GRR1_YEAST - dbPTM
GRR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRR1_YEAST
UniProt AC P24814
Protein Name SCF E3 ubiquitin ligase complex F-box protein GRR1
Gene Name GRR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1151
Subcellular Localization Membrane . Associated with the particulate fraction. Probably forms a complex by protein-protein interactions via its leucine-rich segment.
Protein Description Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. Probably constitutes the primary response element required for the generation or interpretation of the signal that induces glucose repression..
Protein Sequence MDQDNNNHNDSNRLHPPDIHPNLGPQLWLNSSGDFDDNNNNNNNNNNNNSTRPQMPSRTRETATSERNASEVRDATLNNIFRFDSIQRETLLPTNNGQPLNQNFSLTFQPQQQTNALNGIDINTVNTNLMNGVNVQIDQLNRLLPNLPEEERKQIHEFKLIVGKKIQEFLVVIEKRRKKILNEIELDNLKLKELRIDNSPQAISYLHKLQRMRLRALETENMEIRNLRLKILTIIEEYKKSLYAYCHSKLRGQQVENPTDNFIIWINSIDTTESSDLKEGLQDLSRYSRQFINNVLSNPSNQNICTSVTRRSPVFALNMLPSEILHLILDKLNQKYDIVKFLTVSKLWAEIIVKILYYRPHINKKSQLDLFLRTMKLTSEETVFNYRLMIKRLNFSFVGDYMHDTELNYFVGCKNLERLTLVFCKHITSVPISAVLRGCKFLQSVDITGIRDVSDDVFDTLATYCPRVQGFYVPQARNVTFDSLRNFIVHSPMLKRIKITANNNMNDELVELLANKCPLLVEVDITLSPNVTDSSLLKLLTRLVQLREFRITHNTNITDNLFQELSKVVDDMPSLRLIDLSGCENITDKTIESIVNLAPKLRNVFLGKCSRITDASLFQLSKLGKNLQTVHFGHCFNITDNGVRALFHSCTRIQYVDFACCTNLTNRTLYELADLPKLKRIGLVKCTQMTDEGLLNMVSLRGRNDTLERVHLSYCSNLTIYPIYELLMSCPRLSHLSLTAVPSFLRPDITMYCRPAPSDFSENQRQIFCVFSGKGVHKLRHYLVNLTSPAFGPHVDVNDVLTKYIRSKNLIFNGETLEDALRRIITDLNQDSAAIIAATGLNQINGLNNDFLFQNINFERIDEVFSWYLNTFDGIRMSSEEVNSLLLQVNKTFCEDPFSDVDDDQDYVVAPGVNREINSEMCHIVRKFHELNDHIDDFEVNVASLVRVQFQFTGFLLHEMTQTYMQMIELNRQICLVQKTVQESGNIDYQKGLLIWRLLFIDKFIMVVQKYKLSTVVLRLYLKDNITLLTRQRELLIAHQRSAWNNNNDNDANRNANNIVNIVSDAGANDTSNNETNNGNDDNETENPNFWRQFGNRMQISPDQMRNLQMGLRNQNMVRNNNNNTIDESMPDTAIDSQMDEASGTPDEDML
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
65PhosphorylationRTRETATSERNASEV
CCCCCCCCCCCHHHH		31.9028889911
70PhosphorylationATSERNASEVRDATL
CCCCCCHHHHHHHHH		39.9323749301
76PhosphorylationASEVRDATLNNIFRF
HHHHHHHHHHHCCCC		34.0228889911
153UbiquitinationNLPEEERKQIHEFKL
CCCHHHHHCHHCHHH		57.8117644757
164UbiquitinationEFKLIVGKKIQEFLV
CHHHHHCHHHHHHHH		35.4917644757
165UbiquitinationFKLIVGKKIQEFLVV
HHHHHCHHHHHHHHH		43.6317644757
175UbiquitinationEFLVVIEKRRKKILN
HHHHHHHHHHHHHHH		46.5117644757
179UbiquitinationVIEKRRKKILNEIEL
HHHHHHHHHHHHHCC		51.0917644757
190UbiquitinationEIELDNLKLKELRID
HHCCCCCEECCCCCC		64.8617644757
199PhosphorylationKELRIDNSPQAISYL
CCCCCCCCHHHHHHH		18.0325533186
204PhosphorylationDNSPQAISYLHKLQR
CCCHHHHHHHHHHHH		25.3429688323
205PhosphorylationNSPQAISYLHKLQRM
CCHHHHHHHHHHHHH		13.5029688323
208UbiquitinationQAISYLHKLQRMRLR
HHHHHHHHHHHHHHH		43.6624961812
230UbiquitinationEIRNLRLKILTIIEE
HHHHHHHHHHHHHHH		29.2724961812
285PhosphorylationKEGLQDLSRYSRQFI
HHHHHHHHHHHHHHH		37.1528889911
300PhosphorylationNNVLSNPSNQNICTS
HHHHCCCCCCCCCCC		56.1323749301
552PhosphorylationQLREFRITHNTNITD
HHHHHHCCCCCCCCH		12.5728132839
558PhosphorylationITHNTNITDNLFQEL
CCCCCCCCHHHHHHH		22.3928132839
567UbiquitinationNLFQELSKVVDDMPS
HHHHHHHHHHCCCCC		59.9223749301
590PhosphorylationCENITDKTIESIVNL
CCCCCHHHHHHHHHH		32.5524930733
593PhosphorylationITDKTIESIVNLAPK
CCHHHHHHHHHHHHH		28.1724930733
622UbiquitinationASLFQLSKLGKNLQT
HHHHHHHHHCCCCCE		70.6123749301
803UbiquitinationDVNDVLTKYIRSKNL
CHHHHHHHHHHHCCC		34.2217644757
878PhosphorylationTFDGIRMSSEEVNSL
CCCCCCCCHHHHHHH		25.4228132839
884PhosphorylationMSSEEVNSLLLQVNK
CCHHHHHHHHHHHCC		26.1028132839
892PhosphorylationLLLQVNKTFCEDPFS
HHHHHCCHHCCCCCC		28.4527214570
899PhosphorylationTFCEDPFSDVDDDQD
HHCCCCCCCCCCCCC		41.9521440633
1011PhosphorylationFIMVVQKYKLSTVVL
HHHHHHHHCCHHHHH		10.4828132839
1021PhosphorylationSTVVLRLYLKDNITL
HHHHHHHHHHCCEEE		12.7928132839
1027PhosphorylationLYLKDNITLLTRQRE
HHHHCCEEEHHHHHH		23.2127017623
1101PhosphorylationFGNRMQISPDQMRNL
HHHCCCCCHHHHHHH		12.9225752575
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
-KUbiquitinationE3 ubiquitin ligaseGRR1P24814
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRR1_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 GRR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC53_YEASTCDC53physical
11805837
SKP1_YEASTSKP1physical
11805837
COFI_YEASTCOF1physical
11805837
VDAC1_YEASTPOR1physical
11805837
GCH1_YEASTFOL2physical
11805837
H2B2_YEASTHTB2physical
11805837
PFKA1_YEASTPFK1physical
11805837
CYPH_YEASTCPR1physical
11805837
PDC6_YEASTPDC6physical
11805837
SAHH_YEASTSAH1physical
11805837
UBI4P_YEASTUBI4physical
11805837
PDC5_YEASTPDC5physical
11805837
CDC53_YEASTCDC53physical
11259599
CG12_YEASTCLN2physical
11259599
SKP1_YEASTSKP1physical
11259599
CDC53_YEASTCDC53physical
10213692
CDC53_YEASTCDC53physical
9346238
RBX1_YEASTHRT1physical
10213692
SKP1_YEASTSKP1physical
10213692
SKP1_YEASTSKP1physical
9346238
CDC53_YEASTCDC53physical
9499404
SKP1_YEASTSKP1physical
9312022
CG12_YEASTCLN2physical
9819356
RBX1_YEASTHRT1physical
10880467
CG12_YEASTCLN2physical
10582239
CDC53_YEASTCDC53physical
10582239
SKP1_YEASTSKP1physical
10582239
SKP1_YEASTSKP1physical
10430906
CG12_YEASTCLN2physical
15200949
MTH1_YEASTMTH1physical
15456873
GIS4_YEASTGIS4physical
15890364
REG1_YEASTREG1physical
15849787
BMH2_YEASTBMH2physical
15849787
FZF1_YEASTFZF1genetic
9294463
FZF1_YEASTFZF1genetic
8889516
HXT1_YEASTHXT1genetic
7982576
HXT2_YEASTHXT2genetic
7982576
HXT3_YEASTHXT3genetic
7982576
HXT4_YEASTHXT4genetic
7982576
REG1_YEASTREG1genetic
10821175
SKP1_YEASTSKP1genetic
9491072
SKS1_YEASTSKS1genetic
8948096
SSU1_YEASTSSU1genetic
9294463
RBX1_YEASTHRT1genetic
10880467
SNF3_YEASTSNF3genetic
8013905
2ABA_YEASTCDC55genetic
7962097
CG11_YEASTCLN1genetic
11259599
CG12_YEASTCLN2genetic
11259599
RSR1_YEASTRSR1genetic
12221111
RGT1_YEASTRGT1genetic
8889516
RGT1_YEASTRGT1genetic
8013904
RGT1_YEASTRGT1genetic
7862149
CDC12_YEASTCDC12genetic
7498768
PLP1_YEASTPLP1genetic
14573467
TBA3_YEASTTUB3genetic
14573467
SSY5_YEASTSSY5genetic
15509782
GIS4_YEASTGIS4genetic
15890364
CG11_YEASTCLN1genetic
15942932
CG12_YEASTCLN2genetic
15942932
MKS1_YEASTMKS1physical
16093347
RGT1_YEASTRGT1genetic
8013905
6P22_YEASTPFK27physical
17828247
TYE7_YEASTTYE7physical
17828247
CG12_YEASTCLN2physical
18787112
SKP1A_ARATHSKP1physical
12008900
SKP1B_ARATHASK2physical
12008900
NPR2_YEASTNPR2genetic
20154027
NPR2_YEASTNPR2physical
20154027
CDC53_YEASTCDC53physical
20489023
EI2BE_YEASTGCD6physical
20489023
SKP1_YEASTSKP1physical
20489023
STP1_YEASTSTP1physical
21127045
STP2_YEASTSTP2physical
21127045
CDC4_YEASTCDC4genetic
22844257
YIT6_YEASTYIR016Wphysical
23144720
PRP3_YEASTPRP3physical
23144720
CSN10_YEASTRRI2physical
23144720
FOB1_YEASTFOB1physical
23144720
DSE3_YEASTDSE3physical
23144720
6P22_YEASTPFK27physical
23144720
GIC2_YEASTGIC2physical
23144720
SHE3_YEASTSHE3physical
23144720
PP2A1_YEASTPPH21genetic
23518505
PP2A2_YEASTPPH22genetic
23518505
CG11_YEASTCLN1genetic
23518505
CG12_YEASTCLN2genetic
23518505
SNF1_YEASTSNF1genetic
1922034
TRPF_YEASTTRP1genetic
1922034
TYR1_YEASTTYR1genetic
1922034
CHMU_YEASTARO7genetic
1922034
6P22_YEASTPFK27physical
24389104
BUD4_YEASTBUD4physical
24389104
FIR1_YEASTFIR1physical
24389104
GAC1_YEASTGAC1physical
24389104
SBE2_YEASTSBE2physical
24389104
SFG1_YEASTSFG1physical
24389104
CTH2_YEASTTIS11physical
24389104
YHT1_YEASTYHR131Cphysical
24389104
YK25_YEASTYKR045Cphysical
24389104
YNO4_YEASTYNL144Cphysical
24389104
CG11_YEASTCLN1physical
24389104
CG12_YEASTCLN2physical
24389104
GIC2_YEASTGIC2physical
24389104
MTH1_YEASTMTH1physical
24389104
TYE7_YEASTTYE7physical
24389104
CG11_YEASTCLN1physical
9346238
CDK1_YEASTCDC28physical
9346238
FBW1A_HUMANBTRCphysical
10213692
CG11_YEASTCLN1physical
10213692
MED3_YEASTPGD1physical
24550274
CG12_YEASTCLN2physical
10579999
SSY5_YEASTSSY5genetic
21653827
CG13_YEASTCLN3genetic
22844257
CG13_YEASTCLN3physical
22844257
CG12_YEASTCLN2physical
22844257
CG11_YEASTCLN1physical
22844257
SSY5_YEASTSSY5physical
21653827
NDD1_YEASTNDD1physical
25894965
CG12_YEASTCLN2physical
25619768
SSN2_YEASTSSN2physical
29212878
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRR1_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-199 AND SER-300, ANDMASS 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-199, AND MASSSPECTROMETRY.

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