UniProt ID | RIMB2_MOUSE | |
---|---|---|
UniProt AC | Q80U40 | |
Protein Name | RIMS-binding protein 2 | |
Gene Name | Rimbp2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 1072 | |
Subcellular Localization | Cell membrane. Cell junction, synapse. Synaptic plasma membrane.. | |
Protein Description | Plays a role in the synaptic transmission as bifunctional linker that interacts simultaneously with RIMS1, RIMS2, CACNA1D and CACNA1B.. | |
Protein Sequence | MREAAERRQQLELEHEQALAFLNAKQQEIQLLQQAQVEAKKEHEGAVQLLESKVRELEEKCRVQSEQFNLLSRDLEKFRQHTGSIDLLGSSSVALLDVPLAPGKPFPQYMNGLATSIHKGHEGPTGHYSVIGDYIPLSGDKLESPCVKPSFLLRSSSPRCRFESEMDNDRNSNNSKQSSSGKVHLCVARYSYNPFDGPNENPEAELPLTAGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVDFIQDNESRLAGTLGSEQDQNFLNHSGISLERDSILHLHSPTQVDSGITDNGGGTLDVNIDDIGEDTVPYPRKITLIKQLAKSVIVGWEPPAVPPGWGTVSSYNVLVDKETRMSLALGRRTKALIEKLNTAACTYRISVQCVTSRGNSDELQCTLLVGKDVVVAPSQLRVDNITQISAQLSWLPTNSNYSHIIFLNEEELDIVKAARYKYQFFNLRPNMAYKVKVLAQPHQMPWQLPLEQREKKEACVEFSTLPAGPPAPPQDVTVHAGATAASVQVSWKPPALTPTGLSNGANVTGYGVYAKGQRVAEVIAPTADGTAVELIRLRSLEAKAVSVRTLSVQGESMDSALAAIPPDLLVPPAPHPRTAPPPKPLASDMDTKDQHLGPHVKVDESWEQSRSPGPAHGHMLEPPDMHSAGPGRRSPSPSRILPQPQGAPVSTTVAKAMAREAAQRVAESNRLEKRSLFLEQSSAGQYTNSDEEDGYASPEVKRRGTSVDDFLKGSELGKQPHCCHGDEYHTESSRGSDLSDIMEEDEEELYSEMQLEDGGRRRPSGTSHNALKILGNSTLMGRADRMEHVSRRYSHSGGGSHRHRPAMAPSIDEYTGRDHLSPDFYDESETDPGAEELPARIFVALFDYDPLTMSPNPDAAEEELPFKEGQIIKVYGDKDADGFYRGETCARLGLIPCNMVSEIHADDEEMMDQLLRQGFLPLNTPVEKIERSRRSGRGHSVPTRRMVALYDYDPRESSPNVDVEAELPFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEEVPDDVEVHLSDAPPHYSHDPPMRSKAKRKKSVHFTP | |
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 |
---|---|---|---|---|---|
269 | Phosphorylation | DQNFLNHSGISLERD HHHHHHCCCCCCCCC | 36.43 | 29899451 | |
272 | Phosphorylation | FLNHSGISLERDSIL HHHCCCCCCCCCCEE | 27.92 | 25159016 | |
283 | Phosphorylation | DSILHLHSPTQVDSG CCEEECCCCCEECCC | 35.68 | 29899451 | |
381 | Phosphorylation | AACTYRISVQCVTSR CCCCEEEEEEEEECC | 9.35 | 19367708 | |
667 | Phosphorylation | GPGRRSPSPSRILPQ CCCCCCCCHHHCCCC | 36.43 | 29899451 | |
669 | Phosphorylation | GRRSPSPSRILPQPQ CCCCCCHHHCCCCCC | 35.97 | 29899451 | |
681 | O-linked_Glycosylation | QPQGAPVSTTVAKAM CCCCCCCHHHHHHHH | 19.80 | 22517741 | |
683 | O-linked_Glycosylation | QGAPVSTTVAKAMAR CCCCCHHHHHHHHHH | 15.80 | 22517741 | |
706 | Phosphorylation | SNRLEKRSLFLEQSS HCCHHHHHHHEECCC | 34.24 | 29899451 | |
712 | Phosphorylation | RSLFLEQSSAGQYTN HHHHEECCCCCCCCC | 16.87 | 29899451 | |
713 | Phosphorylation | SLFLEQSSAGQYTNS HHHEECCCCCCCCCC | 35.79 | 29899451 | |
717 | Phosphorylation | EQSSAGQYTNSDEED ECCCCCCCCCCCCCC | 13.63 | 29899451 | |
718 | Phosphorylation | QSSAGQYTNSDEEDG CCCCCCCCCCCCCCC | 21.99 | 29899451 | |
720 | Phosphorylation | SAGQYTNSDEEDGYA CCCCCCCCCCCCCCC | 38.30 | 25521595 | |
726 | Phosphorylation | NSDEEDGYASPEVKR CCCCCCCCCCHHHHH | 19.07 | 24759943 | |
728 | Phosphorylation | DEEDGYASPEVKRRG CCCCCCCCHHHHHCC | 17.07 | 25521595 | |
736 | Phosphorylation | PEVKRRGTSVDDFLK HHHHHCCCCHHHHHC | 24.62 | 29899451 | |
737 | Phosphorylation | EVKRRGTSVDDFLKG HHHHCCCCHHHHHCC | 26.77 | 29899451 | |
770 | Phosphorylation | SSRGSDLSDIMEEDE CCCCCCHHHHCHHCH | 30.04 | 29899451 | |
795 | Phosphorylation | DGGRRRPSGTSHNAL CCCCCCCCCCCHHHH | 53.55 | 29899451 | |
797 | Phosphorylation | GRRRPSGTSHNALKI CCCCCCCCCHHHHHH | 31.02 | 29899451 | |
798 | Phosphorylation | RRRPSGTSHNALKIL CCCCCCCCHHHHHHH | 20.47 | 29899451 | |
841 | Phosphorylation | HRPAMAPSIDEYTGR CCCCCCCCCHHHCCC | 32.88 | 29899451 | |
845 | Phosphorylation | MAPSIDEYTGRDHLS CCCCCHHHCCCCCCC | 15.67 | 29899451 | |
846 | Phosphorylation | APSIDEYTGRDHLSP CCCCHHHCCCCCCCC | 24.56 | 29899451 | |
852 | Phosphorylation | YTGRDHLSPDFYDES HCCCCCCCCCCCCCC | 21.00 | 25521595 | |
856 | Phosphorylation | DHLSPDFYDESETDP CCCCCCCCCCCCCCC | 26.61 | 19060867 | |
859 | Phosphorylation | SPDFYDESETDPGAE CCCCCCCCCCCCCHH | 42.79 | 19060867 | |
861 | Phosphorylation | DFYDESETDPGAEEL CCCCCCCCCCCHHHC | 57.69 | 19060867 | |
955 | Phosphorylation | QGFLPLNTPVEKIER CCCCCCCCCHHHHHH | 36.07 | 22324799 | |
966 | Phosphorylation | KIERSRRSGRGHSVP HHHHHHHCCCCCCCC | 31.56 | 29899451 |
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 RIMB2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RIMB2_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 RIMB2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of RIMB2_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852, AND MASSSPECTROMETRY. |