CTNA_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CTNA_DROME
• UniProt AC: P35220
• Protein Name: Catenin alpha
• Gene Name: alpha-Cat {ECO:0000312|FlyBase:FBgn0010215}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 917
• Subcellular Localization: Cytoplasm, cytoskeleton. Cell junction, adherens junction . Cell membrane ; Peripheral membrane protein; Cytoplasmic side. Cell junction. Found only at cell-cell boundaries.
• Protein Description: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties..
• Protein Sequence: MLKPDKMGTLTDFGQIALKWDPKNLEIRTMSVEKTLEPLVLQVTTLVNTKGPSKKKKGKSKRASALVAAVEKATENFIQKGEQIAYENPDITQEMLTAVDEVKKTGDAMSIAAREFSEDPCSSLKRGNMVRAARNLLSAVTRLLILADMVDVHLLLKSLHIVEDDLNKLKNASSQDELMDNMRQFGRNAGELIKQAAKRQQELKDPQLRDDLAAARAMLKKHSTMLLTASKVYVRHPELDLAKVNRDFILKQVCDAVNTISDVAQGKSSQPTDIYSGAGELAAALDDFDEGIVMDPMTYSEKRSRQLLEERLESIISAAALMADADCTRDERRERIVAECNAVRQALQDLLSEYMSNMSQKDNSPGLSRAIDQMCRKTRDLRRQLRKAVVDHVSDSFLETTTPLLDLIEAAKSGNEKKVREKSEIFTKHAEKLVEVANLVCSMSNNEDGVKMVRYAAAQIESLCPQVINAASILTVRPNSKVAQENMTTYRQAWEVQVRILTEAVDDITTIDDFLAVSENHILEDVNKCVMALQVGDARDLRATAGAIQGRSSRVCNVVEAEMDNYEPCIYTKRVLEAVKVLRDQVMMKFDQRVGAAVGALSNNSNKDVDENDFIDASRLVYDGVREIRRAVLMNRSSEDLDTDTEFEPVEDLTLETRSRSSAHTGDQTVDEYPDISGICTAREAMRKMTEEDKQKIAQQVELFRREKLTFDSEVAKWDDTGNDIIFLAKHMCMIMMEMTDFTRGRGPLKTTMDVINAAKKISEAGTKLDKLTREIAEQCPESSTKKDLLAYLQRIALYCHQIQITSKVKADVQNISGELIVSGLDSATSLIQAAKNLMNAVVLTVKYSYVASTKYTRQGTVSSPIVVWKMKAPEKKPLVRPEKPEEVRAKVRKGSQKKVQNPIHALSEFQSPADAV

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
31	Phosphorylation	NLEIRTMSVEKTLEP CCEEEEEEHHHCCCC	26.89	27794539
637	Phosphorylation	RAVLMNRSSEDLDTD HHHHCCCCCCCCCCC	32.83	19429919
638	Phosphorylation	AVLMNRSSEDLDTDT HHHCCCCCCCCCCCC	31.71	19429919
643	Phosphorylation	RSSEDLDTDTEFEPV CCCCCCCCCCCCEEH	52.71	19429919
645	Phosphorylation	SEDLDTDTEFEPVED CCCCCCCCCCEEHHH	44.67	29892262
659	Phosphorylation	DLTLETRSRSSAHTG HCEEEECCCCCCCCC	43.89	22817900
662	Phosphorylation	LETRSRSSAHTGDQT EEECCCCCCCCCCCC	23.98	22817900
665	Phosphorylation	RSRSSAHTGDQTVDE CCCCCCCCCCCCHHC	42.02	22817900

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CTNA_DROME !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CTNA_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CADE_DROME	shg	genetic	22266901
ARP3_DROME	Arp3	genetic	22266901
ARM_DROME	arm	physical	12134162
ARM_DROME	arm	physical	23417122
ARM_DROME	arm	physical	25653389
ARM_DROME	arm	physical	7958432
ARM_DROME	arm	physical	8501118
ARM_DROME	arm	physical	8943306
CADN_DROME	CadN	physical	9247265
CADE_DROME	shg	physical	23417122
CADE_DROME	shg	physical	7958432
CTNA_DROME	alpha-Cat	physical	23417122

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-643; THR-645; SER-659AND SER-662, AND MASS SPECTROMETRY.
PubMed: 18327897