VIR_DROME - dbPTM
VIR_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VIR_DROME
UniProt AC Q9W1R5
Protein Name Protein virilizer {ECO:0000303|PubMed:11156988}
Gene Name vir {ECO:0000303|PubMed:11156988, ECO:0000312|FlyBase:FBgn0003977}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1854
Subcellular Localization Nucleus .
Protein Description Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of mRNAs, a modification that plays a role in the efficiency of mRNA splicing and is required for sex determination. [PubMed: 27919077 Required for sex determination and dosage compensation via Sxl alternative splicing: m6A methylation acts as a key regulator of Sxl pre-mRNA and promotes female-specific alternative splicing of Sxl, which determines female physiognomy]
Protein Sequence MADVDDGSELLFFDTFSHEEVTDINLDLVQFPKPVFITQVRIIPLGARVQADFPGGVRLGATNPSKFDLEFFVNDLGMPAASAFENLGLLRYNQNDCIHLDCSQEKIVTDGLVLRGWYSTITLAIYGIFTNSVTEPIASPTLPCEPVGPEIANLSGEVLLQEDVLKDEWQEPMQAELLTAHKGNVSDYDPEDMEYGMSRDHYHQHAEEQEQREMRRLRRSTHSTDHSPPPPRRSHTHSESNDREYIRCSRDKGSRDWSRSPEYSSHRSRRKRSERSRSVVDEHKWPRTPPASIDSPTRPRSPDTMDYEDEDSRSHYKMQSSHYRHSSESLHRGERDRDDEDRSCTPQEQFEPILSDDEIIGDDEEDDAVDAAAIAEYERELEAAAAAAPPAIDAFEPWQKPLLVFEGDMAAHFCKELETLKLLFKKLVLQTRCENVNAFSEEHGASVDEREQFVYLGEQLNNQLGYLAQHYKRRNFVLQQFFGNDELHLRQAANVLQIALSFQAACMQPQPAFKIRHIKLGARMAELLGSSEELFQHLLKEHKFDIFEAVFRLYHEPYMALSIKLQLLKAVYALLDTRMGIEHFMGAKNNGYQMIVEAIKTAKLTRTKYALQAIIKKLHLWEGLESVQIWCRRLFVDRIIIPGNRDQMEDTVITCQQIEFAFEMLMDALFSSQLSYLQPRRFLPVSKKFEVVTDPTAQRSFGNALQSYLGQNSLAESLLVMLANCKELPATTYLSMLDLMHTLLRSHVGIDYFVDDAFPVTQTIVAILLGLDEVPRNPEEKEEKAEKSDAEDKAMEVENEAVEAGGEKPTPPTADEEGKPVAAPISVPAPAAAPQVRPRPILRPVLPRLARLGIEMSYKVQTRYHLDAIAYAAAAPEYDAVKLATHMHAIYSQTCDPAGRQHTVEVLGLNNNLKIFMDLIKKEQRLQTQRQLSSPGTKYKSPVLSYAVDMVDACVRYCEQLDYLIEHGGVILELAKNHETFEPSVSAVLQEMYVYMKPLEAINVFVYDDIMPLVEVIGRSLDYLTTFPGDLIMAMRILRYLSISKPLAGQKAPPVTEELKHRFVALQLYAADGVQLCIQIMERLCAYFEQPGAHAPALMTIQGVHCCQIMLPTLQILRELLSYAILCRDGTYKDLTAIDHLVKVYYLLYYFPTRCQAGPEVEQCKMEVVQTLLAYTQPNEQDEESLHKSLWTLMIREVLKNVDGPAHFIPGLKLLAELLPLPLPMPQPLCDQLQQQHKQRLITERKLWSAHLHPQSGQIAKLVEALAPSSFPQLSELLQRVCMQLSDLAPNMTLLIAKTITELLCNEYQTSNCIPTTNLERLLRFSTRLCAFAPLKSSMLSILSGKFWELFQSLLALNEFNDVVSNCQEAVHRILDSFLDSGISLISHKSTASPALNLAAALPPKELIPRIIDAVFSNLTSVEVTHGISILAVRNLVILTEHDFTFYHLAQLLKQKITEFQAWMERVILHNETVEYNANIESLILLLRSLTQIEPPPAMSAMPHRTLKLGATELAQLVEFQDIELAKPPVLSRILTVMEKHKAVANEAALSDLKQLILLQASKQEILAGTSTETPPEAEGEANPSASSCSASLTVEPYLPQAEGIVTQYEARPIFTRFCATAENAQLTARYWLDPLPIELIEDMNEPIYERIACDLTDLANVCLNPDLNVAGDSKRVMNLSGSPQSNREMTPTAPCFRTRRVEVEPATGRPEKKMFVSSVRGRGFARPPPSRGDLFRSRPPNTSRPPSLHVDDFLALETCGAQPTGPTGYNKIPSMLRGSRVGRNRGSRISAAAAFRQKKMMRIGSPSSWAESPGSYRSASDSHFSSSDSHYSSPHYSGRPRGRGLRSRPSYLR
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
186PhosphorylationTAHKGNVSDYDPEDM
HHCCCCCCCCCHHHH		34.1622817900
221PhosphorylationMRRLRRSTHSTDHSP
HHHHHHHHCCCCCCC		20.3121082442
223PhosphorylationRLRRSTHSTDHSPPP
HHHHHHCCCCCCCCC		35.3021082442
227PhosphorylationSTHSTDHSPPPPRRS
HHCCCCCCCCCCCCC		41.7425749252
238PhosphorylationPRRSHTHSESNDREY
CCCCCCCCCCCCHHH		43.8222668510
258PhosphorylationDKGSRDWSRSPEYSS
CCCCCCCCCCCCHHH		27.4619429919
260PhosphorylationGSRDWSRSPEYSSHR
CCCCCCCCCCHHHHH		19.3019429919
276PhosphorylationRRKRSERSRSVVDEH
HHHHHHHHCHHCCCC		25.5119429919
278PhosphorylationKRSERSRSVVDEHKW
HHHHHHCHHCCCCCC		27.9519429919
288PhosphorylationDEHKWPRTPPASIDS
CCCCCCCCCCCCCCC		29.5522817900
292PhosphorylationWPRTPPASIDSPTRP
CCCCCCCCCCCCCCC		32.4722817900
295PhosphorylationTPPASIDSPTRPRSP
CCCCCCCCCCCCCCC		26.8822817900
297PhosphorylationPASIDSPTRPRSPDT
CCCCCCCCCCCCCCC		58.2022817900
301PhosphorylationDSPTRPRSPDTMDYE
CCCCCCCCCCCCCCC		29.7919429919
304PhosphorylationTRPRSPDTMDYEDED
CCCCCCCCCCCCCCC		18.4819429919
307PhosphorylationRSPDTMDYEDEDSRS
CCCCCCCCCCCCHHH		17.9222668510
312PhosphorylationMDYEDEDSRSHYKMQ
CCCCCCCHHHHCHHH		33.3719429919
326PhosphorylationQSSHYRHSSESLHRG
HHHHCCCCHHCCCCC		27.1419429919
327PhosphorylationSSHYRHSSESLHRGE
HHHCCCCHHCCCCCC		25.6919429919
329PhosphorylationHYRHSSESLHRGERD
HCCCCHHCCCCCCCC		31.2719429919
933PhosphorylationLQTQRQLSSPGTKYK
HHHHHHHCCCCCCCC		26.5827626673
1681PhosphorylationSKRVMNLSGSPQSNR
CCCCCCCCCCCCCCC		32.0219429919
1683PhosphorylationRVMNLSGSPQSNREM
CCCCCCCCCCCCCCC		19.1819429919
1686PhosphorylationNLSGSPQSNREMTPT
CCCCCCCCCCCCCCC		41.0419429919
1693PhosphorylationSNREMTPTAPCFRTR
CCCCCCCCCCCCCCE		33.7827626673
1806PhosphorylationKKMMRIGSPSSWAES
HCCHHCCCCHHHCCC		21.1622817900
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 VIR_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VIR_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 VIR_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SDHF4_DROMESirupphysical
14605208
U2QL1_DROMECG4502physical
14605208
BICC_DROMEBicCphysical
14605208
RL36_DROMERpL36physical
14605208
MSL2_DROMEmsl-2genetic
8575302
MSL1_DROMEmsl-1genetic
8575302
MLE_DROMEmlegenetic
8575302
SXL_DROMESxlgenetic
8575302
FL2D_DROMEfl(2)dphysical
27919077
MTA70_DROMEIme4physical
27919077
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VIR_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-186; SER-258; SER-260;SER-276; THR-288; SER-295; THR-297; SER-301 AND SER-312, AND MASSSPECTROMETRY.

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