dbPTM

FKBP3_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FKBP3_YEAST
UniProt AC	P38911
Protein Name	FK506-binding nuclear protein
Gene Name	FPR3
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	411
Subcellular Localization	Nucleus, nucleolus.
Protein Description	PPIases accelerate the folding of proteins. FK506- and rapamycin-binding protein. Specifically binds nuclear localization sequences. May be involved in the assembly or folding of ribosomal proteins..
Protein Sequence	MSDLLPLATYSLNVEPYTPVPAIDVTMPITVRITMAALNPEAIDEENKPSTLRIIKRNPDFEDDDFLGGDFDEDEIDEESSEEEEEEKTQKKKKSKGKKAESESEDDEEDDDEDDEFQESVLLTLSPEAQYQQSLDLTITPEEEVQFIVTGSYAISLSGNYVKHPFDTPMGVEGEDEDEDADIYDSEDYDLTPDEDEIIGDDMDDLDDEEEEEVRIEEVQEEDEEDNDGEEEQEEEEEEEQKEEVKPEPKKSKKEKKRKHEEKEEEKKAKKVKKVEFKKDLEEGPTKPKSKKEQDKHKPKSKVLEGGIVIEDRTIGDGPQAKRGARVGMRYIGKLKNGKVFDKNTSGKPFAFKLGRGEVIKGWDIGVAGMSVGGERRIIIPAPYAYGKQALPGIPANSELTFDVKLVSMKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSDLLPLAT ------CCCCCCEEE	36.64	22814378
48	Acetylation	EAIDEENKPSTLRII HHCCCCCCCCCEEHH	43.56	24489116
48	Ubiquitination	EAIDEENKPSTLRII HHCCCCCCCCCEEHH	43.56	23749301
80	Phosphorylation	EDEIDEESSEEEEEE HHHCCCCCCHHHHHH	40.79	17330950
81	Phosphorylation	DEIDEESSEEEEEEK HHCCCCCCHHHHHHH	52.92	17330950
89	Phosphorylation	EEEEEEKTQKKKKSK HHHHHHHHHHHHHHH	49.23	17330950
184	Phosphorylation	EDEDADIYDSEDYDL CCCCCCCCCCCCCCC	17.60	15358193
186	Phosphorylation	EDADIYDSEDYDLTP CCCCCCCCCCCCCCC	18.52	28889911
286	Phosphorylation	KDLEEGPTKPKSKKE HHHCCCCCCCCCHHH	71.48	23749301
287	Acetylation	DLEEGPTKPKSKKEQ HHCCCCCCCCCHHHH	54.29	24489116
322	Succinylation	IGDGPQAKRGARVGM CCCCCCHHCCCCCCC	46.23	23954790
343	Acetylation	KNGKVFDKNTSGKPF CCCEEECCCCCCCCE	51.14	24489116
348	Acetylation	FDKNTSGKPFAFKLG ECCCCCCCCEEEEEC	36.41	24489116
353	Acetylation	SGKPFAFKLGRGEVI CCCCEEEEECCCEEE	46.75	24489116

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
184	Y	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
184	Y	Phosphorylation	Kinase	CK2	-	Uniprot
186	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
186	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FKBP3_YEAST !!

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 FKBP3_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPAL_YEAST	LTP1	physical	15358193
RTF1_YEAST	RTF1	genetic	17314980
DOA1_YEAST	DOA1	genetic	17314980
SWC5_YEAST	SWC5	genetic	17314980
SSB1_YEAST	SSB1	physical	19536198
ENV10_YEAST	ENV10	genetic	20093466
COQ11_YEAST	YLR290C	genetic	20093466
THI22_YEAST	THI22	genetic	20093466
PSH1_YEAST	PSH1	genetic	24514906
IPL1_YEAST	IPL1	genetic	24514906
FKBP4_YEAST	FPR4	genetic	24514906
LOC1_YEAST	LOC1	physical	25877921
NOP53_YEAST	NOP53	physical	25877921
EBP2_YEAST	EBP2	physical	25877921
DBP10_YEAST	DBP10	physical	25877921
SPB1_YEAST	SPB1	physical	25877921
RRP14_YEAST	RRP14	physical	25877921
LSM6_YEAST	LSM6	genetic	27708008
DAL81_YEAST	DAL81	genetic	27708008
THI22_YEAST	THI22	genetic	27708008

Drug and Disease Associations

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

Regulatory Network of FKBP3_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-81, AND MASSSPECTROMETRY.	18407956 [Abstract]
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-81, AND MASSSPECTROMETRY.	17330950 [Abstract]
"Casein kinase II catalyzes tyrosine phosphorylation of the yeastnucleolar immunophilin Fpr3."; Wilson L.K., Dhillon N., Thorner J., Martin G.S.; J. Biol. Chem. 272:12961-12967(1997). Cited for: PHOSPHORYLATION AT TYR-184 AND SER-186.	9148902 [Abstract]