BYE1_YEAST - dbPTM
BYE1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BYE1_YEAST
UniProt AC P36106
Protein Name Transcription factor BYE1
Gene Name BYE1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 594
Subcellular Localization Nucleus .
Protein Description Negative regulator of transcription elongation..
Protein Sequence MSVRTSSRSNKGQNKYIEYLLQEETEAPKKKRTKKKVDSAIEKNKKSDSSQEPRKDTENVRTDEVDEADEGYVRCLCGANNENYDAAEYSHGDMVQCDGCDTWQHIKCMTDGKDTIDGLMSEDSKYYCELCDPSLYAHLETSKEAEVSEDEDYHDDVYKPVNDHDDNDADVFLDEESPRKRKRSPDSAKGIHIKSKQVKKSNGSKKRNKSIDAAKSDTAENEMPTRKDFESEKEHKLRYNAEKMFSTLFSKFIVPETIEAKLYELPDGKDVISISQEFAHNLEEELYKACLNVEFGTLDKIYTEKVRSLYSNLKDKKNLELKAHVVEGKLPLNKLVNMNASELANPDLQEFKEKRDKIILENFIVEVPDKPMYVKTHKGDELIEDIAEPQEDILYSKDSIRLHNIDSIDSDKSKIEQTHAISKEPSPSTIINEESLNCAFLYPGLGLEFTGYLNYIGASQKLRRDIFKEAIGDGKLYVEGRLPTTTAAPYLKEISCSRAILVYQLFPSNDSESKTTFADVVDSLENKGRIAGIKPKTRYEKDFYIVPSKGGEIPEILKDILGSHNDERSERFSRMKSDERTLFAFVVVKQEFIH
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
2Phosphorylation------MSVRTSSRS
------CCCCCCCCC
21.9519823750
5Phosphorylation---MSVRTSSRSNKG
---CCCCCCCCCCCC
28.9719823750
6Phosphorylation--MSVRTSSRSNKGQ
--CCCCCCCCCCCCH
17.1219823750
7Phosphorylation-MSVRTSSRSNKGQN
-CCCCCCCCCCCCHH
38.8319823750
9PhosphorylationSVRTSSRSNKGQNKY
CCCCCCCCCCCHHHH
44.8619823750
15AcetylationRSNKGQNKYIEYLLQ
CCCCCHHHHHHHHHH
39.4524489116
50PhosphorylationKNKKSDSSQEPRKDT
HCCCCCCCCCCCCCC
43.4827214570
62PhosphorylationKDTENVRTDEVDEAD
CCCCCCCCCCCCCCC
32.0328889911
124PhosphorylationDGLMSEDSKYYCELC
CHHCCCCCCEEHHHC
20.6419779198
134PhosphorylationYCELCDPSLYAHLET
EHHHCCHHHHHHHHC
22.2919823750
136PhosphorylationELCDPSLYAHLETSK
HHCCHHHHHHHHCCC
9.0519823750
141PhosphorylationSLYAHLETSKEAEVS
HHHHHHHCCCCCCCC
52.0019823750
142PhosphorylationLYAHLETSKEAEVSE
HHHHHHCCCCCCCCC
21.0819823750
148PhosphorylationTSKEAEVSEDEDYHD
CCCCCCCCCCCCCCC
30.7329136822
153PhosphorylationEVSEDEDYHDDVYKP
CCCCCCCCCCCCCCC
12.7128132839
158PhosphorylationEDYHDDVYKPVNDHD
CCCCCCCCCCCCCCC
19.3019779198
177PhosphorylationDVFLDEESPRKRKRS
CCCCCCCCCCCCCCC
28.1429136822
189AcetylationKRSPDSAKGIHIKSK
CCCCCCCCCCCCCCH
63.4525381059
209AcetylationNGSKKRNKSIDAAKS
CCCCCCCCCCCHHHC
53.4725381059
210PhosphorylationGSKKRNKSIDAAKSD
CCCCCCCCCCHHHCC
29.2925752575
216PhosphorylationKSIDAAKSDTAENEM
CCCCHHHCCCCCCCC
35.1529136822
218PhosphorylationIDAAKSDTAENEMPT
CCHHHCCCCCCCCCC
42.8527717283
399PhosphorylationDILYSKDSIRLHNID
HHCCCCCCEEEECCC
17.2219823750
407PhosphorylationIRLHNIDSIDSDKSK
EEEECCCCCCCCHHH
25.2119823750
410PhosphorylationHNIDSIDSDKSKIEQ
ECCCCCCCCHHHHHH
45.3119823750
418PhosphorylationDKSKIEQTHAISKEP
CHHHHHHHHCCCCCC
10.6519823750
422PhosphorylationIEQTHAISKEPSPST
HHHHHCCCCCCCCCC
31.5822369663
569PhosphorylationGSHNDERSERFSRMK
CCCCHHHHHHHHHCC
30.9527017623

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 BYE1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BYE1_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 BYE1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIF1_YEASTRIF1physical
16554755
RAD4_YEASTRAD4physical
16554755
H3_YEASTHHT1physical
17142463
SODC_YEASTSOD1genetic
20959818
SET3_YEASTSET3genetic
20959818
RPB1_YEASTRPO21physical
25029256
TFS2_YEASTDST1genetic
25029256
PAF1_YEASTPAF1genetic
24003114
THO2_YEASTTHO2genetic
24003114
SNF5_YEASTSNF5genetic
27708008
NPP1_YEASTNPP1genetic
27708008
DYL1_YEASTDYN2genetic
27708008
FAR7_YEASTFAR7genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
SLA1_YEASTSLA1genetic
27708008
VPS10_YEASTPEP1genetic
27708008
AP2A_YEASTAPL3genetic
27708008
TREB_YEASTNTH2genetic
27708008
RCR1_YEASTRCR1genetic
27708008
YBM6_YEASTYBR016Wgenetic
27708008
PP2C4_YEASTPTC4genetic
27708008
BMT2_YEASTBMT2genetic
27708008
ADH5_YEASTADH5genetic
27708008
SMP1_YEASTSMP1genetic
27708008
KTR3_YEASTKTR3genetic
27708008
EFM2_YEASTEFM2genetic
27708008
RIF1_YEASTRIF1genetic
27708008
BSD2_YEASTBSD2genetic
27708008
ATG22_YEASTATG22genetic
27708008
RV161_YEASTRVS161genetic
27708008
RHEB_YEASTRHB1genetic
27708008
YC16_YEASTYCR087C-Agenetic
27708008
NHP10_YEASTNHP10genetic
27708008
GPR1_YEASTGPR1genetic
27708008
NDH2_YEASTNDE2genetic
27708008
ATIF_YEASTINH1genetic
27708008
SNF1_YEASTSNF1genetic
27708008
PUF6_YEASTPUF6genetic
27708008
SAP1_YEASTSAP1genetic
27708008
ODPA_YEASTPDA1genetic
27708008
AAKG_YEASTSNF4genetic
27708008
ITC1_YEASTITC1genetic
27708008
RS25A_YEASTRPS25Agenetic
27708008
ASK10_YEASTASK10genetic
27708008
SPO11_YEASTSPO11genetic
27708008
RIM4_YEASTRIM4genetic
27708008
SLT2_YEASTSLT2genetic
27708008
YKE4_YEASTYKE4genetic
27708008
ICE2_YEASTICE2genetic
27708008
ASF1_YEASTASF1genetic
27708008
YJQ3_YEASTYJL163Cgenetic
27708008
SIC1_YEASTSIC1genetic
27708008
MMR1_YEASTMMR1genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
VAC14_YEASTVAC14genetic
27708008
CDC73_YEASTCDC73genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
MSC1_YEASTMSC1genetic
27708008
GBLP_YEASTASC1genetic
27708008
MRE11_YEASTMRE11genetic
27708008
YNB0_YEASTYNL010Wgenetic
27708008
RL9B_YEASTRPL9Bgenetic
27708008
LAG2_YEASTLAG2genetic
27708008
TCB1_YEASTTCB1genetic
27708008
YOR97_YEASTYOR097Cgenetic
27708008
EF1G1_YEASTCAM1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BYE1_YEAST

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Related Literatures of Post-Translational Modification

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