BMH2_YEAST - dbPTM
BMH2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BMH2_YEAST
UniProt AC P34730
Protein Name Protein BMH2
Gene Name BMH2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 273
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MSQTREDSVYLAKLAEQAERYEEMVENMKAVASSGQELSVEERNLLSVAYKNVIGARRASWRIVSSIEQKEESKEKSEHQVELIRSYRSKIETELTKISDDILSVLDSHLIPSATTGESKVFYYKMKGDYHRYLAEFSSGDAREKATNSSLEAYKTASEIATTELPPTHPIRLGLALNFSVFYYEIQNSPDKACHLAKQAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDISESGQEDQQQQQQQQQQQQQQQQQAPAEQTQGEPTK
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
2Acetylation------MSQTREDSV
------CCCCHHHHH		40.019298649
2Phosphorylation------MSQTREDSV
------CCCCHHHHH		40.0122369663
4Phosphorylation----MSQTREDSVYL
----CCCCHHHHHHH		28.8124909858
8PhosphorylationMSQTREDSVYLAKLA
CCCCHHHHHHHHHHH		14.1224961812
13UbiquitinationEDSVYLAKLAEQAER
HHHHHHHHHHHHHHH		45.7124961812
47PhosphorylationVEERNLLSVAYKNVI
HHHHHHHHHHHHHHH		14.1022369663
50PhosphorylationRNLLSVAYKNVIGAR
HHHHHHHHHHHHCHH		10.8422369663
51UbiquitinationNLLSVAYKNVIGARR
HHHHHHHHHHHCHHH		34.6923749301
65PhosphorylationRASWRIVSSIEQKEE
HHHHHHHHHHHHHHH		24.1922369663
66PhosphorylationASWRIVSSIEQKEES
HHHHHHHHHHHHHHH		21.1724909858
70UbiquitinationIVSSIEQKEESKEKS
HHHHHHHHHHHHCCC		51.1323749301
702-HydroxyisobutyrylationIVSSIEQKEESKEKS
HHHHHHHHHHHHCCC		51.13-
73PhosphorylationSIEQKEESKEKSEHQ
HHHHHHHHHCCCHHH		47.4022369663
74UbiquitinationIEQKEESKEKSEHQV
HHHHHHHHCCCHHHH		72.8822817900
76UbiquitinationQKEESKEKSEHQVEL
HHHHHHCCCHHHHHH		65.9523749301
89PhosphorylationELIRSYRSKIETELT
HHHHHHHHHHHHHHH		29.74-
902-HydroxyisobutyrylationLIRSYRSKIETELTK
HHHHHHHHHHHHHHH		35.25-
90AcetylationLIRSYRSKIETELTK
HHHHHHHHHHHHHHH		35.2525381059
99PhosphorylationETELTKISDDILSVL
HHHHHHHCHHHHHHH		30.6821440633
104PhosphorylationKISDDILSVLDSHLI
HHCHHHHHHHHHCCC		22.4422369663
108PhosphorylationDILSVLDSHLIPSAT
HHHHHHHHCCCCCCC		18.9422369663
113PhosphorylationLDSHLIPSATTGESK
HHHCCCCCCCCCCCE		31.1122369663
115PhosphorylationSHLIPSATTGESKVF
HCCCCCCCCCCCEEE		39.4022369663
116PhosphorylationHLIPSATTGESKVFY
CCCCCCCCCCCEEEE		38.3721440633
119PhosphorylationPSATTGESKVFYYKM
CCCCCCCCEEEEEEE		35.1522369663
1452-HydroxyisobutyrylationSSGDAREKATNSSLE
CCCCHHHHHHHCHHH		55.76-
145UbiquitinationSSGDAREKATNSSLE
CCCCHHHHHHHCHHH		55.7623749301
155AcetylationNSSLEAYKTASEIAT
HCHHHHHHHHHHHHC		44.6624489116
210PhosphorylationDAIAELDTLSEESYK
HHHHHHHCCCHHHCC		44.8222369663
212PhosphorylationIAELDTLSEESYKDS
HHHHHCCCHHHCCCH		41.2222369663
215PhosphorylationLDTLSEESYKDSTLI
HHCCCHHHCCCHHHH		33.1722369663
216PhosphorylationDTLSEESYKDSTLIM
HCCCHHHCCCHHHHH		23.3022369663
219PhosphorylationSEESYKDSTLIMQLL
CHHHCCCHHHHHHHH		22.4419779198
220PhosphorylationEESYKDSTLIMQLLR
HHHCCCHHHHHHHHH		30.3622369663
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 BMH2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BMH2_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 BMH2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BMH1_YEASTBMH1physical
11805826
TREA_YEASTNTH1physical
11805826
TREB_YEASTNTH2physical
11805826
PIK1_YEASTPIK1physical
11805826
RTG2_YEASTRTG2physical
11805826
PSK1_YEASTPSK1physical
11805826
CSR2_YEASTCSR2physical
11805837
BOP3_YEASTBOP3physical
10688190
ECM13_YEASTECM13physical
10688190
FIN1_YEASTFIN1physical
11931638
GCR2_YEASTGCR2physical
11931638
GIC2_YEASTGIC2physical
11931638
LRE1_YEASTLRE1physical
11931638
MBF1_YEASTMBF1physical
11931638
GYP3_YEASTMSB3physical
11931638
PPT1_YEASTPPT1physical
11931638
REG2_YEASTREG2physical
11931638
RSSA1_YEASTRPS0Aphysical
11931638
YL177_YEASTYLR177Wphysical
11931638
BMH1_YEASTBMH1physical
12507503
BMH1_YEASTBMH1physical
11931638
BMH2_YEASTBMH2physical
11931638
GRR1_YEASTGRR1physical
15849787
REG1_YEASTREG1physical
15849787
YPK1_YEASTYPK1genetic
12196392
RTG3_YEASTRTG3genetic
11748725
MED16_YEASTSIN4genetic
11748725
BMH1_YEASTBMH1genetic
14704161
KAPA_YEASTTPK1genetic
8524799
BMH1_YEASTBMH1physical
16554755
FPK1_YEASTFPK1physical
16554755
CDC31_YEASTCDC31physical
16554755
BMH1_YEASTBMH1physical
16429126
RTG2_YEASTRTG2physical
16429126
TREA_YEASTNTH1physical
16429126
PSK1_YEASTPSK1physical
16429126
ESA1_YEASTESA1physical
17339336
RPD3_YEASTRPD3physical
17339336
RAD53_YEASTRAD53physical
17299042
PIK1_YEASTPIK1physical
18172025
H3_YEASTHHT1physical
18268010
KCS1_YEASTKCS1genetic
19269370
OCA6_YEASTOCA6genetic
19269370
KHSE_YEASTTHR1genetic
19269370
ADK_YEASTADO1genetic
19269370
SIW14_YEASTSIW14genetic
19269370
MCM2_YEASTMCM2physical
19934224
ORC2_YEASTORC2physical
19934224
MYO2_YEASTMYO2physical
21182200
GDE1_YEASTGDE1physical
21182200
SSB1_YEASTSSB1physical
21182200
HSP72_YEASTSSA2physical
21182200
RTG2_YEASTRTG2physical
21182200
FAS2_YEASTFAS2physical
21182200
FAS1_YEASTFAS1physical
21182200
BUD3_YEASTBUD3physical
21182200
KCC1_YEASTCMK1physical
21182200
NOP56_YEASTNOP56physical
21182200
RL3_YEASTRPL3physical
21182200
RL4A_YEASTRPL4Aphysical
21182200
HEMH_YEASTHEM15physical
21182200
TREA_YEASTNTH1physical
21182200
REG1_YEASTREG1physical
21182200
MKS1_YEASTMKS1physical
21182200
SSB2_YEASTSSB2physical
21182200
PP2B1_YEASTCNA1physical
21182200
EF1G2_YEASTTEF4physical
21182200
EXO1_YEASTEXO1physical
21533173
EXO1_YEASTEXO1genetic
21533173
ROD1_YEASTROD1physical
22249293
BMH1_YEASTBMH1genetic
22484491
BUL1_YEASTBUL1physical
22966204
REG1_YEASTREG1genetic
23207903
BMH2_YEASTBMH2physical
20384366
SPS1_YEASTSPS1genetic
25409301
RNP1_YEASTRNP1genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
YBQ6_YEASTYBR056Wgenetic
27708008
YPQ3_YEASTRTC2genetic
27708008
YPC1_YEASTYPC1genetic
27708008
AIM4_YEASTAIM4genetic
27708008
YB75_YEASTYBR225Wgenetic
27708008
SWC5_YEASTSWC5genetic
27708008
RMD9L_YEASTYBR238Cgenetic
27708008
CHK1_YEASTCHK1genetic
27708008
PEX19_YEASTPEX19genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
SLX8_YEASTSLX8genetic
27708008
BMH1_YEASTBMH1genetic
27708008
RIM15_YEASTRIM15genetic
27708008
VMA21_YEASTVMA21genetic
27708008
MAL12_YEASTMAL12genetic
27708008
ERG3_YEASTERG3genetic
27708008
SWI6_YEASTSWI6genetic
27708008
YL287_YEASTYLR287Cgenetic
27708008
SEI1_YEASTFLD1genetic
27708008
ECM7_YEASTECM7genetic
27708008
BUL2_YEASTBUL2genetic
27708008
KAR5_YEASTKAR5genetic
27708008
DCAM_YEASTSPE2genetic
27708008
LDB19_YEASTLDB19physical
27261460
ECM21_YEASTECM21physical
27261460
ROD1_YEASTROD1physical
27261460
ALY1_YEASTALY1physical
27261460
ROG3_YEASTROG3physical
27261460
CSR2_YEASTCSR2physical
27261460
PALF_YEASTRIM8physical
27261460
ABF2_YEASTABF2genetic
27453043
KAPB_YEASTTPK2genetic
27453043
VPS75_YEASTVPS75genetic
27453043
SSN8_YEASTSSN8genetic
27453043
GCR2_YEASTGCR2genetic
27453043
BUB1_YEASTBUB1genetic
27453043
PP2A1_YEASTPPH21genetic
27453043
VPS53_YEASTVPS53genetic
27453043
DCOR_YEASTSPE1genetic
27453043
HDA1_YEASTHDA1genetic
27453043
DCAM_YEASTSPE2genetic
27453043
ADE_YEASTAAH1genetic
27453043
BUL2_YEASTBUL2physical
24942738
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BMH2_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2.
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-104 AND SER-212, ANDMASS SPECTROMETRY.

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