MDM1_HUMAN - dbPTM
MDM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MDM1_HUMAN
UniProt AC Q8TC05
Protein Name Nuclear protein MDM1
Gene Name MDM1
Organism Homo sapiens (Human).
Sequence Length 714
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Localizes to the centriole lumen.
Protein Description Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules. [PubMed: 26337392]
Protein Sequence MPVRFKGLSEYQRNFLWKKSYLSESCNSSVGRKYPWAGLRSDQLGITKEPSFISKRRVPYHDPQISKSLEWNGAISESNVVASPEPEAPETPKSQEAEQKDVTQERVHSLEASRVPKRTRSHSADSRAEGASDVENNEGVTNHTPVNENVELEHSTKVLSENVDNGLDRLLRKKAGLTVVPSYNALRNSEYQRQFVWKTSKETAPAFAANQVFHNKSQFVPPFKGNSVIHETEYKRNFKGLSPVKEPKLRNDLRENRNLETVSPERKSNKIDDRLKLEAEMELKDLHQPKRKLTPWKHQRLGKVNSEYRAKFLSPAQYLYKAGAWTHVKGNMPNQVKELREKAEFYRKRVQGTHFSRDHLNQILSDSNCCWDVSSTTSSEGTVSSNIRALDLAGDPTSHKTLQKCPSTEPEEKGNIVEEQPQKNTTEKLGVSAPTIPVRRRLAWDTENTSEDVQKQPGEKEEEDDNEEEGDRKTGKQAFMGEQEKLDVREKSKADKMKEGSDSSVSSEKGGRLPTPKLRELGGIQRTHHDLTTPAVGGAVLVSPSKMKPPAPEQRKRMTSQDCLETSKNDFTKKESRAVSLLTSPAAGIKTVDPLPLREDSEDNIHKFAEATLPVSKIPKYPTNPPGQLPSPPHVPSYWHPSRRIQGSLRDPEFQHNVGKARMNNLQLPQHEAFNDEDEDRLSEISARSAASSLRAFQTLARAKKRKENFWGKT
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
6Methylation--MPVRFKGLSEYQR
--CCCCCCCCHHHHH		48.67115972915
23PhosphorylationLWKKSYLSESCNSSV
HHHHHHHCHHCCCCC		21.1628985074
25PhosphorylationKKSYLSESCNSSVGR
HHHHHCHHCCCCCCC		18.4128985074
28PhosphorylationYLSESCNSSVGRKYP
HHCHHCCCCCCCCCC		30.6327251275
29PhosphorylationLSESCNSSVGRKYPW
HCHHCCCCCCCCCCC		18.0127251275
41PhosphorylationYPWAGLRSDQLGITK
CCCCCCCCCCCCCCC		34.4523285258
47PhosphorylationRSDQLGITKEPSFIS
CCCCCCCCCCCCHHC		27.7923285258
48UbiquitinationSDQLGITKEPSFISK
CCCCCCCCCCCHHCC		66.7529967540
51PhosphorylationLGITKEPSFISKRRV
CCCCCCCCHHCCCCC		35.9827251275
83PhosphorylationSESNVVASPEPEAPE
CCCCCCCCCCCCCCC		20.4127251275
109PhosphorylationVTQERVHSLEASRVP
CCHHHHHHHHHHCCC		25.6620860994
121PhosphorylationRVPKRTRSHSADSRA
CCCCCCCCCCCCCCC		22.6028270605
123PhosphorylationPKRTRSHSADSRAEG
CCCCCCCCCCCCCCC		34.7128270605
126PhosphorylationTRSHSADSRAEGASD
CCCCCCCCCCCCCCC		32.8628270605
132PhosphorylationDSRAEGASDVENNEG
CCCCCCCCCCCCCCC		53.7123401153
141PhosphorylationVENNEGVTNHTPVNE
CCCCCCCCCCCCCCC		31.9427732954
144PhosphorylationNEGVTNHTPVNENVE
CCCCCCCCCCCCCCC		30.8826657352
182PhosphorylationAGLTVVPSYNALRNS
CCCEEECCCHHHCCC		21.2925693802
183PhosphorylationGLTVVPSYNALRNSE
CCEEECCCHHHCCCH		9.8225693802
234PhosphorylationSVIHETEYKRNFKGL
CEEEECCCCCCCCCC		23.75-
242PhosphorylationKRNFKGLSPVKEPKL
CCCCCCCCCCCCHHH		35.9923401153
252UbiquitinationKEPKLRNDLRENRNL
CCHHHHHHHHHCCCC		40.4429967540
261PhosphorylationRENRNLETVSPERKS
HHCCCCCCCCCCHHC		29.4729255136
263PhosphorylationNRNLETVSPERKSNK
CCCCCCCCCCHHCCC		28.5923401153
268PhosphorylationTVSPERKSNKIDDRL
CCCCCHHCCCCCHHH		49.9626074081
294PhosphorylationHQPKRKLTPWKHQRL
CCCCCCCCCCHHHHH		30.0924719451
297UbiquitinationKRKLTPWKHQRLGKV
CCCCCCCHHHHHCCC		30.9429967540
314PhosphorylationEYRAKFLSPAQYLYK
HHHHHHCCHHHHHHH		22.7122617229
353PhosphorylationYRKRVQGTHFSRDHL
HHHHHCCCCCCHHHH		11.5827732954
356PhosphorylationRVQGTHFSRDHLNQI
HHCCCCCCHHHHHHH		29.2427732954
407PhosphorylationKTLQKCPSTEPEEKG
CCHHHCCCCCHHHCC		55.6724719451
408PhosphorylationTLQKCPSTEPEEKGN
CHHHCCCCCHHHCCC		40.4723401153
449PhosphorylationLAWDTENTSEDVQKQ
CCCCCCCCCHHHHCC		27.5329970186
501PhosphorylationADKMKEGSDSSVSSE
HHHHCCCCCCCCCCC		35.1025954137
503PhosphorylationKMKEGSDSSVSSEKG
HHCCCCCCCCCCCCC		34.0426657352
504PhosphorylationMKEGSDSSVSSEKGG
HCCCCCCCCCCCCCC		30.8926657352
506PhosphorylationEGSDSSVSSEKGGRL
CCCCCCCCCCCCCCC		34.4317924679
507PhosphorylationGSDSSVSSEKGGRLP
CCCCCCCCCCCCCCC		40.9725954137
515PhosphorylationEKGGRLPTPKLRELG
CCCCCCCCHHHHHCC		37.3327251275
532PhosphorylationQRTHHDLTTPAVGGA
CCCCCCCCCCCCCCE		36.4726074081
533PhosphorylationRTHHDLTTPAVGGAV
CCCCCCCCCCCCCEE		19.2926074081
543PhosphorylationVGGAVLVSPSKMKPP
CCCEEEECHHHCCCC		21.2123401153
545PhosphorylationGAVLVSPSKMKPPAP
CEEEECHHHCCCCCH		37.5623663014
549PhosphorylationVSPSKMKPPAPEQRK
ECHHHCCCCCHHHHH		27.1332142685
559PhosphorylationPEQRKRMTSQDCLET
HHHHHCCCHHHHHHH		27.5428450419
560PhosphorylationEQRKRMTSQDCLETS
HHHHCCCHHHHHHHC		18.0626074081
566PhosphorylationTSQDCLETSKNDFTK
CHHHHHHHCHHCCCH		31.8628985074
572PhosphorylationETSKNDFTKKESRAV
HHCHHCCCHHHHHHH		44.03-
573MethylationTSKNDFTKKESRAVS
HCHHCCCHHHHHHHH		55.31-
573"N6,N6-dimethyllysine"TSKNDFTKKESRAVS
HCHHCCCHHHHHHHH		55.31-
574"N6,N6-dimethyllysine"SKNDFTKKESRAVSL
CHHCCCHHHHHHHHH		58.84-
574MethylationSKNDFTKKESRAVSL
CHHCCCHHHHHHHHH		58.84-
580PhosphorylationKKESRAVSLLTSPAA
HHHHHHHHHHCCCCC		19.3730108239
583PhosphorylationSRAVSLLTSPAAGIK
HHHHHHHCCCCCCCC		37.6528348404
584PhosphorylationRAVSLLTSPAAGIKT
HHHHHHCCCCCCCCC		16.7125159151
590UbiquitinationTSPAAGIKTVDPLPL
CCCCCCCCCCCCCCC		41.39-
601PhosphorylationPLPLREDSEDNIHKF
CCCCCCCCCCCHHHH		41.9423401153
631PhosphorylationNPPGQLPSPPHVPSY
CCCCCCCCCCCCCCC		60.7130108239
637PhosphorylationPSPPHVPSYWHPSRR
CCCCCCCCCCCCCCC		39.5028634298
638PhosphorylationSPPHVPSYWHPSRRI
CCCCCCCCCCCCCCC		11.1528634298
648PhosphorylationPSRRIQGSLRDPEFQ
CCCCCCCCCCCHHHH		12.1229978859
651PhosphorylationRIQGSLRDPEFQHNV
CCCCCCCCHHHHHHH		52.9933259812
683PhosphorylationDEDEDRLSEISARSA
CCCHHHHHHHHHHHH		33.5027966365
686PhosphorylationEDRLSEISARSAASS
HHHHHHHHHHHHHHH		17.3633259812
689PhosphorylationLSEISARSAASSLRA
HHHHHHHHHHHHHHH		28.0930108239
692PhosphorylationISARSAASSLRAFQT
HHHHHHHHHHHHHHH		29.6230108239
693PhosphorylationSARSAASSLRAFQTL
HHHHHHHHHHHHHHH		19.6930108239
699PhosphorylationSSLRAFQTLARAKKR
HHHHHHHHHHHHHHH		18.8728060719
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

Oops, there are no upstream regulatory protein records of MDM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MDM1_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 MDM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
POC1A_HUMANPOC1Aphysical
28514442
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 MDM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-314 AND SER-584, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504 AND SER-506, ANDMASS SPECTROMETRY.

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