KEL3_YEAST - dbPTM
KEL3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KEL3_YEAST
UniProt AC Q08979
Protein Name Kelch repeat-containing protein 3
Gene Name KEL3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 651
Subcellular Localization
Protein Description
Protein Sequence MAKKNKKDKEAKKARAELKNQKNQKKQEKKFQKNKNKSLNGEEDDESDQDLDEILSSFSKKQIELEHVDITSVEKPSCRTHPLMFANPQHNKHELFIFGGEFTDPETKLTHFYNDLYSYSIKNNSWKKYVSQNAPLPRSSAAVAVHPSGIALLHGGEFSSPKQSKFYHYSDTWLFDCVERKFTKLEFGGRDSSPSARSGHRIIAWKNYFILFGGFRDLGNGQTSYLNDLWCFDISTYKWTKLETNSKPDARSGHCFIPTDNSAILMGGYCKIIAKNNKNLMKGKILNDAWKLNLTPDPKKWQWEKLKNFKNQPSPRVGYSFNLWKQNKSVAFGGVYDLQETEESLESVFYNDLYMFHLELNKWSKLRIKPQRQTNSKNSPATSKRKSNKDQEKELQDLLNSILAKSNLNDDDDDNDDNSTTGPNSIDDDEDNEDDSDLDNQEDITISNQLPHPRFNAATCVVGDSLFIYSGVWELGEKDYPINSFYSIDLNKLDGVKVYWEDLSAIEEAKRLGDRDSDEDEFEYEDDEEDEDDGEEEQDAGPLEGDEDEESESDDDKQAQMEIPDERSWLPHPKPFETLRAFYLREGANFLTWSISNNRNLKGKQLKTKSFELCEDRWWERRDQVTLEEERLEDTGGIIERDTTTKPSKRR
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
38PhosphorylationFQKNKNKSLNGEEDD
HHHHHCCCCCCCCCC		36.1422369663
47PhosphorylationNGEEDDESDQDLDEI
CCCCCCCCHHCHHHH		47.7922369663
56PhosphorylationQDLDEILSSFSKKQI
HCHHHHHHHHCCCCE		34.6921440633
57PhosphorylationDLDEILSSFSKKQIE
CHHHHHHHHCCCCEE		30.0521440633
59PhosphorylationDEILSSFSKKQIELE
HHHHHHHCCCCEEEE		40.6719823750
167PhosphorylationSPKQSKFYHYSDTWL
CCCCCCEEECCCCCH		12.0026447709
169PhosphorylationKQSKFYHYSDTWLFD
CCCCEEECCCCCHHH		9.2526447709
170PhosphorylationQSKFYHYSDTWLFDC
CCCEEECCCCCHHHH		18.4326447709
172PhosphorylationKFYHYSDTWLFDCVE
CEEECCCCCHHHHHC		20.3726447709
374PhosphorylationRIKPQRQTNSKNSPA
CCCCCCCCCCCCCCC		43.5828889911
376PhosphorylationKPQRQTNSKNSPATS
CCCCCCCCCCCCCHH		36.2828889911
379PhosphorylationRQTNSKNSPATSKRK
CCCCCCCCCCHHHCC		21.4628889911
382PhosphorylationNSKNSPATSKRKSNK
CCCCCCCHHHCCCCH		37.8628889911
420PhosphorylationDDNDDNSTTGPNSID
CCCCCCCCCCCCCCC		41.8629734811
425PhosphorylationNSTTGPNSIDDDEDN
CCCCCCCCCCCCCCC		30.4427738172
436PhosphorylationDEDNEDDSDLDNQED
CCCCCCCCCCCCHHC		53.0128889911
499PhosphorylationKLDGVKVYWEDLSAI
HCCCEEEEHHHHHHH		9.4328889911
517PhosphorylationKRLGDRDSDEDEFEY
HHHCCCCCCCCCCCC		43.7419823750
524PhosphorylationSDEDEFEYEDDEEDE
CCCCCCCCCCCCCCC		29.9419823750
551PhosphorylationEGDEDEESESDDDKQ
CCCCCCCCCCCCHHH		40.1119823750
553PhosphorylationDEDEESESDDDKQAQ
CCCCCCCCCCHHHHH		56.4719823750
574AcetylationRSWLPHPKPFETLRA
CCCCCCCCCHHHHHH		60.3424489116
608PhosphorylationLKGKQLKTKSFELCE
CCCCCCCCCCCHHHH		40.2830377154
610PhosphorylationGKQLKTKSFELCEDR
CCCCCCCCCHHHHHH		29.2330377154
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 KEL3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KEL3_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 KEL3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KEL3_YEASTKEL3physical
14759368
PABP_YEASTPAB1physical
14759368
NOP3_YEASTNPL3physical
14759368
YRO2_YEASTYRO2physical
16554755
DYHC_YEASTDYN1physical
16554755
IPYR_YEASTIPP1genetic
27708008
CDK1_YEASTCDC28genetic
27708008
APC11_YEASTAPC11genetic
27708008
TECR_YEASTTSC13genetic
27708008
TAF12_YEASTTAF12genetic
27708008
MOB2_YEASTMOB2genetic
27708008
CDC20_YEASTCDC20genetic
27708008
SWC4_YEASTSWC4genetic
27708008
PRP18_YEASTPRP18genetic
27708008
SYMC_YEASTMES1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
MET30_YEASTMET30genetic
27708008
SHQ1_YEASTSHQ1genetic
27708008
SEC24_YEASTSEC24genetic
27708008
NU159_YEASTNUP159genetic
27708008
RHO3_YEASTRHO3genetic
27708008
NDC80_YEASTNDC80genetic
27708008
SLN1_YEASTSLN1genetic
27708008
MCM10_YEASTMCM10genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
FIP1_YEASTFIP1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAD3_YEASTTAD3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KEL3_YEAST

loading...

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-47 AND SER-436, AND MASSSPECTROMETRY.
"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-47, AND MASSSPECTROMETRY.
"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-47, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory