6P21_YEAST - dbPTM
6P21_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 6P21_YEAST
UniProt AC P40433
Protein Name 6-phosphofructo-2-kinase 1
Gene Name PFK26
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 827
Subcellular Localization
Protein Description Synthesis of fructose 2,6-bisphosphate..
Protein Sequence MFKPVDFSETSPVPPDIDLAPTQSPHHVAPSQDSSYDLLSRSSDDKIDAEKGPHDELSKHLPLFQKRPLSDTPISSNWNSPGITEENTPSDSPENSATNLKSLHRLHINDETQLKNAKIPTNDTTDYMPPSDGANEVTRIDLKDIKSPTRHHKRRPTTIDVPGLTKSKTSPDGLISKEDSGSKLVIVMVGLPATGKSFITNKLSRFLNYSLYYCKVFNVGNTRRKFAKEHGLKDQDSKFFEPKNADSTRLRDKWAMDTLDELLDYLLEGSGSVGIFDATNTSRERRKNVLARIRKRSPHLKVLFLESVCSDHALVQKNIRLKLFGPDYKGKDPESSLKDFKSRLANYLKAYEPIEDDENLQYIKMIDVGKKVIAYNIQGFLASQTVYYLLNFNLADRQIWITRSGESEDNVSGRIGGNSHLTPRGLRFAKSLPKFIARQREIFYQNLMQQKKNNENTDGNIYNDFFVWTSMRARTIGTAQYFNEDDYPIKQMKMLDELSAGDYDGMTYPEIKNNFPEEFEKRQKDKLRYRYPGIGGESYMDVINRLRPVITELERIEDNVLIITHRVVARALLGYFMNLSMGIIANLDVPLHCVYCLEPKPYGITWSLWEYDEASDSFSKVPQTDLNTTRVKEVGLVYNERRYSVIPTAPPSARSSFASDFLSRKRSNPTSASSSQSELSEQPKNSVSAQTGSNNTTLIGSNFNIKNENGDSRIPLSAPLMATNTSNNILDGGGTSISIHRPRVVPNQNNVNPLLANNNKAASNVPNVKKSAATPRQIFEIDKVDEKLSMLKNKSFLLHGKDYPNNADNNDNEDIRAKTMNRSQSHV
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
3Acetylation-----MFKPVDFSET
-----CCCCCCCCCC		42.7216164414
8PhosphorylationMFKPVDFSETSPVPP
CCCCCCCCCCCCCCC		35.1922369663
10PhosphorylationKPVDFSETSPVPPDI
CCCCCCCCCCCCCCC		36.8122369663
11PhosphorylationPVDFSETSPVPPDID
CCCCCCCCCCCCCCC		21.6121551504
22PhosphorylationPDIDLAPTQSPHHVA
CCCCCCCCCCCCCCC		35.7522369663
24PhosphorylationIDLAPTQSPHHVAPS
CCCCCCCCCCCCCCC		28.7822369663
31PhosphorylationSPHHVAPSQDSSYDL
CCCCCCCCCCCCCCH		36.5622369663
34PhosphorylationHVAPSQDSSYDLLSR
CCCCCCCCCCCHHHC		24.1422369663
35PhosphorylationVAPSQDSSYDLLSRS
CCCCCCCCCCHHHCC		30.8422369663
36PhosphorylationAPSQDSSYDLLSRSS
CCCCCCCCCHHHCCC		17.9822369663
40PhosphorylationDSSYDLLSRSSDDKI
CCCCCHHHCCCCCCC		37.1022369663
42PhosphorylationSYDLLSRSSDDKIDA
CCCHHHCCCCCCCCC		34.4421126336
43PhosphorylationYDLLSRSSDDKIDAE
CCHHHCCCCCCCCCC		49.0321126336
70PhosphorylationLFQKRPLSDTPISSN
CCCCCCCCCCCCCCC		41.9620377248
72PhosphorylationQKRPLSDTPISSNWN
CCCCCCCCCCCCCCC		21.1023749301
75PhosphorylationPLSDTPISSNWNSPG
CCCCCCCCCCCCCCC		20.8724961812
76PhosphorylationLSDTPISSNWNSPGI
CCCCCCCCCCCCCCC		46.7324961812
80PhosphorylationPISSNWNSPGITEEN
CCCCCCCCCCCCCCC		19.0023749301
84PhosphorylationNWNSPGITEENTPSD
CCCCCCCCCCCCCCC		43.0619779198
88PhosphorylationPGITEENTPSDSPEN
CCCCCCCCCCCCCCC		27.7021440633
90PhosphorylationITEENTPSDSPENSA
CCCCCCCCCCCCCCC		49.0028889911
92PhosphorylationEENTPSDSPENSATN
CCCCCCCCCCCCCCC		38.1521440633
96PhosphorylationPSDSPENSATNLKSL
CCCCCCCCCCCHHHH		34.5021440633
147PhosphorylationIDLKDIKSPTRHHKR
CCHHHCCCCCCCCCC		31.6625752575
149PhosphorylationLKDIKSPTRHHKRRP
HHHCCCCCCCCCCCC		50.1224909858
157PhosphorylationRHHKRRPTTIDVPGL
CCCCCCCCEECCCCC		34.2717330950
158PhosphorylationHHKRRPTTIDVPGLT
CCCCCCCEECCCCCC		20.1929136822
165PhosphorylationTIDVPGLTKSKTSPD
EECCCCCCCCCCCCC		38.9126447709
167PhosphorylationDVPGLTKSKTSPDGL
CCCCCCCCCCCCCCC		35.6128889911
169PhosphorylationPGLTKSKTSPDGLIS
CCCCCCCCCCCCCCC		53.2123749301
258PhosphorylationRDKWAMDTLDELLDY
HHHHHHHHHHHHHHH		24.0327017623
270PhosphorylationLDYLLEGSGSVGIFD
HHHHHHCCCCCEEEE		20.6527017623
282PhosphorylationIFDATNTSRERRKNV
EEECCCCCHHHHHHH		33.9327017623
322AcetylationVQKNIRLKLFGPDYK
HHCCEEEEECCCCCC		31.7424489116
351PhosphorylationLANYLKAYEPIEDDE
HHHHHHHHCCCCCCC		22.2027017623
362PhosphorylationEDDENLQYIKMIDVG
CCCCCCEEEEEEECC		12.9928889911
475PhosphorylationWTSMRARTIGTAQYF
HHCCCCEECCCCHHC		23.8325371407
478PhosphorylationMRARTIGTAQYFNED
CCCEECCCCHHCCCC		13.5125371407
602PhosphorylationYCLEPKPYGITWSLW
EECCCCCCCEEEEEE		27.5621551504
624PhosphorylationSFSKVPQTDLNTTRV
CCCCCCCCCCCCCCE		36.0621551504
628PhosphorylationVPQTDLNTTRVKEVG
CCCCCCCCCCEEEEE		24.2321551504
629PhosphorylationPQTDLNTTRVKEVGL
CCCCCCCCCEEEEEE		32.1821551504
638PhosphorylationVKEVGLVYNERRYSV
EEEEEEEEECCCEEE		19.1519823750
643PhosphorylationLVYNERRYSVIPTAP
EEEECCCEEECCCCC		17.3222369663
644PhosphorylationVYNERRYSVIPTAPP
EEECCCEEECCCCCC		16.2615037628
648PhosphorylationRRYSVIPTAPPSARS
CCEEECCCCCCCHHH		40.4422369663
652PhosphorylationVIPTAPPSARSSFAS
ECCCCCCCHHHHHHH		34.9422369663
655PhosphorylationTAPPSARSSFASDFL
CCCCCHHHHHHHHHH		29.5322369663
656PhosphorylationAPPSARSSFASDFLS
CCCCHHHHHHHHHHH		21.1922369663
659PhosphorylationSARSSFASDFLSRKR
CHHHHHHHHHHHHCC		27.2122369663
663PhosphorylationSFASDFLSRKRSNPT
HHHHHHHHHCCCCCC		35.4322369663
667PhosphorylationDFLSRKRSNPTSASS
HHHHHCCCCCCCCCC		50.6322369663
670PhosphorylationSRKRSNPTSASSSQS
HHCCCCCCCCCCCHH		40.9722369663
671PhosphorylationRKRSNPTSASSSQSE
HCCCCCCCCCCCHHH		27.6622369663
673PhosphorylationRSNPTSASSSQSELS
CCCCCCCCCCHHHHC		30.2320377248
674PhosphorylationSNPTSASSSQSELSE
CCCCCCCCCHHHHCC		31.9220377248
675PhosphorylationNPTSASSSQSELSEQ
CCCCCCCCHHHHCCC		34.9220377248
677PhosphorylationTSASSSQSELSEQPK
CCCCCCHHHHCCCCC		42.3122369663
680PhosphorylationSSSQSELSEQPKNSV
CCCHHHHCCCCCCCC		30.0820377248
696PhosphorylationAQTGSNNTTLIGSNF
CCCCCCCCEEECCEE		27.5121551504
701PhosphorylationNNTTLIGSNFNIKNE
CCCEEECCEEEEECC		31.1121551504
795PhosphorylationLSMLKNKSFLLHGKD
HHHHHCCEEEECCCC		30.4421440633
823PhosphorylationRAKTMNRSQSHV---
HHHHHCHHHCCC---		30.9123749301
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 6P21_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 6P21_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 6P21_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YO296_YEASTYOR296Wphysical
18467557
BEM1_YEASTBEM1genetic
19269370
TPS2_YEASTTPS2genetic
19269370
GCN2_YEASTGCN2genetic
19269370
MON1_YEASTMON1genetic
19269370
PFKA1_YEASTPFK1genetic
19269370
CTK1_YEASTCTK1genetic
19269370
MSG5_YEASTMSG5genetic
19269370
6P22_YEASTPFK27genetic
19269370
ARO1_YEASTARO1genetic
21623372
6PGD1_YEASTGND1genetic
21623372
TPS2_YEASTTPS2genetic
21623372
6P22_YEASTPFK27genetic
21623372
ERG2_YEASTERG2genetic
21623372
ATPK_YEASTATP17genetic
21623372
COQ4_YEASTCOQ4genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
ICS2_YEASTICS2genetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
DCI1_YEASTDCI1genetic
27708008
STU1_YEASTSTU1genetic
27708008
APC11_YEASTAPC11genetic
27708008
FAL1_YEASTFAL1genetic
27708008
RPC10_YEASTRPC11genetic
27708008
UBC3_YEASTCDC34genetic
27708008
LCB2_YEASTLCB2genetic
27708008
CDC37_YEASTCDC37genetic
27708008
PRP28_YEASTPRP28genetic
27708008
RSP5_YEASTRSP5genetic
27708008
TBP_YEASTSPT15genetic
27708008
ACT_YEASTACT1genetic
27708008
COPD_YEASTRET2genetic
27708008
CDC12_YEASTCDC12genetic
27708008
ARP4_YEASTARP4genetic
27708008
KTHY_YEASTCDC8genetic
27708008
GPN1_YEASTNPA3genetic
27708008
PRS7_YEASTRPT1genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SEC22_YEASTSEC22genetic
27708008
BET5_YEASTBET5genetic
27708008
LCB1_YEASTLCB1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
SGT1_YEASTSGT1genetic
27708008
RPA1_YEASTRPA190genetic
27708008
ARP7_YEASTARP7genetic
27708008
MED10_YEASTNUT2genetic
27708008
MDM10_YEASTMDM10genetic
27708008
GEM1_YEASTGEM1genetic
27708008
PP2C3_YEASTPTC3genetic
27708008
NPL4_YEASTNPL4genetic
27708008
SWC5_YEASTSWC5genetic
27708008
YCZ2_YEASTYCR102Cgenetic
27708008
PP2C1_YEASTPTC1genetic
27708008
SLX5_YEASTSLX5genetic
27708008
TPS2_YEASTTPS2genetic
27708008
INO2_YEASTINO2genetic
27708008
DHAS_YEASTHOM2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
RAV2_YEASTRAV2genetic
27708008
H2A1_YEASTHTA1genetic
27708008
SWR1_YEASTSWR1genetic
27708008
CP56_YEASTDIT2genetic
27708008
RMT2_YEASTRMT2genetic
27708008
AIM11_YEASTAIM11genetic
27708008
UBP3_YEASTUBP3genetic
27708008
OSW7_YEASTOSW7genetic
27708008
AGA2_YEASTAGA2genetic
27708008
ATC1_YEASTPMR1genetic
27708008
MNT2_YEASTMNT2genetic
27708008
TBP7_YEASTYTA7genetic
27708008
SLT2_YEASTSLT2genetic
27708008
MED20_YEASTSRB2genetic
27708008
IRE1_YEASTIRE1genetic
27708008
SDO1L_YEASTRTC3genetic
27708008
PTH_YEASTPTH1genetic
27708008
BFA1_YEASTBFA1genetic
27708008
YKF0_YEASTYKL050Cgenetic
27708008
VPS51_YEASTVPS51genetic
27708008
SA190_YEASTSAP190genetic
27708008
SET3_YEASTSET3genetic
27708008
SHB17_YEASTSHB17genetic
27708008
PAM17_YEASTPAM17genetic
27708008
ALAM_YEASTALT1genetic
27708008
RL37A_YEASTRPL37Agenetic
27708008
MMR1_YEASTMMR1genetic
27708008
UPS1_YEASTUPS1genetic
27708008
PDR8_YEASTPDR8genetic
27708008
ARPC3_YEASTARC18genetic
27708008
ELO3_YEASTELO3genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
MUB1_YEASTMUB1genetic
27708008
RAD14_YEASTRAD14genetic
27708008
PET8_YEASTPET8genetic
27708008
EAF7_YEASTEAF7genetic
27708008
VPS27_YEASTVPS27genetic
27708008
ATP23_YEASTATP23genetic
27708008
SIN3_YEASTSIN3genetic
27708008
VPS21_YEASTVPS21genetic
27708008
IES4_YEASTIES4genetic
27708008
HAP5_YEASTHAP5genetic
27708008
PDE2_YEASTPDE2genetic
27708008
LGE1_YEASTLGE1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
ELP3_YEASTELP3genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 6P21_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-147; THR-157; THR-169;TYR-362; SER-644; SER-652 AND SER-656, 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 THR-157; SER-652; SER-667;SER-671 AND SER-675, AND MASS SPECTROMETRY.
"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-644 AND SER-659, ANDMASS 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 THR-157, AND MASSSPECTROMETRY.
"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 THR-157, AND MASSSPECTROMETRY.

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