UniProt ID | AHP1_YEAST | |
---|---|---|
UniProt AC | P38013 | |
Protein Name | Peroxiredoxin AHP1 {ECO:0000305} | |
Gene Name | AHP1 {ECO:0000303|PubMed:9988687} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 176 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. [PubMed: 10391912] | |
Protein Sequence | MSDLVNKKFPAGDYKFQYIAISQSDADSESCKMPQTVEWSKLISENKKVIITGAPAAFSPTCTVSHIPGYINYLDELVKEKEVDQVIVVTVDNPFANQAWAKSLGVKDTTHIKFASDPGCAFTKSIGFELAVGDGVYWSGRWAMVVENGIVTYAAKETNPGTDVTVSSVESVLAHL | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSDLVNKKF ------CCHHCCCCC | 39.38 | 15665377 | |
2 | Acetylation | ------MSDLVNKKF ------CCHHCCCCC | 39.38 | - | |
7 | Succinylation | -MSDLVNKKFPAGDY -CCHHCCCCCCCCCC | 48.59 | 23954790 | |
7 | Acetylation | -MSDLVNKKFPAGDY -CCHHCCCCCCCCCC | 48.59 | 24489116 | |
8 | Ubiquitination | MSDLVNKKFPAGDYK CCHHCCCCCCCCCCE | 51.91 | 23749301 | |
8 | Acetylation | MSDLVNKKFPAGDYK CCHHCCCCCCCCCCE | 51.91 | 24489116 | |
15 | Acetylation | KFPAGDYKFQYIAIS CCCCCCCEEEEEEEE | 30.63 | 24489116 | |
15 | Ubiquitination | KFPAGDYKFQYIAIS CCCCCCCEEEEEEEE | 30.63 | 17644757 | |
22 | Phosphorylation | KFQYIAISQSDADSE EEEEEEEECCCCCCC | 18.01 | 17287358 | |
24 | Phosphorylation | QYIAISQSDADSESC EEEEEECCCCCCCCC | 28.16 | 23749301 | |
28 | Phosphorylation | ISQSDADSESCKMPQ EECCCCCCCCCCCCC | 32.88 | 20377248 | |
30 | Phosphorylation | QSDADSESCKMPQTV CCCCCCCCCCCCCCH | 24.00 | 20377248 | |
32 | Acetylation | DADSESCKMPQTVEW CCCCCCCCCCCCHHH | 64.00 | 24489116 | |
32 | Ubiquitination | DADSESCKMPQTVEW CCCCCCCCCCCCHHH | 64.00 | 23749301 | |
36 | Phosphorylation | ESCKMPQTVEWSKLI CCCCCCCCHHHHHHH | 17.96 | 22369663 | |
40 | Phosphorylation | MPQTVEWSKLISENK CCCCHHHHHHHCCCC | 12.22 | 21440633 | |
41 | 2-Hydroxyisobutyrylation | PQTVEWSKLISENKK CCCHHHHHHHCCCCC | 51.41 | - | |
41 | Ubiquitination | PQTVEWSKLISENKK CCCHHHHHHHCCCCC | 51.41 | 24961812 | |
41 | Acetylation | PQTVEWSKLISENKK CCCHHHHHHHCCCCC | 51.41 | 24489116 | |
44 | Phosphorylation | VEWSKLISENKKVII HHHHHHHCCCCCEEE | 45.62 | 19795423 | |
47 | Succinylation | SKLISENKKVIITGA HHHHCCCCCEEEECC | 44.35 | 23954790 | |
47 | Ubiquitination | SKLISENKKVIITGA HHHHCCCCCEEEECC | 44.35 | 22817900 | |
47 | Acetylation | SKLISENKKVIITGA HHHHCCCCCEEEECC | 44.35 | 25381059 | |
47 | 2-Hydroxyisobutyrylation | SKLISENKKVIITGA HHHHCCCCCEEEECC | 44.35 | - | |
48 | Ubiquitination | KLISENKKVIITGAP HHHCCCCCEEEECCC | 50.69 | 23749301 | |
59 | Phosphorylation | TGAPAAFSPTCTVSH ECCCCCCCCCEEHHC | 17.99 | 20377248 | |
61 | Phosphorylation | APAAFSPTCTVSHIP CCCCCCCCEEHHCCC | 21.43 | 21440633 | |
65 | Phosphorylation | FSPTCTVSHIPGYIN CCCCEEHHCCCCHHH | 9.50 | 21440633 | |
79 | Acetylation | NYLDELVKEKEVDQV HHHHHHHHHCCCCEE | 75.57 | 25381059 | |
79 | Ubiquitination | NYLDELVKEKEVDQV HHHHHHHHHCCCCEE | 75.57 | 17644757 | |
102 | Ubiquitination | FANQAWAKSLGVKDT HHCHHHHHHCCCCCC | 35.20 | 23749301 | |
103 | Phosphorylation | ANQAWAKSLGVKDTT HCHHHHHHCCCCCCC | 23.70 | 21440633 | |
107 | Acetylation | WAKSLGVKDTTHIKF HHHHCCCCCCCEEEE | 47.78 | 22865919 | |
107 | Ubiquitination | WAKSLGVKDTTHIKF HHHHCCCCCCCEEEE | 47.78 | 23749301 | |
107 | 2-Hydroxyisobutyrylation | WAKSLGVKDTTHIKF HHHHCCCCCCCEEEE | 47.78 | - | |
107 | Succinylation | WAKSLGVKDTTHIKF HHHHCCCCCCCEEEE | 47.78 | 23954790 | |
113 | Ubiquitination | VKDTTHIKFASDPGC CCCCCEEEECCCCCC | 27.55 | 23749301 | |
113 | Acetylation | VKDTTHIKFASDPGC CCCCCEEEECCCCCC | 27.55 | 24489116 | |
116 | Phosphorylation | TTHIKFASDPGCAFT CCEEEECCCCCCCEE | 47.69 | 21440633 | |
123 | Phosphorylation | SDPGCAFTKSIGFEL CCCCCCEECEECCEE | 12.83 | 21440633 | |
124 | Ubiquitination | DPGCAFTKSIGFELA CCCCCEECEECCEEE | 33.35 | 17644757 | |
156 | Ubiquitination | GIVTYAAKETNPGTD CEEEEEECCCCCCCC | 57.82 | 17644757 | |
158 | Phosphorylation | VTYAAKETNPGTDVT EEEEECCCCCCCCCC | 46.11 | 22369663 | |
162 | Phosphorylation | AKETNPGTDVTVSSV ECCCCCCCCCCHHHH | 28.67 | 22369663 | |
165 | Phosphorylation | TNPGTDVTVSSVESV CCCCCCCCHHHHHHH | 19.92 | 22369663 | |
167 | Phosphorylation | PGTDVTVSSVESVLA CCCCCCHHHHHHHHH | 21.21 | 22369663 | |
168 | Phosphorylation | GTDVTVSSVESVLAH CCCCCHHHHHHHHHC | 26.10 | 22369663 | |
171 | Phosphorylation | VTVSSVESVLAHL-- CCHHHHHHHHHCC-- | 21.92 | 22369663 |
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 AHP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AHP1_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 AHP1_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2,AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"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-59 AND SER-171, AND MASSSPECTROMETRY. | |
"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-22, AND MASSSPECTROMETRY. | |
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2,AND MASS SPECTROMETRY. |