GBP1_HUMAN - dbPTM
GBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GBP1_HUMAN
UniProt AC P32455
Protein Name Guanylate-binding protein 1
Gene Name GBP1
Organism Homo sapiens (Human).
Sequence Length 592
Subcellular Localization Cytoplasm . Golgi apparatus membrane
Lipid-anchor
Cytoplasmic side. Cell membrane . Secreted. Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of IFNG induction. Golgi membrane localization req
Protein Description Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes..
Protein Sequence MASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSALLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS
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
22SulfoxidationENTNGRLMANPEALK
ECCCCCCCCCHHHHH		3.0521406390
49PhosphorylationAIVGLYRTGKSYLMN
EEEEHHHHCHHHHHH		35.0923312004
52PhosphorylationGLYRTGKSYLMNKLA
EHHHHCHHHHHHHHC		25.5024719451
53PhosphorylationLYRTGKSYLMNKLAG
HHHHCHHHHHHHHCC		17.2923312004
66PhosphorylationAGKKKGFSLGSTVQS
CCCCCCCCCCHHHHH		40.2523911959
69PhosphorylationKKGFSLGSTVQSHTK
CCCCCCCHHHHHCCC		30.6028857561
70PhosphorylationKGFSLGSTVQSHTKG
CCCCCCHHHHHCCCE		22.29-
75PhosphorylationGSTVQSHTKGIWMWC
CHHHHHCCCEEEEEE		35.89-
154PhosphorylationELTHRIRSKSSPDEN
HHHHHHHCCCCCCCC		34.2227251275
156PhosphorylationTHRIRSKSSPDENEN
HHHHHCCCCCCCCCC		48.6427251275
157PhosphorylationHRIRSKSSPDENENE
HHHHCCCCCCCCCCC		39.8627251275
205PhosphorylationPDEYLTYSLKLKKGT
CHHHHHEEEEECCCC		17.5024719451
215MalonylationLKKGTSQKDETFNLP
ECCCCCCCCCCCCCC		58.2532601280
218PhosphorylationGTSQKDETFNLPRLC
CCCCCCCCCCCCHHH		28.1427251275
278UbiquitinationSYIFSNSKTKTLSGG
HHHHCCCCCCEECCC		59.29-
279PhosphorylationYIFSNSKTKTLSGGI
HHHCCCCCCEECCCE		29.1429083192
281PhosphorylationFSNSKTKTLSGGIQV
HCCCCCCEECCCEEE		31.2429083192
283PhosphorylationNSKTKTLSGGIQVNG
CCCCCEECCCEEECC		39.9629083192
335PhosphorylationVQKAIAHYEQQMGQK
HHHHHHHHHHHCCCC		13.35-
339SulfoxidationIAHYEQQMGQKVQLP
HHHHHHHCCCCCCCC		6.4930846556
371PhosphorylationAIEVFIRSSFKDVDH
HHHHHHHHCCCCHHH		35.00-
372PhosphorylationIEVFIRSSFKDVDHL
HHHHHHHCCCCHHHH		26.85-
374UbiquitinationVFIRSSFKDVDHLFQ
HHHHHCCCCHHHHHH		59.81-
382UbiquitinationDVDHLFQKELAAQLE
CHHHHHHHHHHHHHH		47.5729967540
382AcetylationDVDHLFQKELAAQLE
CHHHHHHHHHHHHHH		47.5725953088
391UbiquitinationLAAQLEKKRDDFCKQ
HHHHHHHHHHHHHHH		52.24-
397UbiquitinationKKRDDFCKQNQEASS
HHHHHHHHHHHHHCH		52.8824816145
403PhosphorylationCKQNQEASSDRCSAL
HHHHHHHCHHHHHHH		31.8328348404
404PhosphorylationKQNQEASSDRCSALL
HHHHHHCHHHHHHHH		35.8028348404
408PhosphorylationEASSDRCSALLQVIF
HHCHHHHHHHHHHHH		23.8928348404
427PhosphorylationEEVKAGIYSKPGGYR
HHHHCCCCCCCCCHH		15.1021253578
439UbiquitinationGYRLFVQKLQDLKKK
CHHHHHHHHHHHHHH		42.70-
439AcetylationGYRLFVQKLQDLKKK
CHHHHHHHHHHHHHH		42.7025953088
453UbiquitinationKYYEEPRKGIQAEEI
HHCCCCCCCCCHHHH		71.70-
464PhosphorylationAEEILQTYLKSKESM
HHHHHHHHHHCCHHH		10.12-
471SulfoxidationYLKSKESMTDAILQT
HHHCCHHHHHHHHHC		4.0530846556
495UbiquitinationEIEVERVKAESAQAS
HHHHHHHHHHHHHHH		53.2924816145
498PhosphorylationVERVKAESAQASAKM
HHHHHHHHHHHHHHH		30.4629978859
502PhosphorylationKAESAQASAKMLQEM
HHHHHHHHHHHHHHH		19.1529978859
516SulfoxidationMQRKNEQMMEQKERS
HHHHHHHHHHHHHHH		2.3230846556
517SulfoxidationQRKNEQMMEQKERSY
HHHHHHHHHHHHHHH		5.0230846556
523PhosphorylationMMEQKERSYQEHLKQ
HHHHHHHHHHHHHHH		32.0627251275
534UbiquitinationHLKQLTEKMENDRVQ
HHHHHHHHHHHHHHH		46.4024816145
544"N6,N6-dimethyllysine"NDRVQLLKEQERTLA
HHHHHHHHHHHHHHH		66.98-
544AcetylationNDRVQLLKEQERTLA
HHHHHHHHHHHHHHH		66.9825953088
544UbiquitinationNDRVQLLKEQERTLA
HHHHHHHHHHHHHHH		66.9824816145
544MethylationNDRVQLLKEQERTLA
HHHHHHHHHHHHHHH		66.9823644510
553AcetylationQERTLALKLQEQEQL
HHHHHHHHHHHHHHH		42.387966085
562UbiquitinationQEQEQLLKEGFQKES
HHHHHHHHHHHHHHH		65.4729967540
562AcetylationQEQEQLLKEGFQKES
HHHHHHHHHHHHHHH		65.477966095
573AcetylationQKESRIMKNEIQDLQ
HHHHHHHHHHHHHHH		49.4025953088
573UbiquitinationQKESRIMKNEIQDLQ
HHHHHHHHHHHHHHH		49.4024816145
573MalonylationQKESRIMKNEIQDLQ
HHHHHHHHHHHHHHH		49.4026320211
582UbiquitinationEIQDLQTKMRRRKAC
HHHHHHHHHHHHHCC		19.9029967540
589FarnesylationKMRRRKACTIS----
HHHHHHCCCCC----		3.788830800
589FarnesylationKMRRRKACTIS----
HHHHHHCCCCC----		3.788830800
589MethylationKMRRRKACTIS----
HHHHHHCCCCC----		3.78-
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
-KUbiquitinationE3 ubiquitin ligaseipaH9.8Q8VSC3
PMID:31216343
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GBP1_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 GBP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATPB_HUMANATP5Bphysical
22863883
FERM2_HUMANFERMT2physical
22863883
G3P_HUMANGAPDHphysical
22863883
PSA_HUMANNPEPPSphysical
22863883
GBP3_HUMANGBP3physical
28514442
GBP2_HUMANGBP2physical
28514442
GBB2_HUMANGNB2physical
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 GBP1_HUMAN

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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"Prenylation of an interferon-gamma-induced GTP-binding protein: thehuman guanylate binding protein, huGBP1.";
Nantais D.E., Schwemmle M., Stickney J.T., Vestal D.J., Buss J.E.;
J. Leukoc. Biol. 60:423-431(1996).
Cited for: ISOPRENYLATION AT CYS-589.

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