GRM4_HUMAN - dbPTM
GRM4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRM4_HUMAN
UniProt AC Q14833
Protein Name Metabotropic glutamate receptor 4
Gene Name GRM4
Organism Homo sapiens (Human).
Sequence Length 912
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity..
Protein Sequence MPGKRGLGWWWARLPLCLLLSLYGPWMPSSLGKPKGHPHMNSIRIDGDITLGGLFPVHGRGSEGKPCGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSRDTHALEQSLTFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILRLFKIPQISYASTAPDLSDNSRYDFFSRVVPSDTYQAQAMVDIVRALKWNYVSTVASEGSYGESGVEAFIQKSREDGGVCIAQSVKIPREPKAGEFDKIIRRLLETSNARAVIIFANEDDIRRVLEAARRANQTGHFFWMGSDSWGSKIAPVLHLEEVAEGAVTILPKRMSVRGFDRYFSSRTLDNNRRNIWFAEFWEDNFHCKLSRHALKKGSHVKKCTNRERIGQDSAYEQEGKVQFVIDAVYAMGHALHAMHRDLCPGRVGLCPRMDPVDGTQLLKYIRNVNFSGIAGNPVTFNENGDAPGRYDIYQYQLRNDSAEYKVIGSWTDHLHLRIERMHWPGSGQQLPRSICSLPCQPGERKKTVKGMPCCWHCEPCTGYQYQVDRYTCKTCPYDMRPTENRTGCRPIPIIKLEWGSPWAVLPLFLAVVGIAATLFVVITFVRYNDTPIVKASGRELSYVLLAGIFLCYATTFLMIAEPDLGTCSLRRIFLGLGMSISYAALLTKTNRIYRIFEQGKRSVSAPRFISPASQLAITFSLISLQLLGICVWFVVDPSHSVVDFQDQRTLDPRFARGVLKCDISDLSLICLLGYSMLLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIVWLAFIPIFFGTSQSADKLYIQTTTLTVSVSLSASVSLGMLYMPKVYIILFHPEQNVPKRKRSLKAVVTAATMSNKFTQKGNFRPNGEAKSELCENLEAPALATKQTYVTYTNHAI
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
98N-linked_GlycosylationNDPDLLPNITLGARI
CCCCCCCCCCHHHHH
39.59UniProtKB CARBOHYD
138PhosphorylationGTEVRCGSGGPPIIT
CCEEECCCCCCCCCC
44.1730576142
145PhosphorylationSGGPPIITKPERVVG
CCCCCCCCCCCEEEE
41.0730576142
301N-linked_GlycosylationLEAARRANQTGHFFW
HHHHHHHHCCCCEEE
37.83UniProtKB CARBOHYD
311PhosphorylationGHFFWMGSDSWGSKI
CCEEEECCCCCCCCE
16.6222210691
333PhosphorylationEVAEGAVTILPKRMS
HHHCCCEEEECCCCC
19.0922210691
414PhosphorylationQFVIDAVYAMGHALH
CHHHHHHHHHHHHHH
7.81-
454N-linked_GlycosylationLKYIRNVNFSGIAGN
HHHHHCCCCCCCCCC
28.99UniProtKB CARBOHYD
484N-linked_GlycosylationIYQYQLRNDSAEYKV
EEEEEECCCCCCEEE
57.06UniProtKB CARBOHYD
555PhosphorylationYQYQVDRYTCKTCPY
CEEEEEEEECCCCCC
16.42-
562PhosphorylationYTCKTCPYDMRPTEN
EECCCCCCCCCCCCC
25.23-
569N-linked_GlycosylationYDMRPTENRTGCRPI
CCCCCCCCCCCCEEE
49.66UniProtKB CARBOHYD
612PhosphorylationVVITFVRYNDTPIVK
HHHHHHCCCCCCCEE
16.4623312004
615PhosphorylationTFVRYNDTPIVKASG
HHHCCCCCCCEECCC
15.9823312004
672PhosphorylationISYAALLTKTNRIYR
HHHHHHHHHCCHHHH
36.3518491316
674PhosphorylationYAALLTKTNRIYRIF
HHHHHHHCCHHHHHH
25.2118491316
678PhosphorylationLTKTNRIYRIFEQGK
HHHCCHHHHHHHCCC
8.40-
695PhosphorylationVSAPRFISPASQLAI
CCCCCCCCHHHHHHH
16.2324043423
698PhosphorylationPRFISPASQLAITFS
CCCCCHHHHHHHHHH
29.1624043423
703PhosphorylationPASQLAITFSLISLQ
HHHHHHHHHHHHHHH
11.1024043423
705PhosphorylationSQLAITFSLISLQLL
HHHHHHHHHHHHHHH
19.0224043423
708PhosphorylationAITFSLISLQLLGIC
HHHHHHHHHHHHCCE
18.5024043423
723PhosphorylationVWFVVDPSHSVVDFQ
EEEECCCCCCCCCCC
24.7524043423
725PhosphorylationFVVDPSHSVVDFQDQ
EECCCCCCCCCCCCC
28.3324043423
816PhosphorylationSQSADKLYIQTTTLT
CCCCCEEEEEEEEEE
9.2024043423
819PhosphorylationADKLYIQTTTLTVSV
CCEEEEEEEEEEEEE
16.5224043423
820PhosphorylationDKLYIQTTTLTVSVS
CEEEEEEEEEEEEEE
11.9324043423
821PhosphorylationKLYIQTTTLTVSVSL
EEEEEEEEEEEEEEE
24.6624043423
823PhosphorylationYIQTTTLTVSVSLSA
EEEEEEEEEEEEECE
14.5124043423
825PhosphorylationQTTTLTVSVSLSASV
EEEEEEEEEEECEEE
10.7624043423
827PhosphorylationTTLTVSVSLSASVSL
EEEEEEEEECEEEEC
14.7524043423
829PhosphorylationLTVSVSLSASVSLGM
EEEEEEECEEEECCC
15.8124043423
831PhosphorylationVSVSLSASVSLGMLY
EEEEECEEEECCCEE
14.6324043423
833PhosphorylationVSLSASVSLGMLYMP
EEECEEEECCCEECC
19.4024043423
838PhosphorylationSVSLGMLYMPKVYII
EEECCCEECCEEEEE
11.5024043423

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

Oops, there are no upstream regulatory protein records of GRM4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRM4_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 GRM4_HUMAN !!

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

Oops, there are no PPI records of GRM4_HUMAN !!

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 GRM4_HUMAN

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Related Literatures of Post-Translational Modification

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