UniProt ID | TECT2_MOUSE | |
---|---|---|
UniProt AC | Q2MV57 | |
Protein Name | Tectonic-2 | |
Gene Name | Tctn2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 700 | |
Subcellular Localization |
Membrane Single-pass type I membrane protein . Cytoplasm, cytoskeleton, cilium basal body . Localizes at the transition zone, a region between the basal body and the ciliary axoneme. |
|
Protein Description | Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for hedgehog signaling transduction.. | |
Protein Sequence | MGSLSPLSLLWGLLLLQGVLRPLRGDPVFIPPFIRMSSPEVRATLVGGSEDVAVSLSLLQVEEGVLPVPTCGGRRNETVDWNVTVSPRESTLEVTIRWKRGLDWCSADETASFSEPPCVLQMLLVSASHNASCLAHLLIQVEIYPNTSVTHNASENMTVIPNQVYQPLGPCPCDLTAKACDIQCCCDQDCQPEVRELFAQSCFSGVFGGHVSPPSHHHCAVSTTHQTPDWFPLLCVQSPPSTSPFLGHFYHGATSPRHSPGFEAHLHFDLRDFADASYKQGDPIMTTEGYFTIPQVSLAGQCLQDAPVAFLRNFDSVCTMDLEVHQGRDEIVLENMKIRTTGGPVTPTVTYEEAIDLDKFITSPDTVLSVGSAPRNVNVEEHYVFRWQNNSISGLDITVIRAEISAQQRGMMTQRFTVKFLSHHSGGEKEFSGNPGYQLGKPVRALHTAGMNVSTLHLWQPAGRGLCTAAALRPILFGENAFSGCLLEVGIKENCTQLRENVLQRLDLLTQATHVARRGNSDYSDLSDGWLEIIRAEAPDTGADLPLSSVNGVCPEVPARLSIRILTAEAGSVEGVAQREILAVETRFSTVTWQYQCGLTCEDKADLLPLSASVEFINVPAQMPHPPTRFQINFTEYDCTRNELCWPQLLYPLTQYYQGEPQSQCVAKGLMLLSLLMLAILLRHPWVRMCKARDSAAIYH | |
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 |
---|---|---|---|---|---|
76 | N-linked_Glycosylation | PTCGGRRNETVDWNV CCCCCCCCCEECEEE | 48.18 | - | |
82 | N-linked_Glycosylation | RNETVDWNVTVSPRE CCCEECEEEEECCCC | 18.34 | - | |
146 | N-linked_Glycosylation | IQVEIYPNTSVTHNA HEEEECCCCCCCCCC | 28.19 | - | |
156 | N-linked_Glycosylation | VTHNASENMTVIPNQ CCCCCCCCEEECCCC | 29.00 | - | |
340 | Phosphorylation | LENMKIRTTGGPVTP EECCEEEECCCCCCC | 33.01 | 25777480 | |
341 | Phosphorylation | ENMKIRTTGGPVTPT ECCEEEECCCCCCCC | 30.23 | 25777480 | |
346 | Phosphorylation | RTTGGPVTPTVTYEE EECCCCCCCCEEHHH | 19.17 | 25777480 | |
348 | Phosphorylation | TGGPVTPTVTYEEAI CCCCCCCCEEHHHCC | 19.00 | 25777480 | |
350 | Phosphorylation | GPVTPTVTYEEAIDL CCCCCCEEHHHCCCH | 27.91 | 25777480 | |
351 | Phosphorylation | PVTPTVTYEEAIDLD CCCCCEEHHHCCCHH | 13.87 | 25777480 | |
389 | N-linked_Glycosylation | HYVFRWQNNSISGLD EEEEEECCCCCCCCE | 36.94 | 19349973 | |
521 | Phosphorylation | HVARRGNSDYSDLSD HHHHCCCCCCHHCCC | 40.52 | 25367039 | |
523 | Phosphorylation | ARRGNSDYSDLSDGW HHCCCCCCHHCCCCE | 12.14 | 25367039 | |
524 | Phosphorylation | RRGNSDYSDLSDGWL HCCCCCCHHCCCCEE | 36.75 | 25367039 | |
527 | Phosphorylation | NSDYSDLSDGWLEII CCCCHHCCCCEEEEE | 38.78 | 25367039 | |
541 | Phosphorylation | IRAEAPDTGADLPLS EEEECCCCCCCCCHH | 32.96 | 25367039 | |
548 | Phosphorylation | TGADLPLSSVNGVCP CCCCCCHHHCCCCCC | 30.24 | 25367039 | |
549 | Phosphorylation | GADLPLSSVNGVCPE CCCCCHHHCCCCCCC | 27.56 | 25367039 |
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 TECT2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TECT2_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 TECT2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MKS1_MOUSE | Mks1 | physical | 21565611 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
N-linked Glycosylation | |
Reference | PubMed |
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-389, AND MASSSPECTROMETRY. |