STX1B_HUMAN - dbPTM
STX1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STX1B_HUMAN
UniProt AC P61266
Protein Name Syntaxin-1B
Gene Name STX1B
Organism Homo sapiens (Human).
Sequence Length 288
Subcellular Localization Isoform 1: Membrane
Single-pass type IV membrane protein .
Isoform 2: Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Colocalizes with Lamin A/C and NuMA in interphasic nuclei, and
Protein Description Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity)..
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
10PhosphorylationDRTQELRSAKDSDDE
HHHHHHHHCCCCCCH
52.9018510355
14PhosphorylationELRSAKDSDDEEEVV
HHHHCCCCCCHHHEE
46.3721082442
45UbiquitinationEIRGCIEKLSEDVEQ
HHHHHHHHHHHHHHH
37.0830230243
58PhosphorylationEQVKKQHSAILAAPN
HHHHHHHHHHHHCCC
17.9519060867
69UbiquitinationAAPNPDEKTKQELED
HCCCCCHHHHHHHHH
69.2932142685
93UbiquitinationNKVRSKLKAIEQSIE
HHHHHHHHHHHHHHH
51.5630230243
98PhosphorylationKLKAIEQSIEQEEGL
HHHHHHHHHHHHHCC
18.4624076635
108PhosphorylationQEEGLNRSSADLRIR
HHHCCCCCCHHHHHH
28.8923312004
109PhosphorylationEEGLNRSSADLRIRK
HHCCCCCCHHHHHHH
23.6724076635
117PhosphorylationADLRIRKTQHSTLSR
HHHHHHHHHCCHHHH
22.9722985185
121PhosphorylationIRKTQHSTLSRKFVE
HHHHHCCHHHHHHHH
26.9922985185
133PhosphorylationFVEVMTEYNATQSKY
HHHHHHHCCCCHHHH
10.8428331001
139UbiquitinationEYNATQSKYRDRCKD
HCCCCHHHHHHHHHH
34.1932142685
160PhosphorylationEITGRTTTNEELEDM
HHHCCCCCHHHHHHH
39.7721082442
170PhosphorylationELEDMLESGKLAIFT
HHHHHHHHCCEEEEC
36.9529083192
172UbiquitinationEDMLESGKLAIFTDD
HHHHHHCCEEEECCC
43.9830230243
181UbiquitinationAIFTDDIKMDSQMTK
EEECCCCCCCHHHHH
43.5832142685
188UbiquitinationKMDSQMTKQALNEIE
CCCHHHHHHHHHHHH
28.3832142685
196PhosphorylationQALNEIETRHNEIIK
HHHHHHHHHHHHHHH
42.78-
248PhosphorylationDYVERAVSDTKKAVK
HHHHHHHHHHHHHHH
38.2826657352
251UbiquitinationERAVSDTKKAVKYQS
HHHHHHHHHHHHHHC
43.6632142685
256PhosphorylationDTKKAVKYQSKARRK
HHHHHHHHHCHHHHC
16.0629116813
258PhosphorylationKKAVKYQSKARRKKI
HHHHHHHCHHHHCHH
25.7822468782

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STX1B_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNP23_HUMANSNAP23physical
12651853
VAPB_HUMANVAPBphysical
12651853
VAMP1_HUMANVAMP1physical
12093152
VAMP2_HUMANVAMP2physical
12093152
VAPB_HUMANVAPBphysical
24885147

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616172Generalized epilepsy with febrile seizures plus 9 (GEFSP9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STX1B_HUMAN

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Related Literatures of Post-Translational Modification

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