LIN7B_HUMAN - dbPTM
LIN7B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIN7B_HUMAN
UniProt AC Q9HAP6
Protein Name Protein lin-7 homolog B
Gene Name LIN7B
Organism Homo sapiens (Human).
Sequence Length 207
Subcellular Localization Cell membrane
Peripheral membrane protein. Basolateral cell membrane
Peripheral membrane protein. Cell junction. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density
Peripheral membrane protein. Cell junction, tight junction. Cell j
Protein Description Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface (By similarity)..
Protein Sequence MAALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRVLQSRFCSAIREVYEQLYDTLDITGSAEIRAHATAKATVAAFTASEGHAHPRVVELPKTDEGLGFNIMGGKEQNSPIYISRVIPGGVADRHGGLKRGDQLLSVNGVSVEGEQHEKAVELLKAAQGSVKLVVRYTPRVLEEMEARFEKMRSARRRQQHQSYSSLESRG
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
87UbiquitinationAAFTASEGHAHPRVV
EHHHCCCCCCCCEEE
22.3023503661
111UbiquitinationGFNIMGGKEQNSPIY
CCEECCCCCCCCCEE
50.8523503661
115PhosphorylationMGGKEQNSPIYISRV
CCCCCCCCCEEEEEE
16.6321815630
118PhosphorylationKEQNSPIYISRVIPG
CCCCCCEEEEEECCC
9.0228152594
120PhosphorylationQNSPIYISRVIPGGV
CCCCEEEEEECCCCC
11.9728152594
147PhosphorylationLLSVNGVSVEGEQHE
EEEECCEEECCCHHH
18.8220068231
173PhosphorylationSVKLVVRYTPRVLEE
CEEEEEEECHHHHHH
14.9722210691
174PhosphorylationVKLVVRYTPRVLEEM
EEEEEEECHHHHHHH
8.2822210691
190PhosphorylationARFEKMRSARRRQQH
HHHHHHHHHHHHHHH
23.72-
199PhosphorylationRRRQQHQSYSSLESR
HHHHHHHHHHHHHHC
25.5128796482
200PhosphorylationRRQQHQSYSSLESRG
HHHHHHHHHHHHHCC
8.8428796482
201PhosphorylationRQQHQSYSSLESRG-
HHHHHHHHHHHHCC-
33.4228796482
202PhosphorylationQQHQSYSSLESRG--
HHHHHHHHHHHCC--
28.1128796482

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 LIN7B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIN7B_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 LIN7B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSKP_HUMANCASKphysical
14960569
APBA1_HUMANAPBA1physical
14960569
KCNJ4_HUMANKCNJ4physical
11742811
DLG4_HUMANDLG4physical
10341223
NMDE2_HUMANGRIN2Bphysical
10341223

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIN7B_HUMAN

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Related Literatures of Post-Translational Modification

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