YCFI_YEAST - dbPTM
YCFI_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YCFI_YEAST
UniProt AC P39109
Protein Name Metal resistance protein YCF1
Gene Name YCF1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1515
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Cooperates for the ATP-dependent vacuolar transport of bilirubin and glutathione conjugates..
Protein Sequence MAGNLVSWACKLCRSPEGFGPISFYGDFTQCFIDGVILNLSAIFMITFGIRDLVNLCKKKHSGIKYRRNWIIVSRMALVLLEIAFVSLASLNISKEEAENFTIVSQYASTMLSLFVALALHWIEYDRSVVANTVLLFYWLFETFGNFAKLINILIRHTYEGIWYSGQTGFILTLFQVITCASILLLEALPKKPLMPHQHIHQTLTRRKPNPYDSANIFSRITFSWMSGLMKTGYEKYLVEADLYKLPRNFSSEELSQKLEKNWENELKQKSNPSLSWAICRTFGSKMLLAAFFKAIHDVLAFTQPQLLRILIKFVTDYNSERQDDHSSLQGFENNHPQKLPIVRGFLIAFAMFLVGFTQTSVLHQYFLNVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRNNKELKNLTKLGCYMAVTSFQFNIVPFLVSCCTFAVFVYTEDRALTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRLFTFFTNEELQPDSVQRLPKVKNIGDVAINIGDDATFLWQRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIMNGTVKENILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITKDADSPLWKLLNNYGKKNNGKSNEFGDSSESSVRESSIPVEGELEQLQKLNDLDFGNSDAISLRRASDATLGSIDFGDDENIAKREHREQGKVKWNIYLEYAKACNPKSVCVFILFIVISMFLSVMGNVWLKHWSEVNSRYGSNPNAARYLAIYFALGIGSALATLIQTIVLWVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVFRLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYADLKSEAPLIVEGHRPPKEWPSQGDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHLKEHVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDEATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKSLFYSLCMEAGLVNEN
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
236UbiquitinationLMKTGYEKYLVEADL
HHHCCHHHHEEHHHH		35.0917644757
245UbiquitinationLVEADLYKLPRNFSS
EEHHHHHCCCCCCCH		60.3517644757
245AcetylationLVEADLYKLPRNFSS
EEHHHHHCCCCCCCH		60.3524489116
251PhosphorylationYKLPRNFSSEELSQK
HCCCCCCCHHHHHHH		40.1522369663
252PhosphorylationKLPRNFSSEELSQKL
CCCCCCCHHHHHHHH		30.8425752575
256PhosphorylationNFSSEELSQKLEKNW
CCCHHHHHHHHHHHH		28.6629688323
258AcetylationSSEELSQKLEKNWEN
CHHHHHHHHHHHHHH		56.0624489116
339UbiquitinationFENNHPQKLPIVRGF
CCCCCCCCCHHHHHH		61.7622817900
495UbiquitinationSEILNNIKSLKLYAW
HHHHHHHHHHCCCCC		52.4324961812
504AcetylationLKLYAWEKPYREKLE
HCCCCCCCCHHHHHH		36.3322865919
504UbiquitinationLKLYAWEKPYREKLE
HCCCCCCCCHHHHHH		36.3323749301
509UbiquitinationWEKPYREKLEEVRNN
CCCCHHHHHHHHHCC		52.8023749301
654UbiquitinationKNINFQAKKGNLTCI
EEEECEEECCCEEEE		50.8917644757
655UbiquitinationNINFQAKKGNLTCIV
EEECEEECCCEEEEE		56.9217644757
664UbiquitinationNLTCIVGKVGSGKTA
CEEEEEEECCCCHHH		32.3117644757
862UbiquitinationYGKKNNGKSNEFGDS
CCCCCCCCCCCCCCC		52.8323749301
863PhosphorylationGKKNNGKSNEFGDSS
CCCCCCCCCCCCCCC		42.8820377248
869PhosphorylationKSNEFGDSSESSVRE
CCCCCCCCCCCHHHH		36.0622369663
870PhosphorylationSNEFGDSSESSVRES
CCCCCCCCCCHHHHC		46.3622369663
872PhosphorylationEFGDSSESSVRESSI
CCCCCCCCHHHHCCC		35.7622369663
873PhosphorylationFGDSSESSVRESSIP
CCCCCCCHHHHCCCC		22.5722369663
877PhosphorylationSESSVRESSIPVEGE
CCCHHHHCCCCCCCH		24.0122369663
878PhosphorylationESSVRESSIPVEGEL
CCHHHHCCCCCCCHH		26.5922369663
890UbiquitinationGELEQLQKLNDLDFG
CHHHHHHHHCCCCCC		58.8323749301
899PhosphorylationNDLDFGNSDAISLRR
CCCCCCCCCHHHHHC		28.8820377248
903PhosphorylationFGNSDAISLRRASDA
CCCCCHHHHHCCCCC		19.9722369663
908PhosphorylationAISLRRASDATLGSI
HHHHHCCCCCCCCCC		26.4322369663
911PhosphorylationLRRASDATLGSIDFG
HHCCCCCCCCCCCCC		36.3222369663
914PhosphorylationASDATLGSIDFGDDE
CCCCCCCCCCCCCCC		23.3022369663
1059UbiquitinationRFSNDIYKVDALLGR
HHCCCHHHHHHHHCC		33.6922817900
1059AcetylationRFSNDIYKVDALLGR
HHCCCHHHHHHHHCC		33.6924489116
1122PhosphorylationRELRRLDSITRSPIY
HHHHCHHHCCCCCHH		30.3728889911
1124PhosphorylationLRRLDSITRSPIYSH
HHCHHHCCCCCHHHH		29.1025005228
1264AcetylationVEGHRPPKEWPSQGD
EECCCCCCCCCCCCC		75.0924489116
1297AcetylationKHINIHIKPNEKVGI
EEEEEEECCCCEEEE		27.8522865919
1312AcetylationVGRTGAGKSSLTLAL
ECCCCCCHHHHHHHH		36.0224489116
1313PhosphorylationGRTGAGKSSLTLALF
CCCCCCHHHHHHHHH		29.6622369663
1314PhosphorylationRTGAGKSSLTLALFR
CCCCCHHHHHHHHHH		28.9422369663
1316PhosphorylationGAGKSSLTLALFRMI
CCCHHHHHHHHHHHH		16.3622369663
1348AcetylationGLYDLRHKLSIIPQD
CCCCHHHCEEECCCC		37.1822865919
1393PhosphorylationHLKEHVLSMSNDGLD
HHHHHHHHCCCCCCC		21.0530377154
1404PhosphorylationDGLDAQLTEGGGNLS
CCCCCEEECCCCCCC		22.0930377154
1428PhosphorylationARAMLVPSKILVLDE
HHHHHCCCEEEEECC		25.5027017623
1437PhosphorylationILVLDEATAAVDVET
EEEECCCCCCCCCCH		17.0727017623
1444PhosphorylationTAAVDVETDKVVQET
CCCCCCCHHHHHHHH		40.7527017623
1451PhosphorylationTDKVVQETIRTAFKD
HHHHHHHHHHHHCCC		9.9227017623
1484UbiquitinationIIVLDNGKVAEFDSP
EEEEECCCEEEECCC		44.5222106047
1484AcetylationIIVLDNGKVAEFDSP
EEEEECCCEEEECCC		44.5224489116
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 YCFI_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YCFI_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 YCFI_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GTS1_YEASTGTS1physical
9914482
AP1_YEASTYAP1genetic
11527213
YBT1_YEASTYBT1genetic
12819858
BPT1_YEASTBPT1genetic
12455987
BPT1_YEASTBPT1genetic
10790694
ARR3_YEASTARR3genetic
14978214
YOR1_YEASTYOR1genetic
16814918
KIN4_YEASTKIN4physical
17434123
TUS1_YEASTTUS1physical
17434123
NUM1_YEASTNUM1physical
17434123
MPG1_YEASTPSA1physical
17434123
FAB1_YEASTFAB1physical
17434123
RGC1_YEASTRGC1physical
17434123
HAL5_YEASTHAL5physical
18667437
CSK21_YEASTCKA1physical
18667437
FPS1_YEASTFPS1genetic
20026328
ARR3_YEASTARR3genetic
20026328
ARR3_YEASTARR3genetic
11527213
ARR3_YEASTARR3genetic
20655873
CSK22_YEASTCKA2physical
20812950
CSK2B_YEASTCKB1physical
20812950
CSK2C_YEASTCKB2physical
20812950
CSK21_YEASTCKA1physical
20812950
ATC1_YEASTPMR1genetic
21911041
GSHR_YEASTGLR1genetic
23242256
VPS33_YEASTVPS33physical
23658021
VAM3_YEASTVAM3physical
23658021
YPT7_YEASTYPT7physical
23658021
KC13_YEASTYCK3physical
23831759
BMH1_YEASTBMH1physical
23831759
ADH1_YEASTADH1physical
23831759
COFI_YEASTCOF1physical
23831759
RAS2_YEASTRAS2physical
23831759
ARC1_YEASTARC1physical
23831759
GBLP_YEASTASC1physical
23831759
NCB5R_YEASTCBR1physical
23831759
KPYK1_YEASTCDC19physical
23831759
EF1B_YEASTEFB1physical
23831759
NACB1_YEASTEGD1physical
23831759
NACA_YEASTEGD2physical
23831759
FAS2_YEASTFAS2physical
23831759
ALF_YEASTFBA1physical
23831759
PMG1_YEASTGPM1physical
23831759
GST1_YEASTGTT1physical
23831759
PABP_YEASTPAB1physical
23831759
PDC1_YEASTPDC1physical
23831759
PGK_YEASTPGK1physical
23831759
PHO81_YEASTPHO81physical
23831759
SNU13_YEASTSNU13physical
23831759
SODC_YEASTSOD1physical
23831759
SSB2_YEASTSSB2physical
23831759
STM1_YEASTSTM1physical
23831759
T2FA_YEASTTFG1physical
23831759
IF4B_YEASTTIF3physical
23831759
TMA7_YEASTTMA7physical
23831759
VATG_YEASTVMA10physical
23831759
YNU8_YEASTYNL208Wphysical
23831759
AHP1_YEASTAHP1genetic
24444374
TSA1_YEASTTSA1genetic
24444374
GSHR_YEASTGLR1genetic
24444374
YCFI_YEASTYCF1physical
24444374
TUS1_YEASTTUS1genetic
24444374
KIN4_YEASTKIN4genetic
24444374
RGC1_YEASTRGC1genetic
24444374
FAB1_YEASTFAB1genetic
24444374
NUM1_YEASTNUM1genetic
24444374
ORC2_YEASTORC2genetic
27708008
CDK1_YEASTCDC28genetic
27708008
TAF5_YEASTTAF5genetic
27708008
NSE4_YEASTNSE4genetic
27708008
RPN5_YEASTRPN5genetic
27708008
SP110_YEASTSPC110genetic
27708008
RSP5_YEASTRSP5genetic
27708008
STT3_YEASTSTT3genetic
27708008
PRS8_YEASTRPT6genetic
27708008
BRL1_YEASTBRL1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
MET30_YEASTMET30genetic
27708008
PSB1_YEASTPRE3genetic
27708008
PRS7_YEASTRPT1genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SSL1_YEASTSSL1genetic
27708008
MED14_YEASTRGR1genetic
27708008
CFT2_YEASTCFT2genetic
27708008
TAD3_YEASTTAD3genetic
27708008
ORC1_YEASTORC1genetic
27708008
ERO1_YEASTERO1genetic
27708008
RNA1_YEASTRNA1genetic
27708008
LST8_YEASTLST8genetic
27708008
DCP2_YEASTDCP2genetic
27708008
NAB3_YEASTNAB3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YCFI_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-251; SER-869; SER-870;SER-872; SER-873; SER-878; SER-903; SER-908; THR-911 AND SER-914, ANDMASS 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-251; SER-908; THR-911AND SER-914, AND MASS SPECTROMETRY.
"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-251, AND MASSSPECTROMETRY.
"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-903; SER-908; THR-911AND SER-914, AND MASS SPECTROMETRY.
"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-878 AND SER-903, ANDMASS SPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908 AND THR-911, ANDMASS SPECTROMETRY.

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