FBX10_HUMAN - dbPTM
FBX10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBX10_HUMAN
UniProt AC Q9UK96
Protein Name F-box only protein 10
Gene Name FBXO10
Organism Homo sapiens (Human).
Sequence Length 956
Subcellular Localization Cytoplasm .
Protein Description Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an antiapoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2..
Protein Sequence MEAGGLPLELWRMILAYLHLPDLGRCSLVCRAWYELILSLDSTRWRQLCLGCTECRHPNWPNQPDVEPESWREAFKQHYLASKTWTKNALDLESSICFSLFRRRRERRTLSVGPGREFDSLGSALAMASLYDRIVLFPGVYEEQGEIILKVPVEIVGQGKLGEVALLASIDQHCSTTRLCNLVFTPAWFSPIMYKTTSGHVQFDNCNFENGHIQVHGPGTCQVKFCTFKNTHIFLHNVPLCVLENCEFVGSENNSVTVEGHPSADKNWAYKYLLGLIKSSPTFLPTEDSDFLMSLDLESRDQAWSPKTCDIVIEGSQSPTSPASSSPKPGSKAGSQEAEVGSDGERVAQTPDSSDGGLSPSGEDEDEDQLMYRLSYQVQGPRPVLGGSFLGPPLPGASIQLPSCLVLNSLQQELQKDKEAMALANSVQGCLIRKCLFRDGKGGVFVCSHGRAKMEGNIFRNLTYAVRCIHNSKIIMLRNDIYRCRASGIFLRLEGGGLIAGNNIYHNAEAGVDIRKKSNPLILCNQIHHGLRSGIVVLGNGKGIIRNNQIFSNKEAGIYILYHGNPVVSGNHIFKGRAAGIAVNENGKGLITENVIRENQWGGVDIRRGGIPVLRSNLICFGYSDGVVVGDEGKGLIEGNTIYANKGCGVWMMSSSLPHVTSNHVSYNGLYGVAVFSQKDGSSELPRGHRAQENFSEDGDAILWETELEKEDDPLRRPITIALVESNSINHNGASGLYVQSSEALHVITNVIHANGDRGITVAQSSQPTRVANNSISCNRQSGVKVEAQCKVELRGNGIYDNRGHGIITKGDSTIVIENDIIGNRGSGLQLLPRSDTKVIKNRIHSFRAYGIAVRGRAKALVQENIIFQGKTSKTIFQQISNNRECIMQNNKFLVFKKKSDTWRLVNPPARPHLENSLRRPSAAHNGQKVTAMATRITARVEGGYHSNRSVFCTIL
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
27PhosphorylationLPDLGRCSLVCRAWY
CCCCCHHHHHHHHHH
23.60-
43PhosphorylationLILSLDSTRWRQLCL
HHHCCCCCHHHHHHC
33.64-
94PhosphorylationKNALDLESSICFSLF
CCCHHHHHHHHHHHH
32.09-
109PhosphorylationRRRRERRTLSVGPGR
HHHHHCCCEECCCCC
29.61-
305PhosphorylationESRDQAWSPKTCDIV
CCCCCCCCCCCCCEE
21.3824719451
316PhosphorylationCDIVIEGSQSPTSPA
CCEEEECCCCCCCCC
18.0721712546
318PhosphorylationIVIEGSQSPTSPASS
EEEECCCCCCCCCCC
31.6621712546
320PhosphorylationIEGSQSPTSPASSSP
EECCCCCCCCCCCCC
53.2221712546
321PhosphorylationEGSQSPTSPASSSPK
ECCCCCCCCCCCCCC
23.1221712546
324PhosphorylationQSPTSPASSSPKPGS
CCCCCCCCCCCCCCC
34.4321712546
325PhosphorylationSPTSPASSSPKPGSK
CCCCCCCCCCCCCCC
53.4121712546
326PhosphorylationPTSPASSSPKPGSKA
CCCCCCCCCCCCCCC
34.1524719451
331PhosphorylationSSSPKPGSKAGSQEA
CCCCCCCCCCCCCEE
28.0523312004
342PhosphorylationSQEAEVGSDGERVAQ
CCEEEECCCCCEEEC
47.8429255136
463PhosphorylationGNIFRNLTYAVRCIH
CCHHHHHHHHHHHHH
17.00-
559PhosphorylationSNKEAGIYILYHGNP
CCCCCCEEEEECCCC
5.5127050516
562PhosphorylationEAGIYILYHGNPVVS
CCCEEEEECCCCEEC
9.7227050516
775PhosphorylationPTRVANNSISCNRQS
CCEEECCCEECCCCC
18.7121712546
777PhosphorylationRVANNSISCNRQSGV
EEECCCEECCCCCCC
12.7421712546
855MethylationRAYGIAVRGRAKALV
HHHEEEECCHHHHHH
21.62-

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 FBX10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBX10_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 FBX10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL1_HUMANCUL1physical
23319600

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FBX10_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP