COT1_YEAST - dbPTM
COT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COT1_YEAST
UniProt AC P32798
Protein Name Cobalt uptake protein COT1
Gene Name COT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 439
Subcellular Localization Mitochondrion membrane
Multi-pass membrane protein. Another possibility exists that it is associated with another unidentified membrane that has been enriched in the mitochondrial membrane fractions.
Protein Description Probably responsible for the uptake of cobalt ions. It appears to act in a dosage-dependent manner to counteract the adverse effects of cobalt ions on cells. It may participate in the regulation of cobalt levels under normal physiological conditions and may be important in the supply of metal that is required for metalloenzyme or cofactor synthesis. It reduces the toxicity of cobalt and rhodium ions. Other components responsible for cobalt transport exist..
Protein Sequence MKLGSKQVKIISLLLLDTVFFGIEITTGYLSHSLALIADSFHMLNDIISLVVALWAVNVAKNRNPDSTYTYGWKRAEILGALINAVFLIALCVSILIEALQRIIAPPVIENPKFVLYVGVAGLISNTVGLFLFHDNDQEHGHGHGHSHGGIFADHEMHMPSSHTHTHAHVDGIENTTPMDSTDNISEIMPNAIVDSFMNENTRLLTPENASKTPSYSTSSHTIASGGNYTEHNKRKRSLNMHGVFLHVLGDALGNIGVMLSAFFIWKTDYSWKYYTDPLVSLIITGIIFSSALPLSCKASKILLQATPSTLSGDQVEGDLLKIPGIIAIHDFHIWNLTESIFIASLHIQLDISPEQFTDLAKIVRSKLHRYGIHSATLQPEFITREVTSTERAGDSQGDHLQNDPLSLRPKTYGTGISGSTCLIDDAANCNTADCLEDH
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
206PhosphorylationNENTRLLTPENASKT
CCCCCCCCCCCCCCC		32.9029136822
211PhosphorylationLLTPENASKTPSYST
CCCCCCCCCCCCCCC		48.9529136822
212UbiquitinationLTPENASKTPSYSTS
CCCCCCCCCCCCCCC		63.1423749301
213PhosphorylationTPENASKTPSYSTSS
CCCCCCCCCCCCCCC		18.2522890988
215PhosphorylationENASKTPSYSTSSHT
CCCCCCCCCCCCCCE		36.6322890988
216PhosphorylationNASKTPSYSTSSHTI
CCCCCCCCCCCCCEE		19.7122890988
217PhosphorylationASKTPSYSTSSHTIA
CCCCCCCCCCCCEEC		26.5922890988
218PhosphorylationSKTPSYSTSSHTIAS
CCCCCCCCCCCEECC		26.4722890988
219PhosphorylationKTPSYSTSSHTIASG
CCCCCCCCCCEECCC		17.7422890988
220PhosphorylationTPSYSTSSHTIASGG
CCCCCCCCCEECCCC		25.4122890988
222PhosphorylationSYSTSSHTIASGGNY
CCCCCCCEECCCCCC		21.8622890988
225PhosphorylationTSSHTIASGGNYTEH
CCCCEECCCCCCCCC		43.3019823750
229PhosphorylationTIASGGNYTEHNKRK
EECCCCCCCCCCCCC		19.4422890988
230PhosphorylationIASGGNYTEHNKRKR
ECCCCCCCCCCCCCH		34.4722890988
234UbiquitinationGNYTEHNKRKRSLNM
CCCCCCCCCCHHCCC		62.2917644757
236UbiquitinationYTEHNKRKRSLNMHG
CCCCCCCCHHCCCCH		48.2017644757
298UbiquitinationSALPLSCKASKILLQ
CCCCCCCHHHHHHHH		52.9322817900
301UbiquitinationPLSCKASKILLQATP
CCCCHHHHHHHHCCC		42.0823749301
396PhosphorylationSTERAGDSQGDHLQN
CCCCCCCCCCCCCCC		34.8327214570
407PhosphorylationHLQNDPLSLRPKTYG
CCCCCCCCCCCCCCC		27.9328889911
411UbiquitinationDPLSLRPKTYGTGIS
CCCCCCCCCCCCCCC		48.2017644757
412PhosphorylationPLSLRPKTYGTGISG
CCCCCCCCCCCCCCC		29.8419779198
421PhosphorylationGTGISGSTCLIDDAA
CCCCCCCEEEECCHH		18.1727017623
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 COT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COT1_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 COT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZRC1_YEASTZRC1genetic
8058041
COT1_YEASTCOT1physical
18467557
FEN1_YEASTRAD27genetic
20093466
ZRC1_YEASTZRC1genetic
20093466
UBP2_YEASTUBP2genetic
20093466
CHS7_YEASTCHS7physical
16093310
MTP1_ARATHZATgenetic
20419142
ZRC1_YEASTZRC1genetic
21998704
NPL4_YEASTNPL4genetic
27708008
ZRC1_YEASTZRC1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COT1_YEAST

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Related Literatures of Post-Translational Modification
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-225, AND MASSSPECTROMETRY.
"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 THR-206, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-301, AND MASSSPECTROMETRY.

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