FBX28_HUMAN - dbPTM
FBX28_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBX28_HUMAN
UniProt AC Q9NVF7
Protein Name F-box only protein 28
Gene Name FBXO28
Organism Homo sapiens (Human).
Sequence Length 368
Subcellular Localization Chromosome, centromere, kinetochore .
Protein Description Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation..
Protein Sequence MAAAAEERMAEEGGGGQGDGGSSLASGSTQRQPPPPAPQHPQPGSQALPAPALAPDQLPQNNTLVALPIVAIENILSFMSYDEISQLRLVCKRMDLVCQRMLNQGFLKVERYHNLCQKQVKAQLPRRESERRNHSLARHADILAAVETRLSLLNMTFMKYVDSNLCCFIPGKVIDEIYRVLRYVNSTRAPQRAHEVLQELRDISSMAMEYFDEKIVPILKRKLPGSDVSGRLMGSPPVPGPSAALTTMQLFSKQNPSRQEVTKLQQQVKTNGAGVTVLRREISELRTKVQEQQKQLQDQDQKLLEQTQIIGEQNARLAELERKLREVMESAVGNSSGSGQNEESPRKRKKATEAIDSLRKSKRLRNRK
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
22PhosphorylationGGQGDGGSSLASGST
CCCCCCCCCCCCCCC		27.9229116813
29PhosphorylationSSLASGSTQRQPPPP
CCCCCCCCCCCCCCC		31.1529116813
108UbiquitinationMLNQGFLKVERYHNL
HHHCCCCHHHHHHHH		39.5321890473
118UbiquitinationRYHNLCQKQVKAQLP
HHHHHHHHHHHHHCC		56.9429967540
129PhosphorylationAQLPRRESERRNHSL
HHCCHHHHHHHHHHH		34.2922817900
178PhosphorylationGKVIDEIYRVLRYVN
HHHHHHHHHHHHHHC		7.8223612710
210PhosphorylationISSMAMEYFDEKIVP
HHHHHHHHHHHHHHH		11.84-
220UbiquitinationEKIVPILKRKLPGSD
HHHHHHHCCCCCCCC		48.4827667366
226PhosphorylationLKRKLPGSDVSGRLM
HCCCCCCCCCCCCCC		32.6624719451
229PhosphorylationKLPGSDVSGRLMGSP
CCCCCCCCCCCCCCC		24.1624719451
235PhosphorylationVSGRLMGSPPVPGPS
CCCCCCCCCCCCCCC		16.4426055452
242PhosphorylationSPPVPGPSAALTTMQ
CCCCCCCCHHHHHHH		31.8922199227
246PhosphorylationPGPSAALTTMQLFSK
CCCCHHHHHHHHHHC		18.5922199227
247PhosphorylationGPSAALTTMQLFSKQ
CCCHHHHHHHHHHCC		12.0822210691
252PhosphorylationLTTMQLFSKQNPSRQ
HHHHHHHHCCCCCHH		41.7622210691
263UbiquitinationPSRQEVTKLQQQVKT
CCHHHHHHHHHHHHH		49.8523000965
269UbiquitinationTKLQQQVKTNGAGVT
HHHHHHHHHCCCCHH		31.7523000965
270PhosphorylationKLQQQVKTNGAGVTV
HHHHHHHHCCCCHHH		39.7720068231
276PhosphorylationKTNGAGVTVLRREIS
HHCCCCHHHHHHHHH		16.9527174698
283PhosphorylationTVLRREISELRTKVQ
HHHHHHHHHHHHHHH		26.3124719451
294UbiquitinationTKVQEQQKQLQDQDQ
HHHHHHHHHHHHHHH		53.3121906983
302UbiquitinationQLQDQDQKLLEQTQI
HHHHHHHHHHHHHHH		64.4329967540
330PhosphorylationKLREVMESAVGNSSG
HHHHHHHHHHCCCCC		15.3428450419
335PhosphorylationMESAVGNSSGSGQNE
HHHHHCCCCCCCCCC		30.1023927012
336PhosphorylationESAVGNSSGSGQNEE
HHHHCCCCCCCCCCC		40.7623927012
338PhosphorylationAVGNSSGSGQNEESP
HHCCCCCCCCCCCCH		38.8723401153
344PhosphorylationGSGQNEESPRKRKKA
CCCCCCCCHHHHHHH		24.6729255136
347UbiquitinationQNEESPRKRKKATEA
CCCCCHHHHHHHHHH		72.4621906983
349UbiquitinationEESPRKRKKATEAID
CCCHHHHHHHHHHHH		50.2022817900
350UbiquitinationESPRKRKKATEAIDS
CCHHHHHHHHHHHHH		65.6522817900
352PhosphorylationPRKRKKATEAIDSLR
HHHHHHHHHHHHHHH		34.5326074081
357PhosphorylationKATEAIDSLRKSKRL
HHHHHHHHHHHHHHH		24.7825159151
361PhosphorylationAIDSLRKSKRLRNRK
HHHHHHHHHHHHHCC		19.30-
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
-KUbiquitinationE3 ubiquitin ligaseFBXO28Q9NVF7
PMID:31678254
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBX28_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 FBX28_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSB1_HUMANPSMB1physical
22939629
GLPK_HUMANGKphysical
21988832
SDCB2_HUMANSDCBP2physical
25416956
PKHF2_HUMANPLEKHF2physical
25416956
GOGA2_HUMANGOLGA2physical
21516116
ARHG7_HUMANARHGEF7physical
28514442
TMCC3_HUMANTMCC3physical
28514442
EMAL4_HUMANEML4physical
28514442
GIT2_HUMANGIT2physical
28514442
GIT1_HUMANGIT1physical
28514442
NEDD1_HUMANNEDD1physical
28514442
TRAF7_HUMANTRAF7physical
28514442
PAK1_HUMANPAK1physical
28514442
TRAF5_HUMANTRAF5physical
28514442
PAK2_HUMANPAK2physical
28514442
CKAP4_HUMANCKAP4physical
28514442
IKIP_HUMANIKBIPphysical
28514442
SUN1_HUMANSUN1physical
28514442
GOPC_HUMANGOPCphysical
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 FBX28_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-344, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASSSPECTROMETRY.

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