AGRG5_HUMAN - dbPTM
AGRG5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGRG5_HUMAN
UniProt AC Q8IZF4
Protein Name Adhesion G-protein coupled receptor G5
Gene Name ADGRG5
Organism Homo sapiens (Human).
Sequence Length 528
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Adhesion G protein-coupled receptor (GPCR). Transduces intracellular signals through coupling to guanine nucleotide-binding protein G(s) subunit alpha and activation of adenylate cyclase pathway. Isoform 1, but not isoform 2, is constitutively active, as evidenced by elevated basal cAMP levels, and responds to mechanical activation (shaking)..
Protein Sequence MDHCGALFLCLCLLTLQNATTETWEELLSYMENMQVSRGRSSVFSSRQLHQLEQMLLNTSFPGYNLTLQTPTIQSLAFKLSCDFSGLSLTSATLKRVPQAGGQHARGQHAMQFPAELTRDACKTRPRELRLICIYFSNTHFFKDENNSSLLNNYVLGAQLSHGHVNNLRDPVNISFWHNQSLEGYTLTCVFWKEGARKQPWGGWSPEGCRTEQPSHSQVLCRCNHLTYFAVLMQLSPALVPAELLAPLTYISLVGCSISIVASLITVLLHFHFRKQSDSLTRIHMNLHASVLLLNIAFLLSPAFAMSPVPGSACTALAAALHYALLSCLTWMAIEGFNLYLLLGRVYNIYIRRYVFKLGVLGWGAPALLVLLSLSVKSSVYGPCTIPVFDSWENGTGFQNMSICWVRSPVVHSVLVMGYGGLTSLFNLVVLAWALWTLRRLRERADAPSVRACHDTVTVLGLTVLLGTTWALAFFSFGVFLLPQLFLFTILNSLYGFFLFLWFCSQRCRSEAEAKAQIEAFSSSQTTQ
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
15PhosphorylationFLCLCLLTLQNATTE
HHHHHHHHHHCCCHH
24043423
18N-linked_GlycosylationLCLLTLQNATTETWE
HHHHHHHCCCHHHHH
UniProtKB CARBOHYD
20PhosphorylationLLTLQNATTETWEEL
HHHHHCCCHHHHHHH
24043423
21PhosphorylationLTLQNATTETWEELL
HHHHCCCHHHHHHHH
24043423
23PhosphorylationLQNATTETWEELLSY
HHCCCHHHHHHHHHH
24043423
29PhosphorylationETWEELLSYMENMQV
HHHHHHHHHHHHHCC
24043423
30PhosphorylationTWEELLSYMENMQVS
HHHHHHHHHHHHCCC
24043423
37PhosphorylationYMENMQVSRGRSSVF
HHHHHCCCCCCCHHC
24043423
58N-linked_GlycosylationQLEQMLLNTSFPGYN
HHHHHHHCCCCCCCC
UniProtKB CARBOHYD
59PhosphorylationLEQMLLNTSFPGYNL
HHHHHHCCCCCCCCE
24043423
60PhosphorylationEQMLLNTSFPGYNLT
HHHHHCCCCCCCCEE
24043423
64PhosphorylationLNTSFPGYNLTLQTP
HCCCCCCCCEEEECC
24043423
65N-linked_GlycosylationNTSFPGYNLTLQTPT
CCCCCCCCEEEECCC
UniProtKB CARBOHYD
67PhosphorylationSFPGYNLTLQTPTIQ
CCCCCCEEEECCCHH
24043423
70PhosphorylationGYNLTLQTPTIQSLA
CCCEEEECCCHHHHH
24043423
72PhosphorylationNLTLQTPTIQSLAFK
CEEEECCCHHHHHHH
24043423
75PhosphorylationLQTPTIQSLAFKLSC
EECCCHHHHHHHHCC
24043423
146N-linked_GlycosylationTHFFKDENNSSLLNN
CCCEECCCCHHHCHH
UniProtKB CARBOHYD
147N-linked_GlycosylationHFFKDENNSSLLNNY
CCEECCCCHHHCHHH
UniProtKB CARBOHYD
173N-linked_GlycosylationNNLRDPVNISFWHNQ
CCCCCCEEEEEEECC
UniProtKB CARBOHYD
179N-linked_GlycosylationVNISFWHNQSLEGYT
EEEEEEECCCCCCEE
UniProtKB CARBOHYD
373PhosphorylationPALLVLLSLSVKSSV
HHHHHHHHHCCCCCC
24719451
394N-linked_GlycosylationPVFDSWENGTGFQNM
EEECCCCCCCCCCCE
UniProtKB CARBOHYD
400N-linked_GlycosylationENGTGFQNMSICWVR
CCCCCCCCEEEEEEC
UniProtKB CARBOHYD
523PhosphorylationAQIEAFSSSQTTQ--
HHHHHHHHCCCCC--
22115753
524PhosphorylationQIEAFSSSQTTQ---
HHHHHHHCCCCC---
22115753
526PhosphorylationEAFSSSQTTQ-----
HHHHHCCCCC-----
22115753
527PhosphorylationAFSSSQTTQ------
HHHHCCCCC------
22115753

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 AGRG5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGRG5_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 AGRG5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLPR3_HUMANLPPR3physical
28514442
TSN10_HUMANTSPAN10physical
28514442
TMM68_HUMANTMEM68physical
28514442
SC11C_HUMANSEC11Cphysical
28514442
CXG1_HUMANGJC1physical
28514442
FZD3_HUMANFZD3physical
28514442
SC6A6_HUMANSLC6A6physical
28514442
EPHB3_HUMANEPHB3physical
28514442
FZD2_HUMANFZD2physical
28514442
REEP6_HUMANREEP6physical
28514442
TMX4_HUMANTMX4physical
28514442
GPM6B_HUMANGPM6Bphysical
28514442
CXA1_HUMANGJA1physical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
GRM1B_HUMANGRAMD1Bphysical
28514442
SIDT2_HUMANSIDT2physical
28514442
OSBL8_HUMANOSBPL8physical
28514442
MSPD2_HUMANMOSPD2physical
28514442
ALG9_HUMANALG9physical
28514442
ZNT1_HUMANSLC30A1physical
28514442
ATLA3_HUMANATL3physical
28514442
ANO6_HUMANANO6physical
28514442
GRM1A_HUMANGRAMD1Aphysical
28514442
TSN3_HUMANTSPAN3physical
28514442
AVR2B_HUMANACVR2Bphysical
28514442
EDEM2_HUMANEDEM2physical
28514442
AT133_HUMANATP13A3physical
28514442
ASPH2_HUMANASPHD2physical
28514442
S39A1_HUMANSLC39A1physical
28514442
FSTL1_HUMANFSTL1physical
28514442
GPM6A_HUMANGPM6Aphysical
28514442
SGMR1_HUMANSIGMAR1physical
28514442
DJC18_HUMANDNAJC18physical
28514442
FLVC1_HUMANFLVCR1physical
28514442
FAM3C_HUMANFAM3Cphysical
28514442
LRP10_HUMANLRP10physical
28514442
VPP1_HUMANATP6V0A1physical
28514442
KLRG2_HUMANKLRG2physical
28514442
PPAL_HUMANACP2physical
28514442
S19A2_HUMANSLC19A2physical
28514442
TMED7_HUMANTMED7physical
28514442
ACV1B_HUMANACVR1Bphysical
28514442
HMDH_HUMANHMGCRphysical
28514442
S29A1_HUMANSLC29A1physical
28514442
LCLT1_HUMANLCLAT1physical
28514442
ABCA3_HUMANABCA3physical
28514442
TMUB1_HUMANTMUB1physical
28514442
S47A1_HUMANSLC47A1physical
28514442
S12A9_HUMANSLC12A9physical
28514442
SPPL3_HUMANSPPL3physical
28514442
CREL1_HUMANCRELD1physical
28514442
PIGO_HUMANPIGOphysical
28514442
SERC1_HUMANSERINC1physical
28514442
MFSD8_HUMANMFSD8physical
28514442
ERGI3_HUMANERGIC3physical
28514442
FZD6_HUMANFZD6physical
28514442
INGR1_HUMANIFNGR1physical
28514442
SOAT1_HUMANSOAT1physical
28514442
PTN1_HUMANPTPN1physical
28514442
F213A_HUMANFAM213Aphysical
28514442
NGBR_HUMANNUS1physical
28514442
SNG2_HUMANSYNGR2physical
28514442
TRI59_HUMANTRIM59physical
28514442
CTGE5_HUMANCTAGE5physical
28514442
MTR1L_HUMANGPR50physical
28514442
SG196_HUMANPOMKphysical
28514442
SPP2B_HUMANSPPL2Bphysical
28514442
ABCB8_HUMANABCB8physical
28514442
PIGM_HUMANPIGMphysical
28514442
ACHA5_HUMANCHRNA5physical
28514442
BRAT1_HUMANBRAT1physical
28514442
CALX_HUMANCANXphysical
28514442
DCAKD_HUMANDCAKDphysical
28514442
RFT1_HUMANRFT1physical
28514442
FITM2_HUMANFITM2physical
28514442
SGPP1_HUMANSGPP1physical
28514442
LSR_HUMANLSRphysical
28514442
ABHEA_HUMANABHD14Aphysical
28514442
TNFL9_HUMANTNFSF9physical
28514442

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 AGRG5_HUMAN

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Related Literatures of Post-Translational Modification

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