-----MYSFELDKLK
-----CCEEECCCCE		15.7930377154
29PhosphorylationDKNKREPTRDDIKSL
CCCCCCCCHHHHHHH		41.8119795423
84PhosphorylationEVVEIGPTPQVYGKA
HCEEECCCCCCCCEE		22.5717167417
93PhosphorylationQVYGKAISIFDMNLS
CCCCEEEEEEECCCC		23.2821551504
100PhosphorylationSIFDMNLSPIKPIYM
EEEECCCCCCCCEEE		21.4111807498
122PhosphorylationVNNDNSKTISNESSP
CCCCCCCCCCCCCCC		29.4727717283
124PhosphorylationNDNSKTISNESSPRK
CCCCCCCCCCCCCCE		39.5125752575
127PhosphorylationSKTISNESSPRKTIL
CCCCCCCCCCCEEEE		50.3127717283
128PhosphorylationKTISNESSPRKTILL
CCCCCCCCCCEEEEE		23.6511807498
132PhosphorylationNESSPRKTILLKSSP
CCCCCCEEEEECCCC		20.3819823750
137PhosphorylationRKTILLKSSPADRTL
CEEEEECCCCCCCEE		41.3322369663
138PhosphorylationKTILLKSSPADRTLV
EEEEECCCCCCCEEE		23.6322369663
143PhosphorylationKSSPADRTLVAEPIS
CCCCCCCEEEECCHH		26.5719823750
150PhosphorylationTLVAEPISSVKRQLN
EEEECCHHHHHHHHC		39.5319823750
151PhosphorylationLVAEPISSVKRQLNF
EEECCHHHHHHHHCC		32.1721440633
164PhosphorylationNFQMLNASSTRTPTS
CCEEECCCCCCCCCC		31.0421440633
166PhosphorylationQMLNASSTRTPTSSP
EEECCCCCCCCCCCC		35.7521440633
168PhosphorylationLNASSTRTPTSSPCK
ECCCCCCCCCCCCCC		30.8911807498
170PhosphorylationASSTRTPTSSPCKNR
CCCCCCCCCCCCCCC		41.0228889911
171PhosphorylationSSTRTPTSSPCKNRN
CCCCCCCCCCCCCCC		33.2221440633
172PhosphorylationSTRTPTSSPCKNRNG
CCCCCCCCCCCCCCC		36.4711807498
188PhosphorylationLVEIKKCSPTINPPL
EEEEEECCCCCCCCC		33.6820377248
190PhosphorylationEIKKCSPTINPPLES
EEEECCCCCCCCCCC		19.6621551504
197PhosphorylationTINPPLESGKPSGYY
CCCCCCCCCCCCCCC		60.8521551504
203PhosphorylationESGKPSGYYGPNSPL
CCCCCCCCCCCCCCC		15.0221551504
208PhosphorylationSGYYGPNSPLKLDEE
CCCCCCCCCCCCCCC		34.4411807498
241PhosphorylationAYPSLQKTPSKDQAD
ECHHHCCCCCCCHHC		21.6011807498
243PhosphorylationPSLQKTPSKDQADIS
HHHCCCCCCCHHCCC		54.8424961812
250PhosphorylationSKDQADISTSFSPSP
CCCHHCCCCCCCCCH		20.6724961812
252PhosphorylationDQADISTSFSPSPLI
CHHCCCCCCCCCHHH		19.5521440633
254PhosphorylationADISTSFSPSPLIRR
HCCCCCCCCCHHHCC		25.0021440633
256PhosphorylationISTSFSPSPLIRRPL
CCCCCCCCHHHCCHH		31.0121440633
264PhosphorylationPLIRRPLTKSLIELA
HHHCCHHHHHHHHHH		22.6724961812
336PhosphorylationEDDDNDDSQAREDTF
CCCCCCCHHHHHHHH		28.7128889911
381AcetylationHKELVKLKRRKVAEF
HHHHHHHHHHHHHHH		44.4325381059
393PhosphorylationAEFLGSTSQISDTEF
HHHHCCCCCCCCCCC		27.4921440633
396PhosphorylationLGSTSQISDTEFEHD
HCCCCCCCCCCCCCC		30.7321440633
398PhosphorylationSTSQISDTEFEHDPE
CCCCCCCCCCCCCCC		35.4621440633
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
84TPhosphorylationKinaseCDC28P00546
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
84TPhosphorylation

16619031
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 SLD2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAM33_YEASTMAM33physical
11805837
IMA1_YEASTSRP1physical
11805837
COPA_YEASTCOP1physical
11805837
CSK21_YEASTCKA1physical
11805837
PP2C7_YEASTPTC7physical
11805837
TRNL_YEASTTRL1physical
11805837
GAL7_YEASTGAL7physical
11805837
MDHM_YEASTMDH1physical
11805837
DSS1_YEASTDSS1physical
11805837
TAL1_YEASTTAL1physical
11805837
IPYR_YEASTIPP1physical
11805837
GRPE_YEASTMGE1physical
11805837
ADH2_YEASTADH2physical
11805837
ADH4_YEASTADH4physical
11805837
DPB11_YEASTDPB11physical
11807498
DPB11_YEASTDPB11physical
9742127
DPB11_YEASTDPB11genetic
11807498
DPB11_YEASTDPB11genetic
10097122
SYEC_YEASTGUS1physical
16554755
CBS_YEASTCYS4physical
16554755
LSM12_YEASTLSM12physical
16554755
MAM33_YEASTMAM33physical
16554755
CGS5_YEASTCLB5physical
15200949
DPB11_YEASTDPB11physical
16619031
DPB11_YEASTDPB11genetic
9742127
DPB11_YEASTDPB11genetic
18948746
MSA1_YEASTMSA1genetic
18948746
DDC1_YEASTDDC1genetic
11973288
DPB11_YEASTDPB11physical
20231317
DPB2_YEASTDPB2physical
20231317
PST2_YEASTPST2physical
20231317
SLD5_YEASTSLD5physical
20231317
PSF1_YEASTPSF1genetic
20231317
PSF3_YEASTPSF3genetic
20231317
CDC6_YEASTCDC6genetic
21698130
MCM2_YEASTMCM2physical
21868389
MCM3_YEASTMCM3physical
21868389
MCM4_YEASTMCM4physical
21868389
MCM5_YEASTMCM5physical
21868389
MCM6_YEASTMCM6physical
21868389
MCM7_YEASTMCM7physical
21868389
SLD3_YEASTSLD3genetic
22081107
SLD7_YEASTSLD7genetic
22081107
SML1_YEASTSML1genetic
22081107
CDC45_YEASTCDC45genetic
22081107
DBF4_YEASTDBF4genetic
22081107
DPB11_YEASTDPB11physical
23629628
DPB11_YEASTDPB11physical
24307213
MCM2_YEASTMCM2physical
24307213
SLD7_YEASTSLD7physical
26338774
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLD2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A CDK-catalysed regulatory phosphorylation for formation of the DNAreplication complex Sld2-Dpb11.";
Tak Y.-S., Tanaka Y., Endo S., Kamimura Y., Araki H.;
EMBO J. 25:1987-1996(2006).
Cited for: INTERACTION WITH DPB11, PHOSPHORYLATION AT THR-84, AND MUTAGENESIS OFTHR-84; SER-100; SER-208 AND THR-241.

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