BFR2_YEAST - dbPTM
BFR2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BFR2_YEAST
UniProt AC Q06631
Protein Name Protein BFR2
Gene Name BFR2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 534
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in endoplasmic reticulum to Golgi transport. Involved in a protein-transport step blocked by brefeldin A, which disrupts the Golgi apparatus and its incoming protein flux. May also be involved for mass growth or cell proliferation..
Protein Sequence MEKSLADQISDIAIKPVNKDFDIEDEENASLFQHNEKNGESDLSDYGNSNTEETKKAHYLEVEKSKLRAEKGLELNDPKYTGVKGSRQALYEEVSENEDEEEEEEEEEEKEEDALSFRTDSEDEEVEIDEEESDADGGETEEAQQKRHALSKLIQQETKQAINKLSQSVQRDASKGYSILQQTKLFDNIIDLRIKLQKAVIAANKLPLTTESWEEAKMDDSEETKRLLKENEKLFNNLFNRLINFRIKFQLGDHITQNEEVAKHKLSKKRSLKELYQETNSLDSELKEYRTAVLNKWSTKVSSASGNAALSSNKFKAINLPADVQVENQLSDMSRLMKRTKLNRRNITPLYFQKDCANGRLPELISPVVKDSVDDNENSDDGLDIPKNYDPRRKDNNAIDITENPYVFDDEDFYRVLLNDLIDKKISNAHNSESAAITITSTNARSNNKLKKNIDTKASKGRKLNYSVQDPIANYEAPITSGYKWSDDQIDEFFAGLLGQRVNFNENEDEEQHARIENDEELEAVKNDDIQIFG
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
4Phosphorylation----MEKSLADQISD
----CCCHHHHHHHH		18.5819684113
10PhosphorylationKSLADQISDIAIKPV
CHHHHHHHHCEEEEC		19.8219684113
15AcetylationQISDIAIKPVNKDFD
HHHHCEEEECCCCCC		33.6124489116
19AcetylationIAIKPVNKDFDIEDE
CEEEECCCCCCCCCH		61.0725381059
30PhosphorylationIEDEENASLFQHNEK
CCCHHHHHHHCCCCC		41.1025521595
41PhosphorylationHNEKNGESDLSDYGN
CCCCCCCCCHHHCCC		45.2922369663
44PhosphorylationKNGESDLSDYGNSNT
CCCCCCHHHCCCCCC		33.5022369663
46PhosphorylationGESDLSDYGNSNTEE
CCCCHHHCCCCCCHH		18.1622369663
49PhosphorylationDLSDYGNSNTEETKK
CHHHCCCCCCHHHHH		40.5422890988
51PhosphorylationSDYGNSNTEETKKAH
HHCCCCCCHHHHHHH		34.7122890988
54PhosphorylationGNSNTEETKKAHYLE
CCCCCHHHHHHHHHH		31.4522890988
64AcetylationAHYLEVEKSKLRAEK
HHHHHHHHHHHHHHC		59.0525381059
71AcetylationKSKLRAEKGLELNDP
HHHHHHHCCCCCCCC		68.7424489116
79SuccinylationGLELNDPKYTGVKGS
CCCCCCCCCCCCCCH		59.3023954790
79AcetylationGLELNDPKYTGVKGS
CCCCCCCCCCCCCCH		59.3024489116
95PhosphorylationQALYEEVSENEDEEE
HHHHHHHHCCCCHHH		37.6728889911
116PhosphorylationEKEEDALSFRTDSED
HHHHHHHHCCCCCCC		17.8828132839
119PhosphorylationEDALSFRTDSEDEEV
HHHHHCCCCCCCCEE		41.7019795423
121PhosphorylationALSFRTDSEDEEVEI
HHHCCCCCCCCEEEE		46.4619795423
133PhosphorylationVEIDEEESDADGGET
EEECCHHCCCCCCCC		41.1819795423
152AcetylationQKRHALSKLIQQETK
HHHHHHHHHHHHHHH		50.9224489116
164AcetylationETKQAINKLSQSVQR
HHHHHHHHHHHHHHH		43.3225381059
233AcetylationRLLKENEKLFNNLFN
HHHHHHHHHHHHHHH		70.7024489116
248AcetylationRLINFRIKFQLGDHI
HHHHHHHCEECCCCC		23.8524489116
281PhosphorylationELYQETNSLDSELKE
HHHHHHCCHHHHHHH		40.7627214570
287AcetylationNSLDSELKEYRTAVL
CCHHHHHHHHHHHHH		48.9624489116
296AcetylationYRTAVLNKWSTKVSS
HHHHHHHHHHCCCCC		38.0624489116
302PhosphorylationNKWSTKVSSASGNAA
HHHHCCCCCCCCCCC		23.0330377154
303PhosphorylationKWSTKVSSASGNAAL
HHHCCCCCCCCCCCC		29.4630377154
311PhosphorylationASGNAALSSNKFKAI
CCCCCCCCCCCCCEE		27.4330377154
312PhosphorylationSGNAALSSNKFKAIN
CCCCCCCCCCCCEEC		44.9130377154
331PhosphorylationVQVENQLSDMSRLMK
HHHHHHHHHHHHHHH		22.8530377154
334PhosphorylationENQLSDMSRLMKRTK
HHHHHHHHHHHHHHC		27.5330377154
366PhosphorylationGRLPELISPVVKDSV
CCCCHHHCHHHHCCC		25.0217330950
372PhosphorylationISPVVKDSVDDNENS
HCHHHHCCCCCCCCC		23.0222369663
379PhosphorylationSVDDNENSDDGLDIP
CCCCCCCCCCCCCCC		30.7922369663
394AcetylationKNYDPRRKDNNAIDI
CCCCCCCCCCCCEEC		67.1224489116
424AcetylationLLNDLIDKKISNAHN
HHHHHHHHHHHCCCC		45.0424489116
434PhosphorylationSNAHNSESAAITITS
HCCCCCCCCCEEEEE		23.8728889911
438PhosphorylationNSESAAITITSTNAR
CCCCCCEEEEECCHH		17.3028889911
440PhosphorylationESAAITITSTNARSN
CCCCEEEEECCHHHC		22.3528889911
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 BFR2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BFR2_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 BFR2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LCP5_YEASTLCP5physical
16554755
NOL10_YEASTENP2physical
16554755
DBP4_YEASTHCA4physical
16554755
NAT10_YEASTKRE33physical
16554755
SSB1_YEASTSSB1physical
19536198
NOL10_YEASTENP2physical
24357410
MPP10_YEASTMPP10physical
24357410
DBP4_YEASTHCA4physical
24357410
RL37A_YEASTRPL37Agenetic
27708008
SRO7_YEASTSRO7genetic
27708008
CDC27_YEASTCDC27genetic
27708008
CALM_YEASTCMD1genetic
27708008
KRR1_YEASTKRR1genetic
27708008
APC11_YEASTAPC11genetic
27708008
FBRL_YEASTNOP1genetic
27708008
PRP9_YEASTPRP9genetic
27708008
NOP14_YEASTNOP14genetic
27708008
NHP2_YEASTNHP2genetic
27708008
TIM22_YEASTTIM22genetic
27708008
FAL1_YEASTFAL1genetic
27708008
RMRP_YEASTSNM1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
RRP41_YEASTSKI6genetic
27708008
XPO1_YEASTCRM1genetic
27708008
BCD1_YEASTBCD1genetic
27708008
RRP3_YEASTRRP3genetic
27708008
UTP9_YEASTUTP9genetic
27708008
MTR4_YEASTMTR4genetic
27708008
ARP3_YEASTARP3genetic
27708008
MIF2_YEASTMIF2genetic
27708008
ABF1_YEASTABF1genetic
27708008
DCA13_YEASTSOF1genetic
27708008
PRP19_YEASTPRP19genetic
27708008
COFI_YEASTCOF1genetic
27708008
SSL1_YEASTSSL1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
NOP56_YEASTNOP56genetic
27708008
UTP13_YEASTUTP13genetic
27708008
DBP9_YEASTDBP9genetic
27708008
UTP15_YEASTUTP15genetic
27708008
RRP5_YEASTRRP5genetic
27708008
HAS1_YEASTHAS1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
NAT10_YEASTKRE33genetic
27708008
RRP44_YEASTDIS3genetic
27708008
SWC5_YEASTSWC5genetic
27708008
TAH1_YEASTTAH1genetic
27708008
NHP10_YEASTNHP10genetic
27708008
UGA4_YEASTUGA4genetic
27708008
MAF1_YEASTMAF1genetic
27708008
KCC1_YEASTCMK1genetic
27708008
CGR1_YEASTCGR1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
LRP1_YEASTLRP1genetic
27708008
THP2_YEASTTHP2genetic
27708008
SWE1_YEASTSWE1genetic
27708008
ECM27_YEASTECM27genetic
27708008
PAN3_YEASTPAN3genetic
27708008
YRA2_YEASTYRA2genetic
27708008
ARP6_YEASTARP6genetic
27708008
RAD10_YEASTRAD10genetic
27708008
TMA23_YEASTTMA23genetic
27708008
PUR1_YEASTADE4genetic
27708008
DOM34_YEASTDOM34genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
LSM7_YEASTLSM7genetic
27708008
VAM3_YEASTVAM3genetic
27708008
PDE2_YEASTPDE2genetic
27708008
SUR1_YEASTSUR1genetic
27708008
CARP_YEASTPEP4genetic
27708008
MDL2_YEASTMDL2genetic
27708008
YP089_YEASTYPR089Wgenetic
27708008
MSS18_YEASTMSS18genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BFR2_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-41; SER-44; SER-366;SER-372 AND SER-379, 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-41; SER-44 AND SER-379,AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-44; SER-366 ANDSER-379, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-44, AND MASSSPECTROMETRY.

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