UniProt ID | YKS7_YEAST | |
---|---|---|
UniProt AC | P34231 | |
Protein Name | Uncharacterized protein YKL187C | |
Gene Name | YKL187C | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 750 | |
Subcellular Localization | Mitochondrion . | |
Protein Description | ||
Protein Sequence | MRIEKHRTPLSKGIIWTILSVCLLFMFTTLILVIVATAGSTANYKPLTNIYIGEADIKHINVSKVIPQIGPILTILGSALTAPNSSLDDIFGAMKNIADTPALTPLLTLLSNADNTTVTIESLTELAPLAISGNPASSTRQLTEINGLLKYSDNATETLDGLSRLVSASLSSASSNSSSDSTTLVLDLLKDSDNPQNSTDALLTLNNLTMSEKAQLLPVFRLFAFSTNQTATMTALATLMNTTISSSLAQTLLTQLQNTISNGGSLNNTFSTLQPLVPQASAPAFDAVELLLNQTTSTNQTLSTLSDLLEQNLTQSSSAKKAFAALTQLMENSDNSTMVVTSVQSLAAVTNTTQSTQQLIGLDDVISSSSNTNETLSILSELQSGLSGNSSSVQYIPYLFSLLGASTDPKTTFSSLVTLTSWAQENPQTFLPILDILADAKSVQPISAEELNAMTPNILEYLKIPIYYRLSIFTLCHANLENKILDCNSPHAVQNLDFRSIIYDALVTSDFQPYLNALNISANDLYLEGKLLHREHQYVPAVRSVLALNLLAIIFSFFTMIFIILLYFNRYMFKQPLWLIALALHVCVGVATVLAAIIISVMIAIIKSGTADDKYGVVFKAGPAYTGLIWTAFALSFIATGLIIYTWWRNRRSGRYMSGSVTNRKGEIYTYGDGSAISADRFGDHNLGDDDDADFEKQVNRNEITAIDNSSSANNTDVTGSTSNRTELSHPDVTPKDSNGPVNNNAHLVA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
61 | N-linked_Glycosylation | EADIKHINVSKVIPQ ECCCCEEEHHHCCCC | 31.56 | - | |
84 | N-linked_Glycosylation | GSALTAPNSSLDDIF HHHHCCCCCCHHHHH | 41.59 | - | |
115 | N-linked_Glycosylation | TLLSNADNTTVTIES HHHCCCCCCEEEEEH | 34.93 | - | |
154 | N-linked_Glycosylation | GLLKYSDNATETLDG CEECCCCCCCCCHHH | 42.70 | - | |
176 | N-linked_Glycosylation | SLSSASSNSSSDSTT HHCCCCCCCCCCCEE | 43.33 | - | |
197 | N-linked_Glycosylation | KDSDNPQNSTDALLT HCCCCCCCHHHHHHH | 48.40 | - | |
207 | N-linked_Glycosylation | DALLTLNNLTMSEKA HHHHHHCCCCCCHHH | 39.75 | - | |
228 | N-linked_Glycosylation | RLFAFSTNQTATMTA HHHHCCCCHHHHHHH | 35.69 | - | |
241 | N-linked_Glycosylation | TALATLMNTTISSSL HHHHHHHHHHHCHHH | 36.86 | - | |
267 | N-linked_Glycosylation | ISNGGSLNNTFSTLQ HHCCCCCCCCCCCCC | 47.39 | - | |
293 | N-linked_Glycosylation | DAVELLLNQTTSTNQ HHHHHHHHCCCCCCH | 36.80 | - | |
299 | N-linked_Glycosylation | LNQTTSTNQTLSTLS HHCCCCCCHHHHHHH | 32.38 | - | |
312 | N-linked_Glycosylation | LSDLLEQNLTQSSSA HHHHHHCCCCCCHHH | 35.36 | - | |
335 | N-linked_Glycosylation | QLMENSDNSTMVVTS HHHHCCCCCEEEEEE | 38.92 | - | |
351 | N-linked_Glycosylation | QSLAAVTNTTQSTQQ HHHHHHCCCCHHHHH | 34.23 | - | |
373 | N-linked_Glycosylation | ISSSSNTNETLSILS HCCCCCHHHHHHHHH | 44.50 | - | |
389 | N-linked_Glycosylation | LQSGLSGNSSSVQYI HHHCCCCCCCHHHHH | 35.03 | - | |
519 | N-linked_Glycosylation | QPYLNALNISANDLY HHHHHHHCCCHHHHH | 24.61 | - | |
538 | Phosphorylation | LLHREHQYVPAVRSV HHCCCCCCHHHHHHH | 15.42 | 24930733 | |
658 | Phosphorylation | RRSGRYMSGSVTNRK CCCCCCCCCCEECCC | 20.98 | 28889911 | |
665 | Ubiquitination | SGSVTNRKGEIYTYG CCCEECCCCCEEEEC | 64.07 | 23749301 | |
669 | Phosphorylation | TNRKGEIYTYGDGSA ECCCCCEEEECCCCE | 6.93 | 29136822 | |
670 | Phosphorylation | NRKGEIYTYGDGSAI CCCCCEEEECCCCEE | 27.04 | 19779198 | |
671 | Phosphorylation | RKGEIYTYGDGSAIS CCCCEEEECCCCEEC | 9.03 | 19779198 | |
675 | Phosphorylation | IYTYGDGSAISADRF EEEECCCCEECCCCC | 27.46 | 29136822 | |
678 | Phosphorylation | YGDGSAISADRFGDH ECCCCEECCCCCCCC | 24.67 | 29136822 | |
697 | Ubiquitination | DDDADFEKQVNRNEI CCCCHHHHHCCHHHE | 60.58 | 23749301 | |
709 | N-linked_Glycosylation | NEITAIDNSSSANNT HHEEEEECCCCCCCC | 37.36 | - | |
710 | Phosphorylation | EITAIDNSSSANNTD HEEEEECCCCCCCCC | 23.17 | 30377154 | |
712 | Phosphorylation | TAIDNSSSANNTDVT EEEECCCCCCCCCCC | 34.53 | 25371407 | |
714 | N-linked_Glycosylation | IDNSSSANNTDVTGS EECCCCCCCCCCCCC | 54.61 | - | |
724 | N-linked_Glycosylation | DVTGSTSNRTELSHP CCCCCCCCCCCCCCC | 55.79 | - | |
726 | Phosphorylation | TGSTSNRTELSHPDV CCCCCCCCCCCCCCC | 45.59 | 29136822 | |
729 | Phosphorylation | TSNRTELSHPDVTPK CCCCCCCCCCCCCCC | 27.09 | 25371407 | |
738 | Phosphorylation | PDVTPKDSNGPVNNN CCCCCCCCCCCCCCC | 50.22 | 25371407 |
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 YKS7_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YKS7_YEAST !! |
* 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 YKS7_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of YKS7_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675 AND SER-678, ANDMASS SPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-697, AND MASSSPECTROMETRY. |