| UniProt ID | RGL3_MOUSE | |
|---|---|---|
| UniProt AC | Q3UYI5 | |
| Protein Name | Ral guanine nucleotide dissociation stimulator-like 3 | |
| Gene Name | Rgl3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 709 | |
| Subcellular Localization | ||
| Protein Description | Guanine nucleotide exchange factor (GEF) for Ral-A. Potential effector of GTPase HRas and Ras-related protein M-Ras. Negatively regulates Elk-1-dependent gene induction downstream of HRas and MEKK1.. | |
| Protein Sequence | MERTAGKELALAPLQDWGEETEDGAVYSVSLRRQRSQRSTPERSGEGQTPIPATDTFLHYRTSKVRALRAARLERLVHELVSGDREQDPGFVPAFLATHRAFVPTARVLGFLLPPPPPPPPPPAGVDSKRTEGQDLNFSKNLRAVVSVLGSWLRNHPQDFRDPPDHQNLGNVRIFLGWAAPGGAEAREAEKLLEDFLKEAKGEQTEEEKRLAWSGPPRIAQTPGSEFAEDCVEEEGPSSEGPELLDFSVDDVAEQLTLMDVELFLRVRSCECLGSMWSQRDRPGAAGISPTVRATVAQFNTVTGCVLGSVLAAPGLAASQRAQRIEKWIRIAQRCRELRNFSSLRAILSALQSNPIYRLKRSWGAVSREPLSVFRKLSQIFSDEDNHLSSRAILSQEETTEDDDCPSGSLPSKLPPGPVPYLGTFLTDLVMLDTALPDTLKGNLINFEKRRKEWEILARIQQLQQRCQRYSLSPRPPILAALRAQRQLSEEQSYRVSRVIEPPAASCPSSPRIRRRISLTKRLSAKLSREKNSSPGGSPGDPSSPTSSVSPGSPPSSPRNREPPPPGSPPASPGPQSPSTKLSLTMDPPGPWPVTLTPSSSRVPLLGQQTSEARVIRVSINNNHGNLYRSILLTCQDKAPSVVQRALEKHNVPQPWARDYQLFQVLPGDRELLIPDGANVFYAMSPAAPGDFLLRRKEGTGHTLSASPT | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 28 | Phosphorylation | TEDGAVYSVSLRRQR CCCCCEEEEEECCHH | 9.91 | 23737553 | |
| 30 | Phosphorylation | DGAVYSVSLRRQRSQ CCCEEEEEECCHHHC | 15.37 | 27555448 | |
| 36 | Phosphorylation | VSLRRQRSQRSTPER EEECCHHHCCCCCCC | 22.93 | - | |
| 140 | Ubiquitination | GQDLNFSKNLRAVVS CCCCCCCHHHHHHHH | 56.73 | 22790023 | |
| 191 | Ubiquitination | AEAREAEKLLEDFLK HHHHHHHHHHHHHHH | 66.47 | 22790023 | |
| 376 | Ubiquitination | EPLSVFRKLSQIFSD CHHHHHHHHHHHCCC | 40.81 | 22790023 | |
| 378 | Phosphorylation | LSVFRKLSQIFSDED HHHHHHHHHHCCCCC | 25.02 | 28973931 | |
| 395 | Phosphorylation | LSSRAILSQEETTED CCHHHHHCCCCCCCC | 29.45 | 28973931 | |
| 471 | Phosphorylation | QQRCQRYSLSPRPPI HHHHHHCCCCCCHHH | 25.26 | 24719451 | |
| 473 | Phosphorylation | RCQRYSLSPRPPILA HHHHCCCCCCHHHHH | 16.96 | 26239621 | |
| 489 | Phosphorylation | LRAQRQLSEEQSYRV HHHHHHCCHHHHCCC | 30.65 | 28973931 | |
| 506 | Phosphorylation | VIEPPAASCPSSPRI ECCCCCHHCCCCHHH | 28.77 | 25521595 | |
| 509 | Phosphorylation | PPAASCPSSPRIRRR CCCHHCCCCHHHHHH | 58.25 | 25521595 | |
| 510 | Phosphorylation | PAASCPSSPRIRRRI CCHHCCCCHHHHHHH | 11.89 | 25521595 | |
| 518 | Phosphorylation | PRIRRRISLTKRLSA HHHHHHHHHHHHHHH | 28.33 | 26824392 | |
| 520 | Phosphorylation | IRRRISLTKRLSAKL HHHHHHHHHHHHHHH | 13.82 | 25367039 | |
| 524 | Phosphorylation | ISLTKRLSAKLSREK HHHHHHHHHHHHHHC | 27.65 | 29514104 | |
| 528 | Phosphorylation | KRLSAKLSREKNSSP HHHHHHHHHHCCCCC | 37.37 | 29514104 | |
| 533 | Phosphorylation | KLSREKNSSPGGSPG HHHHHCCCCCCCCCC | 49.32 | 21183079 | |
| 534 | Phosphorylation | LSREKNSSPGGSPGD HHHHCCCCCCCCCCC | 36.64 | 28973931 | |
| 538 | Phosphorylation | KNSSPGGSPGDPSSP CCCCCCCCCCCCCCC | 31.46 | 29472430 | |
| 543 | Phosphorylation | GGSPGDPSSPTSSVS CCCCCCCCCCCCCCC | 54.40 | 23140645 | |
| 544 | Phosphorylation | GSPGDPSSPTSSVSP CCCCCCCCCCCCCCC | 37.27 | 29472430 | |
| 546 | Phosphorylation | PGDPSSPTSSVSPGS CCCCCCCCCCCCCCC | 35.27 | 26239621 | |
| 547 | Phosphorylation | GDPSSPTSSVSPGSP CCCCCCCCCCCCCCC | 31.93 | 23140645 | |
| 548 | Phosphorylation | DPSSPTSSVSPGSPP CCCCCCCCCCCCCCC | 29.14 | 23140645 | |
| 550 | Phosphorylation | SSPTSSVSPGSPPSS CCCCCCCCCCCCCCC | 26.03 | 26643407 | |
| 553 | Phosphorylation | TSSVSPGSPPSSPRN CCCCCCCCCCCCCCC | 36.70 | 25521595 | |
| 556 | Phosphorylation | VSPGSPPSSPRNREP CCCCCCCCCCCCCCC | 57.25 | 21082442 | |
| 557 | Phosphorylation | SPGSPPSSPRNREPP CCCCCCCCCCCCCCC | 33.38 | 25521595 | |
| 568 | Phosphorylation | REPPPPGSPPASPGP CCCCCCCCCCCCCCC | 33.22 | 25521595 | |
| 572 | Phosphorylation | PPGSPPASPGPQSPS CCCCCCCCCCCCCCC | 35.84 | 25521595 | |
| 577 | Phosphorylation | PASPGPQSPSTKLSL CCCCCCCCCCCCEEE | 24.77 | 27087446 | |
| 579 | Phosphorylation | SPGPQSPSTKLSLTM CCCCCCCCCCEEEEC | 43.34 | 26239621 | |
| 580 | Phosphorylation | PGPQSPSTKLSLTMD CCCCCCCCCEEEECC | 39.11 | 26239621 | |
| 600 | Phosphorylation | PVTLTPSSSRVPLLG CEEECCCCCCCCCCC | 24.30 | - | |
| 700 | Phosphorylation | LLRRKEGTGHTLSAS EEEECCCCCCCCCCC | 27.21 | 23737553 | |
| 703 | Phosphorylation | RKEGTGHTLSASPT- ECCCCCCCCCCCCC- | 24.61 | 23737553 | |
| 705 | Phosphorylation | EGTGHTLSASPT--- CCCCCCCCCCCC--- | 28.05 | 23737553 | |
| 707 | Phosphorylation | TGHTLSASPT----- CCCCCCCCCC----- | 26.20 | 25521595 | |
| 709 | Phosphorylation | HTLSASPT------- CCCCCCCC------- | 49.07 | 23737553 |
| 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 RGL3_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RGL3_MOUSE !! | ||||||
* 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 RGL3_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RIT1_MOUSE | Rit1 | physical | 10869344 | |
| RASH_MOUSE | Hras | physical | 10869344 | |
| RALB_MOUSE | Ralb | physical | 10869344 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506; SER-510; SER-568AND SER-572, AND MASS SPECTROMETRY. | |