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HUMAN:GFAP

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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

PMID:15732097[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1904714

regulation of chaperone-mediated autophagy

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q864W9

P

Seeded From UniProt

complete

colocalizes_with

GO:0005764

lysosome

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q864W9

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:12355421[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:25910212[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P14136

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:25416956[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P14136

F

Seeded From UniProt

complete

enables

GO:0005198

structural molecule activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001664

F

Seeded From UniProt

complete

part_of

GO:0005882

intermediate filament

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001664
InterPro:IPR006821
InterPro:IPR027701

C

Seeded From UniProt

complete

involved_in

GO:0043254

regulation of protein complex assembly

PMID:20176123[5]

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

PMID:20176123[5]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005882

intermediate filament

PMID:2740350[6]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005200

structural constituent of cytoskeleton

PMID:2740350[6]

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

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0403

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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
  2. 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
  3. Sahni, N et al. (2015) Widespread macromolecular interaction perturbations in human genetic disorders. Cell 161 647-660 PubMed GONUTS page
  4. Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page
  5. 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. 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