ZRC1_YEAST - dbPTM
ZRC1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZRC1_YEAST
UniProt AC P20107
Protein Name Zinc/cadmium resistance protein
Gene Name ZRC1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 442
Subcellular Localization Mitochondrion membrane
Multi-pass membrane protein.
Protein Description Probably responsible for the uptake of zinc and cadmium ions..
Protein Sequence MITGKELRIISLLTLDTVFFLLEITIGYMSHSLALIADSFHMLNDIISLLVALWAVDVAKNRGPDAKYTYGWKRAEILGALINAVFLIALCFSIMIEALQRLIEPQEIQNPRLVLYVGVAGLISNVVGLFLFHDHGSDSLHSHSHGSVESGNNDLDIESNATHSHSHASLPNDNLAIDEDAISSPGPSGQIGEVLPQSVVNRLSNESQPLLNHDDHDHSHESKKPGHRSLNMHGVFLHVLGDALGNIGVIAAALFIWKTEYSWRYYSDPIVSLIITIIIFSSALPLSRRASRILLQATPSTISADQIQREILAVPGVIAVHDFHVWNLTESIYIASIHVQIDCAPDKFMSSAKLIRKIFHQHGIHSATVQPEFVSGDVNEDIRRRFSIIAGGSPSSSQEAFDSHGNTEHGRKKRSPTAYGATTASSNCIVDDAVNCNTSNCL
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
67UbiquitinationKNRGPDAKYTYGWKR
HHCCCCCCCCCCHHH		45.5723749301
204PhosphorylationQSVVNRLSNESQPLL
HHHHHHHCCCCCCCC		35.0030377154
207PhosphorylationVNRLSNESQPLLNHD
HHHHCCCCCCCCCCC		41.1529136822
353AcetylationDKFMSSAKLIRKIFH
HHHHCHHHHHHHHHH		46.5224489116
357UbiquitinationSSAKLIRKIFHQHGI
CHHHHHHHHHHHCCC		42.6122106047
387PhosphorylationEDIRRRFSIIAGGSP
HHHHHHHEEEECCCC		15.9817330950
393PhosphorylationFSIIAGGSPSSSQEA
HEEEECCCCCCCHHH		22.2317330950
395PhosphorylationIIAGGSPSSSQEAFD
EEECCCCCCCHHHHH		44.3017330950
396PhosphorylationIAGGSPSSSQEAFDS
EECCCCCCCHHHHHC		39.1517330950
397PhosphorylationAGGSPSSSQEAFDSH
ECCCCCCCHHHHHCC		36.0617330950
403PhosphorylationSSQEAFDSHGNTEHG
CCHHHHHCCCCCCCC		27.1723607784
407PhosphorylationAFDSHGNTEHGRKKR
HHHCCCCCCCCCCCC		33.6729136822
412UbiquitinationGNTEHGRKKRSPTAY
CCCCCCCCCCCCCCC		58.0717644757
413UbiquitinationNTEHGRKKRSPTAYG
CCCCCCCCCCCCCCC		57.6617644757
415PhosphorylationEHGRKKRSPTAYGAT
CCCCCCCCCCCCCCC		35.1720377248
417PhosphorylationGRKKRSPTAYGATTA
CCCCCCCCCCCCCCC		33.4821551504
419PhosphorylationKKRSPTAYGATTASS
CCCCCCCCCCCCCCC		15.1217330950
422PhosphorylationSPTAYGATTASSNCI
CCCCCCCCCCCCCCE		20.6619779198
423PhosphorylationPTAYGATTASSNCIV
CCCCCCCCCCCCCEE		24.8220377248
425PhosphorylationAYGATTASSNCIVDD
CCCCCCCCCCCEECC		21.7120377248
426PhosphorylationYGATTASSNCIVDDA
CCCCCCCCCCEECCC		33.0020377248
438PhosphorylationDDAVNCNTSNCL---
CCCCCCCCCCCC---		24.4221551504
439PhosphorylationDAVNCNTSNCL----
CCCCCCCCCCC----		16.1423749301
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 ZRC1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZRC1_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 ZRC1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MRP8_YEASTMRP8physical
10688190
DEP1_YEASTDEP1genetic
20093466
AP2A_YEASTAPL3genetic
20093466
CCZ1_YEASTCCZ1genetic
20093466
CSN5_YEASTRRI1genetic
20093466
PIL1_YEASTPIL1genetic
20093466
CATT_YEASTCTT1genetic
20093466
DAP2_YEASTDAP2genetic
20093466
MGA2_YEASTMGA2genetic
20093466
PCKA_YEASTPCK1genetic
20093466
JLP1_YEASTJLP1genetic
20093466
ECM38_YEASTECM38genetic
20093466
FAR11_YEASTFAR11genetic
20093466
MSA1_YEASTMSA1genetic
20093466
HES1_YEASTHES1genetic
20093466
VPH1_YEASTVPH1genetic
20093466
COT1_YEASTCOT1genetic
20093466
CSC1_YEASTCSC1physical
16093310
STV1_YEASTSTV1physical
16093310
HXT17_YEASTHXT17physical
16093310
MTP1_ARATHZATgenetic
20419142
CDC27_YEASTCDC27genetic
27708008
SCC1_YEASTMCD1genetic
27708008
FAD1_YEASTFAD1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
SNU56_YEASTSNU56genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
NBP35_YEASTNBP35genetic
27708008
BIG1_YEASTBIG1genetic
27708008
ERO1_YEASTERO1genetic
27708008
APC5_YEASTAPC5genetic
27708008
MGA2_YEASTMGA2genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
VPH1_YEASTVPH1genetic
27708008
COT1_YEASTCOT1genetic
27708008
MSS18_YEASTMSS18genetic
27708008
PDCL2_HUMANPDCL2physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZRC1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-395 AND SER-396, 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-387; SER-393 ANDSER-397, AND MASS SPECTROMETRY.

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