GBP1
Guanylate-binding protein 1
Also known as: GBP1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P32455
- Gene
- GBP1
- Ensembl
- ENSG00000117228
- Chromosome
- 1
- Canonical length
- 592 aa
- Protein class
- Plasma proteins, Predicted intracellular proteins
- Secretome location
- Intracellular and membrane
- Quaternary structure
- Homodimer
OverviewNCBI Gene
Guanylate binding protein expression is induced by interferon. Guanylate binding proteins are characterized by their ability to specifically bind guanine nucleotides (GMP, GDP, and GTP) and are distinguished from the GTP-binding proteins by the presence of 2 binding motifs rather than 3. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
592 residues, UniProt reviewed canonical sequence.
>P32455|GBP1
1 MASEIHMTGP MCLIENTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG KSYLMNKLAG
61 KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG LGDVEKGDNQ NDSWIFALAV
121 LLSSTFVYNS IGTINQQAMD QLYYVTELTH RIRSKSSPDE NENEVEDSAD FVSFFPDFVW
181 TLRDFSLDLE ADGQPLTPDE YLTYSLKLKK GTSQKDETFN LPRLCIRKFF PKKKCFVFDR
241 PVHRRKLAQL EKLQDEELDP EFVQQVADFC SYIFSNSKTK TLSGGIQVNG PRLESLVLTY
301 VNAISSGDLP CMENAVLALA QIENSAAVQK AIAHYEQQMG QKVQLPTETL QELLDLHRDS
361 EREAIEVFIR SSFKDVDHLF QKELAAQLEK KRDDFCKQNQ EASSDRCSAL LQVIFSPLEE
421 EVKAGIYSKP GGYRLFVQKL QDLKKKYYEE PRKGIQAEEI LQTYLKSKES MTDAILQTDQ
481 TLTEKEKEIE VERVKAESAQ ASAKMLQEMQ RKNEQMMEQK ERSYQEHLKQ LTEKMENDRV
541 QLLKEQERTL ALKLQEQEQL LKEGFQKESR IMKNEIQDLQ TKMRRRKACT ISLocalizationUniProt · AlphaFold · HPA
Whether an antibody against GBP1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.27
- Highest tissue expression
- 82 nTPM
Expression across tissuesHPA
Tissue
- liver: 82 nTPM
- appendix: 68 nTPM
- lymph node: 52 nTPM
- spleen: 49 nTPM
- lung: 42 nTPM
- gallbladder: 42 nTPM
Single-cell type
- epididymal basal cells: 754 nCPM
- epididymal efferent duct ciliated cells: 290 nCPM
- decidual stromal cells: 200 nCPM
- migrating cytotrophoblasts: 145 nCPM
- pancreatic duct cells: 112 nCPM
- fallopian secretory cells: 104 nCPM
Immune cell
- T-reg: 174 nTPM
- non-classical monocyte: 135 nTPM
- intermediate monocyte: 127 nTPM
- neutrophil: 107 nTPM
- memory CD8 T-cell: 100 nTPM
- gdT-cell: 95 nTPM
Brain region
- medulla oblongata: 38 nTPM
- pons: 22 nTPM
- spinal cord: 9.6 nTPM
- thalamus: 8.2 nTPM
- white matter: 7.9 nTPM
- hypothalamus: 7.7 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.23
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.45
- DepMap mean gene effect
- 0.1
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cellular response to interleukin-1
- cellular response to tumor necrosis factor
- cellular response to type II interferon
- cytolysis in another organism
- defense response to bacterium
- defense response to protozoan
- defense response to virus
- innate immune response
- negative regulation of ERK1 and ERK2 cascade
- negative regulation of interleukin-2 production
- negative regulation of protein localization to plasma membrane
- negative regulation of substrate adhesion-dependent cell spreading
- negative regulation of T cell receptor signaling pathway
- non-canonical inflammasome complex assembly
- positive regulation of pyroptotic inflammatory response
- protein localization to vacuole
- regulation of calcium-mediated signaling
- regulation of protein localization to plasma membrane
Molecular functions
- actin binding
- cytokine binding
- enzyme binding
- G protein activity
- GDP binding
- GDP phosphatase activity
- GTP binding
- GTPase activity
- Hsp90 protein binding
- identical protein binding
- lipopolysaccharide binding
- protein homodimerization activity
- spectrin binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Guanylate-binding protein/Atlastin, C-terminal
- Guanylate-binding protein, N-terminal
- P-loop containing nucleoside triphosphate hydrolase
- GB1/RHD3-type guanine nucleotide-binding (G) domain
- Guanylate-binding protein, C-terminal domain superfamily
- Guanylate-binding protein, C-terminal
- Guanylate-binding protein, N-terminal domain
- Guanylate-binding protein, C-terminal domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of GBP1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads GBP1 as an antibody target. Whether an autoantibody or antibody against GBP1 could matter depends on whether native GBP1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
GBP1 is annotated at the cell surface, where native GBP1 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label GBP1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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