STRN3_MOUSE - dbPTM
STRN3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRN3_MOUSE
UniProt AC Q9ERG2
Protein Name Striatin-3
Gene Name Strn3
Organism Mus musculus (Mouse).
Sequence Length 796
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
Protein Description Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein (By similarity)..
Protein Sequence MDELAGGGGGGQGMAAPPRPQQGPGGNLSLPPGANGAPGGGGPPAAEAAGPPAGPELSRPQQYTIPGILHYIQHEWARFEMERAHWEVERAELQARIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDLKMPTFESEETKDVEAPPAPQNSQLTWKQGRQLLRQYLQEVGYTDTILDVRSQRVRSLLGLSNSEPNGSVEAKNLEQILNGGESPKQKGQEIKRPPGDVLETFNFLENADDSDEEENDMIEGIPEGKDKLRIHKHKIGNEGLAADLTDDPDTEEALKEFDFLVTAEDGEGAGEARSSGDGTEWDKDDLSPTAEVWDVDQGLISKLKEQYKKERKGKKGVKRVNRTNLCDMITDLGDDELPHIPSGIINQSRSASTRMADHEGARAEEAEPITFPSGGGKSFIMGSDDVLLSVLGLGDLADLTVTNDADYSYDLPANKDAFRKTWNPKYTLRSHFDGVRALAFHPVEPVLVTASEDHTLKLWNLQKTVPAKKSASLDVEPIYTFRAHIGPVLSLAISSNGEQCFSGGIDATIQWWNMPSPNVDPYDTYESNVLAGTLVAHTDAVWGLAYSGIKNQLLSCSADGTIRLWNPQEKLPCVCTYNGDKEHGIPTSVDFIGCDPAHMVTSFNTGSAVIYDLETSQSLVMLSSQVDSGLQSSNHINRVVSHPTLPVTITAHEDRHIKFFDNKTGKMIHSMVAHLDAVTSLAVDPNGIYLMSGSHDCSIRLWNLDSKTCVQEITAHRKKLDESIYDVAFHPSKAYIASAGADALAKVFV
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
1Acetylation-------MDELAGGG
-------CCCCCCCC		9.01-
150PhosphorylationQGDLKMPTFESEETK
CCCCCCCCCCCCCCC		36.2128464351
153PhosphorylationLKMPTFESEETKDVE
CCCCCCCCCCCCCCC		36.2225521595
168PhosphorylationAPPAPQNSQLTWKQG
CCCCCCCCCCCHHHH		22.7125619855
171PhosphorylationAPQNSQLTWKQGRQL
CCCCCCCCHHHHHHH		23.9925619855
173UbiquitinationQNSQLTWKQGRQLLR
CCCCCCHHHHHHHHH		37.3222790023
191PhosphorylationQEVGYTDTILDVRSQ
HHHCCCCHHHHHHHH		18.6825338131
202PhosphorylationVRSQRVRSLLGLSNS
HHHHHHHHHHCCCCC		25.7026824392
207PhosphorylationVRSLLGLSNSEPNGS
HHHHHCCCCCCCCCC		36.1922817900
209PhosphorylationSLLGLSNSEPNGSVE
HHHCCCCCCCCCCCE		51.5622817900
214PhosphorylationSNSEPNGSVEAKNLE
CCCCCCCCCEECCHH		24.3525521595
229PhosphorylationQILNGGESPKQKGQE
HHHCCCCCHHHCCCC		40.4424925903
247PhosphorylationPPGDVLETFNFLENA
CCCCHHHHHCHHHCC		21.5125619855
257PhosphorylationFLENADDSDEEENDM
HHHCCCCCCHHHHCH		47.6824925903
292PhosphorylationEGLAADLTDDPDTEE
CCCCCCCCCCCCHHH		38.6126525534
297PhosphorylationDLTDDPDTEEALKEF
CCCCCCCHHHHHHHC		40.9029899451
321PhosphorylationEGAGEARSSGDGTEW
CCCCCCCCCCCCCCC		45.8024925903
322PhosphorylationGAGEARSSGDGTEWD
CCCCCCCCCCCCCCC		35.0423984901
326PhosphorylationARSSGDGTEWDKDDL
CCCCCCCCCCCHHHC		38.3523984901
334PhosphorylationEWDKDDLSPTAEVWD
CCCHHHCCCCCEEEE		27.4825521595
336PhosphorylationDKDDLSPTAEVWDVD
CHHHCCCCCEEEECC		31.8825521595
474PhosphorylationKTWNPKYTLRSHFDG
HHCCCCCCHHHHCCC		23.0927600695
517PhosphorylationKTVPAKKSASLDVEP
CCCCCCCCCCCCCEE		23.5324759943
519PhosphorylationVPAKKSASLDVEPIY
CCCCCCCCCCCEEEE		31.9929514104
526PhosphorylationSLDVEPIYTFRAHIG
CCCCEEEEEEEECHH		15.5618563927
717PhosphorylationKTGKMIHSMVAHLDA
CCCHHHHHHHHHHHH		12.20-
726PhosphorylationVAHLDAVTSLAVDPN
HHHHHHHHEEEECCC		21.53-
727PhosphorylationAHLDAVTSLAVDPNG
HHHHHHHEEEECCCC		14.03-
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 STRN3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRN3_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 STRN3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
C1QBP_HUMANC1QBPphysical
26496610
TCPZ_HUMANCCT6Aphysical
26496610
CLH1_HUMANCLTCphysical
26496610
IMA1_HUMANKPNA2physical
26496610
MYO1C_HUMANMYO1Cphysical
26496610
PP2AA_HUMANPPP2CAphysical
26496610
PP2AB_HUMANPPP2CBphysical
26496610
2AAA_HUMANPPP2R1Aphysical
26496610
2AAB_HUMANPPP2R1Bphysical
26496610
S10A4_HUMANS100A4physical
26496610
STRN_HUMANSTRNphysical
26496610
TCPA_HUMANTCP1physical
26496610
TKT_HUMANTKTphysical
26496610
TCPG_HUMANCCT3physical
26496610
SLMAP_HUMANSLMAPphysical
26496610
NCOA3_HUMANNCOA3physical
26496610
STK24_HUMANSTK24physical
26496610
ARK72_HUMANAKR7A2physical
26496610
ARPC3_HUMANARPC3physical
26496610
TCPH_HUMANCCT7physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPB_HUMANCCT2physical
26496610
TCPQ_HUMANCCT8physical
26496610
S27A4_HUMANSLC27A4physical
26496610
PDC10_HUMANPDCD10physical
26496610
RRAS2_HUMANRRAS2physical
26496610
TCPE_HUMANCCT5physical
26496610
RIMS1_HUMANRIMS1physical
26496610
PHOCN_HUMANMOB4physical
26496610
FGOP2_HUMANFGFR1OP2physical
26496610
STRN4_HUMANSTRN4physical
26496610
TAF9B_HUMANTAF9Bphysical
26496610
STK26_HUMANSTK26physical
26496610
PALMD_HUMANPALMDphysical
26496610
PINX1_HUMANPINX1physical
26496610
CT2NL_HUMANCTTNBP2NLphysical
26496610
STRP2_HUMANSTRIP2physical
26496610
K1522_HUMANKIAA1522physical
26496610
SIKE1_HUMANSIKE1physical
26496610
ARP5L_HUMANARPC5Lphysical
26496610
STRP1_HUMANSTRIP1physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STRN3_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-229 AND SER-257, ANDMASS SPECTROMETRY.
"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-257, AND MASSSPECTROMETRY.

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