F263_HUMAN - dbPTM
F263_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F263_HUMAN
UniProt AC Q16875
Protein Name 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
Gene Name PFKFB3
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization
Protein Description Synthesis and degradation of fructose 2,6-bisphosphate..
Protein Sequence MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH
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
6Phosphorylation--MPLELTQSRVQKI
--CCCCCCHHHCEEE		18.3420068231
12UbiquitinationLTQSRVQKIWVPVDH
CCHHHCEEEEEECCC		35.36-
22PhosphorylationVPVDHRPSLPRSCGP
EECCCCCCCCCCCCC		51.4628102081
31 (in isoform 4)Phosphorylation-6.5322985185
36PhosphorylationPKLTNSPTVIVMVGL
CCCCCCCEEEEEEEC		23.7622210691
82PhosphorylationRREAVKQYSSYNFFR
HHHHHHHHHCCCCCC		8.2124043423
83PhosphorylationREAVKQYSSYNFFRP
HHHHHHHHCCCCCCC		24.6924043423
84PhosphorylationEAVKQYSSYNFFRPD
HHHHHHHCCCCCCCC		21.1124043423
85PhosphorylationAVKQYSSYNFFRPDN
HHHHHHCCCCCCCCC		15.2824043423
97UbiquitinationPDNEEAMKVRKQCAL
CCCHHHHHHHHHHHH		46.03-
100MalonylationEEAMKVRKQCALAAL
HHHHHHHHHHHHHHH		53.3626320211
100UbiquitinationEEAMKVRKQCALAAL
HHHHHHHHHHHHHHH		53.36-
111UbiquitinationLAALRDVKSYLAKEG
HHHHHHHHHHHHHCC		37.3621890473
111 (in isoform 1)Ubiquitination-37.3621890473
111 (in isoform 2)Ubiquitination-37.3621890473
111UbiquitinationLAALRDVKSYLAKEG
HHHHHHHHHHHHHCC		37.3621906983
116 (in isoform 2)Ubiquitination-55.06-
116UbiquitinationDVKSYLAKEGGQIAV
HHHHHHHHCCCEEEE		55.06-
125UbiquitinationGGQIAVFDATNTTRE
CCEEEEEECCCCHHH		45.98-
130UbiquitinationVFDATNTTRERRHMI
EEECCCCHHHHHHHH		32.38-
171O-linked_GlycosylationNIMEVKISSPDYKDC
CEEEEEECCCCCCCC		30.0532830957
172PhosphorylationIMEVKISSPDYKDCN
EEEEEECCCCCCCCC		25.8421712546
172O-linked_GlycosylationIMEVKISSPDYKDCN
EEEEEECCCCCCCCC		25.8432830957
176UbiquitinationKISSPDYKDCNSAEA
EECCCCCCCCCCHHH		64.28-
189UbiquitinationEAMDDFMKRISCYEA
HHHHHHHHHHCHHHH		46.72-
194PhosphorylationFMKRISCYEASYQPL
HHHHHCHHHHCCCCC		14.0330387612
205UbiquitinationYQPLDPDKCDRDLSL
CCCCCHHHCCCCCCE		43.34-
211PhosphorylationDKCDRDLSLIKVIDV
HHCCCCCCEEEEEEC		32.1324719451
214 (in isoform 1)Ubiquitination-38.1321890473
214 (in isoform 2)Ubiquitination-38.1321890473
214UbiquitinationDRDLSLIKVIDVGRR
CCCCCEEEEEECCHH		38.1321906983
228UbiquitinationRFLVNRVQDHIQSRI
HHHHHHHHHHHHHHH		33.07-
269PhosphorylationQGRIGGDSGLSSRGK
CCCCCCCCCCCHHHH		44.93-
273PhosphorylationGGDSGLSSRGKKFAS
CCCCCCCHHHHHHHH		50.5218452278
277UbiquitinationGLSSRGKKFASALSK
CCCHHHHHHHHHHHH		49.32-
280PhosphorylationSRGKKFASALSKFVE
HHHHHHHHHHHHHHH		32.6421406692
282UbiquitinationGKKFASALSKFVEEQ
HHHHHHHHHHHHHHC		5.4621890473
283PhosphorylationKKFASALSKFVEEQN
HHHHHHHHHHHHHCC		24.6221406692
284UbiquitinationKFASALSKFVEEQNL
HHHHHHHHHHHHCCH		55.04-
292 (in isoform 1)Ubiquitination-63.3721890473
292UbiquitinationFVEEQNLKDLRVWTS
HHHHCCHHHHHHHHH		63.3721906983
292 (in isoform 2)Ubiquitination-63.3721890473
302 (in isoform 1)Ubiquitination-37.6121890473
302UbiquitinationRVWTSQLKSTIQTAE
HHHHHHHHHHHHHHH		37.6122053931
302 (in isoform 2)Ubiquitination-37.6121890473
302UbiquitinationRVWTSQLKSTIQTAE
HHHHHHHHHHHHHHH		37.6121890473
306UbiquitinationSQLKSTIQTAEALRL
HHHHHHHHHHHHHCC		34.4421890473
319UbiquitinationRLPYEQWKALNEIDA
CCCHHHHHHHHHCCC		42.57-
352UbiquitinationYALREQDKYYYRYPT
HHCCCCCCCEECCCC		34.54-
353PhosphorylationALREQDKYYYRYPTG
HCCCCCCCEECCCCC		17.6424043423
354PhosphorylationLREQDKYYYRYPTGE
CCCCCCCEECCCCCC		6.2924043423
355PhosphorylationREQDKYYYRYPTGES
CCCCCCEECCCCCCC		10.6924043423
357PhosphorylationQDKYYYRYPTGESYQ
CCCCEECCCCCCCHH		6.7724043423
359PhosphorylationKYYYRYPTGESYQDL
CCEECCCCCCCHHHH		44.6524043423
362PhosphorylationYRYPTGESYQDLVQR
ECCCCCCCHHHHHHH		29.4624043423
363PhosphorylationRYPTGESYQDLVQRL
CCCCCCCHHHHHHHH		11.1824043423
366UbiquitinationTGESYQDLVQRLEPV
CCCCHHHHHHHHHHH		1.77-
403PhosphorylationLAYFLDKSAEEMPYL
HHHHHCCCHHHCCCC		40.3520068231
411AcetylationAEEMPYLKCPLHTVL
HHHCCCCCCCHHHHH		28.1525953088
411UbiquitinationAEEMPYLKCPLHTVL
HHHCCCCCCCHHHHH		28.15-
446PhosphorylationVCTHRERSEDAKKGP
HHCCHHHCHHHHCCC		34.7728348404
461PhosphorylationNPLMRRNSVTPLASP
CCCCCCCCCCCCCCC		26.0929255136
463PhosphorylationLMRRNSVTPLASPEP
CCCCCCCCCCCCCCC		16.6529255136
467PhosphorylationNSVTPLASPEPTKKP
CCCCCCCCCCCCCCC		37.1629255136
471PhosphorylationPLASPEPTKKPRINS
CCCCCCCCCCCCCCC		50.4629255136
478PhosphorylationTKKPRINSFEEHVAS
CCCCCCCCHHHHHHH		31.5028450419
485PhosphorylationSFEEHVASTSAALPS
CHHHHHHHHCCCCCC		23.0828450419
486PhosphorylationFEEHVASTSAALPSC
HHHHHHHHCCCCCCC		16.7928450419
487PhosphorylationEEHVASTSAALPSCL
HHHHHHHCCCCCCCC		14.7328450419
492PhosphorylationSTSAALPSCLPPEVP
HHCCCCCCCCCCCCC		29.1822210691
500PhosphorylationCLPPEVPTQLPGQNM
CCCCCCCCCCCCCCC		48.1622210691
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
269SPhosphorylationKinaseIKBKBO14920
GPS
461SPhosphorylationKinaseAMPKQ9Y478
Uniprot
461SPhosphorylationKinaseAMPKA1Q13131
PSP
461SPhosphorylationKinasePRKAA1P54645
GPS
461SPhosphorylationKinaseAKT1P31749
PSP
461SPhosphorylationKinasePRKACAP17612
GPS
461SPhosphorylationKinasePRKCAP17252
GPS
461SPhosphorylationKinaseMAPKAPK2P49137
PSP
461SPhosphorylationKinaseAMPK-FAMILY-GPS
461SPhosphorylationKinasePKA-FAMILY-GPS
461SPhosphorylationKinasePKC-FAMILY-GPS
461SPhosphorylationKinaseAMPK_GROUP-PhosphoELM
463TPhosphorylationKinaseCDK6Q00534
PSP
467SPhosphorylationKinaseCDK6Q00534
PSP
471TPhosphorylationKinasePKC-Uniprot
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:20080744
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F263_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 F263_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F264_HUMANPFKFB4physical
28514442
F262_HUMANPFKFB2physical
28514442
CLU_HUMANCLUHphysical
28514442
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 F263_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-461 AND SER-467, ANDMASS SPECTROMETRY.
"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-461; THR-463 ANDSER-467, AND MASS SPECTROMETRY.
"The stimulation of glycolysis by hypoxia in activated monocytes ismediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase.";
Marsin A.S., Bouzin C., Bertrand L., Hue L.;
J. Biol. Chem. 277:30778-30783(2002).
Cited for: PHOSPHORYLATION AT SER-461.

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