BNI5_YEAST - dbPTM
BNI5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BNI5_YEAST
UniProt AC P53890
Protein Name Bud neck protein 5
Gene Name BNI5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 448
Subcellular Localization Cytoplasm. Bud. Arrives at the bud site approximately coincident with bud emergence and dissociates from the septin scaffold before cytokinesis.
Protein Description Required for normal septin function and cytokinesis..
Protein Sequence MGLDQDKIKKRLSQIEIDINQMNQMIDENLQLVEPAEDEAVEDNVKDTGVVDAVKVAETALFSGNDGADSNPGDSAQVEEHKTAQVHIPTENEANKSTDDPSQLSVTQPFIAKEQITHTAIAIGDSYNSFVANSAGNEKAKDSCTENKEDGTVNIDQNRGEADVEIIENNDDEWEDEKSDVEEGRVDKGTEENSEIESFKSPMPQNNTLGGENKLDAELVLDKFSSANKDLDIQPQTIVVGGDNEYNHESSRLADQTPHDDNSENCPNRSGGSTPLDSQTKIFIPKKNSKEDGTNINHFNSDGDGQKKMANFETRRPTNPFRVISVSSNSNSRNGSRKSSLNKYDSPVSSPITSASELGSIAKLEKRHDYLSMKCIKLQKEIDYLNKMNAQGSLSMEDGKRLHRAVVKLQEYLDKKTKEKYEVGVLLSRHLRKQIDRGENGQFWIGTK
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
13PhosphorylationDKIKKRLSQIEIDIN
HHHHHHHHHHCCCHH		32.9028132839
59PhosphorylationDAVKVAETALFSGND
CHHHEEHHHHHCCCC		20.9422369663
63PhosphorylationVAETALFSGNDGADS
EEHHHHHCCCCCCCC		37.2222369663
70PhosphorylationSGNDGADSNPGDSAQ
CCCCCCCCCCCCCCC		44.3722369663
75PhosphorylationADSNPGDSAQVEEHK
CCCCCCCCCCCEECC		26.9022369663
83PhosphorylationAQVEEHKTAQVHIPT
CCCEECCEEEEECCC		24.9922369663
90PhosphorylationTAQVHIPTENEANKS
EEEEECCCCCCCCCC		51.3322369663
97PhosphorylationTENEANKSTDDPSQL
CCCCCCCCCCCHHHC		36.5522369663
98PhosphorylationENEANKSTDDPSQLS
CCCCCCCCCCHHHCC		46.1325521595
102PhosphorylationNKSTDDPSQLSVTQP
CCCCCCHHHCCCCCC		51.2320377248
105PhosphorylationTDDPSQLSVTQPFIA
CCCHHHCCCCCCEEE		18.5822369663
107PhosphorylationDPSQLSVTQPFIAKE
CHHHCCCCCCEEEHH		27.4422369663
126PhosphorylationTAIAIGDSYNSFVAN
EEEEHHCCHHHHHCC		22.4722369663
127PhosphorylationAIAIGDSYNSFVANS
EEEHHCCHHHHHCCC		21.4022369663
129PhosphorylationAIGDSYNSFVANSAG
EHHCCHHHHHCCCCC		16.9222369663
134PhosphorylationYNSFVANSAGNEKAK
HHHHHCCCCCCHHHH		28.0222369663
152PhosphorylationTENKEDGTVNIDQNR
CCCCCCCCEECCCCC		23.7721551504
179PhosphorylationDEWEDEKSDVEEGRV
CCCCHHHCHHHCCCC		44.8622369663
190PhosphorylationEGRVDKGTEENSEIE
CCCCCCCCCCCHHHH		45.9622890988
194PhosphorylationDKGTEENSEIESFKS
CCCCCCCHHHHCCCC		43.1422369663
198PhosphorylationEENSEIESFKSPMPQ
CCCHHHHCCCCCCCC		43.5722369663
201PhosphorylationSEIESFKSPMPQNNT
HHHHCCCCCCCCCCC		25.1522369663
208PhosphorylationSPMPQNNTLGGENKL
CCCCCCCCCCCCCCC		34.0424909858
225PhosphorylationELVLDKFSSANKDLD
HHHHHHHHHCCCCCC		33.9927017623
226PhosphorylationLVLDKFSSANKDLDI
HHHHHHHHCCCCCCC		38.7127017623
237PhosphorylationDLDIQPQTIVVGGDN
CCCCCCCEEEECCCC		23.5622369663
246PhosphorylationVVGGDNEYNHESSRL
EECCCCCCCCCHHCC		28.2422369663
250PhosphorylationDNEYNHESSRLADQT
CCCCCCCHHCCCCCC		17.1322369663
251PhosphorylationNEYNHESSRLADQTP
CCCCCCHHCCCCCCC		28.4722369663
257PhosphorylationSSRLADQTPHDDNSE
HHCCCCCCCCCCCCC		24.1217330950
263PhosphorylationQTPHDDNSENCPNRS
CCCCCCCCCCCCCCC		36.8629136822
270PhosphorylationSENCPNRSGGSTPLD
CCCCCCCCCCCCCCC		54.8922369663
273PhosphorylationCPNRSGGSTPLDSQT
CCCCCCCCCCCCCCC		30.3122369663
274PhosphorylationPNRSGGSTPLDSQTK
CCCCCCCCCCCCCCE		31.0122369663
278PhosphorylationGGSTPLDSQTKIFIP
CCCCCCCCCCEEEEC		47.6422890988
280PhosphorylationSTPLDSQTKIFIPKK
CCCCCCCCEEEECCC		30.0222890988
289PhosphorylationIFIPKKNSKEDGTNI
EEECCCCCCCCCCCC		46.4230377154
294PhosphorylationKNSKEDGTNINHFNS
CCCCCCCCCCCCCCC		45.2928889911
301PhosphorylationTNINHFNSDGDGQKK
CCCCCCCCCCCHHHE		41.8621551504
318PhosphorylationNFETRRPTNPFRVIS
CCCCCCCCCCCEEEE		54.4328889911
325PhosphorylationTNPFRVISVSSNSNS
CCCCEEEEEECCCCC		17.0622369663
327PhosphorylationPFRVISVSSNSNSRN
CCEEEEEECCCCCCC		19.6022369663
328PhosphorylationFRVISVSSNSNSRNG
CEEEEEECCCCCCCC		41.9622369663
330PhosphorylationVISVSSNSNSRNGSR
EEEEECCCCCCCCCC		37.8222369663
332PhosphorylationSVSSNSNSRNGSRKS
EEECCCCCCCCCCCC		27.2622369663
336PhosphorylationNSNSRNGSRKSSLNK
CCCCCCCCCCCHHCC		39.8322369663
338AcetylationNSRNGSRKSSLNKYD
CCCCCCCCCHHCCCC		46.2024489116
339PhosphorylationSRNGSRKSSLNKYDS
CCCCCCCCHHCCCCC		38.6622890988
340PhosphorylationRNGSRKSSLNKYDSP
CCCCCCCHHCCCCCC		38.7122369663
343AcetylationSRKSSLNKYDSPVSS
CCCCHHCCCCCCCCC		56.5824489116
344PhosphorylationRKSSLNKYDSPVSSP
CCCHHCCCCCCCCCC		22.1522369663
346PhosphorylationSSLNKYDSPVSSPIT
CHHCCCCCCCCCCCC		24.9022369663
349PhosphorylationNKYDSPVSSPITSAS
CCCCCCCCCCCCCHH		33.5122369663
350PhosphorylationKYDSPVSSPITSASE
CCCCCCCCCCCCHHH		22.1322369663
353PhosphorylationSPVSSPITSASELGS
CCCCCCCCCHHHHHH		22.9422890988
354PhosphorylationPVSSPITSASELGSI
CCCCCCCCHHHHHHH		30.4322890988
356PhosphorylationSSPITSASELGSIAK
CCCCCCHHHHHHHHH		32.8722890988
360PhosphorylationTSASELGSIAKLEKR
CCHHHHHHHHHHHHH		31.8122890988
363AcetylationSELGSIAKLEKRHDY
HHHHHHHHHHHHHHH		56.3524489116
374AcetylationRHDYLSMKCIKLQKE
HHHHHHHHHHHHHHH		29.4524489116
380AcetylationMKCIKLQKEIDYLNK
HHHHHHHHHHHHHHH		68.0524489116
408AcetylationRLHRAVVKLQEYLDK
HHHHHHHHHHHHHCH		37.5424489116
420AcetylationLDKKTKEKYEVGVLL
HCHHCHHHHHHHHHH		48.5524489116
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 BNI5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BNI5_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 BNI5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC11_YEASTCDC11physical
12215547
CDC10_YEASTCDC10genetic
12215547
CDC11_YEASTCDC11genetic
12215547
CDC12_YEASTCDC12genetic
12215547
CDC3_YEASTCDC3genetic
12215547
SHS1_YEASTSHS1genetic
12215547
CYK2_YEASTHOF1genetic
12215547
CDC11_YEASTCDC11physical
17618228
CDC12_YEASTCDC12physical
17618228
BNI5_YEASTBNI5physical
18467557
CMR1_YEASTCMR1genetic
22842922
MYO1_YEASTMYO1physical
23468521
CDC12_YEASTCDC12physical
23889817
CDC3_YEASTCDC3physical
23889817
CDC11_YEASTCDC11physical
23889817
CDC10_YEASTCDC10physical
23889817
CDC11_YEASTCDC11physical
27806918
BNI5_YEASTBNI5physical
27806918
OLA1_YEASTOLA1genetic
27708008
SWC5_YEASTSWC5genetic
27708008
AIM11_YEASTAIM11genetic
27708008
ICE2_YEASTICE2genetic
27708008
MPCP_YEASTMIR1genetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
UBX2_YEASTUBX2genetic
27708008
PHM7_YEASTPHM7genetic
27708008
FUN30_YEASTFUN30genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
REG2_YEASTREG2genetic
27708008
TPS1_YEASTTPS1genetic
27708008
BSD2_YEASTBSD2genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
SLX5_YEASTSLX5genetic
27708008
CYK3_YEASTCYK3genetic
27708008
PLP1_YEASTPLP1genetic
27708008
DSE1_YEASTDSE1genetic
27708008
ISC10_YEASTISC10genetic
27708008
PALF_YEASTRIM8genetic
27708008
YRB30_YEASTYRB30genetic
27708008
VMA21_YEASTVMA21genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
AIR1_YEASTAIR1genetic
27708008
FMC1_YEASTFMC1genetic
27708008
COX5B_YEASTCOX5Bgenetic
27708008
VPS53_YEASTVPS53genetic
27708008
TOK1_YEASTTOK1genetic
27708008
BCK1_YEASTBCK1genetic
27708008
IME2_YEASTIME2genetic
27708008
MNN5_YEASTMNN5genetic
27708008
IXR1_YEASTIXR1genetic
27708008
TPO5_YEASTTPO5genetic
27708008
NU133_YEASTNUP133genetic
27708008
COA4_YEASTCOA4genetic
27708008
COQ11_YEASTYLR290Cgenetic
27708008
MMS22_YEASTMMS22genetic
27708008
FKS1_YEASTFKS1genetic
27708008
CDC73_YEASTCDC73genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
AEP2_YEASTAEP2genetic
27708008
RTG1_YEASTRTG1genetic
27708008
HMI1_YEASTHMI1genetic
27708008
MTHR1_YEASTMET12genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
SPO19_YEASTSPO19genetic
27708008
AIM44_YEASTAIM44genetic
27708008
GIC1_YEASTGIC1genetic
26351911
GIC2_YEASTGIC2genetic
26351911
ELM1_YEASTELM1physical
26351911
CDC11_YEASTCDC11physical
26416886
CDC12_YEASTCDC12physical
26416886
CDC3_YEASTCDC3physical
26416886
CDC10_YEASTCDC10physical
26416886
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BNI5_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-70; SER-97; SER-105;SER-194; SER-270; SER-273; THR-274; SER-330; SER-336; SER-340;TYR-344; SER-346 AND SER-350, 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-70; SER-273; THR-274;SER-339; SER-346 AND SER-350, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346 AND SER-350, ANDMASS 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-270; THR-274; SER-346AND SER-350, AND MASS SPECTROMETRY.

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