FET3_YEAST - dbPTM
FET3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FET3_YEAST
UniProt AC P38993
Protein Name Iron transport multicopper oxidase FET3
Gene Name FET3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 636
Subcellular Localization Cell membrane
Single-pass type I membrane protein
Extracellular side.
Protein Description Iron transport multicopper ferroxidase required for Fe(2+) ion high affinity uptake. Required to oxidize Fe(2+) and release it from the transporter. Essential component of copper-dependent iron transport..
Protein Sequence MTNALLSIAVLLFSMLSLAQAETHTFNWTTGWDYRNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIKDDSFPYDYDEELSLSLSEWYHDLVTDLTKSFMSVYNPTGAEPIPQNLIVNNTMNLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKFDDTMLDVIPSDLQLNATSYMVYNKTAALPTQNYVDSIDNFLDDFYLQPYEKEAIYGEPDHVITVDVVMDNLKNGVNYAFFNNITYTAPKVPTLMTVLSSGDQANNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRTYDDALGEVPHSFDPDNHPAFPEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWHLLQGLGLVLVEDPFGIQDAHSQQLSENHLEVCQSCSVATEGNAAANTLDLTDLTGENVQHAFIPTGFTKKGIIAMTFSCFAGILGIITIAIYGMMDMEDATEKVIRDLHVDPEVLLNEVDENEERQVNEDRHSTEKHQFLTKAKRFF
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
27N-linked_GlycosylationQAETHTFNWTTGWDY
HHHHCCCCCCCCCCC		36.0216230618
41UbiquitinationYRNVDGLKSRPVITC
CCCCCCCCCCCEEEE		50.3717644757
61UbiquitinationWPDITVNKGDRVQIY
CCCEEECCCCEEEEE		58.8317644757
74N-linked_GlycosylationIYLTNGMNNTNTSMH
EEEECCCCCCCCCEE		54.28-
77N-linked_GlycosylationTNGMNNTNTSMHFHG
ECCCCCCCCCEEECC		32.0716230618
88N-linked_GlycosylationHFHGLFQNGTASMDG
EECCCCCCCEECCCC		42.3116230618
113N-linked_GlycosylationPGSTMLYNFTVDYNV
CCCEEEEEEEEECCC		23.3516230618
194N-linked_GlycosylationIPQNLIVNNTMNLTW
CCCCEEECCCEEEEE		31.1216230618
198N-linked_GlycosylationLIVNNTMNLTWEVQP
EEECCCEEEEEEECC		32.0716230618
244N-linked_GlycosylationDGITTEKNVTDMLYI
ECCCCCCCCCCEEEE		35.3716230618
264UbiquitinationYTVLVHTKNDTDKNF
EEEEEEECCCCCCCE		37.6417644757
265N-linked_GlycosylationTVLVHTKNDTDKNFA
EEEEEECCCCCCCEE		59.58-
269UbiquitinationHTKNDTDKNFAIMQK
EECCCCCCCEEEEEE		56.9317644757
276UbiquitinationKNFAIMQKFDDTMLD
CCEEEEEECCCCCHH		33.1217644757
292N-linked_GlycosylationIPSDLQLNATSYMVY
CCCCCCCCCEEEEEE		28.36-
300N-linked_GlycosylationATSYMVYNKTAALPT
CEEEEEEECCCCCCC		24.6416230618
328UbiquitinationFYLQPYEKEAIYGEP
CCCCCCCHHHHHCCC		46.7517644757
349UbiquitinationDVVMDNLKNGVNYAF
EEEEECCCCCCCEEE		58.8917644757
359N-linked_GlycosylationVNYAFFNNITYTAPK
CCEEEECCCCEECCC		23.8716230618
381N-linked_GlycosylationLSSGDQANNSEIYGS
CCCCCCCCCCEEECC		47.1016230618
622PhosphorylationQVNEDRHSTEKHQFL
CCCCCCHHHHHHHHH		38.8719823750
623PhosphorylationVNEDRHSTEKHQFLT
CCCCCHHHHHHHHHH		42.8224909858
631AcetylationEKHQFLTKAKRFF--
HHHHHHHHHHHHC--		54.8025381059
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 FET3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FET3_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 FET3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FET5_YEASTFET5genetic
9413439
FET4_YEASTFET4genetic
9413439
SMF3_YEASTSMF3genetic
12921533
FRE1_YEASTFRE1genetic
12954629
FTR1_YEASTFTR1physical
16522632
FLC1_YEASTFLC1genetic
16717099
FLC2_YEASTFLC2genetic
16717099
OSTD_YEASTSWP1physical
18467557
HEM1_YEASTHEM1genetic
18326586
TPS1_YEASTTPS1genetic
20093466
RLA1_YEASTRPP1Agenetic
20093466
HXKB_YEASTHXK2genetic
20093466
PALF_YEASTRIM8genetic
20093466
YGB0_YEASTMPO1genetic
20093466
YG34_YEASTYGR122Wgenetic
20093466
PACC_YEASTRIM101genetic
20093466
GRE3_YEASTGRE3genetic
20093466
FET4_YEASTFET4genetic
20093466
DFG16_YEASTDFG16genetic
20093466
PALA_YEASTRIM20genetic
20093466
SLA2_YEASTSLA2genetic
12921533
PHO88_YEASTPHO88physical
16093310
ALG1_YEASTALG1physical
16093310
MKAR_YEASTIFA38physical
16093310
ELO2_YEASTELO2physical
16093310
SHR3_YEASTSHR3physical
16093310
PSS_YEASTCHO1physical
16093310
MST27_YEASTMST27physical
16093310
GUP1_YEASTGUP1physical
16093310
ERV29_YEASTERV29physical
16093310
YHU0_YEASTYHR140Wphysical
16093310
SNL1_YEASTSNL1physical
16093310
PHO86_YEASTPHO86physical
16093310
ELO1_YEASTELO1physical
16093310
LAC1_YEASTLAC1physical
16093310
YET1_YEASTYET1physical
16093310
SRPB_YEASTSRP102physical
16093310
ELO3_YEASTELO3physical
16093310
GSF2_YEASTGSF2physical
16093310
PFA4_YEASTPFA4physical
16093310
ERP4_YEASTERP4physical
16093310
PNS1_YEASTPNS1physical
16093310
SLY41_YEASTSLY41physical
16093310
SEC62_YEASTSEC62physical
16093310
ALG5_YEASTALG5physical
16093310
VATL2_YEASTVMA11physical
16093310
CCS1_YEASTCCS1genetic
20439772
PALH_YEASTRIM21genetic
20439772
DCAM_YEASTSPE2genetic
20439772
SYRM_YEASTMSR1genetic
20439772
MIT1_YEASTMIT1genetic
20439772
FET4_YEASTFET4genetic
20439772
PACC_YEASTRIM101genetic
20439772
PALA_YEASTRIM20genetic
20439772
STP22_YEASTSTP22genetic
20439772
RIB4_YEASTRIB4genetic
20439772
VPS33_YEASTVPS33genetic
20526336
PER1_YEASTPER1genetic
20526336
YPK2_YEASTYPK2genetic
20526336
SRS2_YEASTSRS2genetic
21459050
ENB1_YEASTENB1genetic
21542867
FTR1_YEASTFTR1physical
22579979
TPS1_YEASTTPS1genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
UME6_YEASTUME6genetic
27708008
YGB0_YEASTMPO1genetic
27708008
PALF_YEASTRIM8genetic
27708008
RTG2_YEASTRTG2genetic
27708008
TMA23_YEASTTMA23genetic
27708008
FET4_YEASTFET4genetic
27708008
PALA_YEASTRIM20genetic
27708008
FET4_YEASTFET4genetic
27169355
DUN1_YEASTDUN1genetic
24958100
SML1_YEASTSML1genetic
24958100
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FET3_YEAST

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The copper-iron connection in biology: structure of the metallo-oxidase Fet3p.";
Taylor A.B., Stoj C.S., Ziegler L., Kosman D.J., Hart P.J.;
Proc. Natl. Acad. Sci. U.S.A. 102:15459-15464(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-555, COPPER-BINDING SITES,AND GLYCOSYLATION AT ASN-27; ASN-77; ASN-88; ASN-113; ASN-194;ASN-198; ASN-244; ASN-300; ASN-359 AND ASN-381.
Phosphorylation
ReferencePubMed
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622, AND MASSSPECTROMETRY.

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