FOB1_YEAST - dbPTM
FOB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOB1_YEAST
UniProt AC O13329
Protein Name DNA replication fork-blocking protein FOB1 {ECO:0000303|PubMed:9078378}
Gene Name FOB1 {ECO:0000303|PubMed:9078378}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 566
Subcellular Localization Nucleus, nucleolus .
Protein Description Required for replication fork blocking activity at the replication fork barrier (RFB) site in rDNA and for recombination hot-spot (HOT1) activity, regulating the recombination rate and the number of rDNA copies. Binds directly to two separated sequences in the RFB..
Protein Sequence MTKPRYNDVLFDDDDSVPSESVTRKSQRRKATSPGESRESSKDRLLILPSMGESYTEYVDSYLNLELLERGERETPIFLESLTRQLTQKIYELIKTKSLTADTLQQISDKYDGVVAENKLLFLQRQYYVDDEGNVRDGRNNDKIYCEPKHVYDMVMATHLMNKHLRGKTLHSFLFSHFANISHAIIDWVQQFCSKCNKKGKIKPLKEYKRPDMYDKLLPMERIHIEVFEPFNGEAIEGKYSYVLLCRDYRSSFMWLLPLKSTKFKHLIPVVSSLFLTFARVPIFVTSSTLDKDDLYDICEEIASKYGLRIGLGLKSSARFHTGGILCIQYALNSYKKECLADWGKCLRYGPYRFNRRRNKRTKRKPVQVLLSEVPGHNAKFETKRERVIENTYSRNMFKMAGGKGLIYLEDVNTFALANEADNSCNNNGILHNNNIGNDNFEEEVQKQFDLTEKNYIDEYDDLAHDSSEGEFEPNTLTPEEKPPHNVDEDRIESTGVAAPMQGTEEPEKGDQKESDGASQVDQSVEITRPETSYYQTLESPSTKRQKLDQQGNGDQTRDFGTSMEL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
16PhosphorylationVLFDDDDSVPSESVT
CCCCCCCCCCCHHHC		42.8128152593
32PhosphorylationKSQRRKATSPGESRE
HHHCCCCCCCCCCCC		38.1927214570
33PhosphorylationSQRRKATSPGESRES
HHCCCCCCCCCCCCC		35.4525752575
37PhosphorylationKATSPGESRESSKDR
CCCCCCCCCCCCCCC		47.4627214570
40PhosphorylationSPGESRESSKDRLLI
CCCCCCCCCCCCEEE		41.3919823750
41PhosphorylationPGESRESSKDRLLIL
CCCCCCCCCCCEEEE		33.5519823750
100PhosphorylationLIKTKSLTADTLQQI
HHHCCCCCHHHHHHH		29.5821551504
103PhosphorylationTKSLTADTLQQISDK
CCCCCHHHHHHHHHH		24.8121551504
240PhosphorylationGEAIEGKYSYVLLCR
CCCCCCCEEEEEEEC		18.9827017623
456PhosphorylationFDLTEKNYIDEYDDL
HCCCCCCCCCCCHHC		22.3319823750
460PhosphorylationEKNYIDEYDDLAHDS
CCCCCCCCHHCCCCC		15.8228889911
467PhosphorylationYDDLAHDSSEGEFEP
CHHCCCCCCCCCCCC		22.0328889911
468PhosphorylationDDLAHDSSEGEFEPN
HHCCCCCCCCCCCCC		56.5328889911
476PhosphorylationEGEFEPNTLTPEEKP
CCCCCCCCCCCCCCC		42.6019823750
478PhosphorylationEFEPNTLTPEEKPPH
CCCCCCCCCCCCCCC		26.9819823750
494PhosphorylationVDEDRIESTGVAAPM
CCHHHHHCCCCCCCC		28.2619823750
495PhosphorylationDEDRIESTGVAAPMQ
CHHHHHCCCCCCCCC		23.9219823750
504PhosphorylationVAAPMQGTEEPEKGD
CCCCCCCCCCCCCCC		21.9319795423
515PhosphorylationEKGDQKESDGASQVD
CCCCCCCCCCCCCCC		48.6720377248
519PhosphorylationQKESDGASQVDQSVE
CCCCCCCCCCCCEEE		35.9420377248
524PhosphorylationGASQVDQSVEITRPE
CCCCCCCEEEECCCC		19.7720377248
528PhosphorylationVDQSVEITRPETSYY
CCCEEEECCCCCCCE		27.0221551504
540PhosphorylationSYYQTLESPSTKRQK
CCEEECCCCCHHHHH		27.5428152593
542PhosphorylationYQTLESPSTKRQKLD
EEECCCCCHHHHHCC		56.7019779198
543PhosphorylationQTLESPSTKRQKLDQ
EECCCCCHHHHHCCC		33.3620377248
557PhosphorylationQQGNGDQTRDFGTSM
CCCCCCCCCCCCCCC		36.6223749301
563PhosphorylationQTRDFGTSMEL----
CCCCCCCCCCC----		15.6120377248
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 FOB1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOB1_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 FOB1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NET1_YEASTNET1physical
12923057
SIR2_YEASTSIR2physical
12923057
CDC14_YEASTCDC14physical
12923057
NET1_YEASTNET1physical
15043811
FOB1_YEASTFOB1physical
14576157
NSI1_YEASTNSI1physical
14576157
HXKB_YEASTHXK2genetic
15328540
GPA2_YEASTGPA2genetic
15328540
SMC2_YEASTSMC2genetic
16507999
TOF2_YEASTTOF2physical
17043313
H2B1_YEASTHTB1physical
17043313
H2B2_YEASTHTB2physical
17043313
NET1_YEASTNET1physical
17043313
CDC14_YEASTCDC14physical
17043313
TOP1_YEASTTOP1physical
17043313
NOG1_YEASTNOG1physical
17043313
REB1_YEASTREB1physical
17043313
H1_YEASTHHO1physical
17043313
H2A1_YEASTHTA1physical
17043313
H2A2_YEASTHTA2physical
17043313
H4_YEASTHHF1physical
17043313
SIR2_YEASTSIR2genetic
19557187
APE3_YEASTAPE3genetic
20093466
DOT1_YEASTDOT1genetic
20093466
RPA34_YEASTRPA34genetic
20093466
PHO23_YEASTPHO23genetic
20093466
LRS4_YEASTLRS4genetic
21664583
CSM1_YEASTCSM1genetic
21664583
TSA1_YEASTTSA1genetic
21884982
NSI1_YEASTNSI1physical
22362748
SIR2_YEASTSIR2physical
22362748
MRE11_YEASTMRE11genetic
23376930
SIR2_YEASTSIR2genetic
23993840
UBP3_YEASTUBP3genetic
24760971
TOF2_YEASTTOF2physical
19362534
CG121_YEASTCGI121genetic
25822194
FOB1_YEASTFOB1physical
26063576
APE3_YEASTAPE3genetic
27708008
DOT1_YEASTDOT1genetic
27708008
LRP1_YEASTLRP1genetic
27708008
RPA34_YEASTRPA34genetic
27708008
RRP6_YEASTRRP6genetic
27708008
SPT8_YEASTSPT8genetic
27474729
SPT7_YEASTSPT7genetic
27474729
SIR2_YEASTSIR2genetic
27060141
SIR4_YEASTSIR4genetic
27060141
FOB1_YEASTFOB1physical
26951198
NET1_YEASTNET1physical
26951198
TOF2_YEASTTOF2physical
26951198
SIR2_YEASTSIR2genetic
26837752
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOB1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-519, AND MASSSPECTROMETRY.

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