SFL1_YEAST - dbPTM
SFL1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SFL1_YEAST
UniProt AC P20134
Protein Name Flocculation suppression protein
Gene Name SFL1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 766
Subcellular Localization Nucleus .
Protein Description Involved in cell surface assembly and regulation of the gene related to flocculation (asexual cell aggregation). Mutations in SFL1 causes constitutive cell aggregation..
Protein Sequence MSEEETVSAPAPASTPAPAGTDVGSGGAAAGIANAGAEGGDGAEDVKKHGSKMLVGPRPPQNAIFIHKLYQILEDESLHDLIWWTPSGLSFMIKPVERFSKALATYFKHTNITSFVRQLNIYGFHKVSHDHSSNDANSGDDANTNDDSNTHDDNSGNKNSSGDENTGGGVQEKEKSNPTKIWEFKHSSGIFKKGDIEGLKHIKRRASSRNNSSINSRKNSSNQNYDIDSGARVRPSSIQDPSTSSNSFGNFVPQIPGANNSIPEYFNNSHVTYENANHAPLESNNPEMQEQNRPPNFQDETLKHLKEINFDMVKIIESMQHFISLQHSFCSQSFTFKNVSKKKSENIVKDHQKQLQAFESDMLTFKQHVMSRAHRTIDSLCAVNAAATAASVAPAPAPTSTSAYAPKSQYEMMVPPGNQYVPQKSSSTTNIPSRFNTASVPPSQLFVQYQPQSQQHVTYAKQPAHVPNFINQPIPIQQLPPQYADTFSTPQMMHNPFASKNNNKPGNTKRTNSVLMDPLTPAASVGVQGPLNYPIMNINPSVRDYNKPVPQNMAPSPIYPINEPTTRLYSQPKMRSLGSTSSLPNDRRNSPLKLTPRSSLNEDSLYPKPRNSLKSSISGTSLSSSFTLVANNPAPIRYSQQGLLRSLNKAANCAPDSVTPLDSSVLTGPPPKNMDNLPAVSSNLINSPMNVEHSSSLSQAEPAPQIELPQPSLPTTSTTKNTGEADNSKRKGSGVYSLLNQEDSSTSSADPKTEDKAAPALKKVKM
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------MSEEETVSA
------CCCCCCCCC		54.4324961812
6Phosphorylation--MSEEETVSAPAPA
--CCCCCCCCCCCCC		24.0424961812
14PhosphorylationVSAPAPASTPAPAGT
CCCCCCCCCCCCCCC		33.5930377154
15PhosphorylationSAPAPASTPAPAGTD
CCCCCCCCCCCCCCC		26.1021082442
25PhosphorylationPAGTDVGSGGAAAGI
CCCCCCCCCCHHHHH		33.6228889911
138PhosphorylationHSSNDANSGDDANTN
CCCCCCCCCCCCCCC		45.3730377154
160PhosphorylationDNSGNKNSSGDENTG
CCCCCCCCCCCCCCC		36.9922890988
161PhosphorylationNSGNKNSSGDENTGG
CCCCCCCCCCCCCCC		60.7122890988
166PhosphorylationNSSGDENTGGGVQEK
CCCCCCCCCCCCCCC		34.8522890988
185AcetylationPTKIWEFKHSSGIFK
CCEEEEEECCCCCCC		30.9424489116
207PhosphorylationKHIKRRASSRNNSSI
HHHHHHHHHCCCCCC		28.1927717283
208PhosphorylationHIKRRASSRNNSSIN
HHHHHHHHCCCCCCC		37.7317563356
212PhosphorylationRASSRNNSSINSRKN
HHHHCCCCCCCCCCC		35.8228889911
213PhosphorylationASSRNNSSINSRKNS
HHHCCCCCCCCCCCC		28.1027717283
216PhosphorylationRNNSSINSRKNSSNQ
CCCCCCCCCCCCCCC		42.8530377154
220PhosphorylationSINSRKNSSNQNYDI
CCCCCCCCCCCCCCC		33.4322369663
221PhosphorylationINSRKNSSNQNYDID
CCCCCCCCCCCCCCC		52.4022369663
225PhosphorylationKNSSNQNYDIDSGAR
CCCCCCCCCCCCCCC		12.4322890988
229PhosphorylationNQNYDIDSGARVRPS
CCCCCCCCCCCCCCH		34.3927017623
340PhosphorylationSFTFKNVSKKKSENI
CEEEECCCCHHHHHH		48.4228889911
425PhosphorylationNQYVPQKSSSTTNIP
CCCCCCCCCCCCCCC		25.0322369663
426PhosphorylationQYVPQKSSSTTNIPS
CCCCCCCCCCCCCCC		38.4525005228
427PhosphorylationYVPQKSSSTTNIPSR
CCCCCCCCCCCCCCC		46.4722369663
428PhosphorylationVPQKSSSTTNIPSRF
CCCCCCCCCCCCCCC		26.3022369663
429PhosphorylationPQKSSSTTNIPSRFN
CCCCCCCCCCCCCCC		32.8525752575
433PhosphorylationSSTTNIPSRFNTASV
CCCCCCCCCCCCCCC		45.7827017623
437PhosphorylationNIPSRFNTASVPPSQ
CCCCCCCCCCCCHHH		20.0021551504
511PhosphorylationKPGNTKRTNSVLMDP
CCCCCCCCCCEECCC		33.1430377154
545PhosphorylationINPSVRDYNKPVPQN
CCHHHCCCCCCCCCC		17.9622369663
556PhosphorylationVPQNMAPSPIYPINE
CCCCCCCCCCCCCCC		17.8722369663
559PhosphorylationNMAPSPIYPINEPTT
CCCCCCCCCCCCCCC		11.0522369663
565PhosphorylationIYPINEPTTRLYSQP
CCCCCCCCCCCCCCC		20.5421551504
566PhosphorylationYPINEPTTRLYSQPK
CCCCCCCCCCCCCCC		29.4122369663
573AcetylationTRLYSQPKMRSLGST
CCCCCCCCCCCCCCC		39.0325381059
576PhosphorylationYSQPKMRSLGSTSSL
CCCCCCCCCCCCCCC		33.3222369663
579PhosphorylationPKMRSLGSTSSLPND
CCCCCCCCCCCCCCC		30.3422369663
580PhosphorylationKMRSLGSTSSLPNDR
CCCCCCCCCCCCCCC		22.1222369663
581PhosphorylationMRSLGSTSSLPNDRR
CCCCCCCCCCCCCCC		31.4122369663
582PhosphorylationRSLGSTSSLPNDRRN
CCCCCCCCCCCCCCC		48.1922369663
590PhosphorylationLPNDRRNSPLKLTPR
CCCCCCCCCCCCCCC		29.7822369663
595PhosphorylationRNSPLKLTPRSSLNE
CCCCCCCCCCCCCCC		18.3122369663
598PhosphorylationPLKLTPRSSLNEDSL
CCCCCCCCCCCCCCC		40.1422369663
599PhosphorylationLKLTPRSSLNEDSLY
CCCCCCCCCCCCCCC		36.1722369663
604PhosphorylationRSSLNEDSLYPKPRN
CCCCCCCCCCCCCCC		24.5121440633
606PhosphorylationSLNEDSLYPKPRNSL
CCCCCCCCCCCCCCC		17.1121440633
612PhosphorylationLYPKPRNSLKSSISG
CCCCCCCCCCCCCCC		38.1519779198
615PhosphorylationKPRNSLKSSISGTSL
CCCCCCCCCCCCCCC		37.8924961812
616PhosphorylationPRNSLKSSISGTSLS
CCCCCCCCCCCCCCC		21.1324961812
618PhosphorylationNSLKSSISGTSLSSS
CCCCCCCCCCCCCCC		37.6624961812
620PhosphorylationLKSSISGTSLSSSFT
CCCCCCCCCCCCCEE		21.5024961812
621PhosphorylationKSSISGTSLSSSFTL
CCCCCCCCCCCCEEE		29.7621551504
627PhosphorylationTSLSSSFTLVANNPA
CCCCCCEEEEECCCC		23.4419779198
639PhosphorylationNPAPIRYSQQGLLRS
CCCCCCHHHHHHHHH		13.2328132839
733PhosphorylationDNSKRKGSGVYSLLN
CCCCCCCCCHHHHCC		28.2822369663
736PhosphorylationKRKGSGVYSLLNQED
CCCCCCHHHHCCCCC		9.3422890988
737PhosphorylationRKGSGVYSLLNQEDS
CCCCCHHHHCCCCCC		24.7922890988
744PhosphorylationSLLNQEDSSTSSADP
HHCCCCCCCCCCCCC		34.4622890988
745PhosphorylationLLNQEDSSTSSADPK
HCCCCCCCCCCCCCC		44.6322890988
746PhosphorylationLNQEDSSTSSADPKT
CCCCCCCCCCCCCCC		30.5622890988
747PhosphorylationNQEDSSTSSADPKTE
CCCCCCCCCCCCCCC		26.0222890988
748PhosphorylationQEDSSTSSADPKTED
CCCCCCCCCCCCCCC		36.4622890988
753PhosphorylationTSSADPKTEDKAAPA
CCCCCCCCCCCCCHH		55.6021440633
756AcetylationADPKTEDKAAPALKK
CCCCCCCCCCHHHHH		39.9725381059
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 SFL1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SFL1_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 SFL1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SFL1_YEASTSFL1physical
12024012
MED19_YEASTROX3physical
9755175
MED16_YEASTSIN4physical
9755175
SSN8_YEASTSSN8physical
9755175
SSN2_YEASTSSN2physical
9755175
CYC8_YEASTCYC8physical
11399075
BMH1_YEASTBMH1physical
16554755
RRP5_YEASTRRP5physical
16554755
MSS11_YEASTMSS11genetic
15466424
SWD1_YEASTSWD1genetic
19269370
PP2C1_YEASTPTC1genetic
19269370
CTK3_YEASTCTK3genetic
19269370
SSB2_YEASTSSB2physical
19536198
HSP71_YEASTSSA1physical
19536198
VPS8_YEASTVPS8genetic
20093466
ACH1_YEASTACH1genetic
20093466
ELO2_YEASTELO2genetic
20093466
MTU1_YEASTSLM3genetic
20093466
NHP10_YEASTNHP10genetic
20093466
NRG1_YEASTNRG1genetic
20093466
SWM1_YEASTSWM1genetic
20093466
RLA4_YEASTRPP2Bgenetic
20093466
SPS2_YEASTSPS2genetic
20093466
IES1_YEASTIES1genetic
20093466
MTO1_YEASTMTO1genetic
20093466
SNG1_YEASTSNG1genetic
20093466
OPI1_YEASTOPI1genetic
20093466
ATG32_YEASTATG32genetic
20093466
ELM1_YEASTELM1genetic
20093466
BRE2_YEASTBRE2genetic
20093466
SIC1_YEASTSIC1genetic
20093466
IRC20_YEASTIRC20genetic
20093466
ROM2_YEASTROM2genetic
20093466
EAF7_YEASTEAF7genetic
20093466
EOS1_YEASTEOS1genetic
20093466
OCA2_YEASTOCA2genetic
20093466
AIM39_YEASTAIM39genetic
20093466
NIP80_YEASTNIP100genetic
20093466
SUT2_YEASTSUT2genetic
20093466
EAF3_YEASTEAF3genetic
20093466
MED1_YEASTMED1genetic
20093466
MET16_YEASTMET16genetic
20093466
EAF5_YEASTEAF5genetic
20959818
SIN3_YEASTSIN3genetic
20959818
SAS3_YEASTSAS3genetic
20959818
VPS71_YEASTVPS71genetic
20959818
MED9_YEASTCSE2genetic
20959818
AF9_YEASTYAF9genetic
20959818
IES1_YEASTIES1genetic
20959818
UBP3_YEASTUBP3genetic
20959818
RTG1_YEASTRTG1genetic
21127252
BUB1_YEASTBUB1genetic
21127252
CHA4_YEASTCHA4genetic
21127252
RAD51_YEASTRAD51genetic
21127252
STE12_YEASTSTE12genetic
22384390
TEC1_YEASTTEC1genetic
22384390
GNP1_YEASTGNP1genetic
22844449
DIP5_YEASTDIP5genetic
22844449
FLO11_YEASTFLO11genetic
22844449
TEC1_YEASTTEC1genetic
22844449
KAPB_YEASTTPK2genetic
22844449
CYAA_YEASTCYR1genetic
22844449
GCN4_YEASTGCN4genetic
22844449
SSY1_YEASTSSY1genetic
22844449
PTR3_YEASTPTR3genetic
22844449
FLO8_YEASTFLO8genetic
22984072
MFG1_YEASTMFG1genetic
22984072
MSS1_YEASTMSS1genetic
22984072
FLO11_YEASTFLO11genetic
22984072
PACC_YEASTRIM101genetic
22984072
TEC1_YEASTTEC1genetic
22984072
ELM1_YEASTELM1genetic
22282571
ESP1_YEASTESP1genetic
27708008
CDS1_YEASTCDS1genetic
27708008
CALM_YEASTCMD1genetic
27708008
RPN5_YEASTRPN5genetic
27708008
CDC37_YEASTCDC37genetic
27708008
UTP5_YEASTUTP5genetic
27708008
RSC8_YEASTRSC8genetic
27708008
CDC20_YEASTCDC20genetic
27708008
CWC22_YEASTCWC22genetic
27708008
BRL1_YEASTBRL1genetic
27708008
CDC23_YEASTCDC23genetic
27708008
CTF8_YEASTCTF8genetic
27708008
STS1_YEASTSTS1genetic
27708008
SMC3_YEASTSMC3genetic
27708008
TAF4_YEASTTAF4genetic
27708008
RNA1_YEASTRNA1genetic
27708008
LCB1_YEASTLCB1genetic
27708008
LIP1_YEASTLIP1genetic
27708008
CAP_YEASTSRV2genetic
27708008
RPC6_YEASTRPC34genetic
27708008
HRP1_YEASTHRP1genetic
27708008
ARP7_YEASTARP7genetic
27708008
NPL4_YEASTNPL4genetic
27708008
RMD9L_YEASTYBR238Cgenetic
27708008
SGF29_YEASTSGF29genetic
27708008
ELO2_YEASTELO2genetic
27708008
NHP10_YEASTNHP10genetic
27708008
MTU1_YEASTSLM3genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
RAD55_YEASTRAD55genetic
27708008
IES1_YEASTIES1genetic
27708008
OPI1_YEASTOPI1genetic
27708008
THIK_YEASTPOT1genetic
27708008
ELM1_YEASTELM1genetic
27708008
ROM2_YEASTROM2genetic
27708008
EAF7_YEASTEAF7genetic
27708008
AIM39_YEASTAIM39genetic
27708008
CHL1_YEASTCHL1genetic
27708008
MET16_YEASTMET16genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SFL1_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-161; SER-220; SER-556;SER-576; SER-582; SER-590; THR-595; SER-598; SER-599; SER-733 ANDTYR-736, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-221; SER-579;SER-581; SER-590; THR-595; SER-599 AND SER-733, AND MASS SPECTROMETRY.
"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-220, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-581 AND SER-582, ANDMASS SPECTROMETRY.

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