UniProt ID | PTN20_HUMAN | |
---|---|---|
UniProt AC | Q4JDL3 | |
Protein Name | Tyrosine-protein phosphatase non-receptor type 20 | |
Gene Name | PTPN20 {ECO:0000312|HGNC:HGNC:23423} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 420 | |
Subcellular Localization | Nucleus . Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Colocalizes with the microtubule-organizing center and intracellular membrane compartments. | |
Protein Description | Tyrosine-protein phosphatase targeted to sites of actin polymerization in response of varied extracellular stimuli. Has tyrosine phosphatase activity towards various tyrosyl phosphorylated substrates.. | |
Protein Sequence | MSSPRDFRAEPVNDYEGNDSEAEDLNFRETLPSSSQENTPRSKVFENKVNSEKVKLSLRNFPHNDYEDVFEEPSESGSDPSMWTARGPFRRDRWSSEDEEAAGPSQALSPLLSDTRKIVSEGELDQLAQIRPLIFNFHEQTAIKDCLKILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGKSKDYINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLRKLLTLD | |
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 |
---|---|---|---|---|---|
57 | Phosphorylation | NSEKVKLSLRNFPHN CHHHHEEECCCCCCC | 21.40 | 24719451 | |
76 | Phosphorylation | VFEEPSESGSDPSMW HHCCCCCCCCCCHHC | 48.19 | - | |
84 (in isoform 5) | Phosphorylation | - | 9.61 | 24275569 | |
86 (in isoform 5) | Phosphorylation | - | 46.04 | 24275569 | |
86 (in isoform 15) | Phosphorylation | - | 46.04 | 29978859 | |
87 (in isoform 15) | Phosphorylation | - | 24.20 | 29978859 | |
95 | Phosphorylation | PFRRDRWSSEDEEAA CCCCCCCCCCCHHHC | 25.41 | 30624053 | |
95 (in isoform 13) | Phosphorylation | - | 25.41 | 29978859 | |
96 (in isoform 15) | Phosphorylation | - | 41.95 | 29978859 | |
96 | Phosphorylation | FRRDRWSSEDEEAAG CCCCCCCCCCHHHCC | 41.95 | 17525332 | |
96 (in isoform 13) | Phosphorylation | - | 41.95 | 29978859 | |
100 (in isoform 15) | Phosphorylation | - | 57.02 | 29978859 | |
104 (in isoform 15) | Phosphorylation | - | 20.67 | 29978859 | |
105 | Phosphorylation | DEEAAGPSQALSPLL CHHHCCCCHHHHHHH | 27.45 | 17525332 | |
105 (in isoform 13) | Phosphorylation | - | 27.45 | 29978859 | |
109 | Phosphorylation | AGPSQALSPLLSDTR CCCCHHHHHHHHCHH | 19.27 | 30624053 | |
109 (in isoform 13) | Phosphorylation | - | 19.27 | 29978859 | |
110 (in isoform 15) | Phosphorylation | - | 37.86 | 29978859 | |
111 (in isoform 15) | Phosphorylation | - | 6.85 | 29978859 | |
113 | Phosphorylation | QALSPLLSDTRKIVS HHHHHHHHCHHHHCC | 44.62 | 30624053 | |
113 (in isoform 13) | Phosphorylation | - | 44.62 | 29978859 | |
119 (in isoform 13) | Phosphorylation | - | 4.83 | 29978859 | |
120 (in isoform 13) | Phosphorylation | - | 43.27 | 29978859 | |
120 | Phosphorylation | SDTRKIVSEGELDQL HCHHHHCCCCCHHHH | 43.27 | 22468782 | |
154 | Phosphorylation | LKILEEKTAAYDIMQ HHHHHHHHHHHHHHH | 21.57 | - | |
156 (in isoform 11) | Phosphorylation | - | 14.04 | 24275569 | |
157 | Phosphorylation | LEEKTAAYDIMQEFM HHHHHHHHHHHHHHH | 11.98 | - | |
158 (in isoform 11) | Phosphorylation | - | 25.75 | 24275569 | |
169 | Acetylation | EFMALELKNLPGEFN HHHHHHHHCCCCCCC | 47.25 | 7677739 | |
205 | Phosphorylation | TRVPLGKSKDYINAS CCCCCCCCCCCCCCE | 29.03 | 28509920 | |
208 | Phosphorylation | PLGKSKDYINASYIR CCCCCCCCCCCEEEE | 10.38 | 28509920 | |
306 | Phosphorylation | MFQVVEKSTGTSHSV HHHHHHHCCCCCCCE | 20.68 | 25278378 | |
307 | Phosphorylation | FQVVEKSTGTSHSVK HHHHHHCCCCCCCEE | 56.39 | 25278378 | |
309 | Phosphorylation | VVEKSTGTSHSVKQL HHHHCCCCCCCEEEE | 24.29 | 25278378 | |
310 | Phosphorylation | VEKSTGTSHSVKQLQ HHHCCCCCCCEEEEE | 18.34 | 25278378 | |
312 | Phosphorylation | KSTGTSHSVKQLQFT HCCCCCCCEEEEEEE | 30.67 | 25278378 | |
332 | Phosphorylation | GTPASADSFIKYIRY CCCCCHHHHHHHHHH | 28.70 | 24719451 |
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 PTN20_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTN20_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 PTN20_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PTN20_HUMAN | PTPN20B | physical | 27880917 | |
G3PT_HUMAN | GAPDHS | physical | 28514442 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
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 |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASSSPECTROMETRY. |