AGRB1_HUMAN - dbPTM
AGRB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGRB1_HUMAN
UniProt AC O14514
Protein Name Adhesion G protein-coupled receptor B1 {ECO:0000312|HGNC:HGNC:943}
Gene Name ADGRB1 {ECO:0000312|HGNC:HGNC:943}
Organism Homo sapiens (Human).
Sequence Length 1584
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cell projection, phagocytic cup . Cell junction, focal adhesion . Cell projection, dendritic spine . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density .
Vasculostatin-120: Secreted .
V
Protein Description Phosphatidylserine receptor which enhances the engulfment of apoptotic cells. [PubMed: 24509909 Also mediates the binding and engulfment of Gram-negative bacteria]
Protein Sequence MRGQAAAPGPVWILAPLLLLLLLLGRRARAAAGADAGPGPEPCATLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPVPCSGPGRVRTYQFDSFLESTRTYLGVESFDEVLRLCDPSAPLAFLQASKQFLQMRRQQPPQHDGLRPRAGPPGPTDDFSVEYLVVGNRNPSRAACQMLCRWLDACLAGSRSSHPCGIMQTPCACLGGEAGGPAAGPLAPRGDVCLRDAVAGGPENCLTSLTQDRGGHGATGGWKLWSLWGECTRDCGGGLQTRTRTCLPAPGVEGGGCEGVLEEGRQCNREACGPAGRTSSRSQSLRSTDARRREELGDELQQFGFPAPQTGDPAAEEWSPWSVCSSTCGEGWQTRTRFCVSSSYSTQCSGPLREQRLCNNSAVCPVHGAWDEWSPWSLCSSTCGRGFRDRTRTCRPPQFGGNPCEGPEKQTKFCNIALCPGRAVDGNWNEWSSWSACSASCSQGRQQRTRECNGPSYGGAECQGHWVETRDCFLQQCPVDGKWQAWASWGSCSVTCGAGSQRRERVCSGPFFGGAACQGPQDEYRQCGTQRCPEPHEICDEDNFGAVIWKETPAGEVAAVRCPRNATGLILRRCELDEEGIAYWEPPTYIRCVSIDYRNIQMMTREHLAKAQRGLPGEGVSEVIQTLVEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQILSNLLAEENRDKWEEAQLAGPNAKELFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPASGATDISFPMKGWRATGDWAKVPEDRVTVSKSVFSTGLTEADEASVFVVGTVLYRNLGSFLALQRNTTVLNSKVISVTVKPPPRSLRTPLEIEFAHMYNGTTNQTCILWDETDVPSSSAPPQLGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSADANMEKATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGASLWSSCVVLPLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGNGDSGGSFQNGHAQLMTDFEKDVDLACRSVLNKDIAACRTATITGTLKRPSLPEEEKLKLAHAKGPPTNFNSLPANVSKLHLHGSPRYPGGPLPDFPNHSLTLKRDKAPKSSFVGDGDIFKKLDSELSRAQEKALDTSYVILPTATATLRPKPKEEPKYSIHIDQMPQTRLIHLSTAPEASLPARSPPSRQPPSGGPPEAPPAQPPPPPPPPPPPPQQPLPPPPNLEPAPPSLGDPGEPAAHPGPSTGPSTKNENVATLSVSSLERRKSRYAELDFEKIMHTRKRHQDMFQDLNRKLQHAAEKDKEVLGPDSKPEKQQTPNKRPWESLRKAHGTPTWVKKELEPLQPSPLELRSVEWERSGATIPLVGQDIIDLQTEV
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
64N-linked_GlycosylationAAAVFPANASRCSWT
EEEEEECCHHHCEEE
UniProtKB CARBOHYD
66PhosphorylationAVFPANASRCSWTLR
EEEECCHHHCEEEEC
-
81PhosphorylationNPDPRRYTLYMKVAK
CCCCCCEEEEEEEEC
24719451
83PhosphorylationDPRRYTLYMKVAKAP
CCCCEEEEEEEECCC
24719451
114PhosphorylationFLESTRTYLGVESFD
HHHHHCCCCCCCCHH
24719451
119PhosphorylationRTYLGVESFDEVLRL
CCCCCCCCHHHHHHH
24719451
287PhosphorylationGLQTRTRTCLPAPGV
CCCCCCEEEECCCCC
-
330PhosphorylationRSQSLRSTDARRREE
HHHHHHHCHHHHHHH
-
401N-linked_GlycosylationLREQRLCNNSAVCPV
CHHHCCCCCCCCCCC
UniProtKB CARBOHYD
537PhosphorylationSWGSCSVTCGAGSQR
EEECCEEEECCCCHH
-
607N-linked_GlycosylationAAVRCPRNATGLILR
EEEECCCCCCEEEEE
UniProtKB CARBOHYD
609PhosphorylationVRCPRNATGLILRRC
EECCCCCCEEEEEEC
23186163
692N-linked_GlycosylationSTIDVLRNMTEIFRR
HHHHHHHHHHHHHHH
UniProtKB CARBOHYD
844N-linked_GlycosylationSFLALQRNTTVLNSK
HHHHHCCCCEEEECE
UniProtKB CARBOHYD
877N-linked_GlycosylationIEFAHMYNGTTNQTC
EEEEECCCCCCCCEE
UniProtKB CARBOHYD
881N-linked_GlycosylationHMYNGTTNQTCILWD
ECCCCCCCCEEEEEE
UniProtKB CARBOHYD
1210PhosphorylationQEEGNGDSGGSFQNG
CCCCCCCCCCCCCCC
26471730
1213PhosphorylationGNGDSGGSFQNGHAQ
CCCCCCCCCCCCCEE
26471730
1223PhosphorylationNGHAQLMTDFEKDVD
CCCEEECCHHHHHHH
26471730
1257PhosphorylationTGTLKRPSLPEEEKL
ECCCCCCCCCHHHHH
25850435
1278PhosphorylationGPPTNFNSLPANVSK
CCCCCCCCCCCCCCE
25850435
1306PhosphorylationLPDFPNHSLTLKRDK
CCCCCCCCEEECCCC
25850435
1308PhosphorylationDFPNHSLTLKRDKAP
CCCCCCEEECCCCCC
25850435
1317PhosphorylationKRDKAPKSSFVGDGD
CCCCCCCCCCCCCHH
25850435
1318PhosphorylationRDKAPKSSFVGDGDI
CCCCCCCCCCCCHHH
25850435
1343PhosphorylationAQEKALDTSYVILPT
HHHHHHCCCEEEEEC
24719451
1350PhosphorylationTSYVILPTATATLRP
CCEEEEECCEECCCC
-
1352PhosphorylationYVILPTATATLRPKP
EEEEECCEECCCCCC
24719451
1354PhosphorylationILPTATATLRPKPKE
EEECCEECCCCCCCC
24719451
1382PhosphorylationTRLIHLSTAPEASLP
EEEEEEECCCCCCCC
28348404
1387PhosphorylationLSTAPEASLPARSPP
EECCCCCCCCCCCCC
24719451
1464PhosphorylationTKNENVATLSVSSLE
CCCCCCEEEEHHHHH
27732954
1466PhosphorylationNENVATLSVSSLERR
CCCCEEEEHHHHHHH
27732954
1468PhosphorylationNVATLSVSSLERRKS
CCEEEEHHHHHHHHH
29255136
1469PhosphorylationVATLSVSSLERRKSR
CEEEEHHHHHHHHHH
29255136
1475PhosphorylationSSLERRKSRYAELDF
HHHHHHHHHHHCCCH
28348404
1477PhosphorylationLERRKSRYAELDFEK
HHHHHHHHHCCCHHH
27642862
1528AcetylationEKQQTPNKRPWESLR
HHCCCCCCCCHHHHH
7409377
1554PhosphorylationELEPLQPSPLELRSV
CCCCCCCCCCEECEE
29255136

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 AGRB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGRB1_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 AGRB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAGI1_HUMANMAGI1physical
9647739
BAIP3_HUMANBAIAP3physical
9790924
AGRB1_HUMANBAI1physical
23782696
MAGI1_HUMANMAGI1physical
23782696
MAGI2_HUMANMAGI2physical
23782696
MAGI3_HUMANMAGI3physical
23782696
DLG4_HUMANDLG4physical
23782696
INADL_HUMANINADLphysical
23782696
DLG1_HUMANDLG1physical
23782696
LIN7A_HUMANLIN7Aphysical
23782696
LRRC7_HUMANLRRC7physical
23782696
SNTA1_HUMANSNTA1physical
23782696
SNTB1_HUMANSNTB1physical
23782696
SNTB2_HUMANSNTB2physical
23782696
SNTG2_HUMANSNTG2physical
23782696
PDZD2_HUMANPDZD2physical
23782696
BAIP2_HUMANBAIAP2physical
10343108

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AGRB1_HUMAN

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Related Literatures of Post-Translational Modification

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