STRN3_HUMAN - dbPTM
STRN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRN3_HUMAN
UniProt AC Q13033
Protein Name Striatin-3
Gene Name STRN3
Organism Homo sapiens (Human).
Sequence Length 797
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
Protein Description Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein..
Protein Sequence MDELAGGGGGGPGMAAPPRQQQGPGGNLGLSPGGNGAAGGGGPPASEGAGPAAGPELSRPQQYTIPGILHYIQHEWARFEMERAHWEVERAELQARIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDLKMPTFESEETKDTEAPTAPQNSQLTWKQGRQLLRQYLQEVGYTDTILDVRSQRVRSLLGLSNSEPNGSVETKNLEQILNGGESPKQKGQEIKRSSGDVLETFNFLENADDSDEDEENDMIEGIPEGKDKHRMNKHKIGNEGLAADLTDDPDTEEALKEFDFLVTAEDGEGAGEARSSGDGTEWDKDDLSPTAEVWDVDQGLISKLKEQYKKERKGKKGVKRANRTKLYDMIADLGDDELPHIPSGIINQSRSASTRMTDHEGARAEEAEPITFPSGGGKSFIMGSDDVLLSVLGLGDLADLTVTNDADYSYDLPANKDAFRKTWNPKYTLRSHFDGVRALAFHPVEPVLVTASEDHTLKLWNLQKTVPAKKSASLDVEPIYTFRAHIGPVLSLAISSNGEQCFSGGIDATIQWWNMPSPSVDPYDTYEPNVLAGTLVGHTDAVWGLAYSGIKNQLLSCSADGTVRLWNPQEKLPCICTYNGDKKHGIPTSVDFIGCDPAHMVTSFNTGSAVIYDLETSQSLVILSSQVDSGLQSNNHINRVVSHPTLPVTITAHEDRHIKFFDNKTGKMIHSMVAHLDAVTSLAVDPNGIYLMSGSHDCSIRLWNLDSKTCVQEITAHRKKLDESIYDVAFHSSKAYIASAGADALAKVFV
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		9.0122223895
31PhosphorylationPGGNLGLSPGGNGAA
CCCCCCCCCCCCCCC		21.5025850435
46PhosphorylationGGGGPPASEGAGPAA
CCCCCCCCCCCCCCC		42.1925850435
111UbiquitinationRKGQENLKKDLVRRI
HHCHHHHHHHHHHHH		56.6824816145
126UbiquitinationKMLEYALKQERAKYH
HHHHHHHHHHHHHHH		41.7732015554
136AcetylationRAKYHKLKYGTELNQ
HHHHHHCCCCCCCCC		46.5725953088
137PhosphorylationAKYHKLKYGTELNQG
HHHHHCCCCCCCCCC		39.4528152594
139PhosphorylationYHKLKYGTELNQGDL
HHHCCCCCCCCCCCC		33.9228152594
147UbiquitinationELNQGDLKMPTFESE
CCCCCCCCCCCCCCC		47.8032015554
150PhosphorylationQGDLKMPTFESEETK
CCCCCCCCCCCCCCC		36.2126437602
157 (in isoform 2)Ubiquitination-66.9721890473
157 (in isoform 1)Ubiquitination-66.9721890473
157UbiquitinationTFESEETKDTEAPTA
CCCCCCCCCCCCCCC		66.9722817900
163PhosphorylationTKDTEAPTAPQNSQL
CCCCCCCCCCCCCCC		59.0027732954
168PhosphorylationAPTAPQNSQLTWKQG
CCCCCCCCCCCHHHH		22.7125850435
171PhosphorylationAPQNSQLTWKQGRQL
CCCCCCCCHHHHHHH		23.9930576142
173UbiquitinationQNSQLTWKQGRQLLR
CCCCCCHHHHHHHHH		37.3223000965
173 (in isoform 2)Ubiquitination-37.3221890473
173 (in isoform 1)Ubiquitination-37.3221890473
202PhosphorylationVRSQRVRSLLGLSNS
HHHHHHHHHHCCCCC		25.7030266825
207PhosphorylationVRSLLGLSNSEPNGS
HHHHHCCCCCCCCCC		36.1930266825
209PhosphorylationSLLGLSNSEPNGSVE
HHHCCCCCCCCCCCC		51.5630266825
214PhosphorylationSNSEPNGSVETKNLE
CCCCCCCCCCCCCHH		24.3421815630
217PhosphorylationEPNGSVETKNLEQIL
CCCCCCCCCCHHHHH		24.0723403867
229PhosphorylationQILNGGESPKQKGQE
HHHCCCCCCHHHCCH		40.4419664994
229 (in isoform 2)Phosphorylation-40.44-
240PhosphorylationKGQEIKRSSGDVLET
HCCHHHHCCCCHHHH		33.4023403867
241PhosphorylationGQEIKRSSGDVLETF
CCHHHHCCCCHHHHH		42.9423403867
247PhosphorylationSSGDVLETFNFLENA
CCCCHHHHHHHHHCC		21.5123403867
257 (in isoform 2)Phosphorylation-43.37-
257PhosphorylationFLENADDSDEDEEND
HHHCCCCCCCCHHCC		43.3726503892
293PhosphorylationEGLAADLTDDPDTEE
CCCCCCCCCCCCHHH		38.6130576142
298PhosphorylationDLTDDPDTEEALKEF
CCCCCCCHHHHHHHC		40.9025338102
322 (in isoform 2)Phosphorylation-45.8021712546
322PhosphorylationEGAGEARSSGDGTEW
CCCCCCCCCCCCCCC		45.8026434776
323 (in isoform 2)Phosphorylation-35.0425159151
323PhosphorylationGAGEARSSGDGTEWD
CCCCCCCCCCCCCCC		35.0426434776
327 (in isoform 2)Phosphorylation-38.3528348404
327PhosphorylationARSSGDGTEWDKDDL
CCCCCCCCCCCHHHC		38.3526434776
335PhosphorylationEWDKDDLSPTAEVWD
CCCHHHCCCCCEEEE		27.4828192239
337PhosphorylationDKDDLSPTAEVWDVD
CHHHCCCCCEEEECC		31.8828450419
337 (in isoform 2)Phosphorylation-31.88-
349PhosphorylationDVDQGLISKLKEQYK
ECCHHHHHHHHHHHH		36.6624719451
355PhosphorylationISKLKEQYKKERKGK
HHHHHHHHHHHHCCH		25.7226657352
374PhosphorylationRANRTKLYDMIADLG
HHHHHHHHHHHHHHC		12.6728796482
390 (in isoform 2)Phosphorylation-41.86-
396PhosphorylationPSGIINQSRSASTRM
CCCHHCCCCCCCCCC		24.5827135362
421PhosphorylationAEPITFPSGGGKSFI
CCCCCCCCCCCCEEE		45.97-
427UbiquitinationPSGGGKSFIMGSDDV
CCCCCCEEEECCHHH		5.2027667366
455PhosphorylationTVTNDADYSYDLPAN
EECCCCCCCCCCCCC		15.73-
457PhosphorylationTNDADYSYDLPANKD
CCCCCCCCCCCCCHH		18.44-
464UbiquitinationYDLPANKDAFRKTWN
CCCCCCHHHHHHHCC		51.2327667366
468AcetylationANKDAFRKTWNPKYT
CCHHHHHHHCCCCCC		51.9818603013
474UbiquitinationRKTWNPKYTLRSHFD
HHHCCCCCCHHHHCC		16.5627667366
474PhosphorylationRKTWNPKYTLRSHFD
HHHCCCCCCHHHHCC		16.5623312004
475PhosphorylationKTWNPKYTLRSHFDG
HHCCCCCCHHHHCCC		23.0924719451
511UbiquitinationLKLWNLQKTVPAKKS
EEEEEEECCCCCCCC		55.4427667366
512PhosphorylationKLWNLQKTVPAKKSA
EEEEEECCCCCCCCC		20.8221406692
518PhosphorylationKTVPAKKSASLDVEP
CCCCCCCCCCCCCEE		23.5321406692
520PhosphorylationVPAKKSASLDVEPIY
CCCCCCCCCCCEEEE		31.9921406692
527PhosphorylationSLDVEPIYTFRAHIG
CCCCEEEEEEEECHH		15.5628152594
528PhosphorylationLDVEPIYTFRAHIGP
CCCEEEEEEEECHHC		13.8321406692
603PhosphorylationGIKNQLLSCSADGTV
CHHHCEEECCCCCCE		18.0221406692
605PhosphorylationKNQLLSCSADGTVRL
HHCEEECCCCCCEEC		26.4721406692
609PhosphorylationLSCSADGTVRLWNPQ
EECCCCCCEECCCCC		11.7321406692
689PhosphorylationNHINRVVSHPTLPVT
CCCCCEECCCCCCEE		22.3823312004
692PhosphorylationNRVVSHPTLPVTITA
CCEECCCCCCEEEEE		37.9723312004
703MethylationTITAHEDRHIKFFDN
EEEECCCCCEEEEEC		30.37115916825
712PhosphorylationIKFFDNKTGKMIHSM
EEEEECCCCHHHHHH		48.5726074081
718PhosphorylationKTGKMIHSMVAHLDA
CCCHHHHHHHHHHHH		12.2026074081
727PhosphorylationVAHLDAVTSLAVDPN
HHHHHHHHEEEECCC		21.5326074081
728PhosphorylationAHLDAVTSLAVDPNG
HHHHHHHEEEECCCC		14.0326074081
737PhosphorylationAVDPNGIYLMSGSHD
EECCCCEEEECCCCC		9.5726074081
740PhosphorylationPNGIYLMSGSHDCSI
CCCEEEECCCCCCEE		34.2526074081
742PhosphorylationGIYLMSGSHDCSIRL
CEEEECCCCCCEEEE		14.6226074081
755AcetylationRLWNLDSKTCVQEIT
EEEECCCCHHHHHHH		45.6825953088
771PhosphorylationHRKKLDESIYDVAFH
HHHHHHHHHHHHHHH		26.5628270605
773PhosphorylationKKLDESIYDVAFHSS
HHHHHHHHHHHHHCC		17.4028270605
779PhosphorylationIYDVAFHSSKAYIAS
HHHHHHHCCCHHHHH		27.3827251275
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRN3_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 STRN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAA_HUMANPPP2R1Aphysical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
STRN_HUMANSTRNphysical
18782753
STRP1_HUMANSTRIP1physical
18782753
STK26_HUMANSTK26physical
18782753
STRN4_HUMANSTRN4physical
18782753
PHOCN_HUMANMOB4physical
18782753
PDC10_HUMANPDCD10physical
18782753
CT2NL_HUMANCTTNBP2NLphysical
18782753
SIKE1_HUMANSIKE1physical
18782753
STRP2_HUMANSTRIP2physical
18782753
SLMAP_HUMANSLMAPphysical
18782753
TCPB_HUMANCCT2physical
18782753
TCPQ_HUMANCCT8physical
18782753
CTTB2_HUMANCTTNBP2physical
18782753
TCPG_HUMANCCT3physical
18782753
TCPA_HUMANTCP1physical
18782753
TCPE_HUMANCCT5physical
18782753
FGOP2_HUMANFGFR1OP2physical
18782753
TCPZ_HUMANCCT6Aphysical
18782753
TCPH_HUMANCCT7physical
18782753
TCPD_HUMANCCT4physical
18782753
STRN_HUMANSTRNphysical
22939629
APC_HUMANAPCphysical
24255178
CTNB1_HUMANCTNNB1physical
24255178
CT2NL_HUMANCTTNBP2NLphysical
24255178
STRP1_HUMANSTRIP1physical
24255178
FGOP2_HUMANFGFR1OP2physical
24255178
FKB15_HUMANFKBP15physical
24255178
FMNL1_HUMANFMNL1physical
24255178
K1671_HUMANKIAA1671physical
24255178
PHOCN_HUMANMOB4physical
24255178
NACC1_HUMANNACC1physical
24255178
PARVG_HUMANPARVGphysical
24255178
TOPK_HUMANPBKphysical
24255178
SIKE1_HUMANSIKE1physical
24255178
SLMAP_HUMANSLMAPphysical
24255178
STK24_HUMANSTK24physical
24255178
STRN_HUMANSTRNphysical
24255178
STRN4_HUMANSTRN4physical
24255178
PSD13_HUMANPSMD13physical
22863883
STRN4_HUMANSTRN4physical
22863883
2AAB_HUMANPPP2R1Bphysical
24366813
CO4A5_HUMANCOL4A5physical
24366813
CT2NL_HUMANCTTNBP2NLphysical
24366813
CTTB2_HUMANCTTNBP2physical
24366813
DNJA2_HUMANDNAJA2physical
24366813
FGOP2_HUMANFGFR1OP2physical
24366813
STK26_HUMANSTK26physical
24366813
PDC10_HUMANPDCD10physical
24366813
PGAM5_HUMANPGAM5physical
24366813
PHOCN_HUMANMOB4physical
24366813
RUVB2_HUMANRUVBL2physical
24366813
SIKE1_HUMANSIKE1physical
24366813
SLMAP_HUMANSLMAPphysical
24366813
STK24_HUMANSTK24physical
24366813
STRN_HUMANSTRNphysical
24366813
STRN4_HUMANSTRN4physical
24366813
STRP1_HUMANSTRIP1physical
24366813
STRP2_HUMANSTRIP2physical
24366813
TCPA_HUMANTCP1physical
24366813
TCPB_HUMANCCT2physical
24366813
TCPD_HUMANCCT4physical
24366813
TCPE_HUMANCCT5physical
24366813
TCPG_HUMANCCT3physical
24366813
TCPH_HUMANCCT7physical
24366813
TCPQ_HUMANCCT8physical
24366813
TCPZ_HUMANCCT6Aphysical
24366813
TCPZ_HUMANCCT6Aphysical
26496610
CH10_HUMANHSPE1physical
26496610
PON2_HUMANPON2physical
26496610
PP2AB_HUMANPPP2CBphysical
26496610
2AAA_HUMANPPP2R1Aphysical
26496610
2AAB_HUMANPPP2R1Bphysical
26496610
STRN_HUMANSTRNphysical
26496610
HTF4_HUMANTCF12physical
26496610
TCPA_HUMANTCP1physical
26496610
TCPG_HUMANCCT3physical
26496610
SLMAP_HUMANSLMAPphysical
26496610
STK24_HUMANSTK24physical
26496610
M4K4_HUMANMAP4K4physical
26496610
TCPH_HUMANCCT7physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPB_HUMANCCT2physical
26496610
TCPQ_HUMANCCT8physical
26496610
PDC10_HUMANPDCD10physical
26496610
TCPE_HUMANCCT5physical
26496610
PHOCN_HUMANMOB4physical
26496610
FGOP2_HUMANFGFR1OP2physical
26496610
STRN4_HUMANSTRN4physical
26496610
PKN3_HUMANPKN3physical
26496610
STK26_HUMANSTK26physical
26496610
CT2NL_HUMANCTTNBP2NLphysical
26496610
STRP2_HUMANSTRIP2physical
26496610
SIKE1_HUMANSIKE1physical
26496610
T126A_HUMANTMEM126Aphysical
26496610
STRP1_HUMANSTRIP1physical
26496610
LAMA1_HUMANLAMA1physical
26496610
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 STRN3_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-229 AND SER-257, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASSSPECTROMETRY.
"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-229 AND SER-257, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASSSPECTROMETRY.

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