TECT2_MOUSE - dbPTM
TECT2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
76N-linked_GlycosylationPTCGGRRNETVDWNV
CCCCCCCCCEECEEE
48.18-
82N-linked_GlycosylationRNETVDWNVTVSPRE
CCCEECEEEEECCCC
18.34-
146N-linked_GlycosylationIQVEIYPNTSVTHNA
HEEEECCCCCCCCCC
28.19-
156N-linked_GlycosylationVTHNASENMTVIPNQ
CCCCCCCCEEECCCC
29.00-
340PhosphorylationLENMKIRTTGGPVTP
EECCEEEECCCCCCC
33.0125777480
341PhosphorylationENMKIRTTGGPVTPT
ECCEEEECCCCCCCC
30.2325777480
346PhosphorylationRTTGGPVTPTVTYEE
EECCCCCCCCEEHHH
19.1725777480
348PhosphorylationTGGPVTPTVTYEEAI
CCCCCCCCEEHHHCC
19.0025777480
350PhosphorylationGPVTPTVTYEEAIDL
CCCCCCEEHHHCCCH
27.9125777480
351PhosphorylationPVTPTVTYEEAIDLD
CCCCCEEHHHCCCHH
13.8725777480
389N-linked_GlycosylationHYVFRWQNNSISGLD
EEEEEECCCCCCCCE
36.9419349973
521PhosphorylationHVARRGNSDYSDLSD
HHHHCCCCCCHHCCC
40.5225367039
523PhosphorylationARRGNSDYSDLSDGW
HHCCCCCCHHCCCCE
12.1425367039
524PhosphorylationRRGNSDYSDLSDGWL
HCCCCCCHHCCCCEE
36.7525367039
527PhosphorylationNSDYSDLSDGWLEII
CCCCHHCCCCEEEEE
38.7825367039
541PhosphorylationIRAEAPDTGADLPLS
EEEECCCCCCCCCHH
32.9625367039
548PhosphorylationTGADLPLSSVNGVCP
CCCCCCHHHCCCCCC
30.2425367039
549PhosphorylationGADLPLSSVNGVCPE
CCCCCHHHCCCCCCC
27.5625367039

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 TECT2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TECT2_MOUSE !!

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 TECT2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MKS1_MOUSEMks1physical
21565611

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TECT2_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.

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