MPIP3_HUMAN - dbPTM
MPIP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSTELFSST
------CCCCCCCCC
30.5022814378
2Phosphorylation------MSTELFSST
------CCCCCCCCC
30.5029759185
3Phosphorylation-----MSTELFSSTR
-----CCCCCCCCCC
35.0929759185
7Phosphorylation-MSTELFSSTREEGS
-CCCCCCCCCCCCCC
43.3422199227
8PhosphorylationMSTELFSSTREEGSS
CCCCCCCCCCCCCCC
24.9322199227
9PhosphorylationSTELFSSTREEGSSG
CCCCCCCCCCCCCCC
40.6822199227
14PhosphorylationSSTREEGSSGSGPSF
CCCCCCCCCCCCCCH
34.5021815630
15PhosphorylationSTREEGSSGSGPSFR
CCCCCCCCCCCCCHH
48.0825159151
17PhosphorylationREEGSSGSGPSFRSN
CCCCCCCCCCCHHHH
49.8625159151
20PhosphorylationGSSGSGPSFRSNQRK
CCCCCCCCHHHHHHH
36.5028985074
37PhosphorylationNLLLERDTSFTVCPD
HHHHHCCCCEEECCC
31.7718691976
38PhosphorylationLLLERDTSFTVCPDV
HHHHCCCCEEECCCC
24.1825159151
40PhosphorylationLERDTSFTVCPDVPR
HHCCCCEEECCCCCC
22.4429496963
48PhosphorylationVCPDVPRTPVGKFLG
ECCCCCCCCCHHHCC
19.0925159151
52AcetylationVPRTPVGKFLGDSAN
CCCCCCHHHCCCCCC
37.3425953088
57PhosphorylationVGKFLGDSANLSILS
CHHHCCCCCCEEECC
19.7726055452
57 (in isoform 3)Phosphorylation-19.7724260401
57 (in isoform 4)Phosphorylation-19.7724260401
61PhosphorylationLGDSANLSILSGGTP
CCCCCCEEECCCCCC
22.6926055452
61 (in isoform 3)Phosphorylation-22.6917192257
61 (in isoform 4)Phosphorylation-22.6917192257
64PhosphorylationSANLSILSGGTPKRC
CCCEEECCCCCCCCE
33.2425159151
64 (in isoform 3)Phosphorylation-33.2423090842
64 (in isoform 4)Phosphorylation-33.2423090842
66 (in isoform 3)Phosphorylation-35.1522199227
66 (in isoform 4)Phosphorylation-35.1522199227
67PhosphorylationLSILSGGTPKRCLDL
EEECCCCCCCCEEEC
29.2125159151
95 (in isoform 4)Phosphorylation-65.0830131370
122PhosphorylationDQHLMKCSPAQLLCS
CHHHHHCCHHHHHHC
20.1125159151
129PhosphorylationSPAQLLCSTPNGLDR
CHHHHHHCCCCCCCC
47.0429978859
130PhosphorylationPAQLLCSTPNGLDRG
HHHHHHCCCCCCCCC
21.5617110335
146PhosphorylationRKRDAMCSSSANKEN
HHHHHCCCCCCCCCC
17.7829978859
147PhosphorylationKRDAMCSSSANKEND
HHHHCCCCCCCCCCC
28.6629978859
148PhosphorylationRDAMCSSSANKENDN
HHHCCCCCCCCCCCC
21.4018669648
151UbiquitinationMCSSSANKENDNGNL
CCCCCCCCCCCCCCC
58.5711842186
165PhosphorylationLVDSEMKYLGSPITT
CCCHHHHHCCCCCCC
18.2529396449
168PhosphorylationSEMKYLGSPITTVPK
HHHHHCCCCCCCCCC
15.5522322096
171PhosphorylationKYLGSPITTVPKLDK
HHCCCCCCCCCCCCC
25.7328555341
172PhosphorylationYLGSPITTVPKLDKN
HCCCCCCCCCCCCCC
35.2129978859
191PhosphorylationEDQAEEISDELMEFS
HHHHHHHHHHHHHHC
28.4522199227
198PhosphorylationSDELMEFSLKDQEAK
HHHHHHHCHHHCCCC
22.6214968113
209PhosphorylationQEAKVSRSGLYRSPS
CCCCCCCCCCCCCCC
26.1625159151
212PhosphorylationKVSRSGLYRSPSMPE
CCCCCCCCCCCCCCC
16.7526074081
214PhosphorylationSRSGLYRSPSMPENL
CCCCCCCCCCCCCCC
14.0430266825
216PhosphorylationSGLYRSPSMPENLNR
CCCCCCCCCCCCCCC
48.4923927012
236PhosphorylationVEKFKDNTIPDKVKK
HHHHCCCCCCHHHHH
43.9822817900
251AcetylationKYFSGQGKLRKGLCL
HHCCCCCCCCCCCCC
36.9125953088
261PhosphorylationKGLCLKKTVSLCDIT
CCCCCCCCEEECCEE
17.4628450419
263PhosphorylationLCLKKTVSLCDITIT
CCCCCCEEECCEEEE
28.6330278072
268PhosphorylationTVSLCDITITQMLEE
CEEECCEEEEEEHHH
12.5328450419
270PhosphorylationSLCDITITQMLEEDS
EECCEEEEEEHHHCC
10.1628450419
277PhosphorylationTQMLEEDSNQGHLIG
EEEHHHCCCCCCEEC
34.0427080861
304PhosphorylationGKHQDLKYVNPETVA
CCCCCCCCCCHHHHH
16.8629496907
326PhosphorylationQGLIEKFYVIDCRYP
HHHEEEEEEEECCCC
13.9429496907
451PhosphorylationLLRCRSQSKVQEGER
HHHHHHHHHHHHHHH
35.7225137130
472PhosphorylationALLVKDMSP------
HHHHHCCCC------
37.2821712546

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
48TPhosphorylationKinaseCDK1P06493
PSP
67TPhosphorylationKinaseCDK1P06493
PSP
75SPhosphorylationKinasePLK1P53350
PSP
122SPhosphorylationKinaseCDK1P06493
Uniprot
130TPhosphorylationKinaseCDK1P06493
PSP
168SPhosphorylationKinaseMAPK8P45983
GPS
168SPhosphorylationKinaseMAPK9P45984
GPS
168SPhosphorylationKinaseCDK1P06493
PSP
191SPhosphorylationKinasePLK3Q9H4B4
Uniprot
198SPhosphorylationKinasePLK1P53350
PSP
198SPhosphorylationKinasePLK3Q9H4B4
Uniprot
214SPhosphorylationKinaseCDK1P06493
Uniprot
214SPhosphorylationKinaseCDK2P24941
PSP
216SPhosphorylationKinaseMARK3P27448
PSP
216SPhosphorylationKinaseBRSK1Q8TDC3
Uniprot
216SPhosphorylationKinaseBRSK1Q8TDC3-2
GPS
216SPhosphorylationKinaseMAPK14Q16539
Uniprot
216SPhosphorylationKinaseCHK1O14757
PSP
216SPhosphorylationKinaseCHK2O96017
PSP
216SPhosphorylationKinaseTAK1O43318
PSP
216SPhosphorylationKinaseMAPKAPK2P49137
PSP
236TPhosphorylationKinaseCK2-FAMILY-GPS
236TPhosphorylationKinaseCSNK2A1P68400
GPS
247SPhosphorylationKinaseRPS6KA1Q15418
GPS
-KUbiquitinationE3 ubiquitin ligaseBRCA1P38398
PMID:23246971

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48TPhosphorylation

8119945
67TPhosphorylation

8119945
122SPhosphorylation

8119945
130TPhosphorylation

8119945
168SPhosphorylation

8119945
168SPhosphorylation

8119945
191SPhosphorylation

14968113
198SPhosphorylation

14968113
214SPhosphorylation

8119945
216SPhosphorylation

11333986
216SPhosphorylation

11333986

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIN1_HUMANPIN1physical
9499405
CHK1_HUMANCHEK1physical
9278511
MK14_HUMANMAPK14physical
11333986
PCNA_HUMANPCNAphysical
11896603
NEDD4_HUMANNEDD4physical
10037602
CCNB1_HUMANCCNB1physical
10864927
CDK1_HUMANCDK1physical
10864927
MK03_HUMANMAPK3physical
16582626
MK01_HUMANMAPK1physical
16582626
1433B_HUMANYWHABphysical
15284440
U17L2_HUMANUSP17L2physical
20228808
CDK2_HUMANCDK2physical
8475101
MARK3_HUMANMARK3physical
12941695
MARK3_HUMANMARK3physical
9543386
1433Z_HUMANYWHAZphysical
10681541
1433B_HUMANYWHABphysical
10681541
1433E_HUMANYWHAEphysical
10681541
PKN1_HUMANPKN1physical
15791647
1433B_HUMANYWHABphysical
15791647
1433E_HUMANYWHAEphysical
15791647
1433G_HUMANYWHAGphysical
15791647
1433F_HUMANYWHAHphysical
15791647
1433T_HUMANYWHAQphysical
15791647
1433Z_HUMANYWHAZphysical
15791647
1433S_HUMANSFNphysical
15791647
HS90A_HUMANHSP90AA1physical
17525741
CDC37_HUMANCDC37physical
17525741
HSP74_HUMANHSPA4physical
17525741
CCNB2_HUMANCCNB2physical
27880917
CDK1_HUMANCDK1physical
27880917
SUFU_HUMANSUFUphysical
27880917
1433B_HUMANYWHABphysical
27880917
1433E_HUMANYWHAEphysical
27880917
1433G_HUMANYWHAGphysical
27880917
1433F_HUMANYWHAHphysical
27880917
1433T_HUMANYWHAQphysical
27880917
1433Z_HUMANYWHAZphysical
27880917
MPIP3_HUMANCDC25Cphysical
27432908
APLD1_HUMANAPOLD1physical
27432908
PHLB3_HUMANPHLDB3physical
27432908
LGUL_HUMANGLO1physical
27432908
GRPE1_HUMANGRPEL1physical
27432908
SLIRP_HUMANSLIRPphysical
27432908
1433F_HUMANYWHAHphysical
27432908
TPP1_HUMANTPP1physical
27432908
SUFU_HUMANSUFUphysical
27432908
SCO2_HUMANSCO2physical
27432908
STIP1_HUMANSTIP1physical
27432908
CDC37_HUMANCDC37physical
27432908
1433G_HUMANYWHAGphysical
27432908
CSK22_HUMANCSNK2A2physical
27432908
CTBP2_HUMANCTBP2physical
27432908
ILK_HUMANILKphysical
27432908
RS27A_HUMANRPS27Aphysical
27432908
HPBP1_HUMANHSPBP1physical
27432908
SUFU_HUMANSUFUphysical
28514442
SHC1_HUMANSHC1physical
28514442
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
CING_HUMANCGNphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
MAST3_HUMANMAST3physical
27173435
LRFN1_HUMANLRFN1physical
27173435
RGPS2_HUMANRALGPS2physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
GGYF2_HUMANGIGYF2physical
27173435
NF1_HUMANNF1physical
27173435
CBY1_HUMANCBY1physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LPIN3_HUMANLPIN3physical
27173435
CAMP2_HUMANCAMSAP2physical
27173435
HDAC4_HUMANHDAC4physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
NADK_HUMANNADKphysical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
ZN638_HUMANZNF638physical
27173435
NGAP_HUMANRASAL2physical
27173435
M3K21_HUMANKIAA1804physical
27173435
TIAM1_HUMANTIAM1physical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
SRS12_HUMANSRSF12physical
27173435
TANC2_HUMANTANC2physical
27173435
NAV1_HUMANNAV1physical
27173435
SYDE1_HUMANSYDE1physical
27173435
STA13_HUMANSTARD13physical
27173435
INP5E_HUMANINPP5Ephysical
27173435

Drug and Disease Associations
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.
Regulatory Network of MPIP3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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