FLC3_YEAST - dbPTM
FLC3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLC3_YEAST
UniProt AC P53121
Protein Name Putative flavin carrier protein 3
Gene Name FLC3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 802
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 MRFLQVYKSSALIGLIILLASKVNLAEAKRKLVATSLVTCMENSQLSANSFDVVFNPDDRSLHYDLDMSTQIDSYIFADIDVYAYGFKIITKNVDLCSINWKQFCPVHPGNIQIDSIEYISSEYVNEIPGIAYQVPDIDAYARVKITNNVSEYLACIQIYFSNGKTVSQIGVKWATAVVAGIGLLLSAILSTFGNSTAASHISANTMSLFLYFQSVVVVAMQHVHRVPPIAAAWAENLVWSMGLIRISFMQRIFRWYVQSTGGTPSLYLTSTSMSVLAQRSWQYLMELPLIKRATNVLYGNANTLIFRGIKRLGYKMGIENTSIVCTGFTFFVLCGYVLAGFIIVFKCCVELATRLGWIQKARFWEFRKQWRMILKGALLRYIYIGFVQLTILSFWEFTERDSPAVIVIACLFILLSCGLMLWAAWRTVFFARRSVALYNNPAALLYGDEYVLHKYGFFYTMFNANHYWWNIVLLSYIFVKSLLVGFAQASGQTQVLFMFILDLFYFVAIIYYKPYLDRPTNIMNILIATVTVVNSFLFMFFSDLFNQSYKVAAIMGWIFFIMNAAFSFILLMMILAFAGMMLFSKNPDLRFKPAKDDRTSFQRNTMKPEGTVNRSVANELLALGNVAKDHDDNSDYESNDTGVNDELKQAQDETTPTTVTSSDDNKPTFSEKILSKFSRPKNENASTDALRVEAPKQQTFPHNLTNLSRENLSTLGSKPYPGHTRSQSDAHNGLINSFEEEDTSSNTDPFHDSTEGDLLDTSSSDGGFRSQNYVRDDSINSLGNNKQPLRKPPGFFDEGFM
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
149N-linked_GlycosylationARVKITNNVSEYLAC
EEEEECCCHHHHHEE		30.00-
321N-linked_GlycosylationGYKMGIENTSIVCTG
CCCCCCCCCEEEECH		36.89-
547N-linked_GlycosylationMFFSDLFNQSYKVAA
HHHHHHCCCHHHHHH		36.87-
608UbiquitinationSFQRNTMKPEGTVNR
CCCCCCCCCCCCCCH		37.5723749301
616PhosphorylationPEGTVNRSVANELLA
CCCCCCHHHHHHHHH		22.0025704821
635PhosphorylationAKDHDDNSDYESNDT
CCCCCCCCCCCCCCC		48.8722369663
637PhosphorylationDHDDNSDYESNDTGV
CCCCCCCCCCCCCCC		22.5222890988
639PhosphorylationDDNSDYESNDTGVND
CCCCCCCCCCCCCCH		33.5019823750
642PhosphorylationSDYESNDTGVNDELK
CCCCCCCCCCCHHHH		47.4822890988
649UbiquitinationTGVNDELKQAQDETT
CCCCHHHHHHCCCCC		41.3522817900
656PhosphorylationKQAQDETTPTTVTSS
HHHCCCCCCCCCCCC		19.3221440633
658PhosphorylationAQDETTPTTVTSSDD
HCCCCCCCCCCCCCC		31.6327017623
659PhosphorylationQDETTPTTVTSSDDN
CCCCCCCCCCCCCCC		24.0021551504
661PhosphorylationETTPTTVTSSDDNKP
CCCCCCCCCCCCCCC		22.0321440633
662PhosphorylationTTPTTVTSSDDNKPT
CCCCCCCCCCCCCCC		27.6820377248
663PhosphorylationTPTTVTSSDDNKPTF
CCCCCCCCCCCCCCC		39.3521440633
667UbiquitinationVTSSDDNKPTFSEKI
CCCCCCCCCCCCHHH		53.0523749301
669PhosphorylationSSDDNKPTFSEKILS
CCCCCCCCCCHHHHH		41.2121440633
687PhosphorylationRPKNENASTDALRVE
CCCCCCCCCCCCCCC		38.1022369663
688PhosphorylationPKNENASTDALRVEA
CCCCCCCCCCCCCCC		23.9222369663
700PhosphorylationVEAPKQQTFPHNLTN
CCCCCCCCCCCCCHH		36.3221551504
706PhosphorylationQTFPHNLTNLSRENL
CCCCCCCHHCCHHHH		39.1621440633
709PhosphorylationPHNLTNLSRENLSTL
CCCCHHCCHHHHHHC		39.3522369663
714PhosphorylationNLSRENLSTLGSKPY
HCCHHHHHHCCCCCC		32.9221551504
715PhosphorylationLSRENLSTLGSKPYP
CCHHHHHHCCCCCCC		38.0028889911
718PhosphorylationENLSTLGSKPYPGHT
HHHHHCCCCCCCCCC		33.3028889911
771PhosphorylationSSDGGFRSQNYVRDD
CCCCCCCCCCCCCCC		22.1022369663
774PhosphorylationGGFRSQNYVRDDSIN
CCCCCCCCCCCCCCC		6.8222369663
779PhosphorylationQNYVRDDSINSLGNN
CCCCCCCCCCCCCCC		28.1422369663
782PhosphorylationVRDDSINSLGNNKQP
CCCCCCCCCCCCCCC		35.6622369663
787UbiquitinationINSLGNNKQPLRKPP
CCCCCCCCCCCCCCC		58.2423749301
792UbiquitinationNNKQPLRKPPGFFDE
CCCCCCCCCCCCCCC		64.3523749301
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 FLC3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLC3_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 FLC3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PET8_YEASTPET8genetic
27708008
ALG14_YEASTALG14genetic
27708008
PRP11_YEASTPRP11genetic
27708008
ACT_YEASTACT1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
UTP15_YEASTUTP15genetic
27708008
RNA1_YEASTRNA1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
TYSY_YEASTCDC21genetic
27708008
GRPE_YEASTMGE1genetic
27708008
DYR_YEASTDFR1genetic
27708008
SYA_YEASTALA1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
RAV2_YEASTRAV2genetic
27708008
G3P3_YEASTTDH3genetic
27708008
VPS53_YEASTVPS53genetic
27708008
CBF1_YEASTCBF1genetic
27708008
MPCP_YEASTMIR1genetic
27708008
TDA5_YEASTTDA5genetic
27708008
YPT7_YEASTYPT7genetic
27708008
TSA1_YEASTTSA1genetic
27708008
GBLP_YEASTASC1genetic
27708008
YHM2_YEASTYHM2genetic
27708008
KC12_YEASTYCK2genetic
27708008
YOR22_YEASTYOR022Cgenetic
27708008
PMT3_YEASTPMT3genetic
27708008
YP089_YEASTYPR089Wgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FLC3_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-616; SER-687; THR-688;SER-779 AND SER-782, 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-687; SER-779 ANDSER-782, AND MASS SPECTROMETRY.

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