| UniProt ID | KEX1_YEAST | |
|---|---|---|
| UniProt AC | P09620 | |
| Protein Name | Pheromone-processing carboxypeptidase KEX1 | |
| Gene Name | KEX1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 729 | |
| Subcellular Localization |
Golgi apparatus, trans-Golgi network membrane Single-pass type I membrane protein . |
|
| Protein Description | Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the active cell death program induced by acetic acid stress or during chronological aging. Promotes cell fusion by proteolytically processing substrates that act in parallel to PRM1 as an alternative fusion machine, as cell wall components, or both.. | |
| Protein Sequence | MFYNRWLGTWLAMSALIRISVSLPSSEEYKVAYELLPGLSEVPDPSNIPQMHAGHIPLRSEDADEQDSSDLEYFFWKFTNNDSNGNVDRPLIIWLNGGPGCSSMDGALVESGPFRVNSDGKLYLNEGSWISKGDLLFIDQPTGTGFSVEQNKDEGKIDKNKFDEDLEDVTKHFMDFLENYFKIFPEDLTRKIILSGESYAGQYIPFFANAILNHNKFSKIDGDTYDLKALLIGNGWIDPNTQSLSYLPFAMEKKLIDESNPNFKHLTNAHENCQNLINSASTDEAAHFSYQECENILNLLLSYTRESSQKGTADCLNMYNFNLKDSYPSCGMNWPKDISFVSKFFSTPGVIDSLHLDSDKIDHWKECTNSVGTKLSNPISKPSIHLLPGLLESGIEIVLFNGDKDLICNNKGVLDTIDNLKWGGIKGFSDDAVSFDWIHKSKSTDDSEEFSGYVKYDRNLTFVSVYNASHMVPFDKSLVSRGIVDIYSNDVMIIDNNGKNVMITTDDDSDQDATTESGDKPKENLEEEEQEAQNEEGKEKEGNKDKDGDDDNDNDDDDEDDHNSEGDDDDDDDDDEDDNNEKQSNQGLEDSRHKSSEYEQEEEEVEEFAEEISMYKHKAVVVTIVTFLIVVLGVYAYDRRVRRKARHTILVDPNNRQHDSPNKTVSWADDLESGLGAEDDLEQDEQLEGGAPISSTSNKAGSKLKTKKKKKYTSLPNTEIDESFEMTDF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MFYNRWLGTW -----CCCHHHHHHH | 11.52 | 19823750 | |
| 9 | Phosphorylation | FYNRWLGTWLAMSAL CCHHHHHHHHHHHHH | 18.35 | 19823750 | |
| 14 | Phosphorylation | LGTWLAMSALIRISV HHHHHHHHHHHHHHC | 17.83 | 19823750 | |
| 20 | Phosphorylation | MSALIRISVSLPSSE HHHHHHHHCCCCCCC | 8.87 | 19823750 | |
| 22 | Phosphorylation | ALIRISVSLPSSEEY HHHHHHCCCCCCCHH | 27.98 | 19823750 | |
| 25 | Phosphorylation | RISVSLPSSEEYKVA HHHCCCCCCCHHHHH | 56.53 | 19823750 | |
| 26 | Phosphorylation | ISVSLPSSEEYKVAY HHCCCCCCCHHHHHH | 32.29 | 19823750 | |
| 29 | Phosphorylation | SLPSSEEYKVAYELL CCCCCCHHHHHHHHC | 13.50 | 19823750 | |
| 81 | N-linked_Glycosylation | FFWKFTNNDSNGNVD EEEEECCCCCCCCCC | 51.54 | - | |
| 152 | Ubiquitination | GFSVEQNKDEGKIDK CEECEECCCCCCCCH | 57.77 | 19722269 | |
| 254 | Acetylation | LPFAMEKKLIDESNP CCHHHHHHHHCCCCC | 37.05 | 24489116 | |
| 421 | Acetylation | LDTIDNLKWGGIKGF HHCHHCCCCCCCCCC | 50.47 | 24489116 | |
| 459 | N-linked_Glycosylation | GYVKYDRNLTFVSVY EEEEECCCCEEEEEE | 40.30 | 1469044 | |
| 467 | N-linked_Glycosylation | LTFVSVYNASHMVPF CEEEEEEECHHCCCC | 32.58 | 1469044 | |
| 487 | Phosphorylation | SRGIVDIYSNDVMII HCCCEEECCCCEEEE | 9.28 | 27017623 | |
| 488 | Phosphorylation | RGIVDIYSNDVMIID CCCEEECCCCEEEEC | 27.21 | 27017623 | |
| 564 | Phosphorylation | DDEDDHNSEGDDDDD CCCCCCCCCCCCCCC | 39.27 | 24961812 | |
| 648 | Phosphorylation | VRRKARHTILVDPNN HHHHCCCEEEECCCC | 15.51 | 19823750 | |
| 660 | Phosphorylation | PNNRQHDSPNKTVSW CCCCCCCCCCCEECH | 28.40 | 22369663 | |
| 663 | Ubiquitination | RQHDSPNKTVSWADD CCCCCCCCEECHHHH | 54.40 | 24961812 | |
| 664 | Phosphorylation | QHDSPNKTVSWADDL CCCCCCCEECHHHHH | 26.81 | 19779198 | |
| 666 | Phosphorylation | DSPNKTVSWADDLES CCCCCEECHHHHHHH | 23.06 | 24961812 | |
| 673 | Phosphorylation | SWADDLESGLGAEDD CHHHHHHHCCCCCCC | 46.76 | 25521595 | |
| 723 | Phosphorylation | PNTEIDESFEMTDF- CCCCCCHHCCCCCC- | 23.82 | 24961812 |
| 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 KEX1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KEX1_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 KEX1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-660, AND MASSSPECTROMETRY. | |
