PRIC2_MOUSE - dbPTM
PRIC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRIC2_MOUSE
UniProt AC Q80Y24
Protein Name Prickle-like protein 2
Gene Name Prickle2
Organism Mus musculus (Mouse).
Sequence Length 845
Subcellular Localization Nucleus membrane .
Protein Description
Protein Sequence MVTVMPLEMEKTISKLMFDFQRSSTSDDDSGCALEEYAWVPPGLKPEQVHQYYSCLPEEKVPYVNSAGEKLRIKQLLHQLPPHDNEVRYCNSLDEEEKRELKLFSNQRKRENLGRGNVRPFPVTMTGAICEQCGGQIKGGDIAVFASRAGHGICWHPPCFVCTVCNELLVDLIYFYQDGKIYCGRHHAECLKPRCAACDEIIFADECTEAEGRHWHMRHFCCFECETVLGGQRYIMKEGRPYCCHCFESLYAEYCDTCAQHIGIDQGQMTYDGQHWHATETCFCCAHCKKSLLGRPFLPKQGQIFCSRACSAGEDPNGSDSSDSAFQNARAKESRRSAKIGKNKGKTEEAMLNQHSQLQVSSNRLSADVDPLSVQMDLLSLSSQTPSLNRDPIWRSREEPFHYGNKMEQNQSQSPLQLLSQCNIRTSYSPGGQGAGAQPDMWAKHFSNPKRSSSMALKGHGGSFIQECREDYYPGRLMSQESYSDMSSQSFNETRGSIPVPKYEEEEEEEEGGISTQQCRPRRPLSSLKYTEDMTPTEQTPRGSMESLALSNATGLSAEGGAKRQEHLSRFSMPDLSKDSGMNVSEKLSNMGTLNSSMQFRSAESVRSLLSAQQYQEMEGNLHQLSNPLGYRDLQSHGRMHQSFDFDGGIASSKLPGQEGVHIQPMSERTRRRTTSRDDNRRFRPHRSRRSRRSRSDNALHLASEREVIARLKERPPLRAREDYDQFMRQRSFQESLGQGSRRDLYSQCPRTVSDLALQNAFGERWGPYFTEYDWCSTCSSSSESDNEGYFLGEPIPQPARLRYVTSDELLHKYSSYGVPKSSTLGGRGQLHSRKRQKSKNCIIS
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
23PhosphorylationLMFDFQRSSTSDDDS
HHHHHHCCCCCCCCC		27.4719060867
24PhosphorylationMFDFQRSSTSDDDSG
HHHHHCCCCCCCCCC		33.8321082442
25PhosphorylationFDFQRSSTSDDDSGC
HHHHCCCCCCCCCCC		37.1022817900
26PhosphorylationDFQRSSTSDDDSGCA
HHHCCCCCCCCCCCE		40.7829899451
89PhosphorylationPHDNEVRYCNSLDEE
CCCCCCCCCCCCCHH		10.9329899451
92PhosphorylationNEVRYCNSLDEEEKR
CCCCCCCCCCHHHHH		33.3725521595
124PhosphorylationNVRPFPVTMTGAICE
CCCCCCCCEEHHHHH		14.8419060867
126PhosphorylationRPFPVTMTGAICEQC
CCCCCCEEHHHHHHC		17.6922817900
311PhosphorylationIFCSRACSAGEDPNG
EEEECCCCCCCCCCC		38.0222324799
319PhosphorylationAGEDPNGSDSSDSAF
CCCCCCCCCCCCHHH		40.7425521595
321PhosphorylationEDPNGSDSSDSAFQN
CCCCCCCCCCHHHHH		37.4322324799
322PhosphorylationDPNGSDSSDSAFQNA
CCCCCCCCCHHHHHH		40.3422324799
324PhosphorylationNGSDSSDSAFQNARA
CCCCCCCHHHHHHHH		32.6929899451
337PhosphorylationRAKESRRSAKIGKNK
HHHHHHHHHHCCCCC		32.57-
396PhosphorylationNRDPIWRSREEPFHY
CCCCCHHCCCCCCCC		29.1029899451
412PhosphorylationNKMEQNQSQSPLQLL
CCCCCCCCCCHHHHH		39.9320415495
414PhosphorylationMEQNQSQSPLQLLSQ
CCCCCCCCHHHHHHH		32.5925521595
453PhosphorylationFSNPKRSSSMALKGH
CCCCCCCCCCCCCCC		28.3229899451
454PhosphorylationSNPKRSSSMALKGHG
CCCCCCCCCCCCCCC		14.8829899451
463PhosphorylationALKGHGGSFIQECRE
CCCCCCCCHHHHHHH		24.6225521595
479PhosphorylationYYPGRLMSQESYSDM
CCCCCCCCCCCCCCC		35.0729899451
482PhosphorylationGRLMSQESYSDMSSQ
CCCCCCCCCCCCCCC		23.4629899451
483PhosphorylationRLMSQESYSDMSSQS
CCCCCCCCCCCCCCC		14.1329899451
526PhosphorylationCRPRRPLSSLKYTED
CCCCCCCCCCCCCCC		35.9926824392
527PhosphorylationRPRRPLSSLKYTEDM
CCCCCCCCCCCCCCC		36.2429472430
530PhosphorylationRPLSSLKYTEDMTPT
CCCCCCCCCCCCCCC		22.2123527152
535PhosphorylationLKYTEDMTPTEQTPR
CCCCCCCCCCCCCCC		39.1025521595
537PhosphorylationYTEDMTPTEQTPRGS
CCCCCCCCCCCCCCC		31.4022817900
540PhosphorylationDMTPTEQTPRGSMES
CCCCCCCCCCCCHHH		14.5525521595
544PhosphorylationTEQTPRGSMESLALS
CCCCCCCCHHHHHHH		22.2125521595
547PhosphorylationTPRGSMESLALSNAT
CCCCCHHHHHHHCCC		15.4225521595
551PhosphorylationSMESLALSNATGLSA
CHHHHHHHCCCCCCC		20.8629899451
557PhosphorylationLSNATGLSAEGGAKR
HHCCCCCCCCCCHHH		26.1422817900
569PhosphorylationAKRQEHLSRFSMPDL
HHHHHHHHHCCCCCC		32.9421183079
572PhosphorylationQEHLSRFSMPDLSKD
HHHHHHCCCCCCCCC		28.4426824392
597PhosphorylationNMGTLNSSMQFRSAE
CCCCCCCCCHHCCHH		18.6123527152
602PhosphorylationNSSMQFRSAESVRSL
CCCCHHCCHHHHHHH		37.3629899451
605PhosphorylationMQFRSAESVRSLLSA
CHHCCHHHHHHHHHH		23.6529899451
608PhosphorylationRSAESVRSLLSAQQY
CCHHHHHHHHHHHHH		31.3522817900
611PhosphorylationESVRSLLSAQQYQEM
HHHHHHHHHHHHHHH		29.3529899451
626PhosphorylationEGNLHQLSNPLGYRD
HCCHHHHCCCCCHHH		29.8129899451
631PhosphorylationQLSNPLGYRDLQSHG
HHCCCCCHHHHHHCC		14.5029899451
643PhosphorylationSHGRMHQSFDFDGGI
HCCCCCCEECCCCCE		16.4725521595
667PhosphorylationGVHIQPMSERTRRRT
CCCCCCCCHHHCCCC		30.5222324799
694PhosphorylationRSRRSRRSRSDNALH
CCHHCHHHHCCCHHH		34.7225619855
696PhosphorylationRRSRRSRSDNALHLA
HHCHHHHCCCHHHHH		36.1425521595
704PhosphorylationDNALHLASEREVIAR
CCHHHHHHHHHHHHH		43.4725619855
732PhosphorylationDQFMRQRSFQESLGQ
HHHHHHHHHHHHHCC		23.9625521595
741PhosphorylationQESLGQGSRRDLYSQ
HHHHCCCCHHHHHHH		19.0926824392
746PhosphorylationQGSRRDLYSQCPRTV
CCCHHHHHHHCCCHH		10.8629899451
752PhosphorylationLYSQCPRTVSDLALQ
HHHHCCCHHHHHHHH		14.9822324799
754PhosphorylationSQCPRTVSDLALQNA
HHCCCHHHHHHHHHH		26.7125521595
804PhosphorylationPQPARLRYVTSDELL
CCCCEEEEEEHHHHH		16.8125521595
806PhosphorylationPARLRYVTSDELLHK
CCEEEEEEHHHHHHH		22.8625521595
807PhosphorylationARLRYVTSDELLHKY
CEEEEEEHHHHHHHH		21.0225521595
814PhosphorylationSDELLHKYSSYGVPK
HHHHHHHHHHCCCCC		7.6629899451
842MethylationKRQKSKNCIIS----
CCCCCCCCCCC----		3.16-
842FarnesylationKRQKSKNCIIS----
CCCCCCCCCCC----		3.16-
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 PRIC2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRIC2_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 PRIC2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DVL1_MOUSEDvl1genetic
19788910
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRIC2_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-696 AND SER-807, ANDMASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-732, ANDMASS 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-92 AND SER-696, AND MASSSPECTROMETRY.

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