LCD1_YEAST - dbPTM
LCD1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LCD1_YEAST
UniProt AC Q04377
Protein Name DNA damage checkpoint protein LCD1
Gene Name LCD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 747
Subcellular Localization Cytoplasm. Nucleus. Localizes to nuclear DNA repair foci with other DNA repair proteins in response to DNA double strand breaks. The recruitment to DNA lesion sites requires the presence of the RPA complex on DNA.
Protein Description Forms a complex with the serine/threonine kinase MEC1 which activates checkpoint signaling upon genotoxic stresses. The MEC1-LCD1 complex is recruited by the single-strand-binding protein complex RPA to DNA lesions in order to initiate the DNA repair by homologous recombination, after the MRX-complex and TEL1 are displaced. Required for the recruitment of MEC1 to DNA lesions, the activation of CHK1 and RAD53 kinases and phosphorylation of RAD9 in response to DNA damage. Required for cell growth and meiotic recombination..
Protein Sequence MRRETVGEFSSDDDDDILLELGTRPPRFTQIPPSSAALQTQIPTTLEVTTTTLNNKQSKNDNQLVNQLNKAQGEASMLRDKINFLNIEREKEKNIQAVKVNELQVKHLQELAKLKQELQKLEDEKKFLQMEARGKSKREVITNVKPPSTTLSTNTNTITPDSSSVAIEAKPQSPQSKKRKISDNLLKKNMVPLNPNRIIPDETSLFLESILLHQIIGADLSTIEILNRLKLDYITEFKFKNFVIAKGAPIGKSIVSLLLRCKKTLTLDRFIDTLLEDIAVLIKEISVHPNESKLAVPFLVALMYQIVQFRPSATHNLALKDCFLFICDLIRIYHHVLKVPIHESNMNLHVEPQIFQYELIDYLIISYSFDLLEGILRVLQSHPKQTYMEFFDENILKSFEFVYKLALTISYKPMVNVIFSAVEVVNIITSIILNMDNSSDLKSLISGSWWRDCITRLYALLEKEIKSGDVYNENVDTTTLHMSKYHDFFGLIRNIGDNELGGLISKLIYTDRLQSVPRVISKEDIGMDSDKFTAPIIGYKMEKWLLKLKDEVLNIFENLLMIYGDDATIVNGEMLIHSSKFLSREQALMIERYVGQDSPNLDLRCHLIEHTLTIIYRLWKDHFKQLREEQIKQVESQLIMSLWRFLVCQTETVTANEREMRDHRHLVDSLHDLTIKDQASYYEDAFEDLPEYIEEELKMQLNKRTGRIMQVKYDEKFQEMARTILESKSFDLTTLEEADSLYISMGL
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
10PhosphorylationRETVGEFSSDDDDDI
CCCCCCCCCCCCCCH		28.6721440633
11PhosphorylationETVGEFSSDDDDDIL
CCCCCCCCCCCCCHH		50.8321440633
76PhosphorylationNKAQGEASMLRDKIN
HHHHHHHHHHHHHHH		17.6611983176
142PhosphorylationKSKREVITNVKPPST
CCCCCHHCCCCCCCC		38.8529688323
148PhosphorylationITNVKPPSTTLSTNT
HCCCCCCCCEEECCC		42.4229688323
149PhosphorylationTNVKPPSTTLSTNTN
CCCCCCCCEEECCCC		37.2129688323
150PhosphorylationNVKPPSTTLSTNTNT
CCCCCCCEEECCCCE		24.0529688323
152PhosphorylationKPPSTTLSTNTNTIT
CCCCCEEECCCCEEC		19.9529688323
153PhosphorylationPPSTTLSTNTNTITP
CCCCEEECCCCEECC		49.5329688323
155PhosphorylationSTTLSTNTNTITPDS
CCEEECCCCEECCCC		33.5529688323
157PhosphorylationTLSTNTNTITPDSSS
EEECCCCEECCCCCC		24.9629688323
159PhosphorylationSTNTNTITPDSSSVA
ECCCCEECCCCCCEE		21.0029688323
162PhosphorylationTNTITPDSSSVAIEA
CCEECCCCCCEEEEE		26.2229688323
163PhosphorylationNTITPDSSSVAIEAK
CEECCCCCCEEEEEC		35.8929688323
164PhosphorylationTITPDSSSVAIEAKP
EECCCCCCEEEEECC		21.3729688323
173PhosphorylationAIEAKPQSPQSKKRK
EEEECCCCCCHHCCC		33.1725752575
176PhosphorylationAKPQSPQSKKRKISD
ECCCCCCHHCCCCCH		43.4519779198
182PhosphorylationQSKKRKISDNLLKKN
CHHCCCCCHHHHHCC		24.3927214570
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 LCD1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LCD1_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 LCD1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ILV5_YEASTILV5physical
11805837
RNQ1_YEASTRNQ1physical
11805837
ADH2_YEASTADH2physical
11805837
ADH5_YEASTADH5physical
11805837
HEMH_YEASTHEM15physical
11805837
H4_YEASTHHF1physical
11805837
ATR_YEASTMEC1physical
10950868
ATR_YEASTMEC1physical
11359899
ATR_YEASTMEC1physical
11060031
ATR_YEASTMEC1physical
11154263
XPO1_YEASTCRM1physical
11027275
SML1_YEASTSML1genetic
11239397
SML1_YEASTSML1genetic
11060031
SML1_YEASTSML1genetic
11154263
SML1_YEASTSML1genetic
10950868
ATM_YEASTTEL1genetic
11707419
YJ66_YEASTYJR096Wphysical
16554755
RFA2_YEASTRFA2physical
16554755
RFA1_YEASTRFA1physical
16753272
ATM_YEASTTEL1genetic
17954565
EMC5_YEASTEMC5physical
18467557
DPB11_YEASTDPB11genetic
19028869
PIN4_YEASTPIN4genetic
15024067
CDK1_YEASTCDC28genetic
23045388
SML1_YEASTSML1genetic
18003698
ATR_YEASTMEC1physical
19457865
MMS4_YEASTMMS4genetic
23531881
CDC5_YEASTCDC5genetic
23531881
CDK1_YEASTCDC28genetic
23531881
PP4R3_YEASTPSY2physical
25533186
RFA1_YEASTRFA1physical
25533186
BUL2_YEASTBUL2physical
29129641
RSP5_YEASTRSP5physical
29129641
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LCD1_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-10; SER-11 AND SER-76,AND MASS SPECTROMETRY.

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