SFI1_YEAST - dbPTM
SFI1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SFI1_YEAST
UniProt AC Q12369
Protein Name Protein SFI1
Gene Name SFI1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 946
Subcellular Localization Cytoplasm, cytoskeleton, spindle pole . Spindle pole, half bridge.
Protein Description Component of the spindle pole body (SPB) half-bridge involved in the initial steps of SPB duplication..
Protein Sequence MGKFGTTNKSTENLLRDKFVPETSPTNIPTDVLIKQGQITDSTESLIHGGAERYIVNALKPIELNKTEGFFEDPPFHLPSPPVDSTNLEYEDVTDLPKNGLRYDLNDISVEVIEDLYRQIEAFLVHFKLSRSFLQIFKNYVNILIQEGINPLRDEYFTILEDELKGFFTFNSVIEEILEIFLIHPRNKFIALSLAEYTYAKNKIRRHFNHWKTVCELNEEANRFANQAKLRVQEAVFYIWSDKTLKYSQMANDEAESFRNTWLLFRSFQQWITLTQTLKEQSRLADQAFLNKMFRKILKAQEHWKHLETVNTDNIKKIFLRTTFHIWKLRHKEINYHGLERRIFERIKQKVINYEYNKSIAEKVRSFSLQRKYLNKWEKKNIENEDKLGALYELENKFIKQKFFRKLNRSFQHSQQEAIAKSKLNQTLLRCVFEKMWLKRFEDHLHLYSIVSLKEANLVKRIFHSWKKLLYIDLKASDYSRTNLLKSSLRSWKLEVKLKIFEQKCKKSIQASAYRTWRKRIQYGKISSEHVKTAFCAKYLGVWKRRMLQMNSMNDEASKFYEEGLVNECLAIWKERLIKTKELEDRYNFLCKTHAILTVKRTLMHIDNVHLLYTKLAPSMDRVKLSKAFLKWRKATRFKVRHKLNDILHVYEKSKERELQSQLFNAWRNRFCFYTEECNIQAISKRNYQLEKMVLKKFRERLLEIVKSEELADEVREEFVLVKTFYIWKTHLDEIFYMSTLLEQSEANKQFIITSKFLKMWSLRFLKIKRNDETVEVFRHRWDRATVRGLLLLWKNRSDSSPKRRKDFNLKHELKTPIRSDSQNASTIPGSERIKQHRMEAMKSHYSRARRAIPSPVKSSSVLDSTAKKQINLESTTGLNGSPTRGKPLRYSPRRTTRNMPSKVDHIDFGRIPAVPFSLSANSPKIDQDMDYIREHDKSPLSRKRQ
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
6Phosphorylation--MGKFGTTNKSTEN
--CCCCCCCCCCHHH		30.2619823750
7Phosphorylation-MGKFGTTNKSTENL
-CCCCCCCCCCHHHH		40.8219823750
10PhosphorylationKFGTTNKSTENLLRD
CCCCCCCCHHHHHHC		42.9219823750
11PhosphorylationFGTTNKSTENLLRDK
CCCCCCCHHHHHHCC		30.4221440633
18UbiquitinationTENLLRDKFVPETSP
HHHHHHCCCCCCCCC		41.6519722269
23PhosphorylationRDKFVPETSPTNIPT
HCCCCCCCCCCCCCC		33.6629136822
24PhosphorylationDKFVPETSPTNIPTD
CCCCCCCCCCCCCCC		28.2321551504
26PhosphorylationFVPETSPTNIPTDVL
CCCCCCCCCCCCCCE		45.6129136822
30PhosphorylationTSPTNIPTDVLIKQG
CCCCCCCCCCEEECC		34.6429136822
40PhosphorylationLIKQGQITDSTESLI
EEECCCCCCCCHHHC		18.9329136822
42PhosphorylationKQGQITDSTESLIHG
ECCCCCCCCHHHCCC		25.9829136822
43PhosphorylationQGQITDSTESLIHGG
CCCCCCCCHHHCCCC		32.1923749301
45PhosphorylationQITDSTESLIHGGAE
CCCCCCHHHCCCCCH		32.4823749301
80PhosphorylationDPPFHLPSPPVDSTN
CCCCCCCCCCCCCCC		48.4728889911
103PhosphorylationLPKNGLRYDLNDISV
CCCCCCCCCCCCCCH		29.8025005228
109PhosphorylationRYDLNDISVEVIEDL
CCCCCCCCHHHHHHH		18.3225005228
117PhosphorylationVEVIEDLYRQIEAFL
HHHHHHHHHHHHHHH		16.8825005228
528PhosphorylationIQYGKISSEHVKTAF
HHHCCCCCHHHHHHH		34.8820377248
533PhosphorylationISSEHVKTAFCAKYL
CCCHHHHHHHHHHHH		24.7120377248
619PhosphorylationLYTKLAPSMDRVKLS
EEHHCCCCCCHHHHH		27.9228889911
801PhosphorylationWKNRSDSSPKRRKDF
HHCCCCCCCCHHHCC		39.1628889911
816PhosphorylationNLKHELKTPIRSDSQ
CCCCCCCCCCCCCCC		36.2521700874
820PhosphorylationELKTPIRSDSQNAST
CCCCCCCCCCCCCCC		42.1921440633
855PhosphorylationRARRAIPSPVKSSSV
HHHHHCCCCCCCCHH		35.8917287358
859PhosphorylationAIPSPVKSSSVLDST
HCCCCCCCCHHCCHH		28.2521440633
868AcetylationSVLDSTAKKQINLES
HHCCHHCCCCCCCCC		45.3523572591
869AcetylationVLDSTAKKQINLEST
HCCHHCCCCCCCCCC		54.6823572591
876PhosphorylationKQINLESTTGLNGSP
CCCCCCCCCCCCCCC		18.6021700874
877PhosphorylationQINLESTTGLNGSPT
CCCCCCCCCCCCCCC		49.2921700874
882PhosphorylationSTTGLNGSPTRGKPL
CCCCCCCCCCCCCCC		23.2523749301
892PhosphorylationRGKPLRYSPRRTTRN
CCCCCCCCCCCCCCC		12.9021700874
918PhosphorylationRIPAVPFSLSANSPK
CCCCCCCCCCCCCCC		18.4930377154
920PhosphorylationPAVPFSLSANSPKID
CCCCCCCCCCCCCCC		24.9821700874
923PhosphorylationPFSLSANSPKIDQDM
CCCCCCCCCCCCCCH		27.5629734811
939PhosphorylationYIREHDKSPLSRKRQ
HHHHHCCCCCHHCCC		36.8121440633
942PhosphorylationEHDKSPLSRKRQ---
HHCCCCCHHCCC---		38.8624961812
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 SFI1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SFI1_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 SFI1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC31_YEASTCDC31physical
14504268
SP110_YEASTSPC110physical
14504268
CDC31_YEASTCDC31genetic
14504268
BIK1_YEASTBIK1genetic
16972090
MAD2_YEASTMAD2genetic
16972090
KAR3_YEASTKAR3genetic
16972090
CIN8_YEASTCIN8genetic
16972090
BBP1_YEASTBBP1genetic
17392514
CIN8_YEASTCIN8genetic
17392514
MPS2_YEASTMPS2genetic
17392514
NDC1_YEASTNDC1genetic
17392514
KAR1_YEASTKAR1genetic
17392514
SUL1_YEASTSUL1genetic
20093466
AGP1_YEASTAGP1genetic
20093466
ARO1_YEASTARO1genetic
20093466
RTF1_YEASTRTF1genetic
20093466
UPF3_YEASTUPF3genetic
20093466
NMD2_YEASTNMD2genetic
20093466
UPS1_YEASTUPS1genetic
20093466
NAM7_YEASTNAM7genetic
20093466
CIK1_YEASTCIK1genetic
20093466
MED9_YEASTCSE2genetic
20093466
BRE5_YEASTBRE5genetic
20093466
SIN3_YEASTSIN3genetic
20093466
BUB3_YEASTBUB3genetic
20093466
HSP7F_YEASTSSE1genetic
20093466
KAR3_YEASTKAR3genetic
20093466
CDC31_YEASTCDC31physical
20489023
SFI1_YEASTSFI1physical
26076691
BLM10_YEASTBLM10genetic
27708008
VPS53_YEASTVPS53genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
CALM_YEASTCMD1genetic
27708008
CKS1_YEASTCKS1genetic
27708008
SLI15_YEASTSLI15genetic
27708008
CDK1_YEASTCDC28genetic
27708008
SCC1_YEASTMCD1genetic
27708008
MPS1_YEASTMPS1genetic
27708008
RPN5_YEASTRPN5genetic
27708008
RRP1_YEASTRRP1genetic
27708008
TAF12_YEASTTAF12genetic
27708008
SP110_YEASTSPC110genetic
27708008
HSF_YEASTHSF1genetic
27708008
DAM1_YEASTDAM1genetic
27708008
SDA1_YEASTSDA1genetic
27708008
EXO70_YEASTEXO70genetic
27708008
ARP3_YEASTARP3genetic
27708008
NEP1_YEASTEMG1genetic
27708008
CD123_YEASTCDC123genetic
27708008
PDS5_YEASTPDS5genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
HAS1_YEASTHAS1genetic
27708008
CAP_YEASTSRV2genetic
27708008
MYO2_YEASTMYO2genetic
27708008
TFC8_YEASTTFC8genetic
27708008
IPL1_YEASTIPL1genetic
27708008
DIM1_YEASTDIM1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
MED10_YEASTNUT2genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
CGR1_YEASTCGR1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
UPF3_YEASTUPF3genetic
27708008
BUB1_YEASTBUB1genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
NMD2_YEASTNMD2genetic
27708008
ICE2_YEASTICE2genetic
27708008
MGA2_YEASTMGA2genetic
27708008
MAD2_YEASTMAD2genetic
27708008
YJQ3_YEASTYJL163Cgenetic
27708008
CTK1_YEASTCTK1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
SPSY_YEASTSPE4genetic
27708008
NAM7_YEASTNAM7genetic
27708008
BUB3_YEASTBUB3genetic
27708008
DIA2_YEASTDIA2genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
YP022_YEASTYPR022Cgenetic
27708008
SPEE_YEASTSPE3genetic
27708008
KAR3_YEASTKAR3genetic
27708008
CDC14_YEASTCDC14physical
24954044
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SFI1_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-10; SER-24 AND THR-26,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-24, AND MASSSPECTROMETRY.

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