UniProt ID | RG92B_DROME | |
---|---|---|
UniProt AC | Q9VDS5 | |
Protein Name | Rho GTPase-activating protein 92B | |
Gene Name | RhoGAP92B | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 740 | |
Subcellular Localization | ||
Protein Description | GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.. | |
Protein Sequence | MKRQFAKIKIAAENLSRSSKSDSKDSELEAIERQVDRYRDTIEKIVRKLPALSGGGGSGSGSSEEQDKRTKKNSHYKIAQALDESAKELPKDMPLQKVLANCGELEKTMAECIIESELETEAKVVRRLKNILDKEIQEISTLKRNVSRTLQEYTSLKRSHEAAIRLEEPAAKVNHIKSQQEECELKLEKERDAWAAQMLELIAKEDEIVSCIRDYVLNQRNYHERALQHVNASLARIQDTIQGTEKSRFGTSLKEHLTSTNREISYIVELCCCCLLEHGLEEEGLLRVGCASTKLRRMKHALEAQHVKTPLPLDYQDPHVIGSILKLYLRELPEPLLTYNLYKDFIRIAERHSEAERKTEIKAILTKLPKENYANLRYLTRFLSIVQQRSALNKMSSQNLAIVMSPNMLWPRIDKSSNAPADYIGQVNSSSAANIIVELLISQWDYFFIGEVEFYLTLQKQKLFVEGKSKSNSSNENLDRNDSEVMESPRYGTLRRQKANAPSPPTTNGNGIIMTTSQTSHRPHAKELFPQQTPEKQEKPAKPPLPNLPQFQSPAASQPTQTQLEPLPPPPVTPAKPVPMTRTQFFGLDNLPSPTADRKSTDSIGSFKLKPDVPQKPLLPKRPTVLGVGVPKADGKSDDEGGTTPTQATIDNGNGSVRFKTEHFLDKLRQENGETNGTREVSSTTKENNHNHDPPATAADQNQQQAQPQVTTPISPNSFQTPKRPTVPAPPPPTNWKSSD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
58 | Phosphorylation | ALSGGGGSGSGSSEE HHCCCCCCCCCCHHH | 32.82 | 19429919 | |
60 | Phosphorylation | SGGGGSGSGSSEEQD CCCCCCCCCCHHHHH | 36.88 | 19429919 | |
62 | Phosphorylation | GGGSGSGSSEEQDKR CCCCCCCCHHHHHHH | 35.95 | 19429919 | |
63 | Phosphorylation | GGSGSGSSEEQDKRT CCCCCCCHHHHHHHH | 48.99 | 19429919 | |
323 | Phosphorylation | QDPHVIGSILKLYLR CCHHHHHHHHHHHHH | 17.39 | 21082442 | |
469 | Phosphorylation | KLFVEGKSKSNSSNE EEEEECCCCCCCCCC | 52.77 | 22817900 | |
471 | Phosphorylation | FVEGKSKSNSSNENL EEECCCCCCCCCCCC | 49.38 | 19429919 | |
473 | Phosphorylation | EGKSKSNSSNENLDR ECCCCCCCCCCCCCC | 41.45 | 19429919 | |
474 | Phosphorylation | GKSKSNSSNENLDRN CCCCCCCCCCCCCCC | 53.03 | 19429919 | |
483 | Phosphorylation | ENLDRNDSEVMESPR CCCCCCHHHHHHCCC | 35.32 | 19429919 | |
488 | Phosphorylation | NDSEVMESPRYGTLR CHHHHHHCCCCCCCC | 9.15 | 19429919 | |
593 | Phosphorylation | FGLDNLPSPTADRKS ECCCCCCCCCCCCCC | 37.74 | 19429919 | |
595 | Phosphorylation | LDNLPSPTADRKSTD CCCCCCCCCCCCCCC | 45.59 | 19429919 | |
600 | Phosphorylation | SPTADRKSTDSIGSF CCCCCCCCCCCCCCC | 38.04 | 19429919 | |
601 | Phosphorylation | PTADRKSTDSIGSFK CCCCCCCCCCCCCCC | 36.48 | 19429919 | |
603 | Phosphorylation | ADRKSTDSIGSFKLK CCCCCCCCCCCCCCC | 29.01 | 19429919 | |
606 | Phosphorylation | KSTDSIGSFKLKPDV CCCCCCCCCCCCCCC | 19.96 | 19429919 | |
624 | Phosphorylation | PLLPKRPTVLGVGVP CCCCCCCCEEEECCC | 32.18 | 19429919 | |
637 | Phosphorylation | VPKADGKSDDEGGTT CCCCCCCCCCCCCCC | 56.68 | 19429919 | |
643 | Phosphorylation | KSDDEGGTTPTQATI CCCCCCCCCCCEEEE | 40.22 | 19429919 | |
644 | Phosphorylation | SDDEGGTTPTQATID CCCCCCCCCCEEEEE | 27.84 | 19429919 | |
646 | Phosphorylation | DEGGTTPTQATIDNG CCCCCCCCEEEEECC | 28.83 | 19429919 | |
649 | Phosphorylation | GTTPTQATIDNGNGS CCCCCEEEEECCCCE | 21.03 | 19429919 | |
656 | Phosphorylation | TIDNGNGSVRFKTEH EEECCCCEEEEEHHH | 17.70 | 19429919 | |
712 | Phosphorylation | QAQPQVTTPISPNSF HCCCCCCCCCCCCCC | 21.55 | 19429919 | |
715 | Phosphorylation | PQVTTPISPNSFQTP CCCCCCCCCCCCCCC | 21.16 | 19429919 | |
718 | Phosphorylation | TTPISPNSFQTPKRP CCCCCCCCCCCCCCC | 23.32 | 19429919 | |
721 | Phosphorylation | ISPNSFQTPKRPTVP CCCCCCCCCCCCCCC | 28.85 | 19429919 | |
738 | Phosphorylation | PPPTNWKSSD----- CCCCCCCCCC----- | 31.21 | 18327897 | |
739 | Phosphorylation | PPTNWKSSD------ CCCCCCCCC------ | 43.54 | 18327897 |
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 RG92B_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RG92B_DROME !! |
* 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 RG92B_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RL4_DROME | RpL4 | physical | 14605208 | |
NANOS_DROME | nos | physical | 14605208 | |
ELOA1_DROME | EloA | physical | 14605208 | |
DTBP1_DROME | Dysb | physical | 14605208 | |
TBB1_DROME | betaTub56D | physical | 14605208 | |
60A_DROME | gbb | genetic | 21041451 | |
CDC42_DROME | Cdc42 | physical | 23468526 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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-469; SER-473; SER-715;THR-721; SER-738 AND SER-739, AND MASS SPECTROMETRY. | |
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593 AND THR-595, ANDMASS SPECTROMETRY. |