P03995 (GFAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 119.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glial fibrillary acidic protein Short name=GFAP | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 430 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells. |
| Subunit structure | Interacts with SYNM. Ref.18 |
| Subcellular location | Cytoplasm By similarity. Note: Associated with intermediate filaments By similarity. |
| Tissue specificity | Brain; isoform 2 expressed at 20-fold lower level than isoform 1. Ref.16 |
| Post-translational modification | Phosphorylated by PKN1 By similarity. |
| Sequence similarities | Belongs to the intermediate filament family. |
| Sequence caution | The sequence CAA26571.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: P03995-1) Also known as: GFAP alpha; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: P03995-2) Also known as: GFAP epsilon; The sequence of this isoform differs from the canonical sequence as follows: 388-430: ETSLDTKSVS...SKQEHKDVVM → GGKSTKEGEG...IENGALPALP |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 430 | 430 | Glial fibrillary acidic protein | PRO_0000063806 | |||||
Regions | |||||||||
| Region | 1 – 69 | 69 | Head | ||||||
| Region | 70 – 374 | 305 | Rod | ||||||
| Region | 70 – 101 | 32 | Coil 1A | ||||||
| Region | 102 – 112 | 11 | Linker 1 | ||||||
| Region | 113 – 211 | 99 | Coil 1B | ||||||
| Region | 212 – 227 | 16 | Linker 12 | ||||||
| Region | 228 – 249 | 22 | Coil 2A | ||||||
| Region | 250 – 253 | 4 | Linker 2 | ||||||
| Region | 254 – 374 | 121 | Coil 2B | ||||||
| Region | 375 – 430 | 56 | Tail | ||||||
Amino acid modifications | |||||||||
| Modified residue | 7 | 1 | Phosphothreonine; by AURKB and ROCK1 By similarity | ||||||
| Modified residue | 12 | 1 | Phosphoserine; by AURKB and ROCK1 By similarity | ||||||
| Modified residue | 35 | 1 | Phosphoserine; by AURKB and ROCK1 By similarity | ||||||
| Modified residue | 40 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 107 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 380 | 1 | Phosphothreonine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 388 – 430 | 43 | ETSLD…KDVVM → GGKSTKEGEGQKVTRPLKRL TIQVVPIQAHQIENGALPAL P in isoform 2. | VSP_017053 | |||||
Experimental info | |||||||||
| Sequence conflict | 141 | 1 | F → L in AAP33501. Ref.5 | ||||||
| Sequence conflict | 141 | 1 | F → L in AAK56091. Ref.10 | ||||||
| Sequence conflict | 174 | 1 | D → H in CAA26571. Ref.1 | ||||||
| Sequence conflict | 174 | 1 | D → H in AAA37678. Ref.7 | ||||||
| Sequence conflict | 174 | 1 | D → H in AAA37679. Ref.8 | ||||||
| Sequence conflict | 174 | 1 | D → H in ABI54133. Ref.13 | ||||||
| Sequence conflict | 180 | 1 | R → S in BAE24257. Ref.2 | ||||||
| Sequence conflict | 207 | 1 | E → D in CAA26571. Ref.1 | ||||||
| Sequence conflict | 207 | 1 | E → D in AAA37678. Ref.7 | ||||||
| Sequence conflict | 207 | 1 | E → D in AAA37679. Ref.8 | ||||||
| Sequence conflict | 347 | 1 | Q → H in CAA26571. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structure of the mouse glial fibrillary acidic protein gene: implications for the evolution of the intermediate filament multigene family." Balcarek J.M., Cowan N.J. Nucleic Acids Res. 13:5527-5543(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Corpora quadrigemina. |
| [3] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain. |
| [5] | Sheng J., Wu X., Lin F., Yang X., Deng J. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150. Strain: 129/Sv. |
| [6] | "Identification of two N-terminal non-alpha-helical domain motifs important in the assembly of glial fibrillary acidic protein." Ralton J.E., Lu X., Hutcheson A.M., Quinlan R.A. J. Cell Sci. 107:1935-1948(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. Tissue: Embryo. |
| [7] | "Sequence of a cDNA clone encoding mouse glial fibrillary acidic protein: structural conservation of intermediate filaments." Lewis S.A., Balcarek J.M., Krek V., Shelanski M., Cowan N.J. Proc. Natl. Acad. Sci. U.S.A. 81:2743-2746(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-430 (ISOFORM 1). |
| [8] | "Structural implications of a cDNA clone encoding mouse glial fibrillary acidic protein." Cowan N.J., Lewis S.A., Balcarek J.M., Krek V., Shelanski M.L. Ann. N. Y. Acad. Sci. 455:575-582(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-430 (ISOFORM 1). |
| [9] | "Characterization of human cDNA and genomic clones for glial fibrillary acidic protein." Brenner M., Lampel K., Nakatani Y., Mill J., Banner C., Mearow K., Dohadwala M., Lipsky R., Freese E. Brain Res. Mol. Brain Res. 7:277-286(1990) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO N-TERMINUS. |
| [10] | "High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-430 (ISOFORM 1). Strain: ISS. |
| [11] | "Novel metastatic mouse tumor cells express multiple properties of macrophages." Huysentruyt L.C., Banerjee D., Seyfried T.N. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-275 (ISOFORMS 1/2). Strain: C57BL/6. |
| [12] | Lubec G., Klug S., Kang S.U. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 47-63; 139-149; 187-198; 210-233; 285-297 AND 374-387, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus. |
| [13] | "Progressive demyelination despite a temporary increased number of NG-2 positive putative oligodendroglial progenitor cells in Theiler`s murine encephalomyelitis." Ulrich R., Alldinger S., Baumgaertner W. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 169-237 (ISOFORMS 1/2). Strain: SJL/JHanHsd. Tissue: Brain. |
| [14] | Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 354-364, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus. |
| [15] | "Genetic polymorphism and sequence evolution of an alternatively spliced exon of the glial fibrillary acidic protein gene, GFAP." Singh R., Nielsen A.L., Johansen M.G., Jorgensen A.L. Genomics 82:185-193(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-430 (ISOFORM 2). Tissue: Blood. |
| [16] | "A new splice variant of glial fibrillary acidic protein GFAPepsilon, interacts with the presenilin proteins." Nielsen A.L., Holm I.E., Johansen M., Bonven B., Jorgensen P., Jorgensen A.L. J. Biol. Chem. 277:29983-29991(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [17] | "Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-40, MASS SPECTROMETRY. Tissue: Brain. |
| [18] | "Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks." Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M., Skalli O. J. Cell Sci. 120:1267-1277(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYNM. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X02801 Genomic DNA. Translation: CAA26571.1. Different initiation. AK140151 mRNA. Translation: BAE24257.1. AL731670 Genomic DNA. Translation: CAM25115.1. AY279974 Genomic DNA. Translation: AAP33501.1. X78141 Genomic DNA. Translation: CAA55020.1. BC100728 mRNA. Translation: AAI00729.1. BC100737 mRNA. Translation: AAI00738.1. BC101968 mRNA. Translation: AAI01969.1. BC103571 mRNA. Translation: AAI03572.1. BC139357 mRNA. Translation: AAI39358.1. BC139358 mRNA. Translation: AAI39359.1. K01347 mRNA. Translation: AAA37678.1. M25937 mRNA. Translation: AAA37679.1. AF332061 mRNA. Translation: AAK56090.1. AF332062 mRNA. Translation: AAK56091.1. EF101554 mRNA. Translation: ABK96803.1. DQ887822 mRNA. Translation: ABI54133.1. AY142200 Genomic DNA. Translation: AAN87913.1. |
| IPI | IPI00117042. IPI00649033. |
| PIR | VEMSGF. B60052. |
| RefSeq | NP_001124492.1. NM_001131020.1. NP_034407.2. NM_010277.3. |
| UniGene | Mm.1239. |
3D structure databases | |
| ProteinModelPortal | P03995. |
| SMR | P03995. Positions 62-200, 226-369. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-1084N. |
| IntAct | P03995. 2 interactions. |
PTM databases | |
| PhosphoSite | P03995. |
2D gel databases | |
| UCD-2DPAGE | P03995. |
Proteomic databases | |
| PaxDb | P03995. |
| PRIDE | P03995. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000067444; ENSMUSP00000064691; ENSMUSG00000020932. ENSMUST00000077902; ENSMUSP00000077061; ENSMUSG00000020932. |
| GeneID | 14580. |
| KEGG | mmu:14580. |
| UCSC | uc007lsw.2. mouse. uc007lsx.2. mouse. |
Organism-specific databases | |
| CTD | 2670. |
| MGI | MGI:95697. Gfap. |
Phylogenomic databases | |
| eggNOG | NOG259463. |
| GeneTree | ENSGT00660000095344. |
| HOVERGEN | HBG013015. |
| InParanoid | B2RTI7. |
| KO | K05640. |
| OMA | ASSNMQE. |
| OrthoDB | EOG48WC24. |
Gene expression databases | |
| ArrayExpress | P03995. |
| Bgee | P03995. |
| CleanEx | MM_GFAP. |
| Genevestigator | P03995. |
| GermOnline | ENSMUSG00000020932. Mus musculus. |
Family and domain databases | |
| InterPro | IPR016044. F. IPR001664. IF. IPR006821. Intermed_filament_DNA-bd. IPR018039. Intermediate_filament_CS. [Graphical view] |
| PANTHER | PTHR23239. PTHR23239. 1 hit. |
| Pfam | PF00038. Filament. 1 hit. PF04732. Filament_head. 1 hit. [Graphical view] |
| PROSITE | PS00226. IF. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 286306. |
| SOURCE | Search... |
Entry information
| Entry name | GFAP_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P03995 Secondary accession number(s): A1E2H7 Q925K3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
