STRN_HUMAN - dbPTM
STRN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRN_HUMAN
UniProt AC O43815
Protein Name Striatin
Gene Name STRN
Organism Homo sapiens (Human).
Sequence Length 780
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Cell projection, dendritic spine. CTTNBP2-binding may regulate dendritic spine distribution..
Protein Description Calmodulin-binding protein which may function as scaffolding or signaling protein and may play a role in dendritic Ca(2+) signaling..
Protein Sequence MDEQAGPGVFFSNNHPGAGGAKGLGPLAEAAAAGDGAAAAGAARAQYSLPGILHFLQHEWARFEVERAQWEVERAELQAQIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDMKPPSYDSDEGNETEVQPQQNSQLMWKQGRQLLRQYLQEVGYTDTILDVKSKRVRALLGFSSDVTDREDDKNQDSVVNGTEAEVKETAMIAKSELTDSASVLDNFKFLESAAADFSDEDEDDDVDGREKSVIDTSTIVRKKALPDSGEDRDTKEALKEFDFLVTSEEGDNESRSAGDGTDWEKEDQCLMPEAWNVDQGVITKLKEQYKKERKGKKGVKRPNRSKLQDMLANLRDVDELPSLQPSVGSPSRPSSSRLPEHEINRADEVEALTFPPSSGKSFIMGADEALESELGLGELAGLTVANEADSLTYDIANNKDALRKTWNPKFTLRSHFDGIRALAFHPIEPVLITASEDHTLKMWNLQKTAPAKKSTSLDVEPIYTFRAHKGPVLCVVMSSNGEQCYSGGTDGLIQGWNTTNPNIDPYDSYDPSVLRGPLLGHTDAVWGLAYSAAHQRLLSCSADGTLRLWNTTEVAPALSVFNDTKELGIPASVDLVSSDPSHMVASFSKGYTSIFNMETQQRILTLESNVDTTANSSCQINRVISHPTLPISITAHEDRHIKFYDNNTGKLIHSMVAHLEAVTSLAVDPNGLYLMSGSHDCSIRLWNLESKTCIQEFTAHRKKFEESIHDVAFHPSKCYIASAGADALAKVFV
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
95UbiquitinationRKGQENLKKDLVRRI
HHCHHHHHHHHHHHH		56.6824816145
103AcetylationKDLVRRIKMLEYALK
HHHHHHHHHHHHHHH		35.3025953088
110UbiquitinationKMLEYALKQERAKYH
HHHHHHHHHHHHHHH		41.7732015554
121PhosphorylationAKYHKLKYGTELNQG
HHHHHCCCCCCCCCC		39.4523927012
123PhosphorylationYHKLKYGTELNQGDM
HHHCCCCCCCCCCCC		33.9223927012
134PhosphorylationQGDMKPPSYDSDEGN
CCCCCCCCCCCCCCC		50.5323401153
135PhosphorylationGDMKPPSYDSDEGNE
CCCCCCCCCCCCCCC		25.8223927012
137PhosphorylationMKPPSYDSDEGNETE
CCCCCCCCCCCCCCC		29.3625159151
143PhosphorylationDSDEGNETEVQPQQN
CCCCCCCCCCCHHHH		45.5223927012
151PhosphorylationEVQPQQNSQLMWKQG
CCCHHHHHHHHHHHH		21.9823663014
172PhosphorylationYLQEVGYTDTILDVK
HHHHHCCCCCEEHHC		22.27-
174PhosphorylationQEVGYTDTILDVKSK
HHHCCCCCEEHHCCH		18.68-
179UbiquitinationTDTILDVKSKRVRAL
CCCEEHHCCHHHHHH		50.3432015554
190PhosphorylationVRALLGFSSDVTDRE
HHHHHCCCCCCCCCC		24.6726471730
191PhosphorylationRALLGFSSDVTDRED
HHHHCCCCCCCCCCC		33.5625849741
194PhosphorylationLGFSSDVTDREDDKN
HCCCCCCCCCCCCCC		34.0426471730
200AcetylationVTDREDDKNQDSVVN
CCCCCCCCCCCCCCC		69.6822368931
204PhosphorylationEDDKNQDSVVNGTEA
CCCCCCCCCCCCCHH		20.4321815630
214AcetylationNGTEAEVKETAMIAK
CCCHHHHHHHHEEEH		40.6322368939
221AcetylationKETAMIAKSELTDSA
HHHHEEEHHHCCCCH		33.2722368947
222PhosphorylationETAMIAKSELTDSAS
HHHEEEHHHCCCCHH		28.9023403867
225PhosphorylationMIAKSELTDSASVLD
EEEHHHCCCCHHHHH		24.6930266825
227PhosphorylationAKSELTDSASVLDNF
EHHHCCCCHHHHHHH		19.7430266825
229PhosphorylationSELTDSASVLDNFKF
HHCCCCHHHHHHHHH		27.4530266825
239PhosphorylationDNFKFLESAAADFSD
HHHHHHHHHCCCCCC		25.9229255136
245PhosphorylationESAAADFSDEDEDDD
HHHCCCCCCCCCCCC		40.4119664994
259PhosphorylationDVDGREKSVIDTSTI
CCCCCCCCEEEHHHH		21.3929255136
263PhosphorylationREKSVIDTSTIVRKK
CCCCEEEHHHHEEEC		19.3525850435
264PhosphorylationEKSVIDTSTIVRKKA
CCCEEEHHHHEEECC		16.6429255136
265PhosphorylationKSVIDTSTIVRKKAL
CCEEEHHHHEEECCC		26.1129255136
293PhosphorylationKEFDFLVTSEEGDNE
HHCCEEEECCCCCCC		32.3528348404
294PhosphorylationEFDFLVTSEEGDNES
HCCEEEECCCCCCCC		26.6020873877
301PhosphorylationSEEGDNESRSAGDGT
CCCCCCCCCCCCCCC		37.4827251275
303PhosphorylationEGDNESRSAGDGTDW
CCCCCCCCCCCCCCH		45.9728985074
308PhosphorylationSRSAGDGTDWEKEDQ
CCCCCCCCCHHHHHC		42.55-
316UbiquitinationDWEKEDQCLMPEAWN
CHHHHHCEECCCCCC		5.6321890473
353UbiquitinationVKRPNRSKLQDMLAN
CCCCCHHHHHHHHHH		47.1022817900
353 (in isoform 1)Ubiquitination-47.1021890473
369PhosphorylationRDVDELPSLQPSVGS
CCHHHCCCCCCCCCC		52.8723927012
373PhosphorylationELPSLQPSVGSPSRP
HCCCCCCCCCCCCCC		26.5823401153
376PhosphorylationSLQPSVGSPSRPSSS
CCCCCCCCCCCCCCC		19.9719664994
378PhosphorylationQPSVGSPSRPSSSRL
CCCCCCCCCCCCCCC		59.5330266825
381PhosphorylationVGSPSRPSSSRLPEH
CCCCCCCCCCCCCHH		39.5729255136
382UbiquitinationGSPSRPSSSRLPEHE
CCCCCCCCCCCCHHH		23.3521890473
382PhosphorylationGSPSRPSSSRLPEHE
CCCCCCCCCCCCHHH		23.3529255136
383PhosphorylationSPSRPSSSRLPEHEI
CCCCCCCCCCCHHHC		42.0229255136
400PhosphorylationADEVEALTFPPSSGK
CCEEEEEECCCCCCC		40.94-
404PhosphorylationEALTFPPSSGKSFIM
EEEECCCCCCCCEEE		52.54-
405PhosphorylationALTFPPSSGKSFIMG
EEECCCCCCCCEEEC		56.89-
414UbiquitinationKSFIMGADEALESEL
CCEEECCHHHHHHHC		35.6522817900
419UbiquitinationGADEALESELGLGEL
CCHHHHHHHCCHHHH		38.6821890473
437PhosphorylationTVANEADSLTYDIAN
EEECCCHHCEEECCC		29.6522210691
439PhosphorylationANEADSLTYDIANNK
ECCCHHCEEECCCCH		24.0922210691
440PhosphorylationNEADSLTYDIANNKD
CCCHHCEEECCCCHH		15.6222210691
451UbiquitinationNNKDALRKTWNPKFT
CCHHHHHHHCCCCCE		59.7622817900
456UbiquitinationLRKTWNPKFTLRSHF
HHHHCCCCCEEHHHC		48.0121890473
456AcetylationLRKTWNPKFTLRSHF
HHHHCCCCCEEHHHC		48.0125953088
458PhosphorylationKTWNPKFTLRSHFDG
HHCCCCCEEHHHCCC		27.6428450419
480UbiquitinationPIEPVLITASEDHTL
CCCCEEEEECCCCEE		21.7022817900
485UbiquitinationLITASEDHTLKMWNL
EEEECCCCEEEEEEC		29.1021890473
501PhosphorylationKTAPAKKSTSLDVEP
CCCCCCCCCCCCCEE		23.6328348404
502PhosphorylationTAPAKKSTSLDVEPI
CCCCCCCCCCCCEEC		42.0328348404
503PhosphorylationAPAKKSTSLDVEPIY
CCCCCCCCCCCEECE		29.6625159151
510PhosphorylationSLDVEPIYTFRAHKG
CCCCEECEEEECCCC		15.5624719451
511PhosphorylationLDVEPIYTFRAHKGP
CCCEECEEEECCCCC		13.8324719451
586PhosphorylationAAHQRLLSCSADGTL
HHHHHHHCCCCCCCE		15.6020068231
588PhosphorylationHQRLLSCSADGTLRL
HHHHHCCCCCCCEEE		26.4720068231
592PhosphorylationLSCSADGTLRLWNTT
HCCCCCCCEEEEECC		14.8420068231
633PhosphorylationDPSHMVASFSKGYTS
CHHHHHEEECCCCEE		20.7424719451
672PhosphorylationCQINRVISHPTLPIS
CEECEEECCCCCCEE		22.1327067055
686MethylationSITAHEDRHIKFYDN
EEEECCCCCEEEEEC		30.37115917989
689UbiquitinationAHEDRHIKFYDNNTG
ECCCCCEEEEECCCH		31.5719608861
689AcetylationAHEDRHIKFYDNNTG
ECCCCCEEEEECCCH		31.5719608861
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 STRN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRN_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 STRN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAA_HUMANPPP2R1Aphysical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
STRP1_HUMANSTRIP1physical
18782753
STRN3_HUMANSTRN3physical
18782753
2AAB_HUMANPPP2R1Bphysical
18782753
STRN4_HUMANSTRN4physical
18782753
STK24_HUMANSTK24physical
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
TCPW_HUMANCCT6Bphysical
18782753
APC_HUMANAPCphysical
18502210
ZO1_HUMANTJP1physical
18502210
CT2NL_HUMANCTTNBP2NLphysical
24255178
STRP1_HUMANSTRIP1physical
24255178
FGOP2_HUMANFGFR1OP2physical
24255178
PHOCN_HUMANMOB4physical
24255178
2AAA_HUMANPPP2R1Aphysical
24255178
SIKE1_HUMANSIKE1physical
24255178
SLMAP_HUMANSLMAPphysical
24255178
STK24_HUMANSTK24physical
24255178
STRN3_HUMANSTRN3physical
24255178
STRN4_HUMANSTRN4physical
24255178
TFP11_HUMANTFIP11physical
25416956
RINT1_HUMANRINT1physical
25416956
2AAB_HUMANPPP2R1Bphysical
24366813
CT2NL_HUMANCTTNBP2NLphysical
24366813
CTTB2_HUMANCTTNBP2physical
24366813
FGOP2_HUMANFGFR1OP2physical
24366813
STK26_HUMANSTK26physical
24366813
PDC10_HUMANPDCD10physical
24366813
PGAM5_HUMANPGAM5physical
24366813
PHOCN_HUMANMOB4physical
24366813
SIKE1_HUMANSIKE1physical
24366813
SLMAP_HUMANSLMAPphysical
24366813
STRN3_HUMANSTRN3physical
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
SLMAP_HUMANSLMAPphysical
26344197
TCPZ_HUMANCCT6Aphysical
26496610
HSPB1_HUMANHSPB1physical
26496610
2AAA_HUMANPPP2R1Aphysical
26496610
2AAB_HUMANPPP2R1Bphysical
26496610
TCPA_HUMANTCP1physical
26496610
TCPG_HUMANCCT3physical
26496610
SLMAP_HUMANSLMAPphysical
26496610
STK24_HUMANSTK24physical
26496610
M4K4_HUMANMAP4K4physical
26496610
MCA3_HUMANEEF1E1physical
26496610
BAG2_HUMANBAG2physical
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
S43A3_HUMANSLC43A3physical
26496610
STRN4_HUMANSTRN4physical
26496610
STRN3_HUMANSTRN3physical
26496610
STK26_HUMANSTK26physical
26496610
CT2NL_HUMANCTTNBP2NLphysical
26496610
STRP2_HUMANSTRIP2physical
26496610
AHNK_HUMANAHNAKphysical
26496610
SIKE1_HUMANSIKE1physical
26496610
STRP1_HUMANSTRIP1physical
26496610
PKN3_HUMANPKN3physical
27173435
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 STRN_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-689, AND MASS SPECTROMETRY.
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-245, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY.
"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-245, 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-245, AND MASSSPECTROMETRY.

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