FBXW2_HUMAN - dbPTM
FBXW2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBXW2_HUMAN
UniProt AC Q9UKT8
Protein Name F-box/WD repeat-containing protein 2
Gene Name FBXW2
Organism Homo sapiens (Human).
Sequence Length 454
Subcellular Localization
Protein Description Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex..
Protein Sequence MERKDFETWLDNISVTFLSLTDLQKNETLDHLISLSGAVQLRHLSNNLETLLKRDFLKLLPLELSFYLLKWLDPQTLLTCCLVSKQWNKVISACTEVWQTACKNLGWQIDDSVQDALHWKKVYLKAILRMKQLEDHEAFETSSLIGHSARVYALYYKDGLLCTGSDDLSAKLWDVSTGQCVYGIQTHTCAAVKFDEQKLVTGSFDNTVACWEWSSGARTQHFRGHTGAVFSVDYNDELDILVSGSADFTVKVWALSAGTCLNTLTGHTEWVTKVVLQKCKVKSLLHSPGDYILLSADKYEIKIWPIGREINCKCLKTLSVSEDRSICLQPRLHFDGKYIVCSSALGLYQWDFASYDILRVIKTPEIANLALLGFGDIFALLFDNRYLYIMDLRTESLISRWPLPEYRKSKRGSSFLAGEASWLNGLDGHNDTGLVFATSMPDHSIHLVLWKEHG
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
28PhosphorylationTDLQKNETLDHLISL
HHCCCCCCHHHHHHH
47.0524719451
45PhosphorylationAVQLRHLSNNLETLL
HHHHHHHHHCHHHHH
19.9726074081
50PhosphorylationHLSNNLETLLKRDFL
HHHHCHHHHHHHHHH
40.3226074081
120UbiquitinationVQDALHWKKVYLKAI
HHHHHHHHHHHHHHH
22.93-
125UbiquitinationHWKKVYLKAILRMKQ
HHHHHHHHHHHHHHH
18.72-
131UbiquitinationLKAILRMKQLEDHEA
HHHHHHHHHCCCCCC
45.34-
278UbiquitinationVTKVVLQKCKVKSLL
HHHHHHHHCCHHHHH
31.68-
298AcetylationYILLSADKYEIKIWP
EEEEECCCEEEEEEE
44.4919608861
313UbiquitinationIGREINCKCLKTLSV
CCCEEECEEECEEEE
37.81-
338PhosphorylationRLHFDGKYIVCSSAL
CCEECCEEEEEECCC
12.24-
386PhosphorylationALLFDNRYLYIMDLR
HHHCCCCEEEEEECC
15.3129759185
388PhosphorylationLFDNRYLYIMDLRTE
HCCCCEEEEEECCCC
5.8129759185
396PhosphorylationIMDLRTESLISRWPL
EEECCCCHHHHCCCC
30.3224719451
399PhosphorylationLRTESLISRWPLPEY
CCCCHHHHCCCCHHH
33.3224719451

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 FBXW2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBXW2_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 FBXW2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL1_HUMANCUL1physical
10531035
SKP1_HUMANSKP1physical
10531035
SKP1_HUMANSKP1physical
22388891
RBX1_HUMANRBX1physical
19398581
CUL1_HUMANCUL1physical
19398581
SKP1_HUMANSKP1physical
19398581
REST_HUMANRESTphysical
18354482
BTG1_HUMANBTG1physical
22975506
BTG2_HUMANBTG2physical
22975506
SKP1_HUMANSKP1physical
15070733
CUL1_HUMANCUL1physical
14603323
RACK1_HUMANGNB2L1physical
23651062
GCM1_HUMANGCM1physical
23651062
CUL1_HUMANCUL1physical
22268729
EP300_HUMANEP300physical
19297328
CUL1_HUMANCUL1physical
25515538
SKP1_HUMANSKP1physical
26087183
FBW1A_HUMANBTRCphysical
28090088
SKP2_HUMANSKP2physical
28090088
CUL1_HUMANCUL1physical
28090088
RBX1_HUMANRBX1physical
28090088

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 FBXW2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND MASS SPECTROMETRY.

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