SESD1_HUMAN - dbPTM
SESD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SESD1_HUMAN
UniProt AC Q86VW0
Protein Name SEC14 domain and spectrin repeat-containing protein 1
Gene Name SESTD1
Organism Homo sapiens (Human).
Sequence Length 696
Subcellular Localization
Protein Description May act as the primary docking protein directing membrane turnover and assembly of the transient receptor potential channels TRPC4 and TRPC5. Binds phospholipids such as phosphatidylinositol monophosphates, phosphatidylinositol diphosphates (PIP2s) and phosphatidic acid, but not less polar lipids including phosphatidylcholine, phosphatidylserine, and phosphatidylinositol. The binding to PIP2s is calcium dependent. Might be involved in the plasma membrane localization of CTNNB1..
Protein Sequence MEASVILPILKKKLAFLSGGKDRRSGLILTIPLCLEQTNMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQWNVVKTVVVMLQNVVPAEVSLVCVVKPDEFWDKKVTHFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGSLTYDHMDWLNKRLVFEKFTKESTSLLDELALINNGSDKGNQQEKERSVDLNFLPSVDPETVLQTGHELLSELQQRRFNGSDGGVSWSPMDDELLAQPQVMKLLDSLREQYTRYQEVCRQRSKRTQLEEIQQKVMQVVNWLEGPGSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLVELKSLQQQLSDVCYRQASQLEFRQNLLQAALEFHGVAQDLSQQLDGLLGMLCVDVAPADGASIQQTLKLLEEKLKSVDVGLQGLREKGQGLLDQISNQASWAYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMVDVRRLKMLQMVQLFKCEEDAAQAVEWLSELLDALLKTHIRLGDDAQETKVLLEKHRKFVDVAQSTYDYGRQLLQATVVLCQSLRCTSRSSGDTLPRLNRVWKQFTIASEERVHRLEMAIAFHSNAEKILQDCPEEPEAINDEEQFDEIEAVGKSLLDRLTVPVVYPDGTEQYFGSPSDMASTAENIRDRMKLVNLKRQQLRHPEMVTTES
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
38PhosphorylationIPLCLEQTNMDELSV
EEEHHHHCCHHHHHH
24.1222210691
55PhosphorylationDYLLSIPSEKCKARG
HHHHHCCHHHHCCCC
48.2822210691
168UbiquitinationLVFEKFTKESTSLLD
HHHHHCCHHHHHHHH
53.45-
170PhosphorylationFEKFTKESTSLLDEL
HHHCCHHHHHHHHHH
25.5027251275
171PhosphorylationEKFTKESTSLLDELA
HHCCHHHHHHHHHHH
25.2027251275
172PhosphorylationKFTKESTSLLDELAL
HCCHHHHHHHHHHHH
35.8927251275
186UbiquitinationLINNGSDKGNQQEKE
HHCCCCCCCCHHHHH
62.55-
253PhosphorylationQVMKLLDSLREQYTR
HHHHHHHHHHHHHHH
29.3324719451
258PhosphorylationLDSLREQYTRYQEVC
HHHHHHHHHHHHHHH
6.6124719451
261PhosphorylationLREQYTRYQEVCRQR
HHHHHHHHHHHHHHH
10.9618083107
305PhosphorylationAQWGIGDSIRASQAL
HHHCCHHHHHHHHHH
14.5724076635
423UbiquitinationTLKLLEEKLKSVDVG
HHHHHHHHHHHCCCC
52.41-
455UbiquitinationQASWAYGKDVTIENK
CHHHHHCCCCEECCC
36.03-
535UbiquitinationGDDAQETKVLLEKHR
CCCHHHHHHHHHHHH
30.08-
640PhosphorylationEIEAVGKSLLDRLTV
HHHHHHHHHHHHCCC
28.3824275569
646PhosphorylationKSLLDRLTVPVVYPD
HHHHHHCCCCEECCC
24.5319835603
651PhosphorylationRLTVPVVYPDGTEQY
HCCCCEECCCCCCCC
8.8819835603
655PhosphorylationPVVYPDGTEQYFGSP
CEECCCCCCCCCCCH
27.5619835603
658PhosphorylationYPDGTEQYFGSPSDM
CCCCCCCCCCCHHHH
12.0419835603
661PhosphorylationGTEQYFGSPSDMAST
CCCCCCCCHHHHHHH
16.0119835603
663PhosphorylationEQYFGSPSDMASTAE
CCCCCCHHHHHHHHH
41.5419835603
667PhosphorylationGSPSDMASTAENIRD
CCHHHHHHHHHHHHH
22.8519835603
668PhosphorylationSPSDMASTAENIRDR
CHHHHHHHHHHHHHH
28.5819835603

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 SESD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SESD1_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 SESD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GELS_HUMANGSNphysical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SESD1_HUMAN

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Related Literatures of Post-Translational Modification

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