FLC1_YEAST - dbPTM
FLC1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLC1_YEAST
UniProt AC Q08967
Protein Name Flavin carrier protein 1
Gene Name FLC1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 793
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description May be responsible for the transport of FAD into the endoplasmic reticulum lumen, where it is required for oxidative protein folding..
Protein Sequence MQVLVTLWCLICTCLVLPVAAKKRTLTASSLVTCMENSQLSANSFDVSFSPDDRSLHYDLDMTTQIDSYIYAYVDVYAYGFKIITENFDVCSMGWKQFCPVHPGNIQIDSIEYIAQKYVKMIPGIAYQVPDIDAYVRLNIYNNVSENLACIQVFFSNGKTVSQIGVKWVTAVIAGIGLLTSAVLSTFGNSTAASHISANTMSLFLYFQSVAVVAMQHVDSVPPIAAAWSENLAWSMGLIRITFMQKIFRWYVEATGGSASLYLTATTMSVLTQRGLDYLKNTSVYKRAENVLYGNSNTLIFRGIKRMGYRMKIENTAIVCTGFTFFVLCGYFLAGFIMACKYSIELCIRCGWMRSDRFYQFRKNWRSVLKGSLLRYIYIGFTQLTILSFWEFTERDSAGVIVIACLFIVLSCGLMAWAAYRTIFFASKSVEMYNNPAALLYGDEYVLNKYGFFYTMFNAKHYWWNALLTTYILVKALFVGFAQASGKTQALAIFIIDLAYFVAIIRYKPYLDRPTNIVNIFICTVTLVNSFLFMFFSNLFNQKYAVSAIMGWVFFIMNAAFSLLLLLMILAFTTIILFSKNPDSRFKPAKDDRASFQKHAIPHEGALNKSVANELMALGNVAKDHTENWEYELKSQEGKSEDNLFGVEYDDEKTGTNSENAESSSKETTRPTFSEKVLRSLSIKRNKSKLGSFKRSAPDKITQQEVSPDRASSSPNSKSYPGVSHTRQESEANNGLINAYEDEQFSLMEPSILEDAASSTQMHAMPARDLSLSSVANAQDVTKKANILDPDYL
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
143N-linked_GlycosylationVRLNIYNNVSENLAC
EEHHHCCCCCCCEEE		23.01-
281N-linked_GlycosylationRGLDYLKNTSVYKRA
HCHHHHHCCHHHHCH		34.68-
598UbiquitinationDDRASFQKHAIPHEG
CCHHHHHHHCCCCCC		32.7522817900
609UbiquitinationPHEGALNKSVANELM
CCCCCCCHHHHHHHH		47.3517644757
610PhosphorylationHEGALNKSVANELMA
CCCCCCHHHHHHHHH		25.9521440633
623UbiquitinationMALGNVAKDHTENWE
HHHCCHHHCCCCCCE		45.8423749301
626PhosphorylationGNVAKDHTENWEYEL
CCHHHCCCCCCEEEE		40.9428889911
634UbiquitinationENWEYELKSQEGKSE
CCCEEEECCCCCCCC		37.8524961812
635PhosphorylationNWEYELKSQEGKSED
CCEEEECCCCCCCCC		46.2022369663
639UbiquitinationELKSQEGKSEDNLFG
EECCCCCCCCCCEEE		50.3323749301
640PhosphorylationLKSQEGKSEDNLFGV
ECCCCCCCCCCEEEE		62.1222369663
649PhosphorylationDNLFGVEYDDEKTGT
CCEEEEEECCCCCCC		26.7019779198
653UbiquitinationGVEYDDEKTGTNSEN
EEEECCCCCCCCCCC		60.2823749301
654PhosphorylationVEYDDEKTGTNSENA
EEECCCCCCCCCCCC		47.3819779198
656PhosphorylationYDDEKTGTNSENAES
ECCCCCCCCCCCCCC		40.5819779198
658PhosphorylationDEKTGTNSENAESSS
CCCCCCCCCCCCCCC		31.8720377248
663PhosphorylationTNSENAESSSKETTR
CCCCCCCCCCCCCCC		37.1820377248
664PhosphorylationNSENAESSSKETTRP
CCCCCCCCCCCCCCC		36.6120377248
665PhosphorylationSENAESSSKETTRPT
CCCCCCCCCCCCCCC		43.7320377248
668PhosphorylationAESSSKETTRPTFSE
CCCCCCCCCCCCCCH		31.6620377248
669PhosphorylationESSSKETTRPTFSEK
CCCCCCCCCCCCCHH		35.4221551504
672PhosphorylationSKETTRPTFSEKVLR
CCCCCCCCCCHHHHH		36.1824961812
680PhosphorylationFSEKVLRSLSIKRNK
CCHHHHHHHCCCCCH		23.4724961812
682PhosphorylationEKVLRSLSIKRNKSK
HHHHHHHCCCCCHHH		27.5821440633
692PhosphorylationRNKSKLGSFKRSAPD
CCHHHCCCCCCCCCC		37.7215665377
696PhosphorylationKLGSFKRSAPDKITQ
HCCCCCCCCCCCCCC		44.7523749301
700UbiquitinationFKRSAPDKITQQEVS
CCCCCCCCCCCCCCC		46.7423749301
702PhosphorylationRSAPDKITQQEVSPD
CCCCCCCCCCCCCCC		29.9122369663
707PhosphorylationKITQQEVSPDRASSS
CCCCCCCCCCCCCCC		21.9622369663
712PhosphorylationEVSPDRASSSPNSKS
CCCCCCCCCCCCCCC		32.0425521595
713PhosphorylationVSPDRASSSPNSKSY
CCCCCCCCCCCCCCC		49.1620377248
714PhosphorylationSPDRASSSPNSKSYP
CCCCCCCCCCCCCCC		26.1322369663
717PhosphorylationRASSSPNSKSYPGVS
CCCCCCCCCCCCCCC		26.7722369663
718UbiquitinationASSSPNSKSYPGVSH
CCCCCCCCCCCCCCC		61.7323749301
719PhosphorylationSSSPNSKSYPGVSHT
CCCCCCCCCCCCCCC		36.0628889911
751PhosphorylationQFSLMEPSILEDAAS
CCCCCCCHHHHHHHH		26.8819779198
758PhosphorylationSILEDAASSTQMHAM
HHHHHHHHCCCCCCC		35.3219779198
771PhosphorylationAMPARDLSLSSVANA
CCCHHHCCHHHHCCC		30.4122369663
773PhosphorylationPARDLSLSSVANAQD
CHHHCCHHHHCCCHH		21.2822369663
774PhosphorylationARDLSLSSVANAQDV
HHHCCHHHHCCCHHH		30.4622369663
782PhosphorylationVANAQDVTKKANILD
HCCCHHHHHHHCCCC		34.8122890988
783UbiquitinationANAQDVTKKANILDP
CCCHHHHHHHCCCCC		50.1423749301
784UbiquitinationNAQDVTKKANILDPD
CCHHHHHHHCCCCCC		36.9823749301
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 FLC1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLC1_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 FLC1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FLC2_YEASTFLC2genetic
16717099
FLC3_YEASTFLC3genetic
16717099
KTR4_YEASTKTR4genetic
16717099
VAN1_YEASTVAN1genetic
16717099
HOC1_YEASTHOC1genetic
16717099
MSG5_YEASTMSG5genetic
16717099
PP2C1_YEASTPTC1genetic
16717099
APM2_YEASTAPM2genetic
16717099
SMY2_YEASTSMY2genetic
16717099
SKG3_YEASTSKG3genetic
16717099
MEP3_YEASTMEP3physical
18467557
ALG14_YEASTALG14genetic
27708008
CDC37_YEASTCDC37genetic
27708008
MOB1_YEASTMOB1genetic
27708008
PRI2_YEASTPRI2genetic
27708008
ORC1_YEASTORC1genetic
27708008
ROT1_YEASTROT1genetic
27708008
PROF_YEASTPFY1genetic
27708008
FLC2_YEASTFLC2genetic
27462707
FLC3_YEASTFLC3genetic
27462707
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FLC1_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-771 AND SER-774, ANDMASS 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-771, 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-692 AND SER-771, ANDMASS SPECTROMETRY.

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