PARD3_MOUSE - dbPTM
PARD3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARD3_MOUSE
UniProt AC Q99NH2
Protein Name Partitioning defective 3 homolog
Gene Name Pard3
Organism Mus musculus (Mouse).
Sequence Length 1333
Subcellular Localization Cytoplasm. Endomembrane system. Cell junction. Cell junction, tight junction . Cell junction, adherens junction . Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell membrane. Localized along the cell-cell contact region. Colocalizes with PARD6A an
Protein Description Adapter protein involved in asymmetrical cell division and cell polarization processes (By similarity). Seems to play a central role in the formation of epithelial tight junctions (By similarity). Targets the phosphatase PTEN to cell junctions (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. [PubMed: 11839275 The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (By similarity Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (By similarity Involved in Schwann cell peripheral myelination]
Protein Sequence MKVTVCFGRTRVVVPCGDGRMKVFSLIQQAVTRYRKAVAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRLVAVFDEQDPHHGGDGTSASFTGTQSPEIFGSELGTNNVSAFQPYQATSEIEVTPSVLRANMPLHVRRSSDPALTGLSTSVSDNNFSSEEPSRKNPTRWSTTAGFLKQNTAGSPKTCDRKKDENYRSLPRDPSSWSNQFQRDNARSSLSASHPMVDRWLEKQEQDEEGTEEDSSRVEPVGHADTGLENMPNFSLDDMVKLVQVPNDGGPLGIHVVPFSARGGRTLGLLVKRLEKGGKAEQENLFHENDCIVRINDGDLRNRRFEQAQHMFRQAMRARVIWFHVVPAANKEQYEQLSQREKNNYSPGRFSPDSHCVANRSVANNAPQALPRAPRLSQPPEQLDAHPRLPHSAHASTKPPAAPALAPPSVLSTNVGSVYNTKKVGKRLNIQLKKGTEGLGFSITSRDVTIGGSAPIYVKNILPRGAAIQDGRLKAGDRLIEVNGVDLAGKSQEEVVSLLRSTKMEGTVSLLVFRQEEAFHPREMNAEPSQMQTPKETKAEDEDVVLTPDGTREFLTFEVPLNDSGSAGLGVSVKGNRSKENHADLGIFVKSIINGGAASKDGRLRVNDQLIAVNGESLLGKANQEAMETLRRSMSTEGNKRGMIQLIVARRISRCNELRSPGSPAAPELPIETELDDRERRISHSLYSGIEGLDESPTRNAALSRIMGKCQLSPTVNMPHDDTVMIEDDRLPVLPPHLSDQSSSSSHDDVGFIMTEAGTWAKATISDSADCSLSPDVDPVLAFQREGFGRQSMSEKRTKQFSDASQLDFVKTRKSKSMDLVADETKLNTVDDQRAGSPSRDVGPSLGLKKSSSLESLQTAVAEVTLNGNIPFHRPRPRIIRGRGCNESFRAAIDKSYDKPMVDDDDEGMETLEEDTEESSRSGRESVSTSSDQPSYSLERQMNGDPEKRDKTERKKDKAGKDKKKDREKEKDKLKAKKGMLKGLGDMFRFGKHRKDDKMEKMGRIKIQDSFTSEEDRVRMKEEQERIQAKTREFRERQARERDYAEIQDFHRTFGCDDELLYGGMSSYEGCLALNARPQSPREGHLMDTLYAQVKKPRSSKPGDSNRSTPSNHDRIQRLRQEFQQAKQDEDVEDRRRTYSFEQSWSSSRPASQSGRHSVSVEVQVQRQRQEERESFQQAQRQYSSLPRQSRKNASSISQDSWEQNYAPGEGFQSAKENPRYSSYQGSRNGYLGGHGFNARVMLETQELLRQEQRRKEQQLKKQPPADGVRGPFRQDVPPSPSQVARLNRLQTPEKGRPFYS
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
25PhosphorylationDGRMKVFSLIQQAVT
CCHHHHHHHHHHHHH
27.7926643407
44PhosphorylationAVAKDPNYWIQVHRL
HHHCCCCEEEEEEEC
14.8529514104
91PhosphorylationPHHGGDGTSASFTGT
CCCCCCCCCCCCCCC
26.34-
143PhosphorylationMPLHVRRSSDPALTG
CCEEEECCCCCCHHC
28.6425521595
144PhosphorylationPLHVRRSSDPALTGL
CEEEECCCCCCHHCC
45.8925521595
149PhosphorylationRSSDPALTGLSTSVS
CCCCCCHHCCCCCCC
37.8827087446
152PhosphorylationDPALTGLSTSVSDNN
CCCHHCCCCCCCCCC
21.7125619855
153PhosphorylationPALTGLSTSVSDNNF
CCHHCCCCCCCCCCC
37.8825619855
154PhosphorylationALTGLSTSVSDNNFS
CHHCCCCCCCCCCCC
19.0925619855
156PhosphorylationTGLSTSVSDNNFSSE
HCCCCCCCCCCCCCC
34.0925521595
161PhosphorylationSVSDNNFSSEEPSRK
CCCCCCCCCCCCCCC
38.6825619855
162PhosphorylationVSDNNFSSEEPSRKN
CCCCCCCCCCCCCCC
41.6725619855
166PhosphorylationNFSSEEPSRKNPTRW
CCCCCCCCCCCCCCC
60.2025619855
171PhosphorylationEPSRKNPTRWSTTAG
CCCCCCCCCCCCHHH
54.9122324799
174PhosphorylationRKNPTRWSTTAGFLK
CCCCCCCCCHHHHHH
16.7626824392
175PhosphorylationKNPTRWSTTAGFLKQ
CCCCCCCCHHHHHHH
17.4426160508
176PhosphorylationNPTRWSTTAGFLKQN
CCCCCCCHHHHHHHC
21.1926239621
181UbiquitinationSTTAGFLKQNTAGSP
CCHHHHHHHCCCCCC
38.96-
187PhosphorylationLKQNTAGSPKTCDRK
HHHCCCCCCCCCCCC
22.2822324799
199PhosphorylationDRKKDENYRSLPRDP
CCCCCCCCCCCCCCC
10.2629550500
201PhosphorylationKKDENYRSLPRDPSS
CCCCCCCCCCCCCCH
32.1626824392
207PhosphorylationRSLPRDPSSWSNQFQ
CCCCCCCCHHHHHHH
49.0526160508
208PhosphorylationSLPRDPSSWSNQFQR
CCCCCCCHHHHHHHH
39.6526160508
210PhosphorylationPRDPSSWSNQFQRDN
CCCCCHHHHHHHHHC
23.7726643407
220PhosphorylationFQRDNARSSLSASHP
HHHHCHHHHHHHCCH
32.9722942356
221PhosphorylationQRDNARSSLSASHPM
HHHCHHHHHHHCCHH
22.3125521595
223PhosphorylationDNARSSLSASHPMVD
HCHHHHHHHCCHHHH
29.6725168779
225PhosphorylationARSSLSASHPMVDRW
HHHHHHHCCHHHHHH
25.4226239621
235UbiquitinationMVDRWLEKQEQDEEG
HHHHHHHHHHHCCCC
57.89-
377PhosphorylationSQREKNNYSPGRFSP
HHHHHHCCCCCCCCC
26.1526160508
378PhosphorylationQREKNNYSPGRFSPD
HHHHHCCCCCCCCCC
24.0127087446
383PhosphorylationNYSPGRFSPDSHCVA
CCCCCCCCCCCCCCC
26.8327087446
386PhosphorylationPGRFSPDSHCVANRS
CCCCCCCCCCCCCHH
23.3626643407
393PhosphorylationSHCVANRSVANNAPQ
CCCCCCHHHHCCCCC
25.9528066266
449PhosphorylationVLSTNVGSVYNTKKV
HHCCCCCCEECCCCH
19.6929514104
474PhosphorylationGTEGLGFSITSRDVT
CCCCCCEEEEECCEE
24.1425338131
481PhosphorylationSITSRDVTIGGSAPI
EEEECCEEECCCCCE
20.4228066266
485PhosphorylationRDVTIGGSAPIYVKN
CCEEECCCCCEEEEE
26.1728066266
489PhosphorylationIGGSAPIYVKNILPR
ECCCCCEEEEECCCC
12.3322499769
567UbiquitinationPSQMQTPKETKAEDE
HHHCCCCCCCCCCCC
79.84-
579PhosphorylationEDEDVVLTPDGTREF
CCCCEEECCCCCCEE
14.0225521595
583PhosphorylationVVLTPDGTREFLTFE
EEECCCCCCEEEEEE
34.1125619855
611UbiquitinationSVKGNRSKENHADLG
EEECCCCCCCCCCCE
60.34-
622AcetylationADLGIFVKSIINGGA
CCCEEEEHHHHCCCC
25.7815613441
632UbiquitinationINGGAASKDGRLRVN
HCCCCCCCCCCCEEC
60.52-
661PhosphorylationANQEAMETLRRSMST
HHHHHHHHHHHHHCC
16.6926643407
665PhosphorylationAMETLRRSMSTEGNK
HHHHHHHHHCCCCCH
15.6226643407
667PhosphorylationETLRRSMSTEGNKRG
HHHHHHHCCCCCHHH
25.2626643407
668PhosphorylationTLRRSMSTEGNKRGM
HHHHHHCCCCCHHHH
38.9926643407
673DimethylationMSTEGNKRGMIQLIV
HCCCCCHHHHHHHHH
43.86-
673MethylationMSTEGNKRGMIQLIV
HCCCCCHHHHHHHHH
43.8618965593
682DimethylationMIQLIVARRISRCNE
HHHHHHHHHHHHCHH
26.10-
682MethylationMIQLIVARRISRCNE
HHHHHHHHHHHHCHH
26.1018965603
692PhosphorylationSRCNELRSPGSPAAP
HHCHHCCCCCCCCCC
46.3625619855
695PhosphorylationNELRSPGSPAAPELP
HHCCCCCCCCCCCCC
18.1026824392
705PhosphorylationAPELPIETELDDRER
CCCCCCCEECCHHHH
42.4425619855
714PhosphorylationLDDRERRISHSLYSG
CCHHHHHHHHHHHHC
5.64-
715PhosphorylationDDRERRISHSLYSGI
CHHHHHHHHHHHHCC
12.7625521595
717PhosphorylationRERRISHSLYSGIEG
HHHHHHHHHHHCCCC
23.3921082442
719PhosphorylationRRISHSLYSGIEGLD
HHHHHHHHHCCCCCC
14.1018515860
720PhosphorylationRISHSLYSGIEGLDE
HHHHHHHHCCCCCCC
38.2926239621
724UbiquitinationSLYSGIEGLDESPTR
HHHHCCCCCCCCCCH
36.19-
728PhosphorylationGIEGLDESPTRNAAL
CCCCCCCCCCHHHHH
31.1025521595
728 (in isoform 3)Phosphorylation-31.1030352176
730PhosphorylationEGLDESPTRNAALSR
CCCCCCCCHHHHHHH
45.9226239621
806PhosphorylationDSADCSLSPDVDPVL
CCCCCCCCCCCCHHH
11.6229899451
824PhosphorylationREGFGRQSMSEKRTK
CCCCCCCCCCHHHHH
23.9426824392
826PhosphorylationGFGRQSMSEKRTKQF
CCCCCCCCHHHHHCC
45.2526643407
830PhosphorylationQSMSEKRTKQFSDAS
CCCCHHHHHCCCCHH
40.0218267089
831AcetylationSMSEKRTKQFSDASQ
CCCHHHHHCCCCHHH
54.0721949390
831UbiquitinationSMSEKRTKQFSDASQ
CCCHHHHHCCCCHHH
54.07-
834PhosphorylationEKRTKQFSDASQLDF
HHHHHCCCCHHHCHH
29.7626643407
837PhosphorylationTKQFSDASQLDFVKT
HHCCCCHHHCHHHHC
35.9528066266
843UbiquitinationASQLDFVKTRKSKSM
HHHCHHHHCCCCCCC
42.48-
848AcetylationFVKTRKSKSMDLVAD
HHHCCCCCCCCCEEC
53.4821949390
849PhosphorylationVKTRKSKSMDLVADE
HHCCCCCCCCCEECC
25.3128066266
861PhosphorylationADETKLNTVDDQRAG
ECCCCCCCCCCCCCC
35.4320469934
869PhosphorylationVDDQRAGSPSRDVGP
CCCCCCCCCCCCCCH
20.7926824392
871PhosphorylationDQRAGSPSRDVGPSL
CCCCCCCCCCCCHHC
42.6920469934
877PhosphorylationPSRDVGPSLGLKKSS
CCCCCCHHCCCCCCC
29.1927149854
881AcetylationVGPSLGLKKSSSLES
CCHHCCCCCCCCHHH
49.1321949390
883PhosphorylationPSLGLKKSSSLESLQ
HHCCCCCCCCHHHHH
24.4621082442
884PhosphorylationSLGLKKSSSLESLQT
HCCCCCCCCHHHHHH
48.0721183079
885PhosphorylationLGLKKSSSLESLQTA
CCCCCCCCHHHHHHH
43.1621082442
888PhosphorylationKKSSSLESLQTAVAE
CCCCCHHHHHHHEEE
30.9422817900
891PhosphorylationSSLESLQTAVAEVTL
CCHHHHHHHEEEECC
28.5217242355
920PhosphorylationRGRGCNESFRAAIDK
CCCCCCHHHHHHHCC
13.1727087446
928PhosphorylationFRAAIDKSYDKPMVD
HHHHHCCCCCCCCCC
34.5122817900
929PhosphorylationRAAIDKSYDKPMVDD
HHHHCCCCCCCCCCC
33.4522817900
943PhosphorylationDDDEGMETLEEDTEE
CCCCCCCCHHHHCHH
30.4929899451
954PhosphorylationDTEESSRSGRESVST
HCHHHHHCCCCCCCC
44.1225619855
958PhosphorylationSSRSGRESVSTSSDQ
HHHCCCCCCCCCCCC
21.7325619855
960PhosphorylationRSGRESVSTSSDQPS
HCCCCCCCCCCCCCC
31.6725619855
961PhosphorylationSGRESVSTSSDQPSY
CCCCCCCCCCCCCCC
30.0525619855
962PhosphorylationGRESVSTSSDQPSYS
CCCCCCCCCCCCCCC
25.1425619855
963PhosphorylationRESVSTSSDQPSYSL
CCCCCCCCCCCCCCH
40.1125619855
967PhosphorylationSTSSDQPSYSLERQM
CCCCCCCCCCHHHHH
23.0128066266
969PhosphorylationSSDQPSYSLERQMNG
CCCCCCCCHHHHHCC
28.2626824392
1042PhosphorylationGRIKIQDSFTSEEDR
CCEEECCCCCCHHHH
17.6626824392
1044PhosphorylationIKIQDSFTSEEDRVR
EEECCCCCCHHHHHH
38.9028066266
1045PhosphorylationKIQDSFTSEEDRVRM
EECCCCCCHHHHHHH
36.6628066266
1076PhosphorylationRQARERDYAEIQDFH
HHHHHHCHHHHHHHH
16.6226824392
1085PhosphorylationEIQDFHRTFGCDDEL
HHHHHHHHHCCCCCC
18.7927087446
1112PhosphorylationALNARPQSPREGHLM
HHCCCCCCCCCCCCH
28.7127087446
1121PhosphorylationREGHLMDTLYAQVKK
CCCCCHHHHHHHCCC
14.0122499769
1123PhosphorylationGHLMDTLYAQVKKPR
CCCHHHHHHHCCCCC
9.3320116462
1170PhosphorylationDVEDRRRTYSFEQSW
CHHHHHHHCCHHHHH
23.0023984901
1171PhosphorylationVEDRRRTYSFEQSWS
HHHHHHHCCHHHHHC
15.0026643407
1172PhosphorylationEDRRRTYSFEQSWSS
HHHHHHCCHHHHHCC
22.9929514104
1176PhosphorylationRTYSFEQSWSSSRPA
HHCCHHHHHCCCCCC
23.0226643407
1178PhosphorylationYSFEQSWSSSRPASQ
CCHHHHHCCCCCCCC
24.5526643407
1179PhosphorylationSFEQSWSSSRPASQS
CHHHHHCCCCCCCCC
24.9026643407
1180PhosphorylationFEQSWSSSRPASQSG
HHHHHCCCCCCCCCC
36.4526643407
1184PhosphorylationWSSSRPASQSGRHSV
HCCCCCCCCCCCCCE
27.8026643407
1186PhosphorylationSSRPASQSGRHSVSV
CCCCCCCCCCCCEEE
34.9926643407
1190PhosphorylationASQSGRHSVSVEVQV
CCCCCCCCEEEEHHH
18.0926370283
1207PhosphorylationQRQEERESFQQAQRQ
HHHHHHHHHHHHHHH
34.2826824392
1215PhosphorylationFQQAQRQYSSLPRQS
HHHHHHHHHCCCHHH
11.4722499769
1216PhosphorylationQQAQRQYSSLPRQSR
HHHHHHHHCCCHHHH
19.6322499769
1217PhosphorylationQAQRQYSSLPRQSRK
HHHHHHHCCCHHHHC
37.1422499769
1222PhosphorylationYSSLPRQSRKNASSI
HHCCCHHHHCCCCCC
46.6429514104
1227PhosphorylationRQSRKNASSISQDSW
HHHHCCCCCCCCCHH
37.2823984901
1228PhosphorylationQSRKNASSISQDSWE
HHHCCCCCCCCCHHH
24.6926643407
1230PhosphorylationRKNASSISQDSWEQN
HCCCCCCCCCHHHHH
29.8623984901
1233PhosphorylationASSISQDSWEQNYAP
CCCCCCCHHHHHCCC
25.5223984901
1238PhosphorylationQDSWEQNYAPGEGFQ
CCHHHHHCCCCCCCC
17.5422817900
1255PhosphorylationKENPRYSSYQGSRNG
CCCCCCCCCCCCCCC
16.7325521595
1256PhosphorylationENPRYSSYQGSRNGY
CCCCCCCCCCCCCCC
15.7929514104
1263PhosphorylationYQGSRNGYLGGHGFN
CCCCCCCCCCCCCCC
13.0129514104
1312PhosphorylationFRQDVPPSPSQVARL
CCCCCCCCHHHHHHH
30.9826239621
1314PhosphorylationQDVPPSPSQVARLNR
CCCCCCHHHHHHHHC
41.4425619855
1324PhosphorylationARLNRLQTPEKGRPF
HHHHCCCCCCCCCCC
37.7025338131
1327AcetylationNRLQTPEKGRPFYS-
HCCCCCCCCCCCCC-
62.5121949390
1333PhosphorylationEKGRPFYS-------
CCCCCCCC-------
33.84-

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
830TPhosphorylationKinaseROCK1P70335
PSP
958SPhosphorylationKinaseAURKAP97477
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
824SPhosphorylation

-
958SPhosphorylation

-

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 PARD3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JAM1_HUMANF11Rphysical
11447115
PAR6A_MOUSEPard6aphysical
16510873

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PARD3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-383 AND SER-728, ANDMASS SPECTROMETRY.
"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-144 AND SER-717, ANDMASS SPECTROMETRY.

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