UniProt ID | PEX19_YEAST | |
---|---|---|
UniProt AC | Q07418 | |
Protein Name | Peroxisomal membrane protein import receptor PEX19 | |
Gene Name | PEX19 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 342 | |
Subcellular Localization |
Cytoplasm . Peroxisome membrane Lipid-anchor Cytoplasmic side . Endoplasmic reticulum membrane . Predominantly cytoplasmic (PubMed:9418908). Concentrates in a PEX3-dependent manner to defined foci on the endoplasmic reticulum membrane, which then |
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Protein Description | Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the peroxisomal membrane for subsequent insertion into the membrane. Acts as a chaperone in stabilizing or maintaining PMPs in the lipid bilayer. Directs PEX17, a peripheral component of the peroxisomal matrix protein translocation machinery, to peroxisomes. Stabilizes VPS1, a protein required for peroxisomal fission, at the peroxisomal membrane. Also acts in conjunction with PEX3 in the formation of peroxisomes from preperoxisomal compartments at the endoplasmic reticulum during de novo peroxisome synthesis, probably via the import of additional PMPs.. | |
Protein Sequence | MNENEYDNFDDLDDLLDEDPTKLDEAEPDDVQAKGSVYNDSENKEKNAESKDSDGVQVANESEEDPELKEMMVDLQNEFANLMKNNGNENNVKTEDFNKLISALEEAAKVPHQQMEQGCSSLKSNSTDKGTVNGSNPGFKNIVSNTLDRLKENGNKVDTSLAEETKESQRSGQNNNIDDILSQLLDQMVASGGKESAENQFDLKDGEMDDAITKILDQMTSKEVLYEPMKEMRSEFGVWFQENGENEEHKEKIGTYKRQFNIVDEIVNIYELKDYDELKHKDRVTELLDELEQLGDSPIRSANSPLKHGNEEEELMKMLEIDGNDPNLGNLDKELTDGCKQQ | |
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 |
---|---|---|---|---|---|
36 | Phosphorylation | DDVQAKGSVYNDSEN CCCCCCCCCCCCCCC | 22.26 | 22369663 | |
38 | Phosphorylation | VQAKGSVYNDSENKE CCCCCCCCCCCCCCH | 18.23 | 22369663 | |
41 | Phosphorylation | KGSVYNDSENKEKNA CCCCCCCCCCCHHCC | 39.16 | 22369663 | |
50 | Phosphorylation | NKEKNAESKDSDGVQ CCHHCCCCCCCCCCC | 39.08 | 22369663 | |
53 | Phosphorylation | KNAESKDSDGVQVAN HCCCCCCCCCCCCCC | 39.75 | 22890988 | |
62 | Phosphorylation | GVQVANESEEDPELK CCCCCCCCCCCHHHH | 46.20 | 22369663 | |
93 | Ubiquitination | NGNENNVKTEDFNKL CCCCCCCCHHHHHHH | 48.60 | 23749301 | |
99 | Ubiquitination | VKTEDFNKLISALEE CCHHHHHHHHHHHHH | 47.38 | 24961812 | |
120 | Phosphorylation | QQMEQGCSSLKSNST HHHHHHHHHCCCCCC | 45.59 | 30377154 | |
121 | Phosphorylation | QMEQGCSSLKSNSTD HHHHHHHHCCCCCCC | 43.84 | 21440633 | |
123 | Acetylation | EQGCSSLKSNSTDKG HHHHHHCCCCCCCCC | 49.92 | 25381059 | |
124 | Phosphorylation | QGCSSLKSNSTDKGT HHHHHCCCCCCCCCC | 41.11 | 21440633 | |
126 | Phosphorylation | CSSLKSNSTDKGTVN HHHCCCCCCCCCCCC | 45.11 | 21440633 | |
127 | Phosphorylation | SSLKSNSTDKGTVNG HHCCCCCCCCCCCCC | 46.08 | 21440633 | |
129 | Ubiquitination | LKSNSTDKGTVNGSN CCCCCCCCCCCCCCC | 57.48 | 23749301 | |
131 | Phosphorylation | SNSTDKGTVNGSNPG CCCCCCCCCCCCCCC | 19.28 | 22369663 | |
135 | Phosphorylation | DKGTVNGSNPGFKNI CCCCCCCCCCCHHHH | 34.35 | 22369663 | |
204 | Ubiquitination | AENQFDLKDGEMDDA HHCCCCCCCCCHHHH | 66.58 | 23749301 | |
222 | Acetylation | ILDQMTSKEVLYEPM HHHHHCCHHHHHHHH | 42.55 | 24489116 | |
297 | Phosphorylation | ELEQLGDSPIRSANS HHHHHCCCCCCCCCC | 22.04 | 21440633 | |
301 | Phosphorylation | LGDSPIRSANSPLKH HCCCCCCCCCCCCCC | 32.30 | 29136822 | |
304 | Phosphorylation | SPIRSANSPLKHGNE CCCCCCCCCCCCCCH | 31.18 | 17330950 | |
339 | Methylation | DKELTDGCKQQ---- CHHHCHHHCCC---- | 3.91 | - | |
339 | Farnesylation | DKELTDGCKQQ---- CHHHCHHHCCC---- | 3.91 | 9418908 | |
339 | Farnesylation | DKELTDGCKQQ---- CHHHCHHHCCC---- | 3.91 | 9418908 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of PEX19_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PEX19_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 PEX19_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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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-36; SER-62 AND SER-304,AND MASS 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-304, AND MASSSPECTROMETRY. | |
Prenylation | |
Reference | PubMed |
"Pex19p, a farnesylated protein essential for peroxisome biogenesis."; Goette K., Girzalsky W., Linkert M., Baumgart E., Kammerer S.,Kunau W.-H., Erdmann R.; Mol. Cell. Biol. 18:616-628(1998). Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH PEX3,INDUCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-339, ANDISOPRENYLATION AT CYS-339. |