dbPTM

FBX31_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FBX31_HUMAN
UniProt AC	Q5XUX0
Protein Name	F-box only protein 31
Gene Name	FBXO31
Organism	Homo sapiens (Human).
Sequence Length	539
Subcellular Localization
Protein Description	Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest. May act as a tumor suppressor..
Protein Sequence	MAVCARLCGVGPSRGCRRRQQRRGPAETAAADSEPDTDPEEERIEASAGVGGGLCAGPSPPPPRCSLLELPPELLVEIFASLPGTDLPSLAQVCTKFRRILHTDTIWRRRCREEYGVCENLRKLEITGVSCRDVYAKLLHRYRHILGLWQPDIGPYGGLLNVVVDGLFIIGWMYLPPHDPHVDDPMRFKPLFRIHLMERKAATVECMYGHKGPHHGHIQIVKKDEFSTKCNQTDHHRMSGGRQEEFRTWLREEWGRTLEDIFHEHMQELILMKFIYTSQYDNCLTYRRIYLPPSRPDDLIKPGLFKGTYGSHGLEIVMLSFHGRRARGTKITGDPNIPAGQQTVEIDLRHRIQLPDLENQRNFNELSRIVLEVRERVRQEQQEGGHEAGEGRGRQGPRESQPSPAQPRAEAPSKGPDGTPGEDGGEPGDAVAAAEQPAQCGQGQPFVLPVGVSSRNEDYPRTCRMCFYGTGLIAGHGFTSPERTPGVFILFDEDRFGFVWLELKSFSLYSRVQATFRNADAPSPQAFDEMLKNIQSLTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Methylation	LCGVGPSRGCRRRQQ HCCCCCCHHHHHHHH	51.90	-
14	Dimethylation	LCGVGPSRGCRRRQQ HCCCCCCHHHHHHHH	51.90	-
33	Phosphorylation	AETAAADSEPDTDPE CHHHCCCCCCCCCHH	46.43	23663014
37	Phosphorylation	AADSEPDTDPEEERI CCCCCCCCCHHHHHH	65.26	23663014
59	Phosphorylation	GGLCAGPSPPPPRCS CCCCCCCCCCCCCCC	49.47	23186163
103	Phosphorylation	KFRRILHTDTIWRRR HHHHHHCCHHHHHHH	31.24	27251275
105	Phosphorylation	RRILHTDTIWRRRCR HHHHCCHHHHHHHHH	24.48	27251275
127	Phosphorylation	NLRKLEITGVSCRDV CCCCCEEECCCHHHH	23.35	22461510
135	Phosphorylation	GVSCRDVYAKLLHRY CCCHHHHHHHHHHHH	11.42	22461510
229	Ubiquitination	KKDEFSTKCNQTDHH ECCCCCCCCCCCCCC	29.95	-
276	Phosphorylation	LILMKFIYTSQYDNC HHHHHHHHHHCCCCC	11.94	26503514
277	Phosphorylation	ILMKFIYTSQYDNCL HHHHHHHHHCCCCCC	12.44	-
278	Phosphorylation	LMKFIYTSQYDNCLT HHHHHHHHCCCCCCE	15.12	19412162
280	Phosphorylation	KFIYTSQYDNCLTYR HHHHHHCCCCCCEEE	14.64	26503514
285	Phosphorylation	SQYDNCLTYRRIYLP HCCCCCCEEEEEECC	19.72	26503514
286	Phosphorylation	QYDNCLTYRRIYLPP CCCCCCEEEEEECCC	5.73	26503514
308	Phosphorylation	KPGLFKGTYGSHGLE CCCCCCCCCCCCCEE	25.87	-
309	Phosphorylation	PGLFKGTYGSHGLEI CCCCCCCCCCCCEEE	25.87	-
311	Phosphorylation	LFKGTYGSHGLEIVM CCCCCCCCCCEEEEE	12.17	-
330	Ubiquitination	GRRARGTKITGDPNI CHHCCCCCCCCCCCC	40.89	-
400	Phosphorylation	GRQGPRESQPSPAQP CCCCCCCCCCCCCCC	48.98	22985185
403	Phosphorylation	GPRESQPSPAQPRAE CCCCCCCCCCCCCCC	25.82	28348404
453	Phosphorylation	FVLPVGVSSRNEDYP EEEEEECCCCCCCCC	20.04	27535140
510	Phosphorylation	LKSFSLYSRVQATFR EECCCHHHHHHHHHC	31.13	24719451

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
33	S	Phosphorylation	Kinase	AKT1	P31749	PSP
278	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
278	S	Phosphorylation		19412162
Phosphorylation at Ser-278 by ATM following gamma-irradiation results in its stabilization.

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 FBX31_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUL1_HUMAN	CUL1	physical	16357137
SKP1_HUMAN	SKP1	physical	16357137
RBX1_HUMAN	RBX1	physical	16357137
CCND1_HUMAN	CCND1	physical	19412162
PAR6A_HUMAN	PARD6A	physical	23469015
CUL1_HUMAN	CUL1	physical	23469015
SKP1_HUMAN	SKP1	physical	23469015
CCND1_HUMAN	CCND1	physical	24085301
MP2K6_HUMAN	MAP2K6	physical	24936062
CUL1_HUMAN	CUL1	physical	23319600
CDT1_HUMAN	CDT1	physical	24828503
CCND1_HUMAN	CCND1	physical	24828503
STX3_HUMAN	STX3	physical	26496610
CUL1_HUMAN	CUL1	physical	26496610
PDLI1_HUMAN	PDLIM1	physical	26496610
RT27_HUMAN	MRPS27	physical	26496610
EFR3A_HUMAN	EFR3A	physical	26496610
EDRF1_HUMAN	EDRF1	physical	26496610
QSER1_HUMAN	QSER1	physical	26496610
CR021_HUMAN	C18orf21	physical	26496610
ZCHC9_HUMAN	ZCCHC9	physical	26496610
FA58A_HUMAN	FAM58A	physical	26496610
TIM14_HUMAN	DNAJC19	physical	26496610
GHR_HUMAN	GHR	physical	25505247
MDM2_HUMAN	MDM2	physical	26124108
CUL1_HUMAN	CUL1	physical	26124108
CUL1_HUMAN	CUL1	physical	27568981
RBX1_HUMAN	RBX1	physical	27568981
SKP1_HUMAN	SKP1	physical	27568981
FOXM1_HUMAN	FOXM1	physical	27568981
SNAI2_HUMAN	SNAI2	physical	28500896
SNAI1_HUMAN	SNAI1	physical	29117943

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615979	Mental retardation, autosomal recessive 45 (MRT45)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FBX31_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"F-box protein FBXO31 mediates cyclin D1 degradation to induce G1arrest after DNA damage."; Santra M.K., Wajapeyee N., Green M.R.; Nature 459:722-725(2009). Cited for: FUNCTION, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, INDUCTION,INTERACTION WITH CCND1, PHOSPHORYLATION AT SER-278, AND MUTAGENESIS OFSER-278 AND SER-400.	19412162 [Abstract]

show