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HUMAN:GFAP
Contents
Species (Taxon ID) | Homo sapiens (Human). (9606) | |
Gene Name(s) | GFAP | |
Protein Name(s) | Glial fibrillary acidic protein
GFAP | |
External Links | ||
UniProt | P14136 | |
EMBL | J04569 S40719 AF419299 AK128790 AK222683 AK315398 AL133013 AC015936 CH471178 CH471178 BC013596 BC041765 BC062609 M26638 AJ306447 AY142187 AY142188 AY142191 | |
CCDS | CCDS11491.1 CCDS45708.1 CCDS59296.1 | |
PIR | A32936 T42645 | |
RefSeq | NP_001124491.1 NP_001229305.1 NP_002046.1 | |
UniGene | Hs.514227 | |
ProteinModelPortal | P14136 | |
SMR | P14136 | |
BioGrid | 108938 | |
IntAct | P14136 | |
MINT | MINT-1450103 | |
PhosphoSite | P14136 | |
DMDM | 121135 | |
REPRODUCTION-2DPAGE | P14136 | |
UCD-2DPAGE | P14136 | |
MaxQB | P14136 | |
PaxDb | P14136 | |
PeptideAtlas | P14136 | |
PRIDE | P14136 | |
DNASU | 2670 | |
Ensembl | ENST00000253408 ENST00000435360 ENST00000586793 | |
GeneID | 2670 | |
KEGG | hsa:2670 | |
UCSC | uc002ihq.3 uc021tyh.1 | |
CTD | 2670 | |
GeneCards | GC17M042982 | |
GeneReviews | GFAP | |
HGNC | HGNC:4235 | |
HPA | CAB000039 HPA056030 | |
MIM | 137780 203450 | |
neXtProt | NX_P14136 | |
Orphanet | 363717 363722 | |
PharmGKB | PA28647 | |
eggNOG | NOG259463 | |
GeneTree | ENSGT00760000118905 | |
HOVERGEN | HBG013015 | |
InParanoid | P14136 | |
KO | K05640 | |
OMA | TYRQEAD | |
OrthoDB | EOG7FV3Q8 | |
PhylomeDB | P14136 | |
TreeFam | TF330122 | |
Reactome | REACT_116022 | |
ChiTaRS | GFAP | |
GeneWiki | Glial_fibrillary_acidic_protein | |
GenomeRNAi | 2670 | |
NextBio | 10538 | |
PMAP-CutDB | P14136 | |
PRO | PR:P14136 | |
Proteomes | UP000005640 | |
Bgee | P14136 | |
ExpressionAtlas | P14136 | |
Genevestigator | P14136 | |
GO | GO:0097449 GO:0044297 GO:0005737 GO:0005829 GO:0005882 GO:0016020 GO:0005200 GO:0014002 GO:0060020 GO:0030198 GO:0045109 GO:0060291 GO:0010977 GO:0031102 GO:0010625 GO:0051580 GO:0009611 | |
InterPro | IPR027701 IPR001664 IPR018039 | |
PANTHER | PTHR23239 PTHR23239:SF41 | |
Pfam | PF00038 | |
PROSITE | PS00226 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
involved_in |
GO:0045109 |
intermediate filament organization |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:1904714 |
regulation of chaperone-mediated autophagy |
ECO:0000250 |
sequence similarity evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
colocalizes_with |
GO:0005764 |
lysosome |
ECO:0000250 |
sequence similarity evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0005198 |
structural molecule activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005882 |
intermediate filament |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0043254 |
regulation of protein complex assembly |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
part_of:(GO:0061684) |
Seeded From UniProt |
complete | ||
involved_in |
GO:1904714 |
regulation of chaperone-mediated autophagy |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005882 |
intermediate filament |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0005200 |
structural constituent of cytoskeleton |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005829 |
cytosol |
Reactome:R-HSA-1253321 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
C |
Seeded From UniProt |
complete | ||
part_of |
GO:0005882 |
intermediate filament |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Li, R et al. (2005) Glial fibrillary acidic protein mutations in infantile, juvenile, and adult forms of Alexander disease. Ann. Neurol. 57 310-26 PubMed GONUTS page
- ↑ Ju, WK & Neufeld, AH (2002) Cellular localization of cyclooxygenase-1 and cyclooxygenase-2 in the normal mouse, rat, and human retina. J. Comp. Neurol. 452 392-9 PubMed GONUTS page
- ↑ Sahni, N et al. (2015) Widespread macromolecular interaction perturbations in human genetic disorders. Cell 161 647-660 PubMed GONUTS page
- ↑ Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page
- ↑ 5.0 5.1 Orenstein, SJ & Cuervo, AM (2010) Chaperone-mediated autophagy: molecular mechanisms and physiological relevance. Semin. Cell Dev. Biol. 21 719-26 PubMed GONUTS page
- ↑ 6.0 6.1 Reeves, SA et al. (1989) Molecular cloning and primary structure of human glial fibrillary acidic protein. Proc. Natl. Acad. Sci. U.S.A. 86 5178-82 PubMed GONUTS page
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