FLO1_YEAST - dbPTM
FLO1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLO1_YEAST
UniProt AC P32768
Protein Name Flocculation protein FLO1
Gene Name FLO1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1537
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor. Secreted, cell wall. Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer.
Protein Description Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose. Also involved in cell-substrate adhesion..
Protein Sequence MTMPHRYMFLAVFTLLALTSVASGATEACLPAGQRKSGMNINFYQYSLKDSSTYSNAAYMAYGYASKTKLGSVGGQTDISIDYNIPCVSSSGTFPCPQEDSYGNWGCKGMGACSNSQGIAYWSTDLFGFYTTPTNVTLEMTGYFLPPQTGSYTFKFATVDDSAILSVGGATAFNCCAQQQPPITSTNFTIDGIKPWGGSLPPNIEGTVYMYAGYYYPMKVVYSNAVSWGTLPISVTLPDGTTVSDDFEGYVYSFDDDLSQSNCTVPDPSNYAVSTTTTTTEPWTGTFTSTSTEMTTVTGTNGVPTDETVIVIRTPTTASTIITTTEPWNSTFTSTSTELTTVTGTNGVRTDETIIVIRTPTTATTAITTTEPWNSTFTSTSTELTTVTGTNGLPTDETIIVIRTPTTATTAMTTTQPWNDTFTSTSTELTTVTGTNGLPTDETIIVIRTPTTATTAMTTTQPWNDTFTSTSTELTTVTGTNGLPTDETIIVIRTPTTATTAMTTTQPWNDTFTSTSTEITTVTGTNGLPTDETIIVIRTPTTATTAMTTPQPWNDTFTSTSTEMTTVTGTNGLPTDETIIVIRTPTTATTAITTTEPWNSTFTSTSTEMTTVTGTNGLPTDETIIVIRTPTTATTAITTTQPWNDTFTSTSTEMTTVTGTNGLPTDETIIVIRTPTTATTAMTTTQPWNDTFTSTSTEITTVTGTTGLPTDETIIVIRTPTTATTAMTTTQPWNDTFTSTSTEMTTVTGTNGVPTDETVIVIRTPTSEGLISTTTEPWTGTFTSTSTEMTTVTGTNGQPTDETVIVIRTPTSEGLVTTTTEPWTGTFTSTSTEMTTITGTNGVPTDETVIVIRTPTSEGLISTTTEPWTGTFTSTSTEMTTITGTNGQPTDETVIVIRTPTSEGLISTTTEPWTGTFTSTSTEMTHVTGTNGVPTDETVIVIRTPTSEGLISTTTEPWTGTFTSTSTEVTTITGTNGQPTDETVIVIRTPTSEGLISTTTEPWTGTFTSTSTEMTTVTGTNGQPTDETVIVIRTPTSEGLVTTTTEPWTGTFTSTSTEMSTVTGTNGLPTDETVIVVKTPTTAISSSLSSSSSGQITSSITSSRPIITPFYPSNGTSVISSSVISSSVTSSLFTSSPVISSSVISSSTTTSTSIFSESSKSSVIPTSSSTSGSSESETSSAGSVSSSSFISSESSKSPTYSSSSLPLVTSATTSQETASSLPPATTTKTSEQTTLVTVTSCESHVCTESISPAIVSTATVTVSGVTTEYTTWCPISTTETTKQTKGTTEQTTETTKQTTVVTISSCESDVCSKTASPAIVSTSTATINGVTTEYTTWCPISTTESRQQTTLVTVTSCESGVCSETASPAIVSTATATVNDVVTVYPTWRPQTANEESVSSKMNSATGETTTNTLAAETTTNTVAAETITNTGAAETKTVVTSSLSRSNHAETQTASATDVIGHSSSVVSVSETGNTKSLTSSGLSTMSQQPRSTPASSMVGYSTASLEISTYAGSANSLLAGSGLSVFIASLLLAII
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
2Phosphorylation------MTMPHRYMF
------CCCCHHHHH
51.1923607784
7Phosphorylation-MTMPHRYMFLAVFT
-CCCCHHHHHHHHHH
6.8123607784
14PhosphorylationYMFLAVFTLLALTSV
HHHHHHHHHHHHHHH
17.7923607784
19PhosphorylationVFTLLALTSVASGAT
HHHHHHHHHHHCCCC
18.6223607784
20PhosphorylationFTLLALTSVASGATE
HHHHHHHHHHCCCCC
19.2823607784
23PhosphorylationLALTSVASGATEACL
HHHHHHHCCCCCCCC
27.1423607784
26PhosphorylationTSVASGATEACLPAG
HHHHCCCCCCCCCCC
27.8623607784
135N-linked_GlycosylationGFYTTPTNVTLEMTG
EEEECCCCEEEEEEE
26.44-
187N-linked_GlycosylationQPPITSTNFTIDGIK
CCCCEEECEEEECCC
31.65-
262N-linked_GlycosylationDDDLSQSNCTVPDPS
CCCCCCCCCCCCCHH
20.17-
329N-linked_GlycosylationITTTEPWNSTFTSTS
EEECCCCCCCCEECC
41.72-
374N-linked_GlycosylationITTTEPWNSTFTSTS
EEECCCCCCCCEECC
41.72-
419N-linked_GlycosylationMTTTQPWNDTFTSTS
CCCCCCCCCCCCCCC
45.16-
464N-linked_GlycosylationMTTTQPWNDTFTSTS
CCCCCCCCCCCCCCC
45.16-
509N-linked_GlycosylationMTTTQPWNDTFTSTS
CCCCCCCCCCCCCCC
45.16-
554N-linked_GlycosylationMTTPQPWNDTFTSTS
CCCCCCCCCCCCCCC
45.16-
599N-linked_GlycosylationITTTEPWNSTFTSTS
EEECCCCCCCCEECC
41.72-
644N-linked_GlycosylationITTTQPWNDTFTSTS
EEECCCCCCCCCCCC
45.16-
689N-linked_GlycosylationMTTTQPWNDTFTSTS
CCCCCCCCCCCCCCC
45.16-
734N-linked_GlycosylationMTTTQPWNDTFTSTS
CCCCCCCCCCCCCCE
45.16-
1114N-linked_GlycosylationITPFYPSNGTSVISS
EECCCCCCCCEEEEC
53.94-
1514GPI-anchorLEISTYAGSANSLLA
EEEEECCCCHHHHHC
19.51-

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 FLO1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLO1_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 FLO1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BPH1_YEASTBPH1genetic
23891562
GCS1_YEASTGCS1genetic
27708008
ERG3_YEASTERG3genetic
27708008
AIM34_YEASTAIM34genetic
27708008
FLO1_YEASTFLO1physical
25873380

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FLO1_YEAST

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Related Literatures of Post-Translational Modification

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