EXPA_DROME - dbPTM
EXPA_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXPA_DROME
UniProt AC Q07436
Protein Name Protein expanded
Gene Name ex
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1427
Subcellular Localization Apical cell membrane . Apical surface of disk cells.
Protein Description Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. Ex acts synergistically along with Mer and Kibra to regulate the Hippo signaling pathway. Involved in the control of cell proliferation in imaginal disks. May bind to certain proteins of signal transduction pathways by interaction with their SH3 domains. [PubMed: 20159598 Required for apical localization of Schip1]
Protein Sequence MRAFCTVSAPLEVCASSAEQLSPGSRFLALRLLGQQQPKTLYFLVDAKSRVREVYTQTCLHFATQGMLDTELFGLAVLIDGEYMFADPESKLSKYGPKSWRSSHTHGLDANGRPLLELHFRVQFYIESPFMLKDETSRHNYYLQLRHNILQRDLPREQAEQALVFLAGLALQADLGDAPPGTSNSKDDSGEETSASPSNGGRGLSATTTLPKISKRANERMLRLSTYVASTSKRETIPLPPSLPPNGADYYRIEDYLPSGLHTPWARSAMRACHREHLGMATAEAELLYIQQACSLHETINAHTYRMRLAKSEQGSGSAWFVVYAKGIKILGGESTNSSSNPETTTFLWPNITKLSFERKKFEIRSGESRITLYAASDEKNKLLLTLCKDTHQWSMKLAARLKEVSKREEEEAAESQRLHASYACSRSLLLPYKSKNEQRISVISSTSSNTTSGIVSDRVHSEDELEIMINTPPAPLAAPSTESLALAHLLDRPSVSRQTSSVGQMSLKDLEEQLAALSVRPQDASSNGATIVTNSSVQRNSMGTTANDSSTATDSPSSQHNIGSQCSSTCSTVVVTSPVNGAGASSSGAPIPVHSTSSSLELGFSHTAQNSALSETSPDDFLSTSAREETESVSGASGVYTLAHGAPPTETSGVYTMHSSELTGQSSEIAESEKSSHYGMFQPQKLEETHVQHSDSVDGKKKEDFRPRSDSNVSTGSSFRGDGSDPTDNKHSLLSAEELTNLIVGRGTYPSRKTVSSSLHSDCDYVTLPLGDQGEEEVDQPPAPPPPYSARHEKTGLCGPPIAKPIPKPIAVVAPKPDSPPCSPPVPPAPIPAPPPAIRRRDPPPYSISSKPRPTSLISVSSSAHPAPSAAGSMSSLKSEEVTARFITTRPQISILKAHTSLIPDGAKPSYAAPHHCSSVASSNGSVCSHQLSQQSLHNSNYAGGSQASLHHHHVPSHHRHSGSAAIGIVPYGLHKSTASLHHQQSCVLLPVIKPRQFLAPPPPSLPRQPPPPPPPNHPHLASHLYEREMARKQLELYQQQLYSDVDYVIYPIQDPAVSQQEYLDAKQGSLLAAMAQAAPPPPHHPYLAMQVSPAIYRSTPYLPLTLSTHSRYASTQNLSDTYVQLPGPGYSPLYSPSMASLCSSYEPPPPPPLHPAALAAAAAAGAGSSSSSMFARSRSDDNILNSLDLLPKGKRLPPPPPPPYVNRRLKKPPMPAPSEKPPPIPSKPIPSRMSPIPPRKPPTLNPHHANSPLTKTSSGAQWAGERPRPDLGLGLGLNRGNNSILAQLQASMVAQSHAQAQAQALDIALLREKSKHLDLPLISALCNDRSLLKQTKVVINPKTGQEMPTSSAQPSGATTNGVANSSAGAGTLSKARKGSTVSHRHPQDKLPPLPVQQLAEANNYVIDPAVMMKQQQQQQQHNKTS
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
227PhosphorylationRMLRLSTYVASTSKR
HHHHHHHHHHCCCCC		7.2227462444
423PhosphorylationSQRLHASYACSRSLL
HHHHHHHHHHCCHHC		16.6527462444
428PhosphorylationASYACSRSLLLPYKS
HHHHHCCHHCCCCCC		13.6921082442
500PhosphorylationRPSVSRQTSSVGQMS
CCCCCCCCCCCCCCC		23.1222817900
501PhosphorylationPSVSRQTSSVGQMSL
CCCCCCCCCCCCCCH		18.0622817900
679PhosphorylationESEKSSHYGMFQPQK
HHHHHCCCCCCCCHH		16.5427462444
766PhosphorylationSLHSDCDYVTLPLGD
CCCCCCCEEEEECCC		11.1527462444
963PhosphorylationVPSHHRHSGSAAIGI
CCCCCCCCCCCEEEE		34.1119429919
965PhosphorylationSHHRHSGSAAIGIVP
CCCCCCCCCEEEEEC		19.9719429919
981PhosphorylationGLHKSTASLHHQQSC
CCCCCCCCCCCCCEE		28.4622817900
1100PhosphorylationVSPAIYRSTPYLPLT
CCHHHHCCCCCCCEE		19.4321082442
1101PhosphorylationSPAIYRSTPYLPLTL
CHHHHCCCCCCCEEE		13.6221082442
1103PhosphorylationAIYRSTPYLPLTLST
HHHCCCCCCCEEEEE		22.5027462444
1179PhosphorylationSSSMFARSRSDDNIL
HHHHHCCCCCCCCHH		32.4819429919
1181PhosphorylationSMFARSRSDDNILNS
HHHCCCCCCCCHHHH		51.0319429919
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 EXPA_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXPA_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 EXPA_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYC_DROMEdmgenetic
20885789
AJUBA_DROMEjubgenetic
21666802
SCAL_DROMEsdgenetic
23725764
MERH_DROMEMergenetic
10683183
WNTG_DROMEwggenetic
17258190
HIPPO_DROMEhpogenetic
16341207
KIBRA_DROMEkibragenetic
20159598
KIBRA_DROMEkibragenetic
23733343
KIBRA_DROMEkibragenetic
20159599
WARTS_DROMEwtsgenetic
16341207
WARTS_DROMEwtsgenetic
16980976
SAV_DROMEsavphysical
20159598
CH60_DROMEHsp60physical
24114784
NONA_DROMEnonAphysical
24114784
EXPA_DROMEexphysical
10683183
CUL1_DROMECul1physical
24778256
DRK_DROMEdrkphysical
24114784
HIPPO_DROMEhpophysical
20159598
YAP1_DROMEykiphysical
19289086
LONM_DROMELonphysical
24114784
KIBRA_DROMEkibraphysical
20159598
CRB_DROMEcrbphysical
24778256
RAN_DROMERanphysical
24114784
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EXPA_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1181, AND MASSSPECTROMETRY.

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