ITBN_DROME - dbPTM
ITBN_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITBN_DROME
UniProt AC Q27591
Protein Name Integrin beta-nu
Gene Name Itgbn {ECO:0000312|FlyBase:FBgn0010395}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 799
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Contributes to endodermal integrity and adhesion between the midgut epithelium and the surrounding visceral muscle. Essential for migration of the primordial midgut cells and for maintaining, but not establishing, cell polarity in the midgut epithelium. Can only partially compensate for the loss of beta-PS integrin during primordial midgut cell migration. The two beta subunits mediate midgut migration by distinct mechanisms: beta-PS requires rhea/Talin and beta-nu does not. Integrin alpha-PS3/beta-nu is required for effective phagocytosis of apoptotic cells during embryonic development and for the phagocytic elimination of S.aureus by mediating the binding of S.aureus peptidoglycan to larval hemocytes, which probably activates a signaling pathway involving Rac1 and Rac2. Not required for the production of antimicrobial peptides during S.aureus. Upon activation by LanA, integrin alpha-PS3/beta-nu activates Fak in presynapsis to suppress neuromuscular junction (NMJ) growth during larval development and during low crawling activity, but not during higher-crawling conditions. Mediates, together with LanA, glutamate receptor-modulated NMJ growth..
Protein Sequence MTSLGGRAFLWIYLVFLIAEISHSDADSIDDQCRHADSCERCLSAHLECAWCTDKEYQVGYRCLSRRQLLNYNCSETDIYENQPVLDVLQDKPLKDYETSDQAVQVTPQRAYLKLVKGNTQRMKLSYRTARNNPLDLYVLMDLTWTMRDDKKTLEELGAQLSQTLKNLTGNYRLGFGSFADKPTLPMILPQHRENPCAAERATCEPTYGYRHQLSLTDDIPAFTSAVANSKITGNLDNLEGGLDALMQVIVCTKEIGWKEQARKVVILVTDGFMHLAGDGLLAGIIQRNDKQCHLNKAGEYTGSLNYDYPSLEEIYRELLRRKINVIFAVTEEVVSSYWELSALMKEISYVDILSADSSNILELIKKSYESLIKRTQFADNSPDFIDMAYYTDCGGQFPSLQKRNYCNNVTLGKQIDFYVDVTLKKYPDNQVYTHKIRVEETSLSEFMDLDVELQRPCPCQETPDPENEEGRFLCDYKGYLYCGMCECDEGWTGTYCNCPTDATNVTSNEALLQKCRQPFSDKSTSELVCSNHGDCDCGTCLCDPGYTGPFCECRECLDCDEKLADCFCGQCVCKYGWSGSKCNCDGDTDACVGPTGEICSERGTCQCEECQCEEPYLGKFCEIDPEKDNKLCLFYEPCVTCLIEQKQGMGVCENLTEICSSLDRQETYPYNFVHELDPEQDQCLVRLVNKHGIQCDSFFVYQVIDHSNFLTIQAVDCEPPDYVALVGYISAFTLLIGLLIIFIILWYIRAKDAREYAKFEEDQKNSVRQENPIYRDPVGRYEVPKALSVKYDENPFAS
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
73N-linked_GlycosylationRRQLLNYNCSETDIY
HHHHHCCCCCCCCCC
23.05-
167N-linked_GlycosylationQLSQTLKNLTGNYRL
HHHHHHHHHHCCCEE
46.04-
409N-linked_GlycosylationQKRNYCNNVTLGKQI
CCCCCCCCCCCCCCE
25.29-
505N-linked_GlycosylationNCPTDATNVTSNEAL
CCCCCCCCCCCCHHH
36.47-
655N-linked_GlycosylationQGMGVCENLTEICSS
CCCCHHCHHHHHHHC
47.32-

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 ITBN_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 ITBN_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITA3_DROMEscbphysical
23426364

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

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Related Literatures of Post-Translational Modification

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