| UniProt ID | PEX19_HUMAN | |
|---|---|---|
| UniProt AC | P40855 | |
| Protein Name | Peroxisomal biogenesis factor 19 | |
| Gene Name | PEX19 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 299 | |
| Subcellular Localization |
Cytoplasm . Peroxisome membrane Lipid-anchor Cytoplasmic side . Mainly cytoplasmic. Some fraction membrane-associated to the outer surface of peroxisomes. |
|
| Protein Description | Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53.. | |
| Protein Sequence | MAAAEEGCSVGAEADRELEELLESALDDFDKAKPSPAPPSTTTAPDASGPQKRSPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDMTSQQEFTSCLKETLSGLAKNATDLQNSSMSEEELTKAMEGLGMDEGDGEGNILPIMQSIMQNLLSKDVLYPSLKEITEKYPEWLQSHRESLPPEQFEKYQEQHSVMCKICEQFEAETPTDSETTQKARFEMVLDLMQQLQDLGHPPKELAGEMPPGLNFDLDALNLSGPPGASGEQCLIM | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAAAEEGCS ------CCHHHCCCC | 18.51 | 25944712 | |
| 9 | Phosphorylation | AAAEEGCSVGAEADR CHHHCCCCCCHHHHH | 34.15 | 25159151 | |
| 17 (in isoform 5) | Ubiquitination | - | 62.17 | 21890473 | |
| 24 | Phosphorylation | ELEELLESALDDFDK HHHHHHHHHHHHHHH | 33.82 | 26074081 | |
| 33 (in isoform 1) | Ubiquitination | - | 52.33 | 21890473 | |
| 33 | Ubiquitination | LDDFDKAKPSPAPPS HHHHHHCCCCCCCCC | 52.33 | 21906983 | |
| 35 | Phosphorylation | DFDKAKPSPAPPSTT HHHHCCCCCCCCCCC | 32.75 | 30266825 | |
| 40 (in isoform 5) | Ubiquitination | - | 37.01 | 21890473 | |
| 40 | Phosphorylation | KPSPAPPSTTTAPDA CCCCCCCCCCCCCCC | 37.01 | 30266825 | |
| 41 | Phosphorylation | PSPAPPSTTTAPDAS CCCCCCCCCCCCCCC | 33.66 | 30266825 | |
| 42 | Phosphorylation | SPAPPSTTTAPDASG CCCCCCCCCCCCCCC | 25.87 | 30266825 | |
| 42 | O-linked_Glycosylation | SPAPPSTTTAPDASG CCCCCCCCCCCCCCC | 25.87 | 30379171 | |
| 43 | Phosphorylation | PAPPSTTTAPDASGP CCCCCCCCCCCCCCC | 35.96 | 22199227 | |
| 48 (in isoform 5) | Ubiquitination | - | 59.39 | 21890473 | |
| 48 | Phosphorylation | TTTAPDASGPQKRSP CCCCCCCCCCCCCCC | 59.39 | 30576142 | |
| 52 | Acetylation | PDASGPQKRSPGDTA CCCCCCCCCCCCHHH | 58.96 | 25953088 | |
| 52 (in isoform 1) | Ubiquitination | - | 58.96 | 21890473 | |
| 52 | Ubiquitination | PDASGPQKRSPGDTA CCCCCCCCCCCCHHH | 58.96 | 21906983 | |
| 54 | Phosphorylation | ASGPQKRSPGDTAKD CCCCCCCCCCHHHHH | 40.03 | 23401153 | |
| 54 | O-linked_Glycosylation | ASGPQKRSPGDTAKD CCCCCCCCCCHHHHH | 40.03 | 30379171 | |
| 58 | Phosphorylation | QKRSPGDTAKDALFA CCCCCCHHHHHHHHH | 41.33 | 23927012 | |
| 60 | Ubiquitination | RSPGDTAKDALFASQ CCCCHHHHHHHHHCH | 45.70 | 22053931 | |
| 60 (in isoform 1) | Ubiquitination | - | 45.70 | 21890473 | |
| 66 | Phosphorylation | AKDALFASQEKFFQE HHHHHHHCHHHHHHH | 31.38 | 25159151 | |
| 69 | Ubiquitination | ALFASQEKFFQELFD HHHHCHHHHHHHHHC | 43.79 | - | |
| 89 | Ubiquitination | QATAEFEKAMKELAE HHHHHHHHHHHHHHH | 60.13 | - | |
| 92 | Ubiquitination | AEFEKAMKELAEEEP HHHHHHHHHHHHHCH | 55.20 | - | |
| 107 (in isoform 1) | Ubiquitination | - | 56.09 | 21890473 | |
| 107 | Ubiquitination | HLVEQFQKLSEAAGR HHHHHHHHHHHHHCC | 56.09 | 21890473 | |
| 117 | Phosphorylation | EAAGRVGSDMTSQQE HHHCCCCCCCCCHHH | 22.73 | 27251275 | |
| 119 | Sulfoxidation | AGRVGSDMTSQQEFT HCCCCCCCCCHHHHH | 4.09 | 21406390 | |
| 130 (in isoform 1) | Ubiquitination | - | 53.64 | 21890473 | |
| 130 | Ubiquitination | QEFTSCLKETLSGLA HHHHHHHHHHHHHHH | 53.64 | 21890473 | |
| 134 | Phosphorylation | SCLKETLSGLAKNAT HHHHHHHHHHHHCHH | 38.90 | 27251275 | |
| 138 (in isoform 1) | Ubiquitination | - | 52.75 | 21890473 | |
| 138 | Ubiquitination | ETLSGLAKNATDLQN HHHHHHHHCHHHHHC | 52.75 | 21906983 | |
| 141 | Phosphorylation | SGLAKNATDLQNSSM HHHHHCHHHHHCCCC | 46.78 | 23927012 | |
| 146 | Phosphorylation | NATDLQNSSMSEEEL CHHHHHCCCCCHHHH | 17.92 | 22167270 | |
| 147 | Phosphorylation | ATDLQNSSMSEEELT HHHHHCCCCCHHHHH | 33.60 | 22167270 | |
| 148 | Sulfoxidation | TDLQNSSMSEEELTK HHHHCCCCCHHHHHH | 6.16 | 21406390 | |
| 149 | Phosphorylation | DLQNSSMSEEELTKA HHHCCCCCHHHHHHH | 43.75 | 19664994 | |
| 154 | Phosphorylation | SMSEEELTKAMEGLG CCCHHHHHHHHHHCC | 21.75 | 22167270 | |
| 155 (in isoform 5) | Ubiquitination | - | 59.36 | 21890473 | |
| 177 | Phosphorylation | NILPIMQSIMQNLLS CHHHHHHHHHHHHCC | 11.57 | 28176443 | |
| 184 | Phosphorylation | SIMQNLLSKDVLYPS HHHHHHCCCCCCCHH | 29.94 | 17287340 | |
| 193 | Ubiquitination | DVLYPSLKEITEKYP CCCCHHHHHHHHHCH | 51.94 | - | |
| 198 | Ubiquitination | SLKEITEKYPEWLQS HHHHHHHHCHHHHHH | 58.41 | 21890473 | |
| 198 (in isoform 1) | Ubiquitination | - | 58.41 | 21890473 | |
| 199 | Phosphorylation | LKEITEKYPEWLQSH HHHHHHHCHHHHHHH | 10.51 | - | |
| 236 | Phosphorylation | CEQFEAETPTDSETT HHHHHCCCCCCCHHH | 38.24 | 21815630 | |
| 238 | Phosphorylation | QFEAETPTDSETTQK HHHCCCCCCCHHHHH | 60.62 | 29978859 | |
| 240 | Phosphorylation | EAETPTDSETTQKAR HCCCCCCCHHHHHHH | 39.04 | 29978859 | |
| 245 | Ubiquitination | TDSETTQKARFEMVL CCCHHHHHHHHHHHH | 39.16 | 22053931 | |
| 245 (in isoform 1) | Ubiquitination | - | 39.16 | 21890473 | |
| 296 | Methylation | PGASGEQCLIM---- CCCCCCCCCCC---- | 2.12 | - | |
| 296 | Farnesylation | PGASGEQCLIM---- CCCCCCCCCCC---- | 2.12 | 9339377 | |
| 296 | Farnesylation | PGASGEQCLIM---- CCCCCCCCCCC---- | 2.12 | 9339377 |
| 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 PEX19_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PEX19_HUMAN !! | ||||||
* 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_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H00205 | Zellweger syndrome spectrum, including: Zellweger syndrome (ZS); Adrenoleukodystrophy, neonatal (NAL | |||||
| OMIM Disease | ||||||
| 614886 | Peroxisome biogenesis disorder complementation group 14 (PBD-CG14) | |||||
| 614886 | Peroxisome biogenesis disorder 12A (PBD12A) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASSSPECTROMETRY. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-146; SER-147 ANDSER-149, AND MASS SPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND SER-149, ANDMASS SPECTROMETRY. | |
| "Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-54; SER-146;SER-147; SER-149; SER-177 AND SER-184, AND MASS SPECTROMETRY. | |
| Prenylation | |
| Reference | PubMed |
| "Human PEX19: cDNA cloning by functional complementation, mutationanalysis in a patient with Zellweger syndrome, and potential role inperoxisomal membrane assembly."; Matsuzono Y., Kinoshita N., Tamura S., Shimozawa N., Hamasaki M.,Ghaedi K., Wanders R.J.A., Suzuki Y., Kondo N., Fujiki Y.; Proc. Natl. Acad. Sci. U.S.A. 96:2116-2121(1999). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-296,MUTAGENESIS OF CYS-296, SUBCELLULAR LOCATION, FUNCTION, ANDINVOLVEMENT IN ZWS. | |
| "Genomic organization and molecular characterization of a geneencoding HsPXF, a human peroxisomal farnesylated protein."; Kammerer S., Arnold N., Gutensohn W., Mewes H.-W., Kunau W.-H.,Hoefler G., Roscher A.A., Braun A.; Genomics 45:200-210(1997). Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUESPECIFICITY, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-296, ANDMUTAGENESIS OF CYS-296. | |
