KEL2_YEAST - dbPTM
KEL2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KEL2_YEAST
UniProt AC P50090
Protein Name Kelch repeat-containing protein 2
Gene Name KEL2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 882
Subcellular Localization
Protein Description
Protein Sequence MVPFKLTNKVPTDTGPSLISAQSVPRPIVFMDNRNNTRIVTPTLPPNQHRGISGASTALPWSPESKNTGKYIWNRVKLKNSPFPRYRHSSSFIVTNDNRIFVTGGLHDQSVYGDVWQIAANADGTSFTSKRIDIDQNTPPPRVGHASTICGNAYVVFGGDTHKLNKNGLLDDDLYLFNINSYKWTIPQPIGRRPLGRYGHKISIIASNPMQTKLYLFGGQVDETYFNDLVVFDLSSFRRPNSHWEFLEPVGDLPPPLTNHTMVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKVKTTGEKPPPIQEHASVVYKHLMCVLGGKDTHNAYSNDVYFLNLLSLKWYKLPRMKEGIPQERSGHSLTLMKNEKLLIMGGDKTDYASPNIHDLQTSETDQGEGTLLYTLDLSSLNELCPGIMCESLHAGESFSNSLSGGFTPSKSTESENQEIINILTPRLPDSKVLSYNDIDEGAGSYSSALDDKAFERKSDREEKKPQSSKVDSSINKESPGTGIKVSKKNFPVLRGLTVDSEEYGSSSYKDTSCQKGIPKNLFDDLNLNLQTLRLEAQQKELETARHISQLEKEVQRLMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQITIQNNGLKTCSEHVTIKRDIIDLENKCDVLKRQNEILVNNMQKITPELHTYLNESSCYLGKLLKSYPTSARPPSSEKDNQIYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQRGAITHGNFDAFHRMKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQKK
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
41PhosphorylationRNNTRIVTPTLPPNQ
CCCEEEECCCCCCCC		14.2623749301
62PhosphorylationASTALPWSPESKNTG
CCCCCCCCCCCCCCC		19.4928152593
445PhosphorylationTPSKSTESENQEIIN
CCCCCCCCHHHHHHH		41.7721440633
455PhosphorylationQEIINILTPRLPDSK
HHHHHHHCCCCCCCC		11.5422369663
461PhosphorylationLTPRLPDSKVLSYND
HCCCCCCCCCCCCCC		23.7922369663
465PhosphorylationLPDSKVLSYNDIDEG
CCCCCCCCCCCCCCC		25.5222369663
466PhosphorylationPDSKVLSYNDIDEGA
CCCCCCCCCCCCCCC		16.8228889911
475PhosphorylationDIDEGAGSYSSALDD
CCCCCCCCCCHHHCH		22.7022369663
476PhosphorylationIDEGAGSYSSALDDK
CCCCCCCCCHHHCHH		13.0123749301
477PhosphorylationDEGAGSYSSALDDKA
CCCCCCCCHHHCHHH		15.7220377248
478PhosphorylationEGAGSYSSALDDKAF
CCCCCCCHHHCHHHH		25.3122369663
503PhosphorylationPQSSKVDSSINKESP
CCCCCCCCCCCCCCC		35.7822369663
504PhosphorylationQSSKVDSSINKESPG
CCCCCCCCCCCCCCC		26.2222369663
509PhosphorylationDSSINKESPGTGIKV
CCCCCCCCCCCCCEE		30.1822369663
512PhosphorylationINKESPGTGIKVSKK
CCCCCCCCCCEECCC		38.8327214570
528PhosphorylationFPVLRGLTVDSEEYG
CCEEECEEECCHHHC		25.7022369663
531PhosphorylationLRGLTVDSEEYGSSS
EECEEECCHHHCCCC		28.1722369663
534PhosphorylationLTVDSEEYGSSSYKD
EEECCHHHCCCCCCC		20.4624961812
536PhosphorylationVDSEEYGSSSYKDTS
ECCHHHCCCCCCCCC		18.4024961812
537PhosphorylationDSEEYGSSSYKDTSC
CCHHHCCCCCCCCCC		33.0724961812
538PhosphorylationSEEYGSSSYKDTSCQ
CHHHCCCCCCCCCCC		37.5924961812
714PhosphorylationPTSARPPSSEKDNQI
CCCCCCCCCHHHCCH		54.5428889911
751PhosphorylationKEKLHLETQKLNDER
HHHHHHHHHHCHHHH		37.0527017623
782PhosphorylationLRKLSDGSSKSMDLT
HHHHCCCCCHHHHHH		39.3121440633
796PhosphorylationTKKAIHLSQSELEKY
HHHHHHCCHHHHHHH		19.9322369663
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 KEL2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KEL2_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 KEL2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LTE1_YEASTLTE1physical
12234925
TEM1_YEASTTEM1physical
12234925
KEL1_YEASTKEL1physical
18467557
KEL1_YEASTKEL1physical
18719252
KEL1_YEASTKEL1physical
22615397
HOS4_YEASTHOS4physical
22875988
NNF1_YEASTNNF1physical
22875988
NST1_YEASTNST1physical
22875988
NCA2_YEASTNCA2physical
22875988
KIN3_YEASTKIN3physical
22875988
KEL1_YEASTKEL1physical
22875988
NOT3_YEASTNOT3physical
22875988
NUF2_YEASTNUF2physical
22875988
KEL1_YEASTKEL1physical
24828508
BUD14_YEASTBUD14physical
24828508
ATP10_YEASTATP10genetic
27708008
IRA2_YEASTIRA2genetic
27708008
SEC66_YEASTSEC66genetic
27708008
HPC2_YEASTHPC2genetic
27708008
SWC5_YEASTSWC5genetic
27708008
CHK1_YEASTCHK1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
TPS2_YEASTTPS2genetic
27708008
RPA14_YEASTRPA14genetic
27708008
H2A1_YEASTHTA1genetic
27708008
PMP3_YEASTPMP3genetic
27708008
CEM1_YEASTCEM1genetic
27708008
UBP3_YEASTUBP3genetic
27708008
RAD4_YEASTRAD4genetic
27708008
BUD27_YEASTBUD27genetic
27708008
PALF_YEASTRIM8genetic
27708008
PRM8_YEASTPRM8genetic
27708008
AAKG_YEASTSNF4genetic
27708008
NPR3_YEASTNPR3genetic
27708008
RNP1_YEASTRNP1genetic
27708008
SRN2_YEASTSRN2genetic
27708008
COA4_YEASTCOA4genetic
27708008
LIPB_YEASTLIP2genetic
27708008
CHS5_YEASTCHS5genetic
27708008
PHO84_YEASTPHO84genetic
27708008
MAC1_YEASTMAC1genetic
27708008
UBX4_YEASTUBX4genetic
27708008
LSM7_YEASTLSM7genetic
27708008
PP2A4_YEASTPPG1genetic
27708008
BRE5_YEASTBRE5genetic
27708008
TOP1_YEASTTOP1genetic
27708008
TAT2_YEASTTAT2genetic
27708008
NOP12_YEASTNOP12genetic
27708008
GSHB_YEASTGSH2genetic
27708008
RRP6_YEASTRRP6genetic
27708008
YO012_YEASTYOR012Wgenetic
27708008
CY1_YEASTCYT1genetic
27708008
ATX2_YEASTATX2genetic
27708008
VAM3_YEASTVAM3genetic
27708008
INP53_YEASTINP53genetic
27708008
SLP1_YEASTSLP1genetic
27708008
LGE1_YEASTLGE1genetic
27708008
CSR2_YEASTCSR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KEL2_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 THR-455; SER-465 ANDSER-509, AND MASS SPECTROMETRY.

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