UniProt ID | MPIP3_HUMAN | |
---|---|---|
UniProt AC | P30307 | |
Protein Name | M-phase inducer phosphatase 3 | |
Gene Name | CDC25C | |
Organism | Homo sapiens (Human). | |
Sequence Length | 473 | |
Subcellular Localization | Nucleus . | |
Protein Description | Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity.. | |
Protein Sequence | MSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQGKLRKGLCLKKTVSLCDITITQMLEEDSNQGHLIGDFSKVCALPTVSGKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQYPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHKTELLRCRSQSKVQEGERQLREQIALLVKDMSP | |
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 | Acetylation | ------MSTELFSST ------CCCCCCCCC | 30.50 | 22814378 | |
2 | Phosphorylation | ------MSTELFSST ------CCCCCCCCC | 30.50 | 29759185 | |
3 | Phosphorylation | -----MSTELFSSTR -----CCCCCCCCCC | 35.09 | 29759185 | |
7 | Phosphorylation | -MSTELFSSTREEGS -CCCCCCCCCCCCCC | 43.34 | 22199227 | |
8 | Phosphorylation | MSTELFSSTREEGSS CCCCCCCCCCCCCCC | 24.93 | 22199227 | |
9 | Phosphorylation | STELFSSTREEGSSG CCCCCCCCCCCCCCC | 40.68 | 22199227 | |
14 | Phosphorylation | SSTREEGSSGSGPSF CCCCCCCCCCCCCCH | 34.50 | 21815630 | |
15 | Phosphorylation | STREEGSSGSGPSFR CCCCCCCCCCCCCHH | 48.08 | 25159151 | |
17 | Phosphorylation | REEGSSGSGPSFRSN CCCCCCCCCCCHHHH | 49.86 | 25159151 | |
20 | Phosphorylation | GSSGSGPSFRSNQRK CCCCCCCCHHHHHHH | 36.50 | 28985074 | |
37 | Phosphorylation | NLLLERDTSFTVCPD HHHHHCCCCEEECCC | 31.77 | 18691976 | |
38 | Phosphorylation | LLLERDTSFTVCPDV HHHHCCCCEEECCCC | 24.18 | 25159151 | |
40 | Phosphorylation | LERDTSFTVCPDVPR HHCCCCEEECCCCCC | 22.44 | 29496963 | |
48 | Phosphorylation | VCPDVPRTPVGKFLG ECCCCCCCCCHHHCC | 19.09 | 25159151 | |
52 | Acetylation | VPRTPVGKFLGDSAN CCCCCCHHHCCCCCC | 37.34 | 25953088 | |
57 | Phosphorylation | VGKFLGDSANLSILS CHHHCCCCCCEEECC | 19.77 | 26055452 | |
57 (in isoform 3) | Phosphorylation | - | 19.77 | 24260401 | |
57 (in isoform 4) | Phosphorylation | - | 19.77 | 24260401 | |
61 | Phosphorylation | LGDSANLSILSGGTP CCCCCCEEECCCCCC | 22.69 | 26055452 | |
61 (in isoform 3) | Phosphorylation | - | 22.69 | 17192257 | |
61 (in isoform 4) | Phosphorylation | - | 22.69 | 17192257 | |
64 | Phosphorylation | SANLSILSGGTPKRC CCCEEECCCCCCCCE | 33.24 | 25159151 | |
64 (in isoform 3) | Phosphorylation | - | 33.24 | 23090842 | |
64 (in isoform 4) | Phosphorylation | - | 33.24 | 23090842 | |
66 (in isoform 3) | Phosphorylation | - | 35.15 | 22199227 | |
66 (in isoform 4) | Phosphorylation | - | 35.15 | 22199227 | |
67 | Phosphorylation | LSILSGGTPKRCLDL EEECCCCCCCCEEEC | 29.21 | 25159151 | |
95 (in isoform 4) | Phosphorylation | - | 65.08 | 30131370 | |
122 | Phosphorylation | DQHLMKCSPAQLLCS CHHHHHCCHHHHHHC | 20.11 | 25159151 | |
129 | Phosphorylation | SPAQLLCSTPNGLDR CHHHHHHCCCCCCCC | 47.04 | 29978859 | |
130 | Phosphorylation | PAQLLCSTPNGLDRG HHHHHHCCCCCCCCC | 21.56 | 17110335 | |
146 | Phosphorylation | RKRDAMCSSSANKEN HHHHHCCCCCCCCCC | 17.78 | 29978859 | |
147 | Phosphorylation | KRDAMCSSSANKEND HHHHCCCCCCCCCCC | 28.66 | 29978859 | |
148 | Phosphorylation | RDAMCSSSANKENDN HHHCCCCCCCCCCCC | 21.40 | 18669648 | |
151 | Ubiquitination | MCSSSANKENDNGNL CCCCCCCCCCCCCCC | 58.57 | 11842186 | |
165 | Phosphorylation | LVDSEMKYLGSPITT CCCHHHHHCCCCCCC | 18.25 | 29396449 | |
168 | Phosphorylation | SEMKYLGSPITTVPK HHHHHCCCCCCCCCC | 15.55 | 22322096 | |
171 | Phosphorylation | KYLGSPITTVPKLDK HHCCCCCCCCCCCCC | 25.73 | 28555341 | |
172 | Phosphorylation | YLGSPITTVPKLDKN HCCCCCCCCCCCCCC | 35.21 | 29978859 | |
191 | Phosphorylation | EDQAEEISDELMEFS HHHHHHHHHHHHHHC | 28.45 | 22199227 | |
198 | Phosphorylation | SDELMEFSLKDQEAK HHHHHHHCHHHCCCC | 22.62 | 14968113 | |
209 | Phosphorylation | QEAKVSRSGLYRSPS CCCCCCCCCCCCCCC | 26.16 | 25159151 | |
212 | Phosphorylation | KVSRSGLYRSPSMPE CCCCCCCCCCCCCCC | 16.75 | 26074081 | |
214 | Phosphorylation | SRSGLYRSPSMPENL CCCCCCCCCCCCCCC | 14.04 | 30266825 | |
216 | Phosphorylation | SGLYRSPSMPENLNR CCCCCCCCCCCCCCC | 48.49 | 23927012 | |
236 | Phosphorylation | VEKFKDNTIPDKVKK HHHHCCCCCCHHHHH | 43.98 | 22817900 | |
251 | Acetylation | KYFSGQGKLRKGLCL HHCCCCCCCCCCCCC | 36.91 | 25953088 | |
261 | Phosphorylation | KGLCLKKTVSLCDIT CCCCCCCCEEECCEE | 17.46 | 28450419 | |
263 | Phosphorylation | LCLKKTVSLCDITIT CCCCCCEEECCEEEE | 28.63 | 30278072 | |
268 | Phosphorylation | TVSLCDITITQMLEE CEEECCEEEEEEHHH | 12.53 | 28450419 | |
270 | Phosphorylation | SLCDITITQMLEEDS EECCEEEEEEHHHCC | 10.16 | 28450419 | |
277 | Phosphorylation | TQMLEEDSNQGHLIG EEEHHHCCCCCCEEC | 34.04 | 27080861 | |
304 | Phosphorylation | GKHQDLKYVNPETVA CCCCCCCCCCHHHHH | 16.86 | 29496907 | |
326 | Phosphorylation | QGLIEKFYVIDCRYP HHHEEEEEEEECCCC | 13.94 | 29496907 | |
451 | Phosphorylation | LLRCRSQSKVQEGER HHHHHHHHHHHHHHH | 35.72 | 25137130 | |
472 | Phosphorylation | ALLVKDMSP------ HHHHHCCCC------ | 37.28 | 21712546 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
48 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
67 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
75 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
122 | S | Phosphorylation | Kinase | CDK1 | P06493 | Uniprot |
130 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
168 | S | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
168 | S | Phosphorylation | Kinase | MAPK9 | P45984 | GPS |
168 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
191 | S | Phosphorylation | Kinase | PLK3 | Q9H4B4 | Uniprot |
198 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
198 | S | Phosphorylation | Kinase | PLK3 | Q9H4B4 | Uniprot |
214 | S | Phosphorylation | Kinase | CDK1 | P06493 | Uniprot |
214 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
216 | S | Phosphorylation | Kinase | MARK3 | P27448 | PSP |
216 | S | Phosphorylation | Kinase | BRSK1 | Q8TDC3 | Uniprot |
216 | S | Phosphorylation | Kinase | BRSK1 | Q8TDC3-2 | GPS |
216 | S | Phosphorylation | Kinase | MAPK14 | Q16539 | Uniprot |
216 | S | Phosphorylation | Kinase | CHK1 | O14757 | PSP |
216 | S | Phosphorylation | Kinase | CHK2 | O96017 | PSP |
216 | S | Phosphorylation | Kinase | TAK1 | O43318 | PSP |
216 | S | Phosphorylation | Kinase | MAPKAPK2 | P49137 | PSP |
236 | T | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
236 | T | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
247 | S | Phosphorylation | Kinase | RPS6KA1 | Q15418 | GPS |
- | K | Ubiquitination | E3 ubiquitin ligase | BRCA1 | P38398 | PMID:23246971 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
48 | T | Phosphorylation |
| 8119945 |
67 | T | Phosphorylation |
| 8119945 |
122 | S | Phosphorylation |
| 8119945 |
130 | T | Phosphorylation |
| 8119945 |
168 | S | Phosphorylation |
| 8119945 |
168 | S | Phosphorylation |
| 8119945 |
191 | S | Phosphorylation |
| 14968113 |
198 | S | Phosphorylation |
| 14968113 |
214 | S | Phosphorylation |
| 8119945 |
216 | S | Phosphorylation |
| 11333986 |
216 | S | Phosphorylation |
| 11333986 |
* 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 MPIP3_HUMAN !! |
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 |
"Initiation of a G2/M checkpoint after ultraviolet radiation requiresp38 kinase."; Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V.,Potapova O., Appella E., Fornace A.J. Jr.; Nature 411:102-107(2001). Cited for: PHOSPHORYLATION AT SER-216, AND INTERACTION WITH MAPK14 AND 14-3-3PROTEINS. | |
"Human SAD1 kinase is involved in UV-induced DNA damage checkpointfunction."; Lu R., Niida H., Nakanishi M.; J. Biol. Chem. 279:31164-31170(2004). Cited for: PHOSPHORYLATION AT SER-216. | |
"Cdc25C phosphorylation on serine 191 by Plk3 promotes its nucleartranslocation."; Bahassi el M., Hennigan R.F., Myer D.L., Stambrook P.J.; Oncogene 23:2658-2663(2004). Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-191 AND SER-198, ANDMUTAGENESIS OF SER-191. | |
"MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates theG2/M transition and S phase progression in response to UVirradiation."; Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B.; Mol. Cell 17:37-48(2005). Cited for: PHOSPHORYLATION AT SER-216 BY MAPKAPK2. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-64; SER-168 ANDSER-472, 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-38; THR-48; SER-57;SER-61; SER-64 AND THR-67, AND MASS SPECTROMETRY. |