F264_HUMAN - dbPTM
F264_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F264_HUMAN
UniProt AC Q16877
Protein Name 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4
Gene Name PFKFB4
Organism Homo sapiens (Human).
Sequence Length 469
Subcellular Localization
Protein Description Synthesis and degradation of fructose 2,6-bisphosphate..
Protein Sequence MASPRELTQNPLKKIWMPYSNGRPALHACQRGVCMTNCPTLIVMVGLPARGKTYISKKLTRYLNWIGVPTREFNVGQYRRDVVKTYKSFEFFLPDNEEGLKIRKQCALAALRDVRRFLSEEGGHVAVFDATNTTRERRATIFNFGEQNGYKTFFVESICVDPEVIAANIVQVKLGSPDYVNRDSDEATEDFMRRIECYENSYESLDEDLDRDLSYIKIMDVGQSYVVNRVADHIQSRIVYYLMNIHVTPRSIYLCRHGESELNLKGRIGGDPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEALGVPYEQWKVLNEIDAGVCEEMTYEEIQDNYPLEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKAAEQLPYLKCPLHTVLKLTPVAYGCKVESIFLNVAAVNTHRDRPQNVDISRPPEEALVTVPAHQ
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
3Phosphorylation-----MASPRELTQN
-----CCCHHHHCCC
24.1622199227
8PhosphorylationMASPRELTQNPLKKI
CCCHHHHCCCCCHHC
22.8829514088
13UbiquitinationELTQNPLKKIWMPYS
HHCCCCCHHCCCCCC
43.39-
87UbiquitinationRDVVKTYKSFEFFLP
HHHHHHHCEEEEECC
54.63-
101UbiquitinationPDNEEGLKIRKQCAL
CCCHHHHHHHHHHHH
51.85-
104UbiquitinationEEGLKIRKQCALAAL
HHHHHHHHHHHHHHH
53.88-
119PhosphorylationRDVRRFLSEEGGHVA
HHHHHHHHHCCCEEE
30.78-
131PhosphorylationHVAVFDATNTTRERR
EEEEEECCCCCCCCE
34.6424275569
150PhosphorylationNFGEQNGYKTFFVES
ECCCCCCEEEEEEEE
17.8822817900
176PhosphorylationIVQVKLGSPDYVNRD
EEEEECCCCCCCCCC
25.6521815630
184PhosphorylationPDYVNRDSDEATEDF
CCCCCCCCHHHHHHH
33.8328348404
214PhosphorylationEDLDRDLSYIKIMDV
CHHHCCCCEEEEEEC
29.1524719451
265UbiquitinationGESELNLKGRIGGDP
CCCEECCCCCCCCCC
45.10-
275PhosphorylationIGGDPGLSPRGREFA
CCCCCCCCHHHHHHH
20.6130266825
283UbiquitinationPRGREFAKSLAQFIS
HHHHHHHHHHHHHHC
51.85-
295UbiquitinationFISDQNIKDLKVWTS
HHCCCCHHHHHHHHH
65.64-
305UbiquitinationKVWTSQMKRTIQTAE
HHHHHHHHHHHHHHH
38.46-
362UbiquitinationKYRYRYPKGESYEDL
CCCCCCCCCCCHHHH
67.39-
444PhosphorylationLNVAAVNTHRDRPQN
EEEEEHHCCCCCCCC
16.22-

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
444TPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F264_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 F264_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of F264_HUMAN !!

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 F264_HUMAN

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Related Literatures of Post-Translational Modification

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