MPLKI_HUMAN - dbPTM
MPLKI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPLKI_HUMAN
UniProt AC Q8TAP9
Protein Name M-phase-specific PLK1-interacting protein
Gene Name MPLKIP
Organism Homo sapiens (Human).
Sequence Length 179
Subcellular Localization Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. The subcellular location is regulated during cell cycle. During interphase located in the nucleus. During mitosis located at the centrosome and dispersed in the c
Protein Description May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis..
Protein Sequence MQRQNFRPPTPPYPGPGGGGWGSGSSFRGTPGGGGPRPPSPRDGYGSPHHTPPYGPRSRPYGSSHSPRHGGSFPGGRFGSPSPGGYPGSYSRSPAGSQQQFGYSPGQQQTHPQGSPRTSTPFGSGRVREKRMSNELENYFKPSMLEDPWAGLEPVSVVDISQQYSNTQTFTGKKGRYFC
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
7Methylation-MQRQNFRPPTPPYP
-CCCCCCCCCCCCCC		43.7824376955
7Dimethylation-MQRQNFRPPTPPYP
-CCCCCCCCCCCCCC		43.78-
10PhosphorylationRQNFRPPTPPYPGPG
CCCCCCCCCCCCCCC		39.3122617229
13PhosphorylationFRPPTPPYPGPGGGG
CCCCCCCCCCCCCCC		23.2523898821
23PhosphorylationPGGGGWGSGSSFRGT
CCCCCCCCCCCCCCC		29.0626074081
25PhosphorylationGGGWGSGSSFRGTPG
CCCCCCCCCCCCCCC		28.1826074081
26PhosphorylationGGWGSGSSFRGTPGG
CCCCCCCCCCCCCCC		23.6126074081
28MethylationWGSGSSFRGTPGGGG
CCCCCCCCCCCCCCC		50.4524376965
28DimethylationWGSGSSFRGTPGGGG
CCCCCCCCCCCCCCC		50.45-
30PhosphorylationSGSSFRGTPGGGGPR
CCCCCCCCCCCCCCC		17.9526055452
37Asymmetric dimethylarginineTPGGGGPRPPSPRDG
CCCCCCCCCCCCCCC		60.06-
37MethylationTPGGGGPRPPSPRDG
CCCCCCCCCCCCCCC		60.0624376975
40PhosphorylationGGGPRPPSPRDGYGS
CCCCCCCCCCCCCCC		34.9430266825
42DimethylationGPRPPSPRDGYGSPH
CCCCCCCCCCCCCCC		55.08-
42MethylationGPRPPSPRDGYGSPH
CCCCCCCCCCCCCCC		55.0830763419
45PhosphorylationPPSPRDGYGSPHHTP
CCCCCCCCCCCCCCC		20.7923927012
47PhosphorylationSPRDGYGSPHHTPPY
CCCCCCCCCCCCCCC		16.7523401153
51PhosphorylationGYGSPHHTPPYGPRS
CCCCCCCCCCCCCCC		23.9523401153
54PhosphorylationSPHHTPPYGPRSRPY
CCCCCCCCCCCCCCC		40.7528450419
57MethylationHTPPYGPRSRPYGSS
CCCCCCCCCCCCCCC		40.7224129315
57DimethylationHTPPYGPRSRPYGSS
CCCCCCCCCCCCCCC		40.72-
58PhosphorylationTPPYGPRSRPYGSSH
CCCCCCCCCCCCCCC		40.5226270265
59MethylationPPYGPRSRPYGSSHS
CCCCCCCCCCCCCCC		29.7324129315
59Asymmetric dimethylargininePPYGPRSRPYGSSHS
CCCCCCCCCCCCCCC		29.73-
61PhosphorylationYGPRSRPYGSSHSPR
CCCCCCCCCCCCCCC		28.6426270265
63PhosphorylationPRSRPYGSSHSPRHG
CCCCCCCCCCCCCCC		21.0229978859
64PhosphorylationRSRPYGSSHSPRHGG
CCCCCCCCCCCCCCC		24.5027732954
66PhosphorylationRPYGSSHSPRHGGSF
CCCCCCCCCCCCCCC		26.1029496963
68MethylationYGSSHSPRHGGSFPG
CCCCCCCCCCCCCCC		44.0624129315
68Asymmetric dimethylarginineYGSSHSPRHGGSFPG
CCCCCCCCCCCCCCC		44.06-
72PhosphorylationHSPRHGGSFPGGRFG
CCCCCCCCCCCCCCC		32.6225159151
77Asymmetric dimethylarginineGGSFPGGRFGSPSPG
CCCCCCCCCCCCCCC		38.37-
77MethylationGGSFPGGRFGSPSPG
CCCCCCCCCCCCCCC		38.3724129315
80PhosphorylationFPGGRFGSPSPGGYP
CCCCCCCCCCCCCCC		21.3525159151
82PhosphorylationGGRFGSPSPGGYPGS
CCCCCCCCCCCCCCC		37.5625159151
89PhosphorylationSPGGYPGSYSRSPAG
CCCCCCCCCCCCCCC		18.5426425664
91PhosphorylationGGYPGSYSRSPAGSQ
CCCCCCCCCCCCCCC		28.16-
92MethylationGYPGSYSRSPAGSQQ
CCCCCCCCCCCCCCC		38.13115919105
93PhosphorylationYPGSYSRSPAGSQQQ
CCCCCCCCCCCCCCC		17.1123401153
97PhosphorylationYSRSPAGSQQQFGYS
CCCCCCCCCCCCCCC		27.2423927012
103PhosphorylationGSQQQFGYSPGQQQT
CCCCCCCCCCCCCCC		17.0023927012
104PhosphorylationSQQQFGYSPGQQQTH
CCCCCCCCCCCCCCC		23.9623927012
110PhosphorylationYSPGQQQTHPQGSPR
CCCCCCCCCCCCCCC		31.0522167270
115PhosphorylationQQTHPQGSPRTSTPF
CCCCCCCCCCCCCCC		13.1322167270
117MethylationTHPQGSPRTSTPFGS
CCCCCCCCCCCCCCC		42.9024129315
117DimethylationTHPQGSPRTSTPFGS
CCCCCCCCCCCCCCC		42.90-
118PhosphorylationHPQGSPRTSTPFGSG
CCCCCCCCCCCCCCH		40.0929396449
119PhosphorylationPQGSPRTSTPFGSGR
CCCCCCCCCCCCCHH		35.0520068231
120PhosphorylationQGSPRTSTPFGSGRV
CCCCCCCCCCCCHHH		23.2525159151
124PhosphorylationRTSTPFGSGRVREKR
CCCCCCCCHHHCHHH		24.6523401153
126MethylationSTPFGSGRVREKRMS
CCCCCCHHHCHHHHH		26.4758860199
126DimethylationSTPFGSGRVREKRMS
CCCCCCHHHCHHHHH		26.47-
133PhosphorylationRVREKRMSNELENYF
HHCHHHHHHHHHHHC		31.0519664994
139PhosphorylationMSNELENYFKPSMLE
HHHHHHHHCCHHHHC		12.0130108239
143PhosphorylationLENYFKPSMLEDPWA
HHHHCCHHHHCCCCC		36.2720068231
156PhosphorylationWAGLEPVSVVDISQQ
CCCCCCEEEEEHHHH		27.4320068231
161PhosphorylationPVSVVDISQQYSNTQ
CEEEEEHHHHCCCCC		13.5320068231
164PhosphorylationVVDISQQYSNTQTFT
EEEHHHHCCCCCEEC		9.0320068231
165PhosphorylationVDISQQYSNTQTFTG
EEHHHHCCCCCEECC		29.1220068231
167PhosphorylationISQQYSNTQTFTGKK
HHHHCCCCCEECCCC		24.0520068231
169PhosphorylationQQYSNTQTFTGKKGR
HHCCCCCEECCCCCC		22.5620068231
171PhosphorylationYSNTQTFTGKKGRYF
CCCCCEECCCCCCCC		52.0220068231
173AcetylationNTQTFTGKKGRYFC-
CCCEECCCCCCCCC-		49.3430593139
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
93SPhosphorylationKinaseCDK1P06493
PSP
104SPhosphorylationKinaseCDK1P06493
PSP
120TPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPLKI_HUMAN !!
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 MPLKI_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MPLKI_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
234050Trichothiodystrophy 4, non-photosensitive (TTD4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPLKI_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 TYR-45; SER-47; THR-51;SER-72; SER-80; SER-82; SER-93; SER-104; SER-115; THR-120 AND SER-124,AND MASS SPECTROMETRY.
"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 TYR-13; SER-72; SER-80;SER-82; SER-93; SER-115; THR-120 AND SER-133, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45; SER-47 AND THR-51,AND MASS SPECTROMETRY.
"TTDN1 is a Plk1-interacting protein involved in maintenance of cellcycle integrity.";
Zhang Y., Tian Y., Chen Q., Chen D., Zhai Z., Shu H.-B.;
Cell. Mol. Life Sci. 64:632-640(2007).
Cited for: FUNCTION, INTERACTION WITH PLK1, SUBCELLULAR LOCATION, MUTAGENESIS OFSER-93; SER-104 AND THR-120, AND PHOSPHORYLATION AT SER-93 ANDSER-104.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120, AND MASSSPECTROMETRY.

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