MPRIP_HUMAN - dbPTM
MPRIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPRIP_HUMAN
UniProt AC Q6WCQ1
Protein Name Myosin phosphatase Rho-interacting protein
Gene Name MPRIP
Organism Homo sapiens (Human).
Sequence Length 1025
Subcellular Localization Cytoplasm, cytoskeleton . Colocalizes with F-actin.
Protein Description Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells..
Protein Sequence MSAAKENPCRKFQANIFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEGRTGQKFSLCILTPEKEHFIRAETKEIVSGWLEMLMVYPRTNKQNQKKKRKVEPPTPQEPGPAKVAVTSSSSSSSSSSSIPSAEKVPTTKSTLWQEEMRTKDQPDGSSLSPAQSPSQSQPPAASSLREPGLESKEEESAMSSDRMDCGRKVRVESGYFSLEKTKQDLKAEEQQLPPPLSPPSPSTPNHRRSQVIEKFEALDIEKAEHMETNAVGPSPSSDTRQGRSEKRAFPRKRDFTNEAPPAPLPDASASPLSPHRRAKSLDRRSTEPSVTPDLLNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEIDLSACYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVHPTTAPDVTSSLPEEKNKSSCSFETCPRPTEKQEAELGEPDPEQKRSRARERRREGRSKTFDWAEFRPIQQALAQERVGGVGPADTHEPLRPEAEPGELERERARRREERRKRFGMLDATDGPGTEDAALRMEVDRSPGLPMSDLKTHNVHVEIEQRWHQVETTPLREEKQVPIAPVHLSSEDGGDRLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSVNSDVEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGEATGSPLAQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPDSATVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSVIEQVSWDT
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
5Ubiquitination---MSAAKENPCRKF
---CCCCCCCCCHHH		58.71-
5 (in isoform 2)Ubiquitination-58.71-
123PhosphorylationKFSLCILTPEKEHFI
EEEEEEECCCHHHHH		14.9728674419
126AcetylationLCILTPEKEHFIRAE
EEEECCCHHHHHHHH		58.6626051181
161 (in isoform 2)Malonylation-60.8832601280
166PhosphorylationKRKVEPPTPQEPGPA
CCCCCCCCCCCCCCC		48.6028857561
178O-linked_GlycosylationGPAKVAVTSSSSSSS
CCCEEEEEECCCCCC		17.1030379171
178PhosphorylationGPAKVAVTSSSSSSS
CCCEEEEEECCCCCC		17.1027251275
179PhosphorylationPAKVAVTSSSSSSSS
CCEEEEEECCCCCCC		22.9424732914
180PhosphorylationAKVAVTSSSSSSSSS
CEEEEEECCCCCCCC		25.5224732914
181PhosphorylationKVAVTSSSSSSSSSS
EEEEEECCCCCCCCC		33.7224732914
182PhosphorylationVAVTSSSSSSSSSSS
EEEEECCCCCCCCCC		35.8724732914
183PhosphorylationAVTSSSSSSSSSSSI
EEEECCCCCCCCCCC		35.8724732914
184PhosphorylationVTSSSSSSSSSSSIP
EEECCCCCCCCCCCC		35.8724732914
185PhosphorylationTSSSSSSSSSSSIPS
EECCCCCCCCCCCCC		35.8724732914
186PhosphorylationSSSSSSSSSSSIPSA
ECCCCCCCCCCCCCC		35.8724732914
187PhosphorylationSSSSSSSSSSIPSAE
CCCCCCCCCCCCCCC		30.0124732914
188PhosphorylationSSSSSSSSSIPSAEK
CCCCCCCCCCCCCCC		33.9524732914
189PhosphorylationSSSSSSSSIPSAEKV
CCCCCCCCCCCCCCC		40.2323663014
192PhosphorylationSSSSSIPSAEKVPTT
CCCCCCCCCCCCCCC		47.6025159151
198PhosphorylationPSAEKVPTTKSTLWQ
CCCCCCCCCCHHHHH		50.2523663014
199PhosphorylationSAEKVPTTKSTLWQE
CCCCCCCCCHHHHHH		19.5423663014
210PhosphorylationLWQEEMRTKDQPDGS
HHHHHHHCCCCCCCC		37.3530266825
217PhosphorylationTKDQPDGSSLSPAQS
CCCCCCCCCCCCCCC		35.1730266825
218PhosphorylationKDQPDGSSLSPAQSP
CCCCCCCCCCCCCCC		38.0930266825
219PhosphorylationDQPDGSSLSPAQSPS
CCCCCCCCCCCCCCC		8.3417081983
220PhosphorylationQPDGSSLSPAQSPSQ
CCCCCCCCCCCCCCC		21.8223927012
223PhosphorylationGSSLSPAQSPSQSQP
CCCCCCCCCCCCCCC		60.2917081983
224PhosphorylationSSLSPAQSPSQSQPP
CCCCCCCCCCCCCCC		28.7329255136
226PhosphorylationLSPAQSPSQSQPPAA
CCCCCCCCCCCCCCH		47.9430266825
228PhosphorylationPAQSPSQSQPPAASS
CCCCCCCCCCCCHHH		49.3330266825
234PhosphorylationQSQPPAASSLREPGL
CCCCCCHHHCCCCCC		31.8224732914
235PhosphorylationSQPPAASSLREPGLE
CCCCCHHHCCCCCCC		27.0724732914
243PhosphorylationLREPGLESKEEESAM
CCCCCCCCHHHHHHH		50.8723927012
251PhosphorylationKEEESAMSSDRMDCG
HHHHHHHCCCCCCCC		28.8928674419
260AcetylationDRMDCGRKVRVESGY
CCCCCCCEEEEECCC		21.4826051181
265PhosphorylationGRKVRVESGYFSLEK
CCEEEEECCCCCHHH		35.6221945579
267PhosphorylationKVRVESGYFSLEKTK
EEEEECCCCCHHHHH		10.1621945579
269PhosphorylationRVESGYFSLEKTKQD
EEECCCCCHHHHHHH		27.4321945579
273PhosphorylationGYFSLEKTKQDLKAE
CCCCHHHHHHHHHHH		25.2723312004
288PhosphorylationEQQLPPPLSPPSPST
HCCCCCCCCCCCCCC		17.2917081983
289PhosphorylationQQLPPPLSPPSPSTP
CCCCCCCCCCCCCCC		40.3029255136
291PhosphorylationLPPPLSPPSPSTPNH
CCCCCCCCCCCCCCC		56.3417081983
292PhosphorylationPPPLSPPSPSTPNHR
CCCCCCCCCCCCCCC		34.5629255136
294PhosphorylationPLSPPSPSTPNHRRS
CCCCCCCCCCCCCHH		61.9229255136
295PhosphorylationLSPPSPSTPNHRRSQ
CCCCCCCCCCCCHHH		31.3429255136
301PhosphorylationSTPNHRRSQVIEKFE
CCCCCCHHHHHHHHH		28.8423927012
306UbiquitinationRRSQVIEKFEALDIE
CHHHHHHHHHHCCHH		37.06-
3142-HydroxyisobutyrylationFEALDIEKAEHMETN
HHHCCHHHHHCCCCC		60.45-
320PhosphorylationEKAEHMETNAVGPSP
HHHHCCCCCCCCCCC		22.3924732914
326PhosphorylationETNAVGPSPSSDTRQ
CCCCCCCCCCCCCCC		31.3330266825
328PhosphorylationNAVGPSPSSDTRQGR
CCCCCCCCCCCCCCH		45.2230266825
329PhosphorylationAVGPSPSSDTRQGRS
CCCCCCCCCCCCCHH		46.5130266825
331PhosphorylationGPSPSSDTRQGRSEK
CCCCCCCCCCCHHCC		27.1730266825
336PhosphorylationSDTRQGRSEKRAFPR
CCCCCCHHCCCCCCC		55.0529759185
344UbiquitinationEKRAFPRKRDFTNEA
CCCCCCCCCCCCCCC		57.46-
344 (in isoform 3)Ubiquitination-57.4621890473
348PhosphorylationFPRKRDFTNEAPPAP
CCCCCCCCCCCCCCC		36.1229255136
352 (in isoform 3)Ubiquitination-21.2921890473
353 (in isoform 3)Ubiquitination-54.2621890473
358 (in isoform 3)Ubiquitination-61.9221890473
360PhosphorylationPAPLPDASASPLSPH
CCCCCCCCCCCCCHH		36.3429255136
362PhosphorylationPLPDASASPLSPHRR
CCCCCCCCCCCHHHC		24.7129255136
364PhosphorylationPDASASPLSPHRRAK
CCCCCCCCCHHHCHH		13.2517081983
365PhosphorylationDASASPLSPHRRAKS
CCCCCCCCHHHCHHC		23.2629255136
372PhosphorylationSPHRRAKSLDRRSTE
CHHHCHHCCCCCCCC		34.2225849741
377PhosphorylationAKSLDRRSTEPSVTP
HHCCCCCCCCCCCCH		37.7130266825
378PhosphorylationKSLDRRSTEPSVTPD
HCCCCCCCCCCCCHH		50.5330266825
381PhosphorylationDRRSTEPSVTPDLLN
CCCCCCCCCCHHHHH		32.1830266825
383PhosphorylationRSTEPSVTPDLLNFK
CCCCCCCCHHHHHCC		18.5430266825
3902-HydroxyisobutyrylationTPDLLNFKKGWLTKQ
CHHHHHCCCEEEEEE		49.67-
390UbiquitinationTPDLLNFKKGWLTKQ
CHHHHHCCCEEEEEE		49.67-
391UbiquitinationPDLLNFKKGWLTKQY
HHHHHCCCEEEEEEC		51.70-
396SuccinylationFKKGWLTKQYEDGQW
CCCEEEEEECCCCCE		49.0323954790
396UbiquitinationFKKGWLTKQYEDGQW
CCCEEEEEECCCCCE		49.03-
396 (in isoform 1)Ubiquitination-49.0321890473
396 (in isoform 2)Ubiquitination-49.0321890473
404UbiquitinationQYEDGQWKKHWFVLA
ECCCCCEEEEEEEEE		27.20-
450PhosphorylationEYPVQRNYGFQIHTK
CCCCEECCEEEEEEC		22.8528152594
464PhosphorylationKEGEFTLSAMTSGIR
CCCEEEHHHHCCCHH		16.9723403867
467PhosphorylationEFTLSAMTSGIRRNW
EEEHHHHCCCHHHHH		24.4223403867
468PhosphorylationFTLSAMTSGIRRNWI
EEHHHHCCCHHHHHH		21.0923403867
489 (in isoform 3)Ubiquitination-54.5921890473
491PhosphorylationPTTAPDVTSSLPEEK
CCCCCCCHHCCCCHH		21.7025159151
492PhosphorylationTTAPDVTSSLPEEKN
CCCCCCHHCCCCHHC		29.7125159151
493PhosphorylationTAPDVTSSLPEEKNK
CCCCCHHCCCCHHCC		38.2825159151
501PhosphorylationLPEEKNKSSCSFETC
CCCHHCCCCCCCCCC		46.0721712546
502PhosphorylationPEEKNKSSCSFETCP
CCHHCCCCCCCCCCC		18.5228555341
504PhosphorylationEKNKSSCSFETCPRP
HHCCCCCCCCCCCCC		28.2323898821
507PhosphorylationKSSCSFETCPRPTEK
CCCCCCCCCCCCCHH		26.2928102081
527UbiquitinationGEPDPEQKRSRARER
CCCCHHHHHHHHHHH		51.1621906983
527 (in isoform 1)Ubiquitination-51.1621890473
527 (in isoform 2)Ubiquitination-51.1621890473
540PhosphorylationERRREGRSKTFDWAE
HHHHHHHCCCCCHHH		47.0727273156
542PhosphorylationRREGRSKTFDWAEFR
HHHHHCCCCCHHHHH		28.2422167270
602PhosphorylationRFGMLDATDGPGTED
HHCCCCCCCCCCCHH		40.9520068231
618PhosphorylationALRMEVDRSPGLPMS
HHHCEECCCCCCCHH		50.3417081983
619PhosphorylationLRMEVDRSPGLPMSD
HHCEECCCCCCCHHH		20.8929255136
625PhosphorylationRSPGLPMSDLKTHNV
CCCCCCHHHHCCCEE		37.5425159151
645PhosphorylationQRWHQVETTPLREEK
HHHEECCCCCCCCCC		34.5523312004
646PhosphorylationRWHQVETTPLREEKQ
HHEECCCCCCCCCCC		13.5625159151
662PhosphorylationPIAPVHLSSEDGGDR
CCCCEECCCCCCCCC		19.4629255136
663PhosphorylationIAPVHLSSEDGGDRL
CCCEECCCCCCCCCC		46.1729255136
671PhosphorylationEDGGDRLSTHELTSL
CCCCCCCCHHHHHHH		28.7225849741
672PhosphorylationDGGDRLSTHELTSLL
CCCCCCCHHHHHHHH		24.7829255136
676PhosphorylationRLSTHELTSLLEKEL
CCCHHHHHHHHHHHH		17.8429255136
677PhosphorylationLSTHELTSLLEKELE
CCHHHHHHHHHHHHH		43.5129255136
681UbiquitinationELTSLLEKELEQSQK
HHHHHHHHHHHHHHH		68.51-
686PhosphorylationLEKELEQSQKEASDL
HHHHHHHHHHHHHHH		33.5728985074
688UbiquitinationKELEQSQKEASDLLE
HHHHHHHHHHHHHHH		61.57-
691PhosphorylationEQSQKEASDLLEQNR
HHHHHHHHHHHHHHH		29.8620068231
713PhosphorylationVALGREQSAREGYVL
HHHCCCCHHCCCEEH		25.25-
718PhosphorylationEQSAREGYVLQATCE
CCHHCCCEEHHHHHH		8.01-
731SulfoxidationCERGFAAMEETHQKK
HHHHCHHHHHHHHHH		4.2530846556
793PhosphorylationELEKSQRSQISSVNS
HHHHHHHHHHHHHHH		24.9920068231
796PhosphorylationKSQRSQISSVNSDVE
HHHHHHHHHHHHHHH		22.1620068231
797PhosphorylationSQRSQISSVNSDVEA
HHHHHHHHHHHHHHH		27.2626657352
800PhosphorylationSQISSVNSDVEALRR
HHHHHHHHHHHHHHH		40.6620068231
815PhosphorylationQYLEELQSVQRELEV
HHHHHHHHHHHHHHH		32.61-
878PhosphorylationAEITRLRTLLTGDGG
HHHHHHHHHHCCCCC		30.6123403867
881PhosphorylationTRLRTLLTGDGGGEA
HHHHHHHCCCCCCCC		36.0229255136
889PhosphorylationGDGGGEATGSPLAQG
CCCCCCCCCCCCCCC		33.6130266825
891PhosphorylationGGGEATGSPLAQGKD
CCCCCCCCCCCCCCC		16.6429255136
900PhosphorylationLAQGKDAYELEVLLR
CCCCCCEEEEEEEHH		31.0528064214
9092-HydroxyisobutyrylationLEVLLRVKESEIQYL
EEEEHHCCHHHHHHH		49.44-
915PhosphorylationVKESEIQYLKQEISS
CCHHHHHHHHHHHHH		22.8716674116
917UbiquitinationESEIQYLKQEISSLK
HHHHHHHHHHHHHHH		40.74-
921O-linked_GlycosylationQYLKQEISSLKDELQ
HHHHHHHHHHHHHHH		28.9430379171
921PhosphorylationQYLKQEISSLKDELQ
HHHHHHHHHHHHHHH		28.9416674116
936PhosphorylationTALRDKKYASDKYKD
HHHHHCHHCCHHHHH		19.6528152594
938PhosphorylationLRDKKYASDKYKDIY
HHHCHHCCHHHHHHH		31.3928152594
938 (in isoform 3)Ubiquitination-31.3921890473
9402-HydroxyisobutyrylationDKKYASDKYKDIYTE
HCHHCCHHHHHHHHH		52.27-
940 (in isoform 2)Malonylation-52.2732601280
941PhosphorylationKKYASDKYKDIYTEL
CHHCCHHHHHHHHHH		20.9128152594
945PhosphorylationSDKYKDIYTELSIAK
CHHHHHHHHHHHHHH		12.3328152594
946PhosphorylationDKYKDIYTELSIAKA
HHHHHHHHHHHHHHH		30.6828152594
949PhosphorylationKDIYTELSIAKAKAD
HHHHHHHHHHHHHCC		17.8028152594
970PhosphorylationKEQLKAATEALGEKS
HHHHHHHHHHHCCCC		27.0123927012
976UbiquitinationATEALGEKSPDSATV
HHHHHCCCCCCCCEE		66.542190698
976 (in isoform 1)Ubiquitination-66.5421890473
976 (in isoform 2)Ubiquitination-66.5421890473
976 (in isoform 3)Phosphorylation-66.5423927012
977PhosphorylationTEALGEKSPDSATVS
HHHHCCCCCCCCEEC		29.6329255136
978 (in isoform 3)Phosphorylation-51.1228355574
980PhosphorylationLGEKSPDSATVSGYD
HCCCCCCCCEECHHH		29.2630266825
982PhosphorylationEKSPDSATVSGYDIM
CCCCCCCEECHHHHH		21.1130266825
984PhosphorylationSPDSATVSGYDIMKS
CCCCCEECHHHHHHC		27.5530266825
984 (in isoform 3)Phosphorylation-27.5523927012
986PhosphorylationDSATVSGYDIMKSKS
CCCEECHHHHHHCCC		8.5230266825
990MethylationVSGYDIMKSKSNPDF
ECHHHHHHCCCCCCH		55.88115976729
991PhosphorylationSGYDIMKSKSNPDFL
CHHHHHHCCCCCCHH		24.7623927012
992MethylationGYDIMKSKSNPDFLK
HHHHHHCCCCCCHHH		49.05115976737
993PhosphorylationYDIMKSKSNPDFLKK
HHHHHCCCCCCHHHC		61.7629255136
1014PhosphorylationRQLRNIRSKSVIEQV
HHHHHHHCCHHHHHC		26.0323927012
1014 (in isoform 2)Phosphorylation-26.0323927012
1016PhosphorylationLRNIRSKSVIEQVSW
HHHHHCCHHHHHCCC		29.5825463755
1016 (in isoform 2)Phosphorylation-29.5828355574
1018 (in isoform 2)Ubiquitination-3.85-
1022PhosphorylationKSVIEQVSWDT----
CHHHHHCCCCC----		20.9423403867
1022 (in isoform 2)Phosphorylation-20.9423927012
1025PhosphorylationIEQVSWDT-------
HHHCCCCC-------		33.9623403867
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 MPRIP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPRIP_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 MPRIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP12C_HUMANPPP1R12Cphysical
15469989
1433T_HUMANYWHAQphysical
21988832
RGAP1_HUMANRACGAP1physical
21988832
PIAS4_HUMANPIAS4physical
21988832
YTDC1_HUMANYTHDC1physical
21988832
FTM_HUMANRPGRIP1Lphysical
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 MPRIP_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-289 AND THR-295, ANDMASS 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-220; SER-224; SER-226;SER-289; SER-292; SER-294; THR-295; SER-362; SER-365; SER-619; SER-891AND SER-977, 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 SER-891, AND MASSSPECTROMETRY.
"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 SER-365 AND SER-993, 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-619, AND MASSSPECTROMETRY.
"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-220; SER-224; SER-365;SER-619 AND SER-993, AND MASS SPECTROMETRY.

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