dbPTM

FBX5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FBX5_HUMAN
UniProt AC	Q9UKT4
Protein Name	F-box only protein 5
Gene Name	FBXO5
Organism	Homo sapiens (Human).
Sequence Length	447
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. In interphase, localizes in a punctate manner in the nucleus and cytoplasm with some perinuclear concentration. In mitotic cells, localizes throughout the cell, particularly at the spindle.
Protein Description	Regulates progression through early mitosis by inhibiting the anaphase promoting complex/cyclosome (APC). Binds to the APC activators CDC20 and FZR1/CDH1 to prevent APC activation. Can also bind directly to the APC to inhibit substrate-binding..
Protein Sequence	MSRRPCSCALRPPRCSCSASPSAVTAAGRPRPSDSCKEESSTLSVKMKCDFNCNHVHSGLKLVKPDDIGRLVSYTPAYLEGSCKDCIKDYERLSCIGSPIVSPRIVQLETESKRLHNKENQHVQQTLNSTNEIEALETSRLYEDSGYSSFSLQSGLSEHEEGSLLEENFGDSLQSCLLQIQSPDQYPNKNLLPVLHFEKVVCSTLKKNAKRNPKVDREMLKEIIARGNFRLQNIIGRKMGLECVDILSELFRRGLRHVLATILAQLSDMDLINVSKVSTTWKKILEDDKGAFQLYSKAIQRVTENNNKFSPHASTREYVMFRTPLASVQKSAAQTSLKKDAQTKLSNQGDQKGSTYSRHNEFSEVAKTLKKNESLKACIRCNSPAKYDCYLQRATCKREGCGFDYCTKCLCNYHTTKDCSDGKLLKASCKIGPLPGTKKSKKNLRRL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Phosphorylation	ALRPPRCSCSASPSA CCCCCCCCCCCCCCC	16.64	20068231
18	Ubiquitination	RPPRCSCSASPSAVT CCCCCCCCCCCCCCC	18.58	29967540
18	Phosphorylation	RPPRCSCSASPSAVT CCCCCCCCCCCCCCC	18.58	20068231
20	Phosphorylation	PRCSCSASPSAVTAA CCCCCCCCCCCCCCC	11.77	20068231
22	Phosphorylation	CSCSASPSAVTAAGR CCCCCCCCCCCCCCC	32.64	20068231
25	Phosphorylation	SASPSAVTAAGRPRP CCCCCCCCCCCCCCC	15.54	20068231
38	Ubiquitination	RPSDSCKEESSTLSV CCCCCCCCCCCCEEE	68.39	32015554
64	Ubiquitination	HSGLKLVKPDDIGRL CCCCEEECHHHHHHH	53.84	29967540
67	Ubiquitination	LKLVKPDDIGRLVSY CEEECHHHHHHHHHC	54.49	33845483
84	Ubiquitination	AYLEGSCKDCIKDYE HHHHCCHHHHHHHHH	58.28	32015554
88	Ubiquitination	GSCKDCIKDYERLSC CCHHHHHHHHHHHHC	61.66	-
90	Phosphorylation	CKDCIKDYERLSCIG HHHHHHHHHHHHCCC	9.65	26552605
94	Phosphorylation	IKDYERLSCIGSPIV HHHHHHHHCCCCCCC	15.20	26552605
98	Phosphorylation	ERLSCIGSPIVSPRI HHHHCCCCCCCCCCE	7.49	22199227
102	Phosphorylation	CIGSPIVSPRIVQLE CCCCCCCCCCEEEEE	14.80	22617229
113	Ubiquitination	VQLETESKRLHNKEN EEEEHHHHHHCCHHH	53.39	33845483
142	Phosphorylation	ALETSRLYEDSGYSS HHHHHCCCCCCCCCC	19.31	20717963
145	Phosphorylation	TSRLYEDSGYSSFSL HHCCCCCCCCCCEEE	27.91	22817900
149	Phosphorylation	YEDSGYSSFSLQSGL CCCCCCCCEEECCCC	15.46	22817900
153	Ubiquitination	GYSSFSLQSGLSEHE CCCCEEECCCCCCCC	33.97	32015554
199	Ubiquitination	LPVLHFEKVVCSTLK CCHHCHHHHHHHHHH	38.74	32015554
238	Ubiquitination	LQNIIGRKMGLECVD HHHHHCHHHCHHHHH	31.91	-
243	Ubiquitination	GRKMGLECVDILSEL CHHHCHHHHHHHHHH	3.91	29967540
251	Ubiquitination	VDILSELFRRGLRHV HHHHHHHHHHHHHHH	4.37	32015554
262	Ubiquitination	LRHVLATILAQLSDM HHHHHHHHHHHCCCC	2.20	23000965
289	Ubiquitination	KKILEDDKGAFQLYS HHHHCCCCCHHHHHH	65.54	29967540
297	Ubiquitination	GAFQLYSKAIQRVTE CHHHHHHHHHHHHHH	35.63	32015554
306	Ubiquitination	IQRVTENNNKFSPHA HHHHHHCCCCCCCCC	47.00	29967540
308	Ubiquitination	RVTENNNKFSPHAST HHHHCCCCCCCCCCH	49.71	23000965
318	Phosphorylation	PHASTREYVMFRTPL CCCCHHHEEEEECCH	8.23	-
321	Ubiquitination	STREYVMFRTPLASV CHHHEEEEECCHHHH	5.85	32015554
323	Phosphorylation	REYVMFRTPLASVQK HHEEEEECCHHHHHH	16.05	17001009
331	Phosphorylation	PLASVQKSAAQTSLK CHHHHHHHHHHHHCH	16.25	-
335	Phosphorylation	VQKSAAQTSLKKDAQ HHHHHHHHHCHHHHH	31.16	25690035
336	Phosphorylation	QKSAAQTSLKKDAQT HHHHHHHHCHHHHHH	26.55	-
344	Ubiquitination	LKKDAQTKLSNQGDQ CHHHHHHHHHCCCCC	37.53	-
346	Phosphorylation	KDAQTKLSNQGDQKG HHHHHHHHCCCCCCC	28.76	22496350
352	Ubiquitination	LSNQGDQKGSTYSRH HHCCCCCCCCCHHCC	60.62	29967540
352	Sumoylation	LSNQGDQKGSTYSRH HHCCCCCCCCCHHCC	60.62	-
352	Sumoylation	LSNQGDQKGSTYSRH HHCCCCCCCCCHHCC	60.62	-
356	Phosphorylation	GDQKGSTYSRHNEFS CCCCCCCHHCCHHHH	12.85	-
367	Ubiquitination	NEFSEVAKTLKKNES HHHHHHHHHHHCCCC	60.61	32015554
383	Phosphorylation	KACIRCNSPAKYDCY HHHHCCCCCHHHHCC	29.84	24719451
386	Acetylation	IRCNSPAKYDCYLQR HCCCCCHHHHCCCCC	45.03	25953088
387	Phosphorylation	RCNSPAKYDCYLQRA CCCCCHHHHCCCCCH	17.22	-
430	Acetylation	KLLKASCKIGPLPGT CEEEEEEECCCCCCC	48.48	25953088
437	Phosphorylation	KIGPLPGTKKSKKNL ECCCCCCCHHHHHHH	33.10	-

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
142	Y	Phosphorylation	Kinase	SRC	P12931	PSP
145	S	Phosphorylation	Kinase	PLK1	P53350	PSP
149	S	Phosphorylation	Kinase	PLK1	P53350	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW11	Q9UKB1	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:12820955

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
11	K	ubiquitylation		29875408
Undergoes both 'Lys-11' and 'Lys-48'-linked polyubiquitination by APC-FZR1 complex leading to degradation by proteasome during G1 phase.

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 FBX5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FZR1_HUMAN	FZR1	physical	11988738
CDC20_HUMAN	CDC20	physical	11988738
EVI5_HUMAN	EVI5	physical	16439210
FBW1A_HUMAN	BTRC	physical	15469984
CDC27_HUMAN	CDC27	physical	21454540
FZR1_HUMAN	FZR1	physical	11751633
CDC20_HUMAN	CDC20	physical	11751633
CDC27_HUMAN	CDC27	physical	16921029
CDC16_HUMAN	CDC16	physical	16921029
APC1_HUMAN	ANAPC1	physical	16921029
APC5_HUMAN	ANAPC5	physical	16921029
APC7_HUMAN	ANAPC7	physical	16921029
ANC2_HUMAN	ANAPC2	physical	16921029
APC4_HUMAN	ANAPC4	physical	16921029
CDC23_HUMAN	CDC23	physical	16921029
APC11_HUMAN	ANAPC11	physical	16921029
FZR1_HUMAN	FZR1	physical	16921029
BRCA1_HUMAN	BRCA1	physical	23086937
BARD1_HUMAN	BARD1	physical	23086937
TPM3_HUMAN	TPM3	physical	21988832
SKP1_HUMAN	SKP1	physical	17463251
FBW1A_HUMAN	BTRC	physical	28514442
FZR1_HUMAN	FZR1	physical	28514442
CDC27_HUMAN	CDC27	physical	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 FBX5_HUMAN

Related Literatures of Post-Translational Modification

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