BIT61_YEAST - dbPTM
BIT61_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BIT61_YEAST
UniProt AC P47041
Protein Name Target of rapamycin complex 2 subunit BIT61
Gene Name BIT61
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 543
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side. Vacuole membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway..
Protein Sequence MTAEDILLRERTSTTTQRPVNSEQYLNVQLATAPVKNFQTTSEISRQTLVDTSNDDVYSIKNLKGSRNPISPSVSNVGFQSIFHTVDHPRSKVSVASNHSLRSNDNASAATSKSGSSQIGESHSVDTVECSNNLSKKLSSDAISITQKSLHSTPSGRYMKGKASGFFNRRNRAHTTISSDPASFLTDSSTLHNSSHSFRNVIKNFFQNKSHRHIGQDAIEPAIPNSLSKFLHSSYGRHKSPSQFIHTNAGQLVDSGTSVYSLNVNPSGVNPNTIVEDPLSGTDPASPNPVSMLHDLLRNLPSLEANYKHFNSQELTTLTNNIWNIFCSNVAELFRTQRIWKLRAKIENFNEVLEFYCILKTDPRVTHSGMNRIISDLKEFLVSSLYNLENQIVFNYSNEDTINNALKRLGVIWRIFYQEVYYDLAAVLLPLDQSIREDGNSTVLKSGNESRTHINGNYSIGFLLLMCFRDSIVLPCYENFVNSNDGISKSFQLYIFNQEEESNVTETDKLTLLQCFGILSTIQSNDRNQRIIEELLAGIRMSI
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
53PhosphorylationRQTLVDTSNDDVYSI
CCEEECCCCCCEEEE		33.5228889911
58PhosphorylationDTSNDDVYSIKNLKG
CCCCCCEEEEECCCC		16.2128889911
59PhosphorylationTSNDDVYSIKNLKGS
CCCCCEEEEECCCCC		27.2528152593
71PhosphorylationKGSRNPISPSVSNVG
CCCCCCCCCCHHHHC		16.6328889911
73PhosphorylationSRNPISPSVSNVGFQ
CCCCCCCCHHHHCHH		31.2424961812
75PhosphorylationNPISPSVSNVGFQSI
CCCCCCHHHHCHHHE		30.0924961812
91PhosphorylationHTVDHPRSKVSVASN
ECCCCCCCCEEHHHC		41.6928889911
97PhosphorylationRSKVSVASNHSLRSN
CCCEEHHHCCCCCCC		32.6821551504
100PhosphorylationVSVASNHSLRSNDNA
EEHHHCCCCCCCCCC		29.7221440633
103PhosphorylationASNHSLRSNDNASAA
HHCCCCCCCCCCCCC		54.5521440633
111PhosphorylationNDNASAATSKSGSSQ
CCCCCCCCCCCCCCC		36.0821440633
112PhosphorylationDNASAATSKSGSSQI
CCCCCCCCCCCCCCC		21.7920377248
117PhosphorylationATSKSGSSQIGESHS
CCCCCCCCCCCCCCC		29.3728889911
122PhosphorylationGSSQIGESHSVDTVE
CCCCCCCCCCCCEEE		18.8221440633
124PhosphorylationSQIGESHSVDTVECS
CCCCCCCCCCEEECC		30.8520377248
127PhosphorylationGESHSVDTVECSNNL
CCCCCCCEEECCCCH		18.9520377248
135PhosphorylationVECSNNLSKKLSSDA
EECCCCHHHHHHCCC		29.8427017623
139PhosphorylationNNLSKKLSSDAISIT
CCHHHHHHCCCEEEE		34.7422369663
140PhosphorylationNLSKKLSSDAISITQ
CHHHHHHCCCEEEEH		41.3122369663
144PhosphorylationKLSSDAISITQKSLH
HHHCCCEEEEHHHHC		22.7022369663
146PhosphorylationSSDAISITQKSLHST
HCCCEEEEHHHHCCC		24.1322890988
149PhosphorylationAISITQKSLHSTPSG
CEEEEHHHHCCCCCC		22.8419684113
152PhosphorylationITQKSLHSTPSGRYM
EEHHHHCCCCCCCCC		47.5121440633
153PhosphorylationTQKSLHSTPSGRYMK
EHHHHCCCCCCCCCC		15.6621440633
155PhosphorylationKSLHSTPSGRYMKGK
HHHCCCCCCCCCCCC		35.6721440633
158PhosphorylationHSTPSGRYMKGKASG
CCCCCCCCCCCCCCC		13.5024961812
176PhosphorylationRRNRAHTTISSDPAS
CCCCCCCEECCCCHH		14.7021082442
189PhosphorylationASFLTDSSTLHNSSH
HHHHCCCCCCCCCCH		37.4930377154
197PhosphorylationTLHNSSHSFRNVIKN
CCCCCCHHHHHHHHH		28.0530377154
210PhosphorylationKNFFQNKSHRHIGQD
HHHHCCCCCCCCCHH		33.0524961812
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 BIT61_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BIT61_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 BIT61_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLM2_YEASTSLM2physical
15689497
SLM1_YEASTSLM1physical
15689497
ADA2_YEASTADA2physical
18719252
DIG2_YEASTDIG2physical
18719252
MUM2_YEASTMUM2physical
18719252
URE2_YEASTURE2physical
18719252
BIT61_YEASTBIT61physical
18719252
AK_YEASTHOM3physical
18719252
ATG17_YEASTATG17physical
18719252
MDV1_YEASTMDV1physical
18719252
MND2_YEASTMND2physical
18719252
PPA3_YEASTPHO3genetic
19269370
IPYR2_YEASTPPA2genetic
19269370
CHK1_YEASTCHK1genetic
20093466
BCS1_YEASTBCS1genetic
20093466
ROG3_YEASTROG3genetic
20093466
HAP2_YEASTHAP2genetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
HUR1_YEASTHUR1genetic
20093466
ASK10_YEASTASK10genetic
20093466
PCP1_YEASTPCP1genetic
20093466
CHO2_YEASTCHO2genetic
20093466
CBT1_YEASTCBT1genetic
20093466
DCOR_YEASTSPE1genetic
20093466
NDUF7_YEASTYKL162Cgenetic
20093466
MRT4_YEASTMRT4genetic
20093466
DBP7_YEASTDBP7genetic
20093466
OSW2_YEASTOSW2genetic
20093466
CSC1_YEASTCSC1genetic
20093466
ELO3_YEASTELO3genetic
20093466
SEI1_YEASTFLD1genetic
20093466
CY1_YEASTCYT1genetic
20093466
RAD1_YEASTRAD1genetic
20093466
CHK1_YEASTCHK1genetic
22282571
CHK1_YEASTCHK1genetic
27708008
RIM1_YEASTRIM1genetic
27708008
ELO2_YEASTELO2genetic
27708008
GPR1_YEASTGPR1genetic
27708008
ROG3_YEASTROG3genetic
27708008
ASK10_YEASTASK10genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
ILM1_YEASTILM1genetic
27708008
MRT4_YEASTMRT4genetic
27708008
COXM1_YEASTCMC1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
CBT1_YEASTCBT1genetic
27708008
OSW2_YEASTOSW2genetic
27708008
ENT2_YEASTENT2genetic
27708008
ELO3_YEASTELO3genetic
27708008
AEP2_YEASTAEP2genetic
27708008
NOP12_YEASTNOP12genetic
27708008
RTC1_YEASTRTC1genetic
27708008
CY1_YEASTCYT1genetic
27708008
PDP1_YEASTPTC5genetic
27708008
SET6_YEASTSET6genetic
27708008
CEP70_HUMANCEP70physical
27107014
CCD33_HUMANCCDC33physical
27107014
SPERT_HUMANSPERTphysical
27107014
GFAP_HUMANGFAPphysical
27107014
IHO1_HUMANCCDC36physical
27107014
K1C19_HUMANKRT19physical
27107014
ATRIP_HUMANATRIPphysical
27107014
K1C15_HUMANKRT15physical
27107014
FBF1_HUMANFBF1physical
27107014
IKZF3_HUMANIKZF3physical
27107014
DYDC1_HUMANDYDC1physical
27107014
TRI27_HUMANTRIM27physical
27107014
MTUS2_HUMANMTUS2physical
27107014
DNJA3_HUMANDNAJA3physical
27107014
GOGA2_HUMANGOLGA2physical
27107014
RIM3A_HUMANRIMBP3physical
27107014
TEX11_HUMANTEX11physical
27107014
TRIP6_HUMANTRIP6physical
27107014
ADIP_HUMANSSX2IPphysical
27107014
TRIM1_HUMANMID2physical
27107014
EFHC2_HUMANEFHC2physical
27107014
PAK5_HUMANPAK7physical
27107014
TOR2_YEASTTOR2physical
29170376
AVO1_YEASTAVO1physical
29170376
AVO2_YEASTAVO2physical
29170376
TSC11_YEASTTSC11physical
29170376
HSP71_YEASTSSA1physical
29170376
HSP72_YEASTSSA2physical
29170376
SSB1_YEASTSSB1physical
29170376
SSB2_YEASTSSB2physical
29170376
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BIT61_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-100; SER-139; SER-140AND SER-144, AND MASS 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-139, AND MASSSPECTROMETRY.

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