FLC2_YEAST - dbPTM
FLC2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLC2_YEAST
UniProt AC P39719
Protein Name Flavin carrier protein 2
Gene Name FLC2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 783
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 MIFLNTFARCLLTCFVLCSGTARSSDTNDTTPASAKHLQTTSLLTCMDNSQLTASFFDVKFYPDNNTVIFDIDATTTLNGNVTVKAELLTYGLKVLDKTFDLCSLGQVSLCPLSAGRIDVMSTQVIESSITKQFPGIAYTIPDLDAQVRVVAYAQNDTEFETPLACVQAILSNGKTVQTKYAAWPIAAISGVGVLTSGFVSVIGYSATAAHIASNSISLFIYFQNLAITAMMGVSRVPPIAAAWTQNFQWSMGIINTNFMQKIFDWYVQATNGVSNVVVANKDVLSISVQKRAISMASSSDYNFDTILDDSNLYTTSEKDPSNYSAKILVLRGIERVAYLANIELSNFFLTGIVFFLFFLFVVVVSLIFFKALLEVLTRARILKETSNFFQYRKNWGSIIKGTLFRLSIIAFPQVSLLAIWEFTQVNSPAIVVDAVVILLIITGLLVYGTIRVFIKGRESLRLYKNPAYLLYSDTYFLNKFGFLYVQFKADKFWWLLPLLSYAFLRSLFVAVLQNQGKAQAMIIFVIELAYFVCLCWIRPYLDKRTNVFNIAIHLVNLINAFFFLFFSNLFKQPAVVSSVMAVILFVLNAVFALFLLLFTIVTCTLALLHRNPDVRYQPMKDDRVSFIPKIQNDFDGKNKNDSELFELRKAVMDTNENEEEKMFRDDTFGKNLNANTNTARLFDDETSSSSFKQNSSPFDASEVTEQPVQPTSAVMGTGGSFLSPQYQRASSASRTNLAPNNTSTSSLMKPESSLYLGNSNKSYSHFNNNGSNENARNNNPYL
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--MIFLNTFARCLLT
--CCCHHHHHHHHHH		22.3330377154
13PhosphorylationTFARCLLTCFVLCSG
HHHHHHHHHHHHHHC		7.3130377154
21PhosphorylationCFVLCSGTARSSDTN
HHHHHHCCCCCCCCC		11.5630377154
28N-linked_GlycosylationTARSSDTNDTTPASA
CCCCCCCCCCCCCCH		50.01-
65N-linked_GlycosylationDVKFYPDNNTVIFDI
EEEEECCCCEEEEEE		41.38-
81N-linked_GlycosylationATTTLNGNVTVKAEL
CCCEECCEEEEEEEH		25.80-
156N-linked_GlycosylationRVVAYAQNDTEFETP
EEEEEECCCCCCCCH		50.42-
323N-linked_GlycosylationTSEKDPSNYSAKILV
CCCCCCCCCCEEEEE		39.92-
621UbiquitinationDVRYQPMKDDRVSFI
CCCCCCCCCCCEEEC		64.2623749301
626PhosphorylationPMKDDRVSFIPKIQN
CCCCCCEEECCCCCC		20.5328889911
630UbiquitinationDRVSFIPKIQNDFDG
CCEEECCCCCCCCCC		52.7023749301
630AcetylationDRVSFIPKIQNDFDG
CCEEECCCCCCCCCC		52.7024489116
638UbiquitinationIQNDFDGKNKNDSEL
CCCCCCCCCCCHHHH		67.6023749301
643PhosphorylationDGKNKNDSELFELRK
CCCCCCHHHHHHHHH		45.6623607784
650UbiquitinationSELFELRKAVMDTNE
HHHHHHHHHHHCCCC		58.9423793018
662UbiquitinationTNENEEEKMFRDDTF
CCCCHHHHHHCCCCC		46.7723749301
668PhosphorylationEKMFRDDTFGKNLNA
HHHHCCCCCCCCCCC		38.2821440633
671UbiquitinationFRDDTFGKNLNANTN
HCCCCCCCCCCCCCC		54.8123749301
677PhosphorylationGKNLNANTNTARLFD
CCCCCCCCCCCCCCC		31.3819823750
679PhosphorylationNLNANTNTARLFDDE
CCCCCCCCCCCCCCC		15.8924961812
687PhosphorylationARLFDDETSSSSFKQ
CCCCCCCCCCCCCCC		40.6922890988
688PhosphorylationRLFDDETSSSSFKQN
CCCCCCCCCCCCCCC		26.6125521595
689PhosphorylationLFDDETSSSSFKQNS
CCCCCCCCCCCCCCC		37.1022369663
690PhosphorylationFDDETSSSSFKQNSS
CCCCCCCCCCCCCCC		39.2922890988
691PhosphorylationDDETSSSSFKQNSSP
CCCCCCCCCCCCCCC		38.1122369663
731PhosphorylationSPQYQRASSASRTNL
CHHHHCCCCCCCCCC		28.7321082442
732PhosphorylationPQYQRASSASRTNLA
HHHHCCCCCCCCCCC		29.3121082442
734PhosphorylationYQRASSASRTNLAPN
HHCCCCCCCCCCCCC		41.4023749301
736PhosphorylationRASSASRTNLAPNNT
CCCCCCCCCCCCCCC		31.8922369663
743PhosphorylationTNLAPNNTSTSSLMK
CCCCCCCCCCCCCCC		39.7722369663
744PhosphorylationNLAPNNTSTSSLMKP
CCCCCCCCCCCCCCC		28.5422369663
745PhosphorylationLAPNNTSTSSLMKPE
CCCCCCCCCCCCCCC		21.9422369663
746PhosphorylationAPNNTSTSSLMKPES
CCCCCCCCCCCCCCC		22.6522369663
747PhosphorylationPNNTSTSSLMKPESS
CCCCCCCCCCCCCCC		32.3522369663
750UbiquitinationTSTSSLMKPESSLYL
CCCCCCCCCCCCEEC		51.4223749301
753PhosphorylationSSLMKPESSLYLGNS
CCCCCCCCCEECCCC		33.8823749301
754PhosphorylationSLMKPESSLYLGNSN
CCCCCCCCEECCCCC		21.2623749301
756PhosphorylationMKPESSLYLGNSNKS
CCCCCCEECCCCCCC		17.9522369663
760PhosphorylationSSLYLGNSNKSYSHF
CCEECCCCCCCCCCC		43.7822369663
763PhosphorylationYLGNSNKSYSHFNNN
ECCCCCCCCCCCCCC		35.8022369663
764PhosphorylationLGNSNKSYSHFNNNG
CCCCCCCCCCCCCCC		14.0522369663
765PhosphorylationGNSNKSYSHFNNNGS
CCCCCCCCCCCCCCC		28.7922369663
772PhosphorylationSHFNNNGSNENARNN
CCCCCCCCCCCCCCC		42.9922369663
782PhosphorylationNARNNNPYL------
CCCCCCCCC------		27.4519823750
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 FLC2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLC2_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 FLC2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATC3_YEASTDRS2physical
11805826
FKS1_YEASTFKS1physical
11805826
PDR5_YEASTPDR5physical
11805826
TCB3_YEASTTCB3physical
11805826
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
KEX1_YEASTKEX1physical
18467557
SYP1_YEASTSYP1physical
18467557
FMP45_YEASTFMP45physical
18467557
FTR1_YEASTFTR1physical
18467557
SFK1_YEASTSFK1physical
18467557
ITR1_YEASTITR1physical
18467557
WSC3_YEASTWSC3physical
18467557
GPA2_YEASTGPA2physical
18467557
CHS1_YEASTCHS1physical
18467557
GAS1_YEASTGAS1physical
18467557
CHS5_YEASTCHS5physical
18467557
PST2_YEASTPST2physical
18467557
HNM1_YEASTHNM1physical
18467557
WSC2_YEASTWSC2physical
18467557
CHS3_YEASTCHS3physical
18467557
SMI1_YEASTSMI1physical
18467557
DFG5_YEASTDFG5physical
18467557
PLM2_YEASTPLM2physical
18467557
MUP1_YEASTMUP1physical
18467557
KEX1_YEASTKEX1physical
22615397
SSB1_YEASTSSB1physical
22940862
KPC1_YEASTPKC1genetic
27708008
SLT2_YEASTSLT2genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
VPS27_YEASTVPS27genetic
27708008
CDC1_YEASTCDC1genetic
27708008
GPI8_YEASTGPI8genetic
27708008
MOB2_YEASTMOB2genetic
27708008
STT3_YEASTSTT3genetic
27708008
BIG1_YEASTBIG1genetic
27708008
GRP78_YEASTKAR2genetic
27708008
KRE9_YEASTKRE9genetic
27708008
CDC91_YEASTGAB1genetic
27708008
ROT1_YEASTROT1genetic
27708008
APC5_YEASTAPC5genetic
27708008
KRE5_YEASTKRE5genetic
27708008
HAP3_YEASTHAP3genetic
27708008
ALG3_YEASTALG3genetic
27708008
NRG2_YEASTNRG2genetic
27708008
ECM33_YEASTECM33genetic
27708008
GLU2A_YEASTROT2genetic
27708008
YD012_YEASTYDL012Cgenetic
27708008
VHS1_YEASTVHS1genetic
27708008
RV167_YEASTRVS167genetic
27708008
BST1_YEASTBST1genetic
27708008
HXKB_YEASTHXK2genetic
27708008
CHO2_YEASTCHO2genetic
27708008
TRS65_YEASTTRS65genetic
27708008
SMI1_YEASTSMI1genetic
27708008
DNPEP_YEASTAPE4genetic
27708008
VPS53_YEASTVPS53genetic
27708008
GSH1_YEASTGSH1genetic
27708008
SNA3_YEASTSNA3genetic
27708008
CBF1_YEASTCBF1genetic
27708008
DCW1_YEASTDCW1genetic
27708008
CASP_YEASTCOY1genetic
27708008
LOT5_YEASTLOT5genetic
27708008
MEH1_YEASTMEH1genetic
27708008
VPS51_YEASTVPS51genetic
27708008
TRM2_YEASTTRM2genetic
27708008
GTO2_YEASTECM4genetic
27708008
RIC1_YEASTRIC1genetic
27708008
SKG3_YEASTSKG3genetic
27708008
YPT6_YEASTYPT6genetic
27708008
YMY9_YEASTYMR099Cgenetic
27708008
YM35_YEASTYMR160Wgenetic
27708008
RAD14_YEASTRAD14genetic
27708008
GAS1_YEASTGAS1genetic
27708008
SGT2_YEASTSGT2genetic
27708008
CY1_YEASTCYT1genetic
27708008
OST3_YEASTOST3genetic
27708008
PALA_YEASTRIM20genetic
27708008
FLC1_YEASTFLC1genetic
27708008
NEW1_YEASTNEW1genetic
27708008
QCR2_YEASTQCR2genetic
27708008
FLC3_YEASTFLC3genetic
27462707
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FLC2_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-689 AND SER-744, ANDMASS SPECTROMETRY.

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