UniProt ID | STRN4_MOUSE | |
---|---|---|
UniProt AC | P58404 | |
Protein Name | Striatin-4 | |
Gene Name | Strn4 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 760 | |
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 | MMEERAAAAVASAASSCRPLGSGTAPNPTAAAPASSPAPGPGPVGKGGGGGGSPGPTAGPEPLSLPGILHFIQHEWARFEAEKARWEAERAELQAQVAFLQGERKGQENLKTDLVRRIKMLEYALKQERAKYHKLKFGTDLNQGEKKTDLSEQVSNGPVESVTLENSPLVWKEGRQLLRQYLEEVGYTDTILDMRSKRVRSLLGRSLELNGAGEPVEGAPRASPGPGGLSGGESLLVKQIEEQIKRNAAGKDGKERLGGSVLEQIPFLQNCEDEDSDEDDELDSVQHKKQRVRLPSKALVPEMEDEDEEDDSEDAINEFDFLGSGEDGEGSPDPRRCTSEGNPHELESRRVKLQGILADLRDVDGLPPKVTVPPPGTPQPRPHEGSFGFSSDVFIMDTIGGGEVSLGDLADLTVTNDNDLSCDLSDSKDAFKKTWNPKFTLRSHYDGIRSLAFHHSQSALLTASEDGTLKLWNLQKAVTAKKNAALDVEPIHAFRAHRGPVLAVTMGSNSEYCYSGGADARIHSWKIPDLNMDPYDGYDPSVLSHVLEGHGDAVWGLAFSPTSQRLASCSADGTVRIWDPSSSGPSCLCTFPMDGEHGIPTSVAFTSTEPAHVVASFRSGDTVLYDLEAGSALLTLESRGSSGPAQINQVVSHPSQPLTITAHDDRGIRFLDNRTGKSVHSMVAHLDAVTCLAVDPNGVFLMSGSHDCSLRLWSLDNKTCVQEITAHRKKHEEAIHAVACHPSKALIASAGADALAKVFV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
16 | Phosphorylation | AVASAASSCRPLGSG HHHHHHHHCCCCCCC | 14.93 | 24453211 | |
17 | Glutathionylation | VASAASSCRPLGSGT HHHHHHHCCCCCCCC | 4.87 | 24333276 | |
35 | Phosphorylation | PTAAAPASSPAPGPG CCCCCCCCCCCCCCC | 35.48 | 29233185 | |
36 | Phosphorylation | TAAAPASSPAPGPGP CCCCCCCCCCCCCCC | 27.47 | 26643407 | |
53 | Phosphorylation | KGGGGGGSPGPTAGP CCCCCCCCCCCCCCC | 29.92 | 26824392 | |
57 | Phosphorylation | GGGSPGPTAGPEPLS CCCCCCCCCCCCCCC | 50.60 | 26745281 | |
64 | Phosphorylation | TAGPEPLSLPGILHF CCCCCCCCCCCHHHH | 43.14 | 25777480 | |
148 | Phosphorylation | LNQGEKKTDLSEQVS CCCCCCCCCHHHHHH | 53.92 | 23984901 | |
151 | Phosphorylation | GEKKTDLSEQVSNGP CCCCCCHHHHHHCCC | 28.88 | 23984901 | |
155 | Phosphorylation | TDLSEQVSNGPVESV CCHHHHHHCCCCCEE | 35.45 | 23984901 | |
161 | Phosphorylation | VSNGPVESVTLENSP HHCCCCCEEEECCCC | 22.19 | 23984901 | |
163 | Phosphorylation | NGPVESVTLENSPLV CCCCCEEEECCCCCC | 37.32 | 23984901 | |
167 | Phosphorylation | ESVTLENSPLVWKEG CEEEECCCCCCHHHH | 15.38 | 23984901 | |
201 | Phosphorylation | MRSKRVRSLLGRSLE HHHHHHHHHHCCCEE | 25.70 | 26745281 | |
206 | Phosphorylation | VRSLLGRSLELNGAG HHHHHCCCEECCCCC | 25.13 | 25521595 | |
223 | Phosphorylation | VEGAPRASPGPGGLS CCCCCCCCCCCCCCC | 31.50 | 26824392 | |
230 | Phosphorylation | SPGPGGLSGGESLLV CCCCCCCCCHHHHHH | 48.29 | 28833060 | |
234 | Phosphorylation | GGLSGGESLLVKQIE CCCCCHHHHHHHHHH | 30.22 | 28833060 | |
260 | Phosphorylation | GKERLGGSVLEQIPF CCHHCCCCHHHHCCC | 23.02 | 23984901 | |
276 | Phosphorylation | QNCEDEDSDEDDELD HCCCCCCCCCCCCHH | 40.63 | 27087446 | |
284 | Phosphorylation | DEDDELDSVQHKKQR CCCCCHHHHHHHHHH | 35.98 | 25159016 | |
296 | Phosphorylation | KQRVRLPSKALVPEM HHHCCCCHHCCCCCC | 34.84 | - | |
312 | Phosphorylation | DEDEEDDSEDAINEF CCCCCCCCCHHHHHC | 50.09 | 29899451 | |
324 | Phosphorylation | NEFDFLGSGEDGEGS HHCCCCCCCCCCCCC | 40.95 | 25195567 | |
331 | Phosphorylation | SGEDGEGSPDPRRCT CCCCCCCCCCCCCCC | 23.10 | 25338131 | |
377 | Phosphorylation | VTVPPPGTPQPRPHE CCCCCCCCCCCCCCC | 25.23 | 26824392 | |
438 | Ubiquitination | FKKTWNPKFTLRSHY HHHHCCCCEEEECCC | 48.01 | 22790023 | |
440 | Phosphorylation | KTWNPKFTLRSHYDG HHCCCCEEEECCCCH | 27.64 | 27600695 | |
569 | Glutathionylation | TSQRLASCSADGTVR CHHHHHCCCCCCCEE | 3.02 | 24333276 | |
720 | S-nitrosocysteine | WSLDNKTCVQEITAH EEECCCHHHHHHHHH | 2.96 | - | |
720 | S-nitrosylation | WSLDNKTCVQEITAH EEECCCHHHHHHHHH | 2.96 | 20925432 |
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 STRN4_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STRN4_MOUSE !! |
* 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 STRN4_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of STRN4_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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-206 AND SER-223, ANDMASS SPECTROMETRY. | |
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND MASSSPECTROMETRY. |