GBRR1_HUMAN - dbPTM
GBRR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GBRR1_HUMAN
UniProt AC P24046
Protein Name Gamma-aminobutyric acid receptor subunit rho-1
Gene Name GABRR1
Organism Homo sapiens (Human).
Sequence Length 479
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein.
Protein Description GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-1 GABA receptor could play a role in retinal neurotransmission..
Protein Sequence MLAVPNMRFGIFLLWWGWVLATESRMHWPGREVHEMSKKGRPQRQRREVHEDAHKQVSPILRRSPDITKSPLTKSEQLLRIDDHDFSMRPGFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTNNLSMTFDGRLVKKIWVPDMFFVHSKRSFIHDTTTDNVMLRVQPDGKVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKKGNDSLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVPLGITTVLTMSTIITGVNASMPRVSYIKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKEQKLREKLPCTSGLPPPRTAMLDGNYSDGEVNDLDNYMPENGEKPDRMMVQLTLASERSSPQRKSQRSSYVSMRIDTHAIDKYSRIIFPAAYILFNLIYWSIFS
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
134PhosphorylationYWKDERLSFPSTNNL
HHCCCCCCCCCCCCE
41.13-
140N-linked_GlycosylationLSFPSTNNLSMTFDG
CCCCCCCCEEEEECC
33.31UniProtKB CARBOHYD
166PhosphorylationFFVHSKRSFIHDTTT
EEEEECCCCEEECCC
32.08-
171PhosphorylationKRSFIHDTTTDNVML
CCCCEEECCCCCEEE
19.89-
172PhosphorylationRSFIHDTTTDNVMLR
CCCEEECCCCCEEEE
37.90-
189PhosphorylationPDGKVLYSLRVTVTA
CCCCEEEEEEEEEEE
12.9224719451
219PhosphorylationCSLEIESYAYTEDDL
CEEEEEEEEECCCCE
7.2820736484
221PhosphorylationLEIESYAYTEDDLML
EEEEEEEECCCCEEE
11.4820736484
229PhosphorylationTEDDLMLYWKKGNDS
CCCCEEEEEECCCCC
10.9620736484
234N-linked_GlycosylationMLYWKKGNDSLKTDE
EEEEECCCCCCCHHH
44.57UniProtKB CARBOHYD
239PhosphorylationKGNDSLKTDERISLS
CCCCCCCHHHCCCHH
48.6726074081
274N-linked_GlycosylationWYNRLYINFTLRRHI
CCCCEEEEEHHHHHH
15.42UniProtKB CARBOHYD
276PhosphorylationNRLYINFTLRRHIFF
CCEEEEEHHHHHHHH
18.1824719451
288PhosphorylationIFFFLLQTYFPATLM
HHHHHHHHHCHHHHH
27.4026552605
289PhosphorylationFFFLLQTYFPATLMV
HHHHHHHHCHHHHHH
8.4626552605
293PhosphorylationLQTYFPATLMVMLSW
HHHHCHHHHHHHHHH
18.6726552605
299PhosphorylationATLMVMLSWVSFWID
HHHHHHHHHHHHHHH
13.8226552605
302PhosphorylationMVMLSWVSFWIDRRA
HHHHHHHHHHHHCCC
14.4926552605
319PhosphorylationARVPLGITTVLTMST
CCCCCCHHEEEEHHH
14.7322210691
320PhosphorylationRVPLGITTVLTMSTI
CCCCCHHEEEEHHHH
16.1722210691
323PhosphorylationLGITTVLTMSTIITG
CCHHEEEEHHHHHHC
12.5326552605
325PhosphorylationITTVLTMSTIITGVN
HHEEEEHHHHHHCCC
15.9526552605
326PhosphorylationTTVLTMSTIITGVNA
HEEEEHHHHHHCCCC
12.9426552605
329PhosphorylationLTMSTIITGVNASMP
EEHHHHHHCCCCCCC
31.0926552605
334PhosphorylationIITGVNASMPRVSYI
HHHCCCCCCCCHHHH
24.9026552605
352UbiquitinationDIYLWVSFVFVFLSV
HHHHHHHHHHHHHHH
3.4221963094
362PhosphorylationVFLSVLEYAAVNYLT
HHHHHHHHHHHHHHH
8.8329759185
394PhosphorylationSGLPPPRTAMLDGNY
CCCCCCCEEEECCCC
23.3812175859
402PhosphorylationAMLDGNYSDGEVNDL
EEECCCCCCCCCCCH
43.0412175859
422UbiquitinationENGEKPDRMMVQLTL
CCCCCCCCEEEHHHH
24.5121963094
431PhosphorylationMVQLTLASERSSPQR
EEHHHHHCCCCCCCH
36.3324719451
434PhosphorylationLTLASERSSPQRKSQ
HHHHCCCCCCCHHHH
42.1724144214
435PhosphorylationTLASERSSPQRKSQR
HHHCCCCCCCHHHHH
31.1324144214
439UbiquitinationERSSPQRKSQRSSYV
CCCCCCHHHHHHHHH
45.7721963094
440PhosphorylationRSSPQRKSQRSSYVS
CCCCCHHHHHHHHHH
32.7724144214
443PhosphorylationPQRKSQRSSYVSMRI
CCHHHHHHHHHHEEE
20.5512175859
444PhosphorylationQRKSQRSSYVSMRID
CHHHHHHHHHHEEEC
31.5712175859
447PhosphorylationSQRSSYVSMRIDTHA
HHHHHHHHEEECHHH
8.2910779366

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
394TPhosphorylationKinaseMAPK-FAMILY-GPS
402SPhosphorylationKinaseCAMK2-FAMILY-GPS
434SPhosphorylationKinaseMAPK-FAMILY-GPS
435SPhosphorylationKinaseMAPK-FAMILY-GPS
440SPhosphorylationKinasePKC-FAMILY-GPS
443SPhosphorylationKinasePKA-FAMILY-GPS
443SPhosphorylationKinasePKC-FAMILY-GPS
443SPhosphorylationKinasePKG-FAMILY-GPS
444SPhosphorylationKinasePKA-FAMILY-GPS
444SPhosphorylationKinasePKC-FAMILY-GPS
444SPhosphorylationKinasePKG-FAMILY-GPS
447SPhosphorylationKinasePKC-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GBRR1_HUMAN !!

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 GBRR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAXB1_HUMANTAX1BP1physical
16999686
GBRR1_HUMANGABRR1physical
16999686
BCR_HUMANBCRphysical
16999686
DNM1L_HUMANDNM1Lphysical
16999686
IP6K2_HUMANIP6K2physical
16999686
FEZF1_HUMANFEZF1physical
16999686

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GBRR1_HUMAN

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Related Literatures of Post-Translational Modification

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