F261_HUMAN - dbPTM
F261_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F261_HUMAN
UniProt AC P16118
Protein Name 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
Gene Name PFKFB1
Organism Homo sapiens (Human).
Sequence Length 471
Subcellular Localization
Protein Description Synthesis and degradation of fructose 2,6-bisphosphate..
Protein Sequence MSPEMGELTQTRLQKIWIPHSSGSSRLQRRRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAVSYKNYEFFLPDNMEALQIRKQCALAALKDVHNYLSHEEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPGIIAENIRQVKLGSPDYIDCDREKVLEDFLKRIECYEVNYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHIQSRTVYYLMNIHVTPRSIYLCRHGESELNIRGRIGGDSGLSVRGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKSSDELPYLKCPLHTVLKLTPVAYGCKVESIYLNVEAVNTHREKPENVDITREPEEALDTVPAHY
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------MSPEMGELT
------CCHHHHHCC
29.57-
2Phosphorylation------MSPEMGELT
------CCHHHHHCC
29.5720166139
9PhosphorylationSPEMGELTQTRLQKI
CHHHHHCCCHHHHHH
24.4829083192
11PhosphorylationEMGELTQTRLQKIWI
HHHHCCCHHHHHHCC
28.2829083192
21PhosphorylationQKIWIPHSSGSSRLQ
HHHCCCCCCCCHHHH
30.9222210691
22PhosphorylationKIWIPHSSGSSRLQR
HHCCCCCCCCHHHHH
39.3922210691
24PhosphorylationWIPHSSGSSRLQRRR
CCCCCCCCHHHHHHC
17.7724275569
33PhosphorylationRLQRRRGSSIPQFTN
HHHHHCCCCCCCCCC
24.2324275569
34PhosphorylationLQRRRGSSIPQFTNS
HHHHCCCCCCCCCCC
40.9028348404
39PhosphorylationGSSIPQFTNSPTMVI
CCCCCCCCCCCCEEE
29.5524275569
133PhosphorylationHVAVFDATNTTRERR
CEEEEECCCCHHHHH
34.6426437602
141PhosphorylationNTTRERRSLILQFAK
CCHHHHHHHHHHHHH
26.44-
200PhosphorylationFLKRIECYEVNYQPL
HHHHCCEEECCCCCC
15.32-
204PhosphorylationIECYEVNYQPLDEEL
CCEEECCCCCCCHHH
19.38-
227PhosphorylationIFDVGTRYMVNRVQD
EEECCHHHHHHHHHH
12.7825884760
242PhosphorylationHIQSRTVYYLMNIHV
HHHHCCEEEEEECCC
7.11-
243PhosphorylationIQSRTVYYLMNIHVT
HHHCCEEEEEECCCC
8.6425884760
262PhosphorylationYLCRHGESELNIRGR
EEECCCCCEEEECCE
52.5624719451
277PhosphorylationIGGDSGLSVRGKQYA
ECCCCCCCCCCHHHH
17.1924719451
297PhosphorylationFIQSQGISSLKVWTS
HHHHCCCCHHHHHHH
36.1224719451
299UbiquitinationQSQGISSLKVWTSHM
HHCCCCHHHHHHHHH
4.07-
364UbiquitinationKYRYRYPKGESYEDL
CCCCCCCCCCCHHHH
67.39-
438PhosphorylationGCKVESIYLNVEAVN
CCEEEEEEEEEEEHH
11.0819651622

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
33SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F261_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 F261_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
F261_HUMANPFKFB1physical
25416956

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 F261_HUMAN

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Related Literatures of Post-Translational Modification

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