MPRIP_MOUSE - dbPTM
MPRIP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPRIP_MOUSE
UniProt AC P97434
Protein Name Myosin phosphatase Rho-interacting protein
Gene Name Mprip
Organism Mus musculus (Mouse).
Sequence Length 1024
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 MSAAKENPCRKFQANIFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPRTNKQNQKKKRKVEPPTPQEPGPAKMAVTSSSGGSSGSSSSIPSAEKVPTTKSTLWQEEMRAKDQPDGTSLSPAQSPSQSQPPAACTPREPGLESKEDESTISGDRVDGGRKVRVESGYFSLEKAKQDLRAEEQLPPLLSPPSPSTPHSRRSQVIEKFEALDIEKAEHMETNMLILTTPSSDTRQGRSERRAIPRKRDFASEAPTAPLSDACPLSPHRRAKSLDRRSTESSMTPDLLNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEINLSTCYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVLPASAPDVTSSLPEGKNKSTSFETCSRSTEKQEAEPGEPDPEQKKSRARERRREGRSKTFDWAEFRPIQQALAQERASAVGSSDSGDPGCLEAEPGELERERARRREERRKRFGMLDTIDGPGMEDTALRMDIDRSPGLLGTPDLKTQNVHVEIEQRWHQVETTPLREEKQVPIAPLHLSLEDRSERLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPEGTTVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSVIEQVSWDN
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
166PhosphorylationKRKVEPPTPQEPGPA
CCCCCCCCCCCCCCC		48.6026824392
185PhosphorylationTSSSGGSSGSSSSIP
ECCCCCCCCCCCCCC		46.0725338131
193PhosphorylationGSSSSIPSAEKVPTT
CCCCCCCCCCCCCCC		47.60-
202PhosphorylationEKVPTTKSTLWQEEM
CCCCCCCHHHHHHHH		27.0021183079
203PhosphorylationKVPTTKSTLWQEEMR
CCCCCCHHHHHHHHH		33.3021183079
218PhosphorylationAKDQPDGTSLSPAQS
HHCCCCCCCCCCCCC		33.6025168779
219PhosphorylationKDQPDGTSLSPAQSP
HCCCCCCCCCCCCCC		32.1727087446
221PhosphorylationQPDGTSLSPAQSPSQ
CCCCCCCCCCCCCCC		20.2525521595
225PhosphorylationTSLSPAQSPSQSQPP
CCCCCCCCCCCCCCC		28.7325521595
227PhosphorylationLSPAQSPSQSQPPAA
CCCCCCCCCCCCCCC		47.9421082442
229PhosphorylationPAQSPSQSQPPAACT
CCCCCCCCCCCCCCC		49.3325168779
236PhosphorylationSQPPAACTPREPGLE
CCCCCCCCCCCCCCC		22.2125619855
252PhosphorylationKEDESTISGDRVDGG
CCCCCCCCCCCCCCC		34.4322067460
266PhosphorylationGRKVRVESGYFSLEK
CCEEEEEECEEEHHH		35.6226824392
268PhosphorylationKVRVESGYFSLEKAK
EEEEEECEEEHHHHH		10.1629472430
270PhosphorylationRVESGYFSLEKAKQD
EEEECEEEHHHHHHH		27.4326824392
289PhosphorylationEQLPPLLSPPSPSTP
HHCCCCCCCCCCCCC		42.3125521595
292PhosphorylationPPLLSPPSPSTPHSR
CCCCCCCCCCCCCCH		34.5624925903
294PhosphorylationLLSPPSPSTPHSRRS
CCCCCCCCCCCCHHH		59.9324925903
295PhosphorylationLSPPSPSTPHSRRSQ
CCCCCCCCCCCHHHH		28.5324925903
298PhosphorylationPSPSTPHSRRSQVIE
CCCCCCCCHHHHHHH		30.5024925903
301PhosphorylationSTPHSRRSQVIEKFE
CCCCCHHHHHHHHHH		27.9126824392
320PhosphorylationEKAEHMETNMLILTT
HHHHCCCCCEEEEEC		20.5329895711
326PhosphorylationETNMLILTTPSSDTR
CCCEEEEECCCCCCC		29.6629895711
329PhosphorylationMLILTTPSSDTRQGR
EEEEECCCCCCCCCH		38.4629895711
350PhosphorylationPRKRDFASEAPTAPL
CCCCCCCCCCCCCCH		33.9925619855
354PhosphorylationDFASEAPTAPLSDAC
CCCCCCCCCCHHHCC		48.2127742792
358PhosphorylationEAPTAPLSDACPLSP
CCCCCCHHHCCCCCH		23.3127742792
364PhosphorylationLSDACPLSPHRRAKS
HHHCCCCCHHHCCCC		12.1027087446
371PhosphorylationSPHRRAKSLDRRSTE
CHHHCCCCCCCCCCC		34.2226824392
376PhosphorylationAKSLDRRSTESSMTP
CCCCCCCCCCCCCCH		37.1025263469
377PhosphorylationKSLDRRSTESSMTPD
CCCCCCCCCCCCCHH		37.7726643407
379PhosphorylationLDRRSTESSMTPDLL
CCCCCCCCCCCHHHH		26.0426643407
380PhosphorylationDRRSTESSMTPDLLN
CCCCCCCCCCHHHHH		22.0526643407
382PhosphorylationRSTESSMTPDLLNFK
CCCCCCCCHHHHHCC		18.6525777480
395UbiquitinationFKKGWLTKQYEDGQW
CCCEEEEEECCCCCE		49.03-
485PhosphorylationMKHVLPASAPDVTSS
HHHHCCCCCCCCHHC		38.0927087446
490PhosphorylationPASAPDVTSSLPEGK
CCCCCCCHHCCCCCC		21.7026824392
491PhosphorylationASAPDVTSSLPEGKN
CCCCCCHHCCCCCCC		29.7125777480
492PhosphorylationSAPDVTSSLPEGKNK
CCCCCHHCCCCCCCC		38.2825777480
502PhosphorylationEGKNKSTSFETCSRS
CCCCCCCCHHHCCCC		28.3322067460
538PhosphorylationERRREGRSKTFDWAE
HHHHHHHCCCCCHHH		47.0725177544
540PhosphorylationRREGRSKTFDWAEFR
HHHHHCCCCCHHHHH		28.2427087446
599PhosphorylationKRFGMLDTIDGPGME
HHHCCCCCCCCCCCC		19.60-
617PhosphorylationLRMDIDRSPGLLGTP
HHCCCCCCCCCCCCC		21.4125521595
623PhosphorylationRSPGLLGTPDLKTQN
CCCCCCCCCCCCCCC		17.3824068923
645PhosphorylationRWHQVETTPLREEKQ
HHEECCCCCCCCCCC		13.5625338131
661PhosphorylationPIAPLHLSLEDRSER
CCCCEECCHHHHHHH		20.9725521595
666PhosphorylationHLSLEDRSERLSTHE
ECCHHHHHHHCCHHH		39.1126160508
670PhosphorylationEDRSERLSTHELTSL
HHHHHHCCHHHHHHH		33.6621659605
671PhosphorylationDRSERLSTHELTSLL
HHHHHCCHHHHHHHH		24.7821659605
690PhosphorylationEQSQKEASDLLEQNR
HHHHHHHHHHHHHHH		29.8620531401
775AcetylationISAIEAMKNAHREEM
HHHHHHHHHHCHHHH		59.0122826441
792PhosphorylationELEKSQRSQISSINS
HHHHHHHHHHHHHHH		24.9922871156
795PhosphorylationKSQRSQISSINSDIE
HHHHHHHHHHHHHHH		19.9622871156
799PhosphorylationSQISSINSDIEALRR
HHHHHHHHHHHHHHH		37.99-
944PhosphorylationSDKYKDIYTELSIAK
CHHHHHHHHHHHHHH		12.3318563927
969PhosphorylationKEQLKAATEALGEKS
HHHHHHHHHHHCCCC		27.0126239621
976PhosphorylationTEALGEKSPEGTTVS
HHHHCCCCCCCCEEC		24.7125521595
977 (in isoform 3)Phosphorylation-55.9225266776
979 (in isoform 3)Phosphorylation-30.0327149854
980PhosphorylationGEKSPEGTTVSGYDI
CCCCCCCCEECHHHH		23.5124068923
981PhosphorylationEKSPEGTTVSGYDIM
CCCCCCCEECHHHHH		24.4324068923
983PhosphorylationSPEGTTVSGYDIMKS
CCCCCEECHHHHHCC		29.5524068923
985PhosphorylationEGTTVSGYDIMKSKS
CCCEECHHHHHCCCC		8.5224925903
985 (in isoform 3)Phosphorylation-8.5225777480
990PhosphorylationSGYDIMKSKSNPDFL
CHHHHHCCCCCCCHH		24.7624925903
992PhosphorylationYDIMKSKSNPDFLKK
HHHHCCCCCCCHHHC		61.7624925903
1013 (in isoform 2)Phosphorylation-26.0325266776
1013PhosphorylationRQLRNIRSKSVIEQV
HHHHHHHCCHHHHHC		26.0327087446
1015 (in isoform 2)Phosphorylation-29.5827149854
1015PhosphorylationLRNIRSKSVIEQVSW
HHHHHCCHHHHHCCC		29.5825521595
1021 (in isoform 2)Phosphorylation-28.5425777480
1021PhosphorylationKSVIEQVSWDN----
CHHHHHCCCCC----		28.5425619855
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPRIP_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UACA_HUMANUACAphysical
20360068
CDK1_HUMANCDK1physical
20360068
RAI14_HUMANRAI14physical
20360068
MPRIP_HUMANMPRIPphysical
20360068
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPRIP_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-364; SER-1013AND SER-1015, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1015, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND MASSSPECTROMETRY.

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