GABR1_MOUSE - dbPTM
GABR1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GABR1_MOUSE
UniProt AC Q9WV18
Protein Name Gamma-aminobutyric acid type B receptor subunit 1
Gene Name Gabbr1
Organism Mus musculus (Mouse).
Sequence Length 960
Subcellular Localization Cell membrane
Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein. Cell projection, dendrite. Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma me
Protein Description Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. [PubMed: 10773016]
Protein Sequence MLLLLLVPLFLRPLGAGGAQTPNVTSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKTYDPSINCTVEEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRSQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQIRSRRHPPTPPDPSGGLPRGPSEPPDRLSCDGSRVHLLYK
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
23N-linked_GlycosylationAGGAQTPNVTSEGCQ
CCCCCCCCCCCCCCE		53.76-
83N-linked_GlycosylationKVRKCLANGSWTDMD
HHHHHHHCCCCCCCC		31.89-
246PhosphorylationIILMPGCSSVSTLVA
EEEECCCCHHHHHHH		39.4222817900
247PhosphorylationILMPGCSSVSTLVAE
EEECCCCHHHHHHHH		24.9422817900
249PhosphorylationMPGCSSVSTLVAEAA
ECCCCHHHHHHHHHH		20.2621183079
268PhosphorylationLIVLSYGSSSPALSN
EEEEECCCCCHHHHC		21.29-
408N-linked_GlycosylationKTYDPSINCTVEEMT
HHCCCCCCCCHHHHH		21.53-
439N-linked_GlycosylationANTRSISNMTSQEFV
CCCCCCCCCCHHHHH		35.76-
481N-linked_GlycosylationWALALALNKTSGGGG
HHHHHHHHCCCCCCC		39.70-
483PhosphorylationLALALNKTSGGGGRS
HHHHHHCCCCCCCCC		31.3722871156
484PhosphorylationALALNKTSGGGGRSG
HHHHHCCCCCCCCCC		36.7322871156
501N-linked_GlycosylationLEDFNYNNQTITDQI
HHHCCCCCCCHHHHH		29.97-
513N-linked_GlycosylationDQIYRAMNSSSFEGV
HHHHHHHHCCCCCCC		37.44-
545PhosphorylationIEQLQGGSYKKIGYY
HHHHCCCCCEEEEEC		40.3720415495
546PhosphorylationEQLQGGSYKKIGYYD
HHHCCCCCEEEEECC		21.4120415495
735UbiquitinationQIVDPLHRTIETFAK
HHHHHHHHHHHHHCC		45.1127667366
742UbiquitinationRTIETFAKEEPKEDI
HHHHHHCCCCCCCCC		59.4227667366
761PhosphorylationLPQLEHCSSKKMNTW
HHCHHHHCCCCCCHH		47.2929514104
762PhosphorylationPQLEHCSSKKMNTWL
HCHHHHCCCCCCHHH		41.5129514104
767PhosphorylationCSSKKMNTWLGIFYG
HCCCCCCHHHHHHHH		20.68-
775PhosphorylationWLGIFYGYKGLLLLL
HHHHHHHHHHHHHHH		7.18-
867PhosphorylationITRGEWQSEAQDTMK
HHCCCHHHHHHHHHH		35.6522817900
872PhosphorylationWQSEAQDTMKTGSST
HHHHHHHHHHCCCCC		14.4225521595
875PhosphorylationEAQDTMKTGSSTNNN
HHHHHHHCCCCCCCC		31.3222324799
877PhosphorylationQDTMKTGSSTNNNEE
HHHHHCCCCCCCCHH		38.9425521595
878PhosphorylationDTMKTGSSTNNNEEE
HHHHCCCCCCCCHHH		36.1822324799
879PhosphorylationTMKTGSSTNNNEEEK
HHHCCCCCCCCHHHH		43.6025521595
879UbiquitinationTMKTGSSTNNNEEEK
HHHCCCCCCCCHHHH		43.6027667366
885UbiquitinationSTNNNEEEKSRLLEK
CCCCCHHHHHHHHHH		50.5927667366
886UbiquitinationTNNNEEEKSRLLEKE
CCCCHHHHHHHHHHH		44.1227667366
887PhosphorylationNNNEEEKSRLLEKEN
CCCHHHHHHHHHHHH		31.2922324799
892UbiquitinationEKSRLLEKENRELEK
HHHHHHHHHHHHHHH		61.3322790023
897UbiquitinationLEKENRELEKIIAEK
HHHHHHHHHHHHHHH		7.9927667366
899UbiquitinationKENRELEKIIAEKEE
HHHHHHHHHHHHHHH		52.6227667366
904UbiquitinationLEKIIAEKEERVSEL
HHHHHHHHHHHHHHH		56.7227667366
909PhosphorylationAEKEERVSELRHQLQ
HHHHHHHHHHHHHHH		36.8127149854
923PhosphorylationQSRQQIRSRRHPPTP
HHHHHHHHCCCCCCC		34.9820047950
929PhosphorylationRSRRHPPTPPDPSGG
HHCCCCCCCCCCCCC		52.4825521595
934PhosphorylationPPTPPDPSGGLPRGP
CCCCCCCCCCCCCCC		53.5322817900
949PhosphorylationSEPPDRLSCDGSRVH
CCCCCCCCCCCCEEE		15.8529899451
953PhosphorylationDRLSCDGSRVHLLYK
CCCCCCCCEEEEEEC		20.2029899451
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
867SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
867SPhosphorylationKinaseCAMK2AP11798
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GABR1_MOUSE !!
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 GABR1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATF4_MOUSEAtf4physical
15013631
KIF1B_MOUSEKif1bphysical
17532644
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GABR1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-929, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-929, AND MASSSPECTROMETRY.

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