STRN_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STRN_MOUSE
• UniProt AC: O55106
• Protein Name: Striatin
• Gene Name: Strn
• Organism: Mus musculus (Mouse).
• Sequence Length: 780
• Subcellular Localization: Cytoplasm. Membrane; Peripheral membrane protein. Cell projection, dendritic spine. CTTNBP2-binding may regulate dendritic spine distribution..
• Protein Description: Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein..
• Protein Sequence: MDEQAGPGVFFSNNHPGAGGAKGLGPLAEAAAAGDGAAAAGAARAQYSLPGILHFLQHEWARFEVERAQWEVERAELQAQIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDMKPPSYDSDEGNETEVQPQQNSQLMWKQGRQLLRQYLQEVGYTDTILDVKSKRVRALLGFSSDVTDREDDKNQDSVINGTEAEVKETAMIGKSELTDSASVLDNFKFLESAAADVSDEDEDEDTDGRAKSVIDTSTIVRKKALPDTSEDRDTKEALKEFDFLVTSEEGDNESRSAGDGTDWEKEDQCLTPEAWNVDQGVISKLKEQYKKERKGKKGVKRPNRSKLQDMLANLRDVDELPSLQPSVGSPSRPSSSRLPEQELSRADEVEALTFPPSSGKSFIMGADEALESELGLGELAGLTVANEADSLAYDIANNKDALRKTWNPKFTLRSHFDGIRALAFHPIEPVLITASEDHTLKMWNLQKTAPAKKSTSLDVEPIYTFRAHKGPVLCVVMSSNGEQCYSGGTDGRIQSWSTTNPNVDPYDAYDPSVLRGPLLGHTDAVWGLAYSAAHQRLLSCSADGTLRLWNTTEVAPALSVFNDNQELGIPASVDLVSSDPSHMVASFSKGYTSIFNMETQQRVLTLESNVDSTSSSSCQINRVISHPTLPISITAHEDRHIKFYDNNTGKLIHSMVAHLEAVTSLAVDPNGLYLMSGSHDCSIRLWNLESKTCIQEFTAHRKKFEESIHDVAFHPSKCYIASAGADALAKVFV

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
47	Phosphorylation	AGAARAQYSLPGILH HHHHHHHHCCHHHHH	15.93	22802335
48	Phosphorylation	GAARAQYSLPGILHF HHHHHHHCCHHHHHH	18.92	22802335
121	Phosphorylation	AKYHKLKYGTELNQG HHHHHCCCCCCCCCC	39.45	25619855
123	Phosphorylation	YHKLKYGTELNQGDM HHHCCCCCCCCCCCC	33.92	25619855
134	Phosphorylation	QGDMKPPSYDSDEGN CCCCCCCCCCCCCCC	50.53	25521595
135	Phosphorylation	GDMKPPSYDSDEGNE CCCCCCCCCCCCCCC	25.82	25619855
137	Phosphorylation	MKPPSYDSDEGNETE CCCCCCCCCCCCCCC	29.36	25521595
143	Phosphorylation	DSDEGNETEVQPQQN CCCCCCCCCCCHHHH	45.52	24925903
151	Phosphorylation	EVQPQQNSQLMWKQG CCCHHHHHHHHHHHH	21.98	25619855
190	Phosphorylation	VRALLGFSSDVTDRE HHHHHCCCCCCCCCC	24.67	25521595
191	Phosphorylation	RALLGFSSDVTDRED HHHHCCCCCCCCCCC	33.56	25521595
194	Phosphorylation	LGFSSDVTDREDDKN HCCCCCCCCCCCCCC	34.04	25521595
204	Phosphorylation	EDDKNQDSVINGTEA CCCCCCCCCCCCCHH	18.35	23375375
216	Phosphorylation	TEAEVKETAMIGKSE CHHHHHHEEEECCHH	18.79	26643407
222	Phosphorylation	ETAMIGKSELTDSAS HEEEECCHHCCCCCH	32.40	29899451
225	Phosphorylation	MIGKSELTDSASVLD EECCHHCCCCCHHHH	24.69	26525534
227	Phosphorylation	GKSELTDSASVLDNF CCHHCCCCCHHHHHH	19.74	25521595
229	Phosphorylation	SELTDSASVLDNFKF HHCCCCCHHHHHHHH	27.45	25521595
239	Phosphorylation	DNFKFLESAAADVSD HHHHHHHHHCCCCCC	25.92	27180971
245	Phosphorylation	ESAAADVSDEDEDED HHHCCCCCCCCCCCC	35.51	25521595
253	Phosphorylation	DEDEDEDTDGRAKSV CCCCCCCCCCCCCCE	38.00	22324799
259	Phosphorylation	DTDGRAKSVIDTSTI CCCCCCCCEEEHHHH	24.26	25521595
263	Phosphorylation	RAKSVIDTSTIVRKK CCCCEEEHHHHHHHC	19.35	23984901
264	Phosphorylation	AKSVIDTSTIVRKKA CCCEEEHHHHHHHCC	16.64	23984901
265	Phosphorylation	KSVIDTSTIVRKKAL CCEEEHHHHHHHCCC	26.11	30352176
275	Phosphorylation	RKKALPDTSEDRDTK HHCCCCCCCCCCCHH	31.88	29899451
276	Phosphorylation	KKALPDTSEDRDTKE HCCCCCCCCCCCHHH	44.90	29899451
293	Phosphorylation	KEFDFLVTSEEGDNE HHCCEEEECCCCCCC	32.35	26525534
294	Phosphorylation	EFDFLVTSEEGDNES HCCEEEECCCCCCCC	26.60	25293948
301	Phosphorylation	SEEGDNESRSAGDGT CCCCCCCCCCCCCCC	37.48	25293948
308	Phosphorylation	SRSAGDGTDWEKEDQ CCCCCCCCCHHHHCC	42.55	26525534
318	Phosphorylation	EKEDQCLTPEAWNVD HHHCCCCCHHHHCCC	27.06	26643407
369	Phosphorylation	RDVDELPSLQPSVGS CCHHHCCCCCCCCCC	52.87	25619855
373	Phosphorylation	ELPSLQPSVGSPSRP HCCCCCCCCCCCCCC	26.58	25619855
376	Phosphorylation	SLQPSVGSPSRPSSS CCCCCCCCCCCCCCC	19.97	25521595
378	Phosphorylation	QPSVGSPSRPSSSRL CCCCCCCCCCCCCCC	59.53	25619855
381	Phosphorylation	VGSPSRPSSSRLPEQ CCCCCCCCCCCCCHH	39.57	25619855
382	Phosphorylation	GSPSRPSSSRLPEQE CCCCCCCCCCCCHHH	23.35	25619855
383	Phosphorylation	SPSRPSSSRLPEQEL CCCCCCCCCCCHHHH	42.02	25619855
456	Ubiquitination	LRKTWNPKFTLRSHF HHHHCCCCCEEHHHC	48.01	-
458	Phosphorylation	KTWNPKFTLRSHFDG HHCCCCCEEHHHCCC	27.64	27600695
510	Phosphorylation	SLDVEPIYTFRAHKG CCCCEECEEEECCCC	15.56	22817900
672	Phosphorylation	CQINRVISHPTLPIS CEEEEEECCCCCCEE	22.13	26370283

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of STRN_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of STRN_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of STRN_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of STRN_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY.
PubMed: 19131326

"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-264, AND MASSSPECTROMETRY.
PubMed: 17242355