F262_HUMAN - dbPTM
F262_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F262_HUMAN
UniProt AC O60825
Protein Name 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
Gene Name PFKFB2
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization
Protein Description Synthesis and degradation of fructose 2,6-bisphosphate..
Protein Sequence MSGASSSEQNNNSYETKTPNLRMSEKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCALVALEDVKAYLTEENGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMEDFLKRIECYKVTYRPLDPDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVYYLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPVAYGCKVETIKLNVEAVNTHRDKPTNNFPKNQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLKPLSPLRAQDMQEGAD
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------MSGASSSEQ
------CCCCCCCCC		42.9622814378
2Phosphorylation------MSGASSSEQ
------CCCCCCCCC		42.9625159151
5Phosphorylation---MSGASSSEQNNN
---CCCCCCCCCCCC		37.6125159151
6Phosphorylation--MSGASSSEQNNNS
--CCCCCCCCCCCCC		37.0425159151
7Phosphorylation-MSGASSSEQNNNSY
-CCCCCCCCCCCCCC		40.4825159151
13PhosphorylationSSEQNNNSYETKTPN
CCCCCCCCCCCCCCC		26.8625159151
14PhosphorylationSEQNNNSYETKTPNL
CCCCCCCCCCCCCCC		29.7320860994
16PhosphorylationQNNNSYETKTPNLRM
CCCCCCCCCCCCCCC		31.8024043423
17UbiquitinationNNNSYETKTPNLRMS
CCCCCCCCCCCCCCC		50.4724816145
24PhosphorylationKTPNLRMSEKKCSWA
CCCCCCCCCCCCHHH		39.5725159151
29PhosphorylationRMSEKKCSWASYMTN
CCCCCCCHHHHHHCC		34.2620068231
32PhosphorylationEKKCSWASYMTNSPT
CCCCHHHHHHCCCCE		14.8029116813
33PhosphorylationKKCSWASYMTNSPTL
CCCHHHHHHCCCCEE		10.5429116813
35PhosphorylationCSWASYMTNSPTLIV
CHHHHHHCCCCEEEE		25.0629116813
37PhosphorylationWASYMTNSPTLIVMI
HHHHHCCCCEEEEEE		15.3129116813
39PhosphorylationSYMTNSPTLIVMIGL
HHHCCCCEEEEEEEC		29.0129116813
52PhosphorylationGLPARGKTYVSKKLT
ECCCCCCHHHHHHHH		31.7920068231
53PhosphorylationLPARGKTYVSKKLTR
CCCCCCHHHHHHHHH		13.2520068231
55PhosphorylationARGKTYVSKKLTRYL
CCCCHHHHHHHHHHH		17.4120068231
59PhosphorylationTYVSKKLTRYLNWIG
HHHHHHHHHHHHHHC		26.5821964256
63UbiquitinationKKLTRYLNWIGVPTK
HHHHHHHHHHCCCCE		21.2723000965
84PhosphorylationYRREAVKSYKSYDFF
CCHHHHHHHCCCCCC		31.0624719451
86UbiquitinationREAVKSYKSYDFFRH
HHHHHHHCCCCCCCC		50.0229967540
100UbiquitinationHDNEEAMKIRKQCAL
CCCHHHHHHHHHHHH		46.5424816145
103UbiquitinationEEAMKIRKQCALVAL
HHHHHHHHHHHHHHH		53.8829967540
113UbiquitinationALVALEDVKAYLTEE
HHHHHHHHHHHEECC		2.5224816145
130PhosphorylationQIAVFDATNTTRERR
EEEEEECCCCCHHHH		34.6422210691
132PhosphorylationAVFDATNTTRERRDM
EEEECCCCCHHHHHH		23.9122210691
133PhosphorylationVFDATNTTRERRDMI
EEECCCCCHHHHHHH		32.3822210691
174PhosphorylationNILEVKVSSPDYPER
EEEEEEECCCCCCHH		30.3626270265
175PhosphorylationILEVKVSSPDYPERN
EEEEEECCCCCCHHC		25.4426462736
192UbiquitinationNVMEDFLKRIECYKV
CHHHHHHHHHCEEEE		51.8529967540
211UbiquitinationLDPDNYDKDLSFIKV
CCCCCCCCCCCEEEE		50.6529967540
214PhosphorylationDNYDKDLSFIKVINV
CCCCCCCCEEEEEEC		34.7524719451
275PhosphorylationIGGDSGLSVRGKQFA
ECCCCCCCHHHHHHH		17.1924719451
279UbiquitinationSGLSVRGKQFAQALR
CCCCHHHHHHHHHHH		31.5129967540
287UbiquitinationQFAQALRKFLEEQEI
HHHHHHHHHHHHHCC		55.9729967540
298UbiquitinationEQEITDLKVWTSQLK
HHCCCCHHHHHHHHH		38.2429967540
305UbiquitinationKVWTSQLKRTIQTAE
HHHHHHHHHHHHHHH		39.6023000965
355UbiquitinationFALRDQEKYLYRYPG
HHCCCHHHHHHCCCC		34.6224816145
356PhosphorylationALRDQEKYLYRYPGG
HCCCHHHHHHCCCCC		14.2822817900
358PhosphorylationRDQEKYLYRYPGGES
CCHHHHHHCCCCCCC		12.6622817900
366PhosphorylationRYPGGESYQDLVQRL
CCCCCCCHHHHHHHH		11.1822817900
458PhosphorylationNNFPKNQTPVRMRRN
CCCCCCCCCCCCCCC		32.9030576142
463 (in isoform 2)Phosphorylation-24.8627273156
466 (in isoform 2)Phosphorylation-28.7822617229
466PhosphorylationPVRMRRNSFTPLSSS
CCCCCCCCCCCCCCC		28.7829255136
468PhosphorylationRMRRNSFTPLSSSNT
CCCCCCCCCCCCCCC		24.1222167270
471PhosphorylationRNSFTPLSSSNTIRR
CCCCCCCCCCCCCCC		32.6823927012
472PhosphorylationNSFTPLSSSNTIRRP
CCCCCCCCCCCCCCC		34.9825159151
472O-linked_GlycosylationNSFTPLSSSNTIRRP
CCCCCCCCCCCCCCC		34.9831373491
473PhosphorylationSFTPLSSSNTIRRPR
CCCCCCCCCCCCCCC		34.3223927012
475PhosphorylationTPLSSSNTIRRPRNY
CCCCCCCCCCCCCCC		20.1523927012
482PhosphorylationTIRRPRNYSVGSRPL
CCCCCCCCCCCCCCC		13.1527273156
483PhosphorylationIRRPRNYSVGSRPLK
CCCCCCCCCCCCCCC		24.4522167270
486PhosphorylationPRNYSVGSRPLKPLS
CCCCCCCCCCCCCCC		28.6823927012
493PhosphorylationSRPLKPLSPLRAQDM
CCCCCCCCCCCHHHH		30.3429255136
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
29SPhosphorylationKinasePKA-Uniprot
466SPhosphorylationKinaseAMPKQ9Y478
Uniprot
466SPhosphorylationKinasePRKAA1Q13131
GPS
466SPhosphorylationKinaseAKT1P31749
PSP
466SPhosphorylationKinasePRKACAP17612
GPS
466SPhosphorylationKinaseAKT-FAMILY-GPS
466SPhosphorylationKinaseAMPK-FAMILY-GPS
466SPhosphorylationKinaseAMPK_GROUP-PhosphoELM
466SPhosphorylationKinasePKB_GROUP-PhosphoELM
483SPhosphorylationKinaseAKT1P31749
PSP
483SPhosphorylationKinaseAKT-FAMILY-GPS
483SPhosphorylationKinasePKB_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F262_HUMAN !!
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 F262_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433T_HUMANYWHAQphysical
12853467
PDE4D_HUMANPDE4Dphysical
26496610
RO52_HUMANTRIM21physical
26496610
ZC11A_HUMANZC3H11Aphysical
26496610
SRRM2_HUMANSRRM2physical
26496610
PGAP2_HUMANPGAP2physical
26496610
NO40_HUMANZCCHC17physical
26496610
RMD3_HUMANRMDN3physical
26496610
RBM15_HUMANRBM15physical
26496610
CPSF7_HUMANCPSF7physical
26496610
DOCK8_HUMANDOCK8physical
26496610
PDIP3_HUMANPOLDIP3physical
26496610
SARNP_HUMANSARNPphysical
26496610
FA83B_HUMANFAM83Bphysical
26496610
CBY1_HUMANCBY1physical
27173435
RAB3I_HUMANRAB3IPphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F262_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-468; SER-483AND SER-493, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND MASSSPECTROMETRY.
"Phosphorylation and activation of heart PFK-2 by AMPK has a role inthe stimulation of glycolysis during ischaemia.";
Marsin A.S., Bertrand L., Rider M.H., Deprez J., Beauloye C.,Vincent M.F., Van den Berghe G., Carling D., Hue L.;
Curr. Biol. 10:1247-1255(2000).
Cited for: PHOSPHORYLATION AT SER-466, AND MUTAGENESIS OF SER-466.

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