STX1B_MOUSE - dbPTM
STX1B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STX1B_MOUSE
UniProt AC P61264
Protein Name Syntaxin-1B
Gene Name Stx1b
Organism Mus musculus (Mouse).
Sequence Length 288
Subcellular Localization Membrane
Single-pass type IV membrane protein .
Protein Description Potentially involved in docking of synaptic vesicles at presynaptic active zones (By similarity). May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm..
Protein Sequence MKDRTQELRSAKDSDDEEEVVHVDRDHFMDEFFEQVEEIRGCIEKLSEDVEQVKKQHSAILAAPNPDEKTKQELEDLTADIKKTANKVRSKLKAIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMTEYNATQSKYRDRCKDRIQRQLEITGRTTTNEELEDMLESGKLAIFTDDIKMDSQMTKQALNEIETRHNEIIKLETSIRELHDMFVDMAMLVESQGEMIDRIEYNVEHSVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVVLGVVLASSIGGTLGL
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
5Phosphorylation---MKDRTQELRSAK
---CCHHHHHHHHCC
36.2129899451
10PhosphorylationDRTQELRSAKDSDDE
HHHHHHHHCCCCCCH
52.9025521595
14PhosphorylationELRSAKDSDDEEEVV
HHHHCCCCCCHHHEE
46.3725521595
45UbiquitinationEIRGCIEKLSEDVEQ
HHHHHHHHHHHHHHH
37.0822790023
50UbiquitinationIEKLSEDVEQVKKQH
HHHHHHHHHHHHHHH
4.9427667366
54UbiquitinationSEDVEQVKKQHSAIL
HHHHHHHHHHHHHHH
46.5422790023
55UbiquitinationEDVEQVKKQHSAILA
HHHHHHHHHHHHHHH
55.1522790023
58PhosphorylationEQVKKQHSAILAAPN
HHHHHHHHHHHHCCC
17.9525521595
65UbiquitinationSAILAAPNPDEKTKQ
HHHHHCCCCCHHHHH
52.5127667366
69UbiquitinationAAPNPDEKTKQELED
HCCCCCHHHHHHHHH
69.2922790023
71UbiquitinationPNPDEKTKQELEDLT
CCCCHHHHHHHHHHH
53.4922790023
82AcetylationEDLTADIKKTANKVR
HHHHHHHHHHHHHHH
44.628264491
82UbiquitinationEDLTADIKKTANKVR
HHHHHHHHHHHHHHH
44.6222790023
89UbiquitinationKKTANKVRSKLKAIE
HHHHHHHHHHHHHHH
29.6827667366
93UbiquitinationNKVRSKLKAIEQSIE
HHHHHHHHHHHHHHH
51.5622790023
98PhosphorylationKLKAIEQSIEQEEGL
HHHHHHHHHHHHHCC
18.4625521595
108PhosphorylationQEEGLNRSSADLRIR
HHHCCCCCCHHHHHH
28.8929899451
109PhosphorylationEEGLNRSSADLRIRK
HHCCCCCCHHHHHHH
23.6722817900
125UbiquitinationQHSTLSRKFVEVMTE
HCCHHHHHHHHHHHH
50.8422790023
136PhosphorylationVMTEYNATQSKYRDR
HHHHCCCCHHHHHHH
29.7229899451
139UbiquitinationEYNATQSKYRDRCKD
HCCCCHHHHHHHHHH
34.1922790023
155PhosphorylationIQRQLEITGRTTTNE
HHHHHHHHCCCCCHH
15.9624925903
158PhosphorylationQLEITGRTTTNEELE
HHHHHCCCCCHHHHH
39.0422871156
159PhosphorylationLEITGRTTTNEELED
HHHHCCCCCHHHHHH
26.6829899451
160PhosphorylationEITGRTTTNEELEDM
HHHCCCCCHHHHHHH
39.7725521595
170PhosphorylationELEDMLESGKLAIFT
HHHHHHHHCCEEEEC
36.9529899451
172UbiquitinationEDMLESGKLAIFTDD
HHHHHHCCEEEECCC
43.9822790023
177UbiquitinationSGKLAIFTDDIKMDS
HCCEEEECCCCCCCH
27.0127667366
181UbiquitinationAIFTDDIKMDSQMTK
EEECCCCCCCHHHHH
43.5822790023
184UbiquitinationTDDIKMDSQMTKQAL
CCCCCCCHHHHHHHH
20.5327667366
187UbiquitinationIKMDSQMTKQALNEI
CCCCHHHHHHHHHHH
16.6227667366
188UbiquitinationKMDSQMTKQALNEIE
CCCHHHHHHHHHHHH
28.3822790023
203UbiquitinationTRHNEIIKLETSIRE
HHHHHHHHHHHHHHH
46.0322790023
206PhosphorylationNEIIKLETSIRELHD
HHHHHHHHHHHHHHH
39.6319854140
211UbiquitinationLETSIRELHDMFVDM
HHHHHHHHHHHHHHH
2.7427667366
224PhosphorylationDMAMLVESQGEMIDR
HHHHHHHCCCCEECE
35.6919854140
248UbiquitinationDYVERAVSDTKKAVK
HHHHHHHHHHHHHHH
38.2827667366
251UbiquitinationERAVSDTKKAVKYQS
HHHHHHHHHHHHHHC
43.6627667366
252UbiquitinationRAVSDTKKAVKYQSK
HHHHHHHHHHHHHCH
61.5827667366
255UbiquitinationSDTKKAVKYQSKARR
HHHHHHHHHHCHHHH
42.2927667366
299Ubiquitination------------------
------------------
27667366
306Ubiquitination-------------------------
-------------------------
27667366
370Ubiquitination-----------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------
27667366
373Ubiquitination--------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------
27667366

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 STX1B_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STX1B_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 STX1B_MOUSE !!

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

Oops, there are no PPI records of STX1B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STX1B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-14; SER-58 AND THR-160,AND MASS SPECTROMETRY.
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol.";
Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.;
Proteomics 5:388-398(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.

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