6P22_YEAST - dbPTM
6P22_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 6P22_YEAST
UniProt AC Q12471
Protein Name 6-phosphofructo-2-kinase 2
Gene Name PFK27
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 397
Subcellular Localization
Protein Description Synthesis of fructose 2,6-bisphosphate..
Protein Sequence MGGSSDSDSHDGYLTSEYNSSNSLFSLNTGNSYSSASLDRATLDCQDSVFFDNHKSSLLSTEVPRFISNDPLHLPITLNYKRDNADPTYTNGKVNKFMIVLIGLPATGKSTISSHLIQCLKNNPLTNSLRCKVFNAGKIRRQISCATISKPLLLSNTSSEDLFNPKNNDKKETYARITLQKLFHEINNDECDVGIFDATNSTIERRRFIFEEVCSFNTDELSSFNLVPIILQVSCFNRSFIKYNIHNKSFNEDYLDKPYELAIKDFAKRLKHYYSQFTPFSLDEFNQIHRYISQHEEIDTSLFFFNVINAGVVEPHSLNQSHYPSTCGKQIRDTIMVIENFINHYSQMFGFEYIEAVKLFFESFGNSSEETLTTLDSVVNDKFFDDLQSLIESNGFA
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
55UbiquitinationSVFFDNHKSSLLSTE
CCEECCCCHHCCCCC		48.2523749301
81UbiquitinationLPITLNYKRDNADPT
CCEEEECCCCCCCCC		52.8023749301
96UbiquitinationYTNGKVNKFMIVLIG
CCCCCCCEEEEEEEE		39.0217644757
109UbiquitinationIGLPATGKSTISSHL
EECCCCCCHHHHHHH		39.8217644757
121UbiquitinationSHLIQCLKNNPLTNS
HHHHHHHHHCCCCCC		63.4117644757
144PhosphorylationGKIRRQISCATISKP
HHCCCEEEEEEECCC		6.8623749301
150UbiquitinationISCATISKPLLLSNT
EEEEEECCCEECCCC		35.5223749301
155PhosphorylationISKPLLLSNTSSEDL
ECCCEECCCCCHHHH		37.7223749301
157PhosphorylationKPLLLSNTSSEDLFN
CCEECCCCCHHHHCC		30.1923749301
158PhosphorylationPLLLSNTSSEDLFNP
CEECCCCCHHHHCCC		35.6620377248
159PhosphorylationLLLSNTSSEDLFNPK
EECCCCCHHHHCCCC		32.8423749301
166UbiquitinationSEDLFNPKNNDKKET
HHHHCCCCCCCHHHH		70.2817644757
181UbiquitinationYARITLQKLFHEINN
HHHHHHHHHHHHHCC		57.1217644757
248UbiquitinationIKYNIHNKSFNEDYL
HCCEECCCCCCHHHC		42.1117644757
257UbiquitinationFNEDYLDKPYELAIK
CCHHHCCCHHHHHHH		47.0717644757
264UbiquitinationKPYELAIKDFAKRLK
CHHHHHHHHHHHHHH		40.9817644757
268UbiquitinationLAIKDFAKRLKHYYS
HHHHHHHHHHHHHHH		59.2517644757
271UbiquitinationKDFAKRLKHYYSQFT
HHHHHHHHHHHHHCC		33.3317644757
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 6P22_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 6P22_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 6P22_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
6P21_YEASTPFK26genetic
21623372
COQ2_YEASTCOQ2genetic
21623372
PTM1_YEASTPTM1genetic
27708008
DCW1_YEASTDCW1genetic
27708008
FPS1_YEASTFPS1genetic
27708008
AVT7_YEASTAVT7genetic
27708008
6P21_YEASTPFK26genetic
27708008
MND2_YEASTMND2genetic
27708008
ALN_YEASTDAL1genetic
27708008
SA185_YEASTSAP185genetic
27708008
PBS2_YEASTPBS2genetic
27708008
YJQ3_YEASTYJL163Cgenetic
27708008
YJU6_YEASTYJL206Cgenetic
27708008
SFC1_YEASTSFC1genetic
27708008
YKK7_YEASTYKL107Wgenetic
27708008
SWI6_YEASTSWI6genetic
27708008
CRR1_YEASTCRR1genetic
27708008
YPT6_YEASTYPT6genetic
27708008
SKY1_YEASTSKY1genetic
27708008
YNB0_YEASTYNL010Wgenetic
27708008
PHO91_YEASTPHO91genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 6P22_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-158, AND MASSSPECTROMETRY.

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