FBX42_HUMAN - dbPTM
FBX42_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBX42_HUMAN
UniProt AC Q6P3S6
Protein Name F-box only protein 42
Gene Name FBXO42
Organism Homo sapiens (Human).
Sequence Length 717
Subcellular Localization
Protein Description Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Specifically recognizes p53/TP53, promoting its ubiquitination and degradation..
Protein Sequence MASSSDSEDDSFMAVDQEETVLEGTMDQDEEPHPVLEAEETRHNRSMSELPEEVLEYILSFLSPYQEHKTAALVCKQWYRLIKGVAHQCYHGFMKAVQEGNIQWESRTYPYPGTPITQRFSHSACYYDANQSMYVFGGCTQSSCNAAFNDLWRLDLNSKEWIRPLASGSYPSPKAGATLVVYKDLLVLFGGWTRPSPYPLHQPERFFDEIHTYSPSKNWWNCIVTTHGPPPMAGHSSCVIDDKMIVFGGSLGSRQMSNDVWVLDLEQWAWSKPNISGPSPHPRGGQSQIVIDDATILILGGCGGPNALFKDAWLLHMHSGPWAWQPLKVENEEHGAPELWCHPACRVGQCVVVFSQAPSGRAPLSPSLNSRPSPISATPPALVPETREYRSQSPVRSMDEAPCVNGRWGTLRPRAQRQTPSGSREGSLSPARGDGSPILNGGSLSPGTAAVGGSSLDSPVQAISPSTPSAPEGYDLKIGLSLAPRRGSLPDQKDLRLGSIDLNWDLKPASSSNPMDGMDNRTVGGSMRHPPEQTNGVHTPPHVASALAGAVSPGALRRSLEAIKAMSSKGPSASAALSPPLGSSPGSPGSQSLSSGETVPIPRPGPAQGDGHSLPPIARRLGHHPPQSLNVGKPLYQSMNCKPMQMYVLDIKDTKEKGRVKWKVFNSSSVVGPPETSLHTVVQGRGELIIFGGLMDKKQNVKYYPKTNALYFVRAKR
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
70PhosphorylationSPYQEHKTAALVCKQ
CHHHHHHHHHHHHHH		21.0429457462
79PhosphorylationALVCKQWYRLIKGVA
HHHHHHHHHHHHHHH		7.9529457462
159UbiquitinationWRLDLNSKEWIRPLA
HEECCCCCCHHHHCC		56.8721906983
167PhosphorylationEWIRPLASGSYPSPK
CHHHHCCCCCCCCCC		35.6321406692
169PhosphorylationIRPLASGSYPSPKAG
HHHCCCCCCCCCCCC		31.2321406692
170PhosphorylationRPLASGSYPSPKAGA
HHCCCCCCCCCCCCC		15.9721406692
172PhosphorylationLASGSYPSPKAGATL
CCCCCCCCCCCCCEE		30.6921406692
178PhosphorylationPSPKAGATLVVYKDL
CCCCCCCEEEEECCE		21.1121406692
182PhosphorylationAGATLVVYKDLLVLF
CCCEEEEECCEEHHC		7.4221406692
262UbiquitinationQMSNDVWVLDLEQWA
CCCCCEEEEEHHHHH		2.7522817900
276UbiquitinationAWSKPNISGPSPHPR
HHCCCCCCCCCCCCC		51.8222817900
287PhosphorylationPHPRGGQSQIVIDDA
CCCCCCCCCEEECCC		25.75-
333UbiquitinationPLKVENEEHGAPELW
CEEECCCCCCCCCCE		60.2427667366
338UbiquitinationNEEHGAPELWCHPAC
CCCCCCCCCEECCCC		55.1322817900
365PhosphorylationPSGRAPLSPSLNSRP
CCCCCCCCCCCCCCC		16.0429255136
367PhosphorylationGRAPLSPSLNSRPSP
CCCCCCCCCCCCCCC		36.4923927012
370PhosphorylationPLSPSLNSRPSPISA
CCCCCCCCCCCCCCC		51.3523927012
373PhosphorylationPSLNSRPSPISATPP
CCCCCCCCCCCCCCC		33.4823927012
376PhosphorylationNSRPSPISATPPALV
CCCCCCCCCCCCCCC		29.4923927012
378PhosphorylationRPSPISATPPALVPE
CCCCCCCCCCCCCCC		24.0223927012
386PhosphorylationPPALVPETREYRSQS
CCCCCCCCCHHHCCC		23.8022199227
391PhosphorylationPETREYRSQSPVRSM
CCCCHHHCCCCCCCC		33.8228450419
393PhosphorylationTREYRSQSPVRSMDE
CCHHHCCCCCCCCCC		26.9823401153
397PhosphorylationRSQSPVRSMDEAPCV
HCCCCCCCCCCCCCC		30.7122199227
410PhosphorylationCVNGRWGTLRPRAQR
CCCCCCCCCCCCCCC		16.78-
427PhosphorylationPSGSREGSLSPARGD
CCCCCCCCCCCCCCC		22.4129255136
429PhosphorylationGSREGSLSPARGDGS
CCCCCCCCCCCCCCC		20.4323401153
481PhosphorylationYDLKIGLSLAPRRGS
CCCEEEEEECCCCCC		19.7824719451
488PhosphorylationSLAPRRGSLPDQKDL
EECCCCCCCCCCCCC		34.6123401153
493UbiquitinationRGSLPDQKDLRLGSI
CCCCCCCCCCCCCCE		67.1421906983
499PhosphorylationQKDLRLGSIDLNWDL
CCCCCCCCEECCCCC		19.9528348404
507UbiquitinationIDLNWDLKPASSSNP
EECCCCCCCCCCCCC		35.7421906983
534PhosphorylationMRHPPEQTNGVHTPP
CCCCCCCCCCCCCCH		32.0723927012
539PhosphorylationEQTNGVHTPPHVASA
CCCCCCCCCHHHHHH		35.7923401153
545PhosphorylationHTPPHVASALAGAVS
CCCHHHHHHHHCCCC		23.7923927012
552PhosphorylationSALAGAVSPGALRRS
HHHHCCCCHHHHHHH		19.6523401153
559PhosphorylationSPGALRRSLEAIKAM
CHHHHHHHHHHHHHH		24.9124719451
564UbiquitinationRRSLEAIKAMSSKGP
HHHHHHHHHHHCCCC		45.1221906983
564MethylationRRSLEAIKAMSSKGP
HHHHHHHHHHHCCCC		45.12-
564"N6,N6-dimethyllysine"RRSLEAIKAMSSKGP
HHHHHHHHHHHCCCC		45.12-
569UbiquitinationAIKAMSSKGPSASAA
HHHHHHCCCCCHHHH		68.4822817900
569"N6,N6-dimethyllysine"AIKAMSSKGPSASAA
HHHHHHCCCCCHHHH		68.48-
569MethylationAIKAMSSKGPSASAA
HHHHHHCCCCCHHHH		68.48-
572PhosphorylationAMSSKGPSASAALSP
HHHCCCCCHHHHCCC		43.4527690223
574PhosphorylationSSKGPSASAALSPPL
HCCCCCHHHHCCCCC		20.5727690223
578PhosphorylationPSASAALSPPLGSSP
CCHHHHCCCCCCCCC		21.5329449344
583PhosphorylationALSPPLGSSPGSPGS
HCCCCCCCCCCCCCC		40.8327690223
584PhosphorylationLSPPLGSSPGSPGSQ
CCCCCCCCCCCCCCC		31.3327690223
587PhosphorylationPLGSSPGSPGSQSLS
CCCCCCCCCCCCCCC		29.4927135362
590PhosphorylationSSPGSPGSQSLSSGE
CCCCCCCCCCCCCCC		21.7127690223
592PhosphorylationPGSPGSQSLSSGETV
CCCCCCCCCCCCCEE		31.7329449344
594PhosphorylationSPGSQSLSSGETVPI
CCCCCCCCCCCEECC		41.3629449344
595PhosphorylationPGSQSLSSGETVPIP
CCCCCCCCCCEECCC		46.0429449344
598PhosphorylationQSLSSGETVPIPRPG
CCCCCCCEECCCCCC		34.8029449344
698AcetylationFGGLMDKKQNVKYYP
ECCCCCCCCCCCCCC		42.7219822971
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 FBX42_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBX42_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 FBX42_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
19509332
CUL1_HUMANCUL1physical
19509332
SKP1_HUMANSKP1physical
19509332
RBX1_HUMANRBX1physical
19509332
SUH_HUMANRBPJphysical
28514442
GSK3A_HUMANGSK3Aphysical
28514442
CUL1_HUMANCUL1physical
28514442
RAB28_HUMANRAB28physical
28514442
SKP1_HUMANSKP1physical
28514442
CCDC6_HUMANCCDC6physical
28514442
CYTN_HUMANCST1physical
28514442
KLK6_HUMANKLK6physical
28514442
P53_HUMANTP53physical
21127074
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 FBX42_HUMAN

loading...

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-373, 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-365; SER-373 ANDTHR-378, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory