dbPTM

FBX4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FBX4_HUMAN
UniProt AC	Q9UKT5
Protein Name	F-box only protein 4
Gene Name	FBXO4
Organism	Homo sapiens (Human).
Sequence Length	387
Subcellular Localization	Cytoplasm.
Protein Description	Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1..
Protein Sequence	MAGSEPRSGTNSPPPPFSDWGRLEAAILSGWKTFWQSVSKERVARTTSREEVDEAASTLTRLPIDVQLYILSFLSPHDLCQLGSTNHYWNETVRDPILWRYFLLRDLPSWSSVDWKSLPDLEILKKPISEVTDGAFFDYMAVYRMCCPYTRRASKSSRPMYGAVTSFLHSLIIQNEPRFAMFGPGLEELNTSLVLSLMSSEELCPTAGLPQRQIDGIGSGVNFQLNNQHKFNILILYSTTRKERDRAREEHTSAVNKMFSRHNEGDDQQGSRYSVIPQIQKVCEVVDGFIYVANAEAHKRHEWQDEFSHIMAMTDPAFGSSGRPLLVLSCISQGDVKRMPCFYLAHELHLNLLNHPWLVQDTEAETLTGFLNGIEWILEEVESKRAR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAGSEPRSGTN ----CCCCCCCCCCC	34.58	26074081
8	Phosphorylation	MAGSEPRSGTNSPPP CCCCCCCCCCCCCCC	61.76	23401153
10	Phosphorylation	GSEPRSGTNSPPPPF CCCCCCCCCCCCCCC	33.50	30266825
12	Phosphorylation	EPRSGTNSPPPPFSD CCCCCCCCCCCCCCH	38.32	22167270
18	Phosphorylation	NSPPPPFSDWGRLEA CCCCCCCCHHHHHHH	37.92	23403867
37	Phosphorylation	GWKTFWQSVSKERVA CHHHHHHHHCHHHHC	20.96	23186163
40	Ubiquitination	TFWQSVSKERVARTT HHHHHHCHHHHCCCC	47.59	-
46	Phosphorylation	SKERVARTTSREEVD CHHHHCCCCCHHHHH	21.27	23401153
47	Phosphorylation	KERVARTTSREEVDE HHHHCCCCCHHHHHH	21.89	21712546
48	Phosphorylation	ERVARTTSREEVDEA HHHCCCCCHHHHHHH	36.76	23911959
57	Phosphorylation	EEVDEAASTLTRLPI HHHHHHHHHHHCCCH	30.88	28060719
58	Phosphorylation	EVDEAASTLTRLPID HHHHHHHHHHCCCHH	27.67	28060719
60	Phosphorylation	DEAASTLTRLPIDVQ HHHHHHHHCCCHHHH	30.19	28060719
144	Methylation	FDYMAVYRMCCPYTR HHHHHHHHHHCCCHH	12.69	-
238	Phosphorylation	FNILILYSTTRKERD EEEEEEEECCHHHHH	21.62	17924679
239	Phosphorylation	NILILYSTTRKERDR EEEEEEECCHHHHHH	19.64	17924679
240	Phosphorylation	ILILYSTTRKERDRA EEEEEECCHHHHHHH	33.53	17924679
252	Phosphorylation	DRAREEHTSAVNKMF HHHHHHHHHHHHHHH	22.97	22210691
253	Phosphorylation	RAREEHTSAVNKMFS HHHHHHHHHHHHHHH	31.93	22210691
257	Ubiquitination	EHTSAVNKMFSRHNE HHHHHHHHHHHHCCC	34.42	-
273	Phosphorylation	DDQQGSRYSVIPQIQ CCCCCCCCCHHHHHH	14.69	28674419
274	Phosphorylation	DQQGSRYSVIPQIQK CCCCCCCCHHHHHHH	16.68	28555341
343	Phosphorylation	VKRMPCFYLAHELHL HHHCCHHHHHHHHHH	15.08	-

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
12	S	Phosphorylation	Kinase	GSK3B	P49841	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
12	S	Phosphorylation	18598945
Phosphorylation at Ser-12 promotes homodimerization and is necessary for optimal ubiquitin ligase activity towards CCND1.
12	S	Phosphorylation	18598945
Phosphorylation at Ser-12 varies during the cell cycle.
12	S	ubiquitylation	18598945
Phosphorylation at Ser-12 promotes homodimerization and is necessary for optimal ubiquitin ligase activity towards CCND1.

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 FBX4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUL1_HUMAN	CUL1	physical	17353931
SKP1_HUMAN	SKP1	physical	17353931
NEDD8_HUMAN	NEDD8	physical	17353931
CUL1_HUMAN	CUL1	physical	10531035
SKP1_HUMAN	SKP1	physical	10531035
TERF1_HUMAN	TERF1	physical	16275645
TERF1_HUMAN	TERF1	physical	20159592
FBX4_HUMAN	FBXO4	physical	20181953
CCND1_HUMAN	CCND1	physical	17081987
TERF1_HUMAN	TERF1	physical	20181953
1433E_HUMAN	YWHAE	physical	21242966
FBX4_HUMAN	FBXO4	physical	21242966
CCND1_HUMAN	CCND1	physical	21242966
SKP1_HUMAN	SKP1	physical	16278047
CUL1_HUMAN	CUL1	physical	16278047
CUL1_HUMAN	CUL1	physical	22013077
TERF1_HUMAN	TERF1	physical	24019069
SKP1_HUMAN	SKP1	physical	24019069
CUL1_HUMAN	CUL1	physical	22268729
CUL1_HUMAN	CUL1	physical	23319600
SKP1_HUMAN	SKP1	physical	26087183
CCND1_HUMAN	CCND1	physical	19767775
SKP1_HUMAN	SKP1	physical	28514442
CUL1_HUMAN	CUL1	physical	28514442
DCAM_HUMAN	AMD1	physical	28514442
AP1B1_HUMAN	AP1B1	physical	28514442
AP1M1_HUMAN	AP1M1	physical	28514442
ESPL1_HUMAN	ESPL1	physical	28514442
TERF1_HUMAN	TERF1	physical	28216227
FXR1_MOUSE	Fxr1	physical	29142209
FMR1_HUMAN	FMR1	physical	29142209
FXR1_HUMAN	FXR1	physical	29142209
SKP1_HUMAN	SKP1	physical	29142209
CCND1_HUMAN	CCND1	physical	29142209

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FBX4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-12, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-12, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase andcontribute to cyclin D1 overexpression in human cancer."; Barbash O., Zamfirova P., Lin D.I., Chen X., Yang K., Nakagawa H.,Lu F., Rustgi A.K., Diehl J.A.; Cancer Cell 14:68-78(2008). Cited for: FUNCTION, SUBUNIT, INTERACTION WITH SKP1, PHOSPHORYLATION AT SER-12,VARIANTS ARG-8; LEU-12; SER-13; GLN-23 AND THR-76, ANDCHARACTERIZATION OF VARIANTS LEU-12; SER-13 AND GLN-23.	18598945 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238; THR-239 ANDTHR-240, AND MASS SPECTROMETRY.	17924679 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.	15302935 [Abstract]

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