YOX1_YEAST - dbPTM
YOX1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YOX1_YEAST
UniProt AC P34161
Protein Name Homeobox protein YOX1
Gene Name YOX1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 385
Subcellular Localization Nucleus.
Protein Description Transcriptional repressor required to restrict transcription of ECB-dependent genes to the G1/M phase by repressing their transcription during the interval from late G1 to M phases. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. In vitro, is capable of binding to the DNA of the leucine tRNA gene..
Protein Sequence MSQETKMLPSLSSLLSGTEISSSPVSPSFTNPRTSFHLDDRGTIKLPPLNTSINRPRSVESALRHTVTSLHENSSAYGDDMLKHTQSDSALSSQLNSSQETVDESHENLLLTPLNSKKRDYSVSSKKNDILTPLSAAKSIIIPSASKEKRRAFAFITHSQETFPKKEPKIDNAPLARRKRRRTSSQELSILQAEFEKCPAPSKEKRIELAESCHMTEKAVQIWFQNKRQAVKRQRIATSKSTTIIQTVSPPSPPLDVHATPLASRVKADILRDGSSCSRSSSSSPLENTPPRPHHSLNRRSSTPSIKRSQALTFHLNPQKKTLTPVKTSPNSRVNKLINSIDHSPSKAKRPVSNPSGSPKRKRKFGFKIVDQQPLKDLDPNAFRG
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
34PhosphorylationPSFTNPRTSFHLDDR
CCCCCCCCCEECCCC		36.6830377154
35PhosphorylationSFTNPRTSFHLDDRG
CCCCCCCCEECCCCC		16.3723749301
58PhosphorylationTSINRPRSVESALRH
CCCCCCCHHHHHHHH		32.6825752575
61PhosphorylationNRPRSVESALRHTVT
CCCCHHHHHHHHHHH		30.3730377154
85PhosphorylationGDDMLKHTQSDSALS
CCCHHHHCCCHHHHH		28.3422369663
87PhosphorylationDMLKHTQSDSALSSQ
CHHHHCCCHHHHHHH		34.3921440633
89PhosphorylationLKHTQSDSALSSQLN
HHHCCCHHHHHHHHC		36.0322369663
92PhosphorylationTQSDSALSSQLNSSQ
CCCHHHHHHHHCCCC		18.7622369663
93PhosphorylationQSDSALSSQLNSSQE
CCHHHHHHHHCCCCC		39.2722369663
97PhosphorylationALSSQLNSSQETVDE
HHHHHHCCCCCCCCH		41.8322369663
98PhosphorylationLSSQLNSSQETVDES
HHHHHCCCCCCCCHH		30.8424961812
101PhosphorylationQLNSSQETVDESHEN
HHCCCCCCCCHHHHC		26.1424961812
105PhosphorylationSQETVDESHENLLLT
CCCCCCHHHHCCEEC		31.4724961812
112PhosphorylationSHENLLLTPLNSKKR
HHHCCEECCCCCCCC		26.2124961812
116PhosphorylationLLLTPLNSKKRDYSV
CEECCCCCCCCCCCC		47.4322369663
132PhosphorylationSKKNDILTPLSAAKS
CCCCCCCCHHHHCCE		23.6321440633
135PhosphorylationNDILTPLSAAKSIII
CCCCCHHHHCCEEEC		27.6421440633
144PhosphorylationAKSIIIPSASKEKRR
CCEEECCCCCHHHHH		34.4621440633
241PhosphorylationQRIATSKSTTIIQTV
HHHCCCCCCEEEEEC		30.4729688323
242PhosphorylationRIATSKSTTIIQTVS
HHCCCCCCEEEEECC		26.2529688323
243PhosphorylationIATSKSTTIIQTVSP
HCCCCCCEEEEECCC		24.1529688323
249PhosphorylationTTIIQTVSPPSPPLD
CEEEEECCCCCCCCC		34.1821551504
252PhosphorylationIQTVSPPSPPLDVHA
EEECCCCCCCCCCCC		42.4020377248
260PhosphorylationPPLDVHATPLASRVK
CCCCCCCCCHHHHHH		12.1721440633
264PhosphorylationVHATPLASRVKADIL
CCCCCHHHHHHHHHH		45.3429688323
289PhosphorylationSSSPLENTPPRPHHS
CCCCCCCCCCCCCCC		25.8728889911
302PhosphorylationHSLNRRSSTPSIKRS
CCCCCCCCCCCCCHH		42.3928889911
303PhosphorylationSLNRRSSTPSIKRSQ
CCCCCCCCCCCCHHH		23.4628889911
305PhosphorylationNRRSSTPSIKRSQAL
CCCCCCCCCCHHHCE		40.6128889911
309PhosphorylationSTPSIKRSQALTFHL
CCCCCCHHHCEEEEE		18.1423607784
322PhosphorylationHLNPQKKTLTPVKTS
EECCCCCCCCCCCCC		42.7922369663
324PhosphorylationNPQKKTLTPVKTSPN
CCCCCCCCCCCCCCC		31.1322369663
328PhosphorylationKTLTPVKTSPNSRVN
CCCCCCCCCCCHHHH		50.0422369663
329PhosphorylationTLTPVKTSPNSRVNK
CCCCCCCCCCHHHHH		19.1622369663
332PhosphorylationPVKTSPNSRVNKLIN
CCCCCCCHHHHHHHH		40.7820377248
336AcetylationSPNSRVNKLINSIDH
CCCHHHHHHHHHCCC		48.1424489116
340PhosphorylationRVNKLINSIDHSPSK
HHHHHHHHCCCCCCC		23.5428889911
344PhosphorylationLINSIDHSPSKAKRP
HHHHCCCCCCCCCCC		27.4122369663
346PhosphorylationNSIDHSPSKAKRPVS
HHCCCCCCCCCCCCC		48.5422369663
353PhosphorylationSKAKRPVSNPSGSPK
CCCCCCCCCCCCCCC		45.7819823750
356PhosphorylationKRPVSNPSGSPKRKR
CCCCCCCCCCCCHHC		57.0421551504
358PhosphorylationPVSNPSGSPKRKRKF
CCCCCCCCCCHHCCC		31.4219823750
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 YOX1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YOX1_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 YOX1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BUB1_YEASTBUB1genetic
20959818
STB4_YEASTSTB4genetic
20959818
AFT1_YEASTAFT1genetic
20959818
IES3_YEASTIES3genetic
20959818
MET18_YEASTMET18genetic
21127252
CHA4_YEASTCHA4genetic
21127252
UPC2_YEASTUPC2genetic
21127252
KCS1_YEASTKCS1genetic
21127252
BCK2_YEASTBCK2genetic
23675312
2A5D_YEASTRTS1genetic
24493588
MED14_YEASTRGR1genetic
27708008
APC11_YEASTAPC11genetic
27708008
CDC53_YEASTCDC53genetic
27708008
UBC3_YEASTCDC34genetic
27708008
GPI11_YEASTGPI11genetic
27708008
RPN11_YEASTRPN11genetic
27708008
MED6_YEASTMED6genetic
27708008
SEC22_YEASTSEC22genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
SLX5_YEASTSLX5genetic
27708008
MTU1_YEASTSLM3genetic
27708008
OCA2_YEASTOCA2genetic
27708008
DIA2_YEASTDIA2genetic
27708008
SUCA_YEASTLSC1genetic
27708008
SPEE_YEASTSPE3genetic
27708008
CGS5_YEASTCLB5genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YOX1_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-358, AND MASSSPECTROMETRY.

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