dbPTM

ITA3_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ITA3_DROME
UniProt AC	O44386
Protein Name	Integrin alpha-PS3
Gene Name	scb
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1115
Subcellular Localization	Apical cell membrane Single-pass type I membrane protein. Lateral cell membrane Single-pass type I membrane protein. Cytoplasm. Apical membrane localization in primordial dorsal-appendage cells at oogenesis stages 10B and 11. Later, weakly expresse
Protein Description	Integrin alpha-PS3/beta-PS is a receptor for laminin. Also binds to wb. Important during embryogenesis for the development of the trachea, dorsal vessel and salivary gland, as well as for dorsal closure. Required for short-term memory processes. Minor involvement in the establishment of the oocyte anterior-posterior length. Plays a role in timely border cell migration during oogenesis, probably mediated by JNK signaling. Integrin alpha-PS3/Itgbn 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. Integrin alpha-PS3/Itgbn also regulates Fak activity during neuromuscular junction (NMJ) growth and is required for its activation in presynapsis of NMJs. Seems to be dispensable for major morphogenetic processes..
Protein Sequence	MNAESTMFPHIFLALLALISHIEAFNFMPRPSRVINSPKHLKFHINQTRSSYFGYTLVIRQTSIIVGAPRAQSTLESQRTINETGAIYRCSLTNGVCSPYVLDSRGNVDAPYSEYTFDSERKDFQWLGGSMDGGTKDTDKLLVCAPRFYAPSSRDNHLHGVCYWVNNTVASTPQHVTRISPLRLKSEQVKEEDNGNKASFFYIMGELGLSAHVADDNTKFLIGAPGINTWRGSVILYRQVDPVDNPTASRRDTSKALRRTYRDVDSNDYTPEHYAPEIPTPGLWGQEEDSYFGYAVSSGFFDSSNPTKLLYVATAPQANKQSGEAYIFDVRGKSIHKYHVFRGEQFGEYFGYSVLAEDLNGDGKTDVIVSAPQHALEDSHDNGAIYVFINKGFFNFERQILRSPVETMARFGTALSRLGDINHDGYNDVAVGAPFAGNGTVFIYLGSENGLRDQPSQRLDAPSQQPSKYGSHMFGHGLSRGSDIDGNGFNDFAIGAPNAEAVYLYRAYPVVKVHATVKSESREIKPEQEKVKITACYRLSTTSTDKLVQEQELAIRIAMDKQLKRVKFTQTQTNEISFKVNANFGEQCRDFETQVRYSEKDIFTPIDLEMHYELTKKVPDSEEFCETCAIVDPTEPKVSTQNIIFSTGCATDVCTADLQLRSKDVSPTYILGSADTLRLNYEITNIGETAYLPQFNVTSTSRLAFAQVPGNCKVVDAVMVCDLNRGRPLAKGDTDSVTISFDVSQLSGQSLIIHAEVFSTGYEQNPTDNRQTNVIGLKEFTEIDASGGQTNSQIDLEHYSNSAEIVNNYEIKSNGPSVIEQLTVSFYIPIAYKVAGSTAIIPIINVTSLKMQASYDSQLLSIDLYDQNNTMLVVDPVEVTTTLSGGLERTVITQNRQSYDIHTSGHVHQTMEVLDTSMVATASMSRKRRDLKALTANREQYARISNVKAHDLLSDDFKGKLPVNRTIVFNCRDPEMTICVRAEMRVHFRPEKSINLNMRYSVDLNEVNAILVDPWEYFVILTDLKLQKKGDPTSTSFSINRRIEPNIISKHQETGLPIWIIIVSVIGGLLLLSAISYLLYKFGFFNRTKKDELDRLVQQNPVEPEAENLNSGGNN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
46	N-linked_Glycosylation	KHLKFHINQTRSSYF CEEEEEEECCCCCCC	28.71	-
82	N-linked_Glycosylation	LESQRTINETGAIYR HHHCCCCCCCCCEEE	39.92	17893096
166	N-linked_Glycosylation	HGVCYWVNNTVASTP CEEEEEECCCCCCCC	25.06	-
438	N-linked_Glycosylation	VGAPFAGNGTVFIYL EECCCCCCCEEEEEE	39.26	-
696	N-linked_Glycosylation	TAYLPQFNVTSTSRL CEEECCCCCCCCCEE	30.80	-
845	N-linked_Glycosylation	TAIIPIINVTSLKMQ EEEEEEEECCEEEEE	31.56	-
868	N-linked_Glycosylation	SIDLYDQNNTMLVVD EEEEECCCCCEEEEC	42.94	-
964	N-linked_Glycosylation	FKGKLPVNRTIVFNC CCCCCCCCEEEEEEC	33.18	-

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 ITA3_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ITA3_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 ITA3_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ITBX_DROME	mys	physical	9409675
SOG_DROME	sog	genetic	12835400
SLIT_DROME	sli	genetic	12040052
SLIT_DROME	sli	genetic	16516189
LAMA_DROME	LanA	genetic	12040052
ITBN_DROME	Itgbetanu	physical	23426364

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ITA3_DROME

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82, AND MASS SPECTROMETRY.	19349973 [Abstract]
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster."; Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.; Glycobiology 17:1388-1403(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82, AND MASS SPECTROMETRY.	17893096 [Abstract]