FBX9_HUMAN - dbPTM
FBX9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBX9_HUMAN
UniProt AC Q9UK97
Protein Name F-box only protein 9
Gene Name FBXO9
Organism Homo sapiens (Human).
Sequence Length 447
Subcellular Localization Cytoplasm .
Protein Description Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTORC1 is inactivated to restrain cell growth and protein translation, while mTORC2 is activated due to the relief of feedback inhibition by mTORC1..
Protein Sequence MPDIIWVFPPQAEAEEDCHSDTVRADDDEENESPAETDLQAQLQMFRAQWMFELAPGVSSSNLENRPCRAARGSLQKTSADTKGKQEQAKEEKARELFLKAVEEEQNGALYEAIKFYRRAMQLVPDIEFKITYTRSPDGDGVGNSYIEDNDDDSKMADLLSYFQQQLTFQESVLKLCQPELESSQIHISVLPMEVLMYIFRWVVSSDLDLRSLEQLSLVCRGFYICARDPEIWRLACLKVWGRSCIKLVPYTSWREMFLERPRVRFDGVYISKTTYIRQGEQSLDGFYRAWHQVEYYRYIRFFPDGHVMMLTTPEEPQSIVPRLRTRNTRTDAILLGHYRLSQDTDNQTKVFAVITKKKEEKPLDYKYRYFRRVPVQEADQSFHVGLQLCSSGHQRFNKLIWIHHSCHITYKSTGETAVSAFEIDKMYTPLFFARVRSYTAFSERPL
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
10 (in isoform 2)Phosphorylation-34.2524719451
20PhosphorylationEAEEDCHSDTVRADD
HHCCCCCCCCCCCCC
41.1123663014
33UbiquitinationDDDEENESPAETDLQ
CCCCCCCCCHHHHHH
40.7829967540
33PhosphorylationDDDEENESPAETDLQ
CCCCCCCCCHHHHHH
40.7827732954
37PhosphorylationENESPAETDLQAQLQ
CCCCCHHHHHHHHHH
44.0826471730
41UbiquitinationPAETDLQAQLQMFRA
CHHHHHHHHHHHHHH
21.2424816145
67UbiquitinationSSNLENRPCRAARGS
CCCCCCCCCHHHHHC
24.4329967540
71 (in isoform 3)Ubiquitination-9.3021890473
71UbiquitinationENRPCRAARGSLQKT
CCCCCHHHHHCCCCC
9.3021890473
74PhosphorylationPCRAARGSLQKTSAD
CCHHHHHCCCCCCCC
23.2928102081
75UbiquitinationCRAARGSLQKTSADT
CHHHHHCCCCCCCCC
7.2424816145
77UbiquitinationAARGSLQKTSADTKG
HHHHCCCCCCCCCCC
50.1429967540
85UbiquitinationTSADTKGKQEQAKEE
CCCCCCCHHHHHHHH
52.8224816145
105 (in isoform 2)Ubiquitination-35.5221890473
105UbiquitinationFLKAVEEEQNGALYE
HHHHHHHHHCCHHHH
35.5221890473
111PhosphorylationEEQNGALYEAIKFYR
HHHCCHHHHHHHHHH
11.6321945579
115 (in isoform 1)Ubiquitination-43.3121890473
115UbiquitinationGALYEAIKFYRRAMQ
CHHHHHHHHHHHHHH
43.3121890473
115AcetylationGALYEAIKFYRRAMQ
CHHHHHHHHHHHHHH
43.3118603043
115UbiquitinationGALYEAIKFYRRAMQ
CHHHHHHHHHHHHHH
43.3122817900
121SulfoxidationIKFYRRAMQLVPDIE
HHHHHHHHHHCCCEE
2.7621406390
130AcetylationLVPDIEFKITYTRSP
HCCCEEEEEEEEECC
22.7318603053
132PhosphorylationPDIEFKITYTRSPDG
CCEEEEEEEEECCCC
21.3028450419
133PhosphorylationDIEFKITYTRSPDGD
CEEEEEEEEECCCCC
12.0228450419
134PhosphorylationIEFKITYTRSPDGDG
EEEEEEEEECCCCCC
18.9328450419
136PhosphorylationFKITYTRSPDGDGVG
EEEEEEECCCCCCCC
21.3925159151
145PhosphorylationDGDGVGNSYIEDNDD
CCCCCCCCCCCCCCC
22.8923186163
195 (in isoform 2)Phosphorylation-2.7924719451
205PhosphorylationYIFRWVVSSDLDLRS
HHHHHHHCCCCCCCC
14.4424719451
207 (in isoform 2)Phosphorylation-36.3724719451
217PhosphorylationLRSLEQLSLVCRGFY
CCCHHHHHHHHHEEE
20.6024719451
266 (in isoform 2)Phosphorylation-9.7924719451
276PhosphorylationVYISKTTYIRQGEQS
EEEECCEEEEECCCC
10.1924719451
296PhosphorylationRAWHQVEYYRYIRFF
HHHHHHEEEEEEEEC
8.39-
297PhosphorylationAWHQVEYYRYIRFFP
HHHHHEEEEEEEECC
5.39-
345PhosphorylationHYRLSQDTDNQTKVF
EEEECCCCCCCEEEE
29.2522210691
349PhosphorylationSQDTDNQTKVFAVIT
CCCCCCCEEEEEEEE
35.1222210691
429PhosphorylationFEIDKMYTPLFFARV
EEECCCCCCCHHHHH
15.2630631047

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 FBX9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBX9_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 FBX9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKP1_HUMANSKP1physical
17463251
EF2_HUMANEEF2physical
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 FBX9_HUMAN

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Related Literatures of Post-Translational Modification

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