dbPTM

FKB39_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FKB39_DROME
UniProt AC	P54397
Protein Name	39 kDa FK506-binding nuclear protein
Gene Name	FK506-bp1
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	357
Subcellular Localization	Nucleus .
Protein Description	PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development..
Protein Sequence	MSMFWGLNMKPERKYSQTIIKSFHISGVALDKGQEAKLYLAAEKQEYIVATVTKAIPQVALDLNFSKGDRIMFYTAGDASVSLLGYLHDIDSEDDEDDDQMTIENLLNSKAIKNSKKSEDDEDENESGEEDEEDTDDDSQIIEEYESFLENGEEEDDDDVDEDNEESGEEDEQDSDDSEAEEEQPKAKVAKLSPGASAKKSGKEQNGVAKKEEAKQQQKKKEKPEAKKEQPKAKEPAKQQPASKDPRTITGGVKIVDQVVGKGEEAKQGKRVSVYYIGRLQSNNKTFDSLLKGKPFKFALGGGEVIKGWDVGVAGMKVGGKRVITCPPHMAYGARGAPPKIGPNSTLVFEVELKAVH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Acetylation	MFWGLNMKPERKYSQ CCCCCCCCCCCCCCH	42.53	21791702
16	Phosphorylation	MKPERKYSQTIIKSF CCCCCCCCHHHHHHE	24.71	25749252
18	Phosphorylation	PERKYSQTIIKSFHI CCCCCCHHHHHHEEE	20.80	22817900
92	Phosphorylation	GYLHDIDSEDDEDDD HEECCCCCCCCCCCC	43.17	22817900
193	Phosphorylation	KAKVAKLSPGASAKK HHHHHHCCCCCCHHH	22.15	21082442
197	Phosphorylation	AKLSPGASAKKSGKE HHCCCCCCHHHCCCC	46.68	28490779
285	Acetylation	GRLQSNNKTFDSLLK EEEECCCCCHHHHHC	55.61	21791702
286	Phosphorylation	RLQSNNKTFDSLLKG EEECCCCCHHHHHCC	34.49	22817900
292	Acetylation	KTFDSLLKGKPFKFA CCHHHHHCCCCEEEE	70.90	21791702
297	Acetylation	LLKGKPFKFALGGGE HHCCCCEEEEECCCC	37.95	21791702

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 FKB39_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FKB39_DROME !!

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 FKB39_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FKB39_DROME	FK506-bp1	physical	25813344
HEAT1_DROME	l(2)k09022	physical	25813344
NAT10_DROME	l(1)G0020	physical	25813344
NOL6_DROME	Mat89Ba	physical	25813344
NOP14_DROME	l(3)07882	physical	25813344
RCL1_DROME	Rtc1	physical	25813344
NH2L1_DROME	hoip	physical	25813344
FBRL_DROME	Fib	physical	25813344
PNO1_DROME	l(1)G0004	physical	25813344
SAS10_DROME	Sas10	physical	25813344
AATF_DROME	Aatf	physical	25813344
UTP18_DROME	wcd	physical	25813344
RRP1L_DROME	Nnp-1	physical	25813344
NOC2L_DROME	CG9246	physical	25813344
BOP1_DROME	CG5033	physical	25813344
KRR1_DROME	dbe	physical	25813344
PESC_DROME	CG4364	physical	25813344
SLE_DROME	sle	physical	25813344
WDR12_DROME	CG6724	physical	25813344
NO66_DROME	CG2982	physical	25813344
BRX1_DROME	CG11583	physical	25813344
NEP1_DROME	CG3527	physical	25813344
DKC1_DROME	Nop60B	physical	25813344
DDX18_DROME	pit	physical	25813344
EBP2_DROME	CG1542	physical	25813344
NOL9_DROME	CG8414	physical	25813344
RPF2_DROME	Non3	physical	25813344
PP12_DROME	Pp1-87B	physical	25813344
NOG1_DROME	Non1	physical	25813344
H2AV_DROME	His2Av	physical	25813344
KARG_DROME	Argk	physical	25813344
USP_DROME	usp	physical	17956872
ECR_DROME	EcR	physical	17956872
FKB39_DROME	FK506-bp1	physical	28074868

Drug and Disease Associations

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

Regulatory Network of FKB39_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-197, ANDMASS SPECTROMETRY.	18327897 [Abstract]
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASSSPECTROMETRY.	17372656 [Abstract]