ORB2_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ORB2_DROME
• UniProt AC: Q9VSR3
• Protein Name: Translational regulator orb2
• Gene Name: orb2 {ECO:0000312|EMBL:AAF50350.1}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 704
• Subcellular Localization: Perikaryon . Cell projection, axon . Cell projection, dendrite . Cell junction, synapse . Cytoplasm . Cytoplasm, perinuclear region . In embryonic and larval nervous system, concentrated in the perikaryon (PubMed:21900268). In the adult central nervo
• Protein Description: Required in mushroom body gamma neurons for long-term memory in male courtship. [PubMed: 17965711]
• Protein Sequence: MDSLKLPKANSATSSASGSNSNLSGSTSASASAATSPTSSGTAVGGILSGAPKSPPGLGSSTPISVRFNANEESLDDILQSFHHSKHSPSGGASGGGDASPTSNLLGMKNNGLGLVVGNCDSLSSSPSQPQMHAGSASLFGNDEVSLRNNFMQAGGFFNRKSCGGLPNLNLNKPPQLHQQQHQQQHQQHQQHQQQQQLHQHQQQLSPNLSALHHHHQQQQQLRESGGSHSPSSPGGGGGGSPYNGSQAGCSSGGISPIPPQMGVSPKYRRSISFPIKGNSPTAIYGNMHMDGMGSGHMNIPTLSIGNGGGGGSTGMVSAGATGGGDAPYLGNSYGNMMTSNGQMHHGGGLDNSLCDYMRNMSLGGNGGGDGSNSMSLMQDRMRVMGGPKHLSEADAMAIAASGNDPSVYLNALKMGSPSRLSPHSPHSPIQGGNGGNVGDGTARFSRKVFVGGLPPDIDEDEITTSFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQDESSVQQLIDSCITDEDKLYLCVSSPTIKDKAVQIRPWRLADADYVLDATMSLDPRKTVFVGGVPRPLKAFELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGDIDKRVEVKPYVLDDQMCDECEGQRCGGKFAPFFCANVTCLQYYCEHCWAVIHSRPGREYHKPLVKEGADRPRAVPFRWC

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
54	Phosphorylation	ILSGAPKSPPGLGSS HHCCCCCCCCCCCCC	34.96	19429919
74	Phosphorylation	RFNANEESLDDILQS EECCCCCCHHHHHHH	30.81	19429919
88	Phosphorylation	SFHHSKHSPSGGASG HHHHCCCCCCCCCCC	25.21	19429919
90	Phosphorylation	HHSKHSPSGGASGGG HHCCCCCCCCCCCCC	53.53	19429919
94	Phosphorylation	HSPSGGASGGGDASP CCCCCCCCCCCCCCC	41.04	19429919
100	Phosphorylation	ASGGGDASPTSNLLG CCCCCCCCCCCCCCC	33.19	19429919
102	Phosphorylation	GGGDASPTSNLLGMK CCCCCCCCCCCCCCC	27.96	22668510
103	Phosphorylation	GGDASPTSNLLGMKN CCCCCCCCCCCCCCC	28.94	19429919
271	Phosphorylation	VSPKYRRSISFPIKG CCCCCCCEECCEECC	17.37	19429919
273	Phosphorylation	PKYRRSISFPIKGNS CCCCCEECCEECCCC	26.64	19429919
425	Phosphorylation	PSRLSPHSPHSPIQG CCCCCCCCCCCCCCC	27.91	18327897
428	Phosphorylation	LSPHSPHSPIQGGNG CCCCCCCCCCCCCCC	27.38	10731132

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

Oops, there are no upstream regulatory protein records of ORB2_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ORB2_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 ORB2_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VTU2_DROME	Vm26Ab	physical	15575970
RAD51_DROME	spn-A	physical	15575970
DIMM_DROME	dimm	physical	15575970
PP2B2_DROME	Pp2B-14D	physical	15575970
DFD_DROME	Dfd	physical	15575970
LIMK1_DROME	LIMK1	physical	24523662
FLOT2_DROME	Flo2	physical	24523662
U2AF2_DROME	U2af50	physical	24523662
EIF3I_DROME	Trip1	physical	24523662
LIG_DROME	lig	physical	24913805
PABP2_DROME	Pabp2	physical	24523662
CAB32_DROME	Cbp53E	physical	24523662
ORB2_DROME	orb2	physical	23083740
ORB2_DROME	orb2	physical	24830287
ORB2_DROME	orb2	physical	22284910
ORB2_DROME	orb2	physical	24523662
ORB2_DROME	orb2	physical	26812143
SMG_DROME	smg	physical	26638074
MSIR6_DROME	Rbp6	physical	24523662
OSKA_DROME	osk	physical	26812143
APKC_DROME	aPKC	physical	24830287

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 SER-74; SER-88; SER-100;SER-425 AND SER-428, AND MASS SPECTROMETRY.
PubMed: 18327897