GLRB_HUMAN - dbPTM
GLRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLRB_HUMAN
UniProt AC P48167
Protein Name Glycine receptor subunit beta
Gene Name GLRB
Organism Homo sapiens (Human).
Sequence Length 497
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein . Cell junction, synapse . Cell projection, dendrite . Cell membrane
Multi-pass membrane protein . Cytoplasm . Retained in the cytoplasm upon heterologous expression b
Protein Description Glycine receptors are ligand-gated chloride channels. GLRB does not form ligand-gated ion channels by itself, but is part of heteromeric ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. [PubMed: 8717357]
Protein Sequence MKFLLTTAFLILISLWVEEAYSKEKSSKKGKGKKKQYLCPSQQSAEDLARVPANSTSNILNRLLVSYDPRIRPNFKGIPVDVVVNIFINSFGSIQETTMDYRVNIFLRQKWNDPRLKLPSDFRGSDALTVDPTMYKCLWKPDLFFANEKSANFHDVTQENILLFIFRDGDVLVSMRLSITLSCPLDLTLFPMDTQRCKMQLESFGYTTDDLRFIWQSGDPVQLEKIALPQFDIKKEDIEYGNCTKYYKGTGYYTCVEVIFTLRRQVGFYMMGVYAPTLLIVVLSWLSFWINPDASAARVPLGIFSVLSLASECTTLAAELPKVSYVKALDVWLIACLLFGFASLVEYAVVQVMLNNPKRVEAEKARIAKAEQADGKGGNVAKKNTVNGTGTPVHISTLQVGETRCKKVCTSKSDLRSNDFSIVGSLPRDFELSNYDCYGKPIEVNNGLGKSQAKNNKKPPPAKPVIPTAAKRIDLYARALFPFCFLFFNVIYWSIYL
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
28AcetylationYSKEKSSKKGKGKKK
HHHHCCCCCCCCCCC
73.05164297
31AcetylationEKSSKKGKGKKKQYL
HCCCCCCCCCCCCCC
76.16164301
34AcetylationSKKGKGKKKQYLCPS
CCCCCCCCCCCCCCC
54.50164305
35AcetylationKKGKGKKKQYLCPSQ
CCCCCCCCCCCCCCC
47.89164309
54N-linked_GlycosylationDLARVPANSTSNILN
HHHCCCCCCHHHHHH
39.49UniProtKB CARBOHYD
117UbiquitinationKWNDPRLKLPSDFRG
CCCCCCCCCCCCCCC
60.6829967540
125PhosphorylationLPSDFRGSDALTVDP
CCCCCCCCCCCCCCH
18.56-
129PhosphorylationFRGSDALTVDPTMYK
CCCCCCCCCCHHHHH
25.28-
136UbiquitinationTVDPTMYKCLWKPDL
CCCHHHHHHHCCCCE
16.42-
140UbiquitinationTMYKCLWKPDLFFAN
HHHHHHCCCCEEECC
18.73-
178PhosphorylationVLVSMRLSITLSCPL
EEEEEEEEEEEECCC
11.8022210691
188PhosphorylationLSCPLDLTLFPMDTQ
EECCCCEEEEECCHH
26.4822210691
194PhosphorylationLTLFPMDTQRCKMQL
EEEEECCHHHHHHHH
16.2022210691
198UbiquitinationPMDTQRCKMQLESFG
ECCHHHHHHHHHHCC
31.69-
203PhosphorylationRCKMQLESFGYTTDD
HHHHHHHHCCCCHHC
32.34-
206PhosphorylationMQLESFGYTTDDLRF
HHHHHCCCCHHCEEE
12.40-
242N-linked_GlycosylationKEDIEYGNCTKYYKG
HHHCCCCCCCEEECC
29.41UniProtKB CARBOHYD
261PhosphorylationTCVEVIFTLRRQVGF
EEEEHHHHHHHHHCH
14.2924719451
274PhosphorylationGFYMMGVYAPTLLIV
CHHHHCCHHHHHHHH
10.92-
277PhosphorylationMMGVYAPTLLIVVLS
HHCCHHHHHHHHHHH
26.48-
369UbiquitinationAEKARIAKAEQADGK
HHHHHHHHHHHCCCC
50.51-
391PhosphorylationNTVNGTGTPVHISTL
CCCCCCCCEEEEEEE
23.2124076635
411PhosphorylationRCKKVCTSKSDLRSN
EECEEECCHHHHHCC
25.65-
435PhosphorylationRDFELSNYDCYGKPI
CCEECCCCEECCCEE
12.1922817900
440UbiquitinationSNYDCYGKPIEVNNG
CCCEECCCEEEECCC
19.1529967540

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
435YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLRB_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 GLRB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GEPH_HUMANGPHNphysical
7546736

Drug and Disease Associations
Kegg Disease
H00769 Hyperekplexia
OMIM Disease
614619Hyperekplexia 2 (HKPX2)
Kegg Drug
D00011 Glycine (JP16/USP)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLRB_HUMAN

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Related Literatures of Post-Translational Modification

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