Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P03995 (GFAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glial fibrillary acidic protein

Short name=GFAP
Gene names
Name:Gfap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Keywords
   Cellular componentCytoplasm
Intermediate filament
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMCitrullination
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processBergmann glial cell differentiation

Inferred from mutant phenotype PubMed 10816608. Source: MGI

astrocyte development

Inferred from genetic interaction PubMed 11487638. Source: MGI

extracellular matrix organization

Inferred from mutant phenotype PubMed 11487638. Source: MGI

intermediate filament organization

Inferred from mutant phenotype PubMed 8692820. Source: MGI

intermediate filament-based process

Inferred from mutant phenotype PubMed 12177195. Source: MGI

long-term synaptic potentiation

Inferred from mutant phenotype PubMed 8692820. Source: MGI

negative regulation of neuron projection development

Inferred from mutant phenotype PubMed 11487638. Source: MGI

neuron projection regeneration

Inferred from mutant phenotype PubMed 16988027. Source: MGI

positive regulation of Schwann cell proliferation

Inferred from mutant phenotype PubMed 16988027. Source: MGI

regulation of neurotransmitter uptake

Inferred from mutant phenotype PubMed 15135219. Source: MGI

response to wounding

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentastrocyte projection

Inferred from direct assay PubMed 19646951PubMed 23861879PubMed 24035762. Source: MGI

cell body

Inferred from direct assay PubMed 20578039PubMed 24035762PubMed 8793730. Source: MGI

cell projection

Inferred from direct assay PubMed 10989258. Source: MGI

cytoplasm

Inferred from direct assay PubMed 11064363PubMed 11834298PubMed 12074840PubMed 15965470PubMed 18076286. Source: MGI

intermediate filament

Inferred from direct assay PubMed 11487638PubMed 12533615PubMed 12878680PubMed 15656993PubMed 9364068. Source: MGI

membrane

Inferred from direct assay PubMed 11283023. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction Ref.18. Source: UniProtKB

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: Ensembl

structural molecule activity

Inferred from mutant phenotype PubMed 12177195. Source: MGI

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Glial fibrillary acidic protein
PRO_0000063806

Regions

Region1 – 6969Head
Region70 – 374305Rod
Region70 – 10132Coil 1A
Region102 – 11211Linker 1
Region113 – 21199Coil 1B
Region212 – 22716Linker 12
Region228 – 24922Coil 2A
Region250 – 2534Linker 2
Region254 – 374121Coil 2B
Region375 – 43056Tail

Amino acid modifications

Modified residue71Phosphothreonine; by AURKB and ROCK1 By similarity
Modified residue121Phosphoserine; by AURKB and ROCK1 By similarity
Modified residue331Citrulline By similarity
Modified residue351Phosphoserine; by AURKB and ROCK1 By similarity
Modified residue401Phosphothreonine Ref.17
Modified residue1071Phosphothreonine By similarity
Modified residue2671Citrulline By similarity
Modified residue3801Phosphothreonine By similarity
Modified residue4031Citrulline By similarity
Modified residue4131Citrulline By similarity

Natural variations

Alternative sequence388 – 43043ETSLD…KDVVM → GGKSTKEGEGQKVTRPLKRL TIQVVPIQAHQIENGALPAL P in isoform 2.
VSP_017053

Experimental info

Sequence conflict1411F → L in AAP33501. Ref.5
Sequence conflict1411F → L in AAK56091. Ref.10
Sequence conflict1741D → H in CAA26571. Ref.1
Sequence conflict1741D → H in AAA37678. Ref.7
Sequence conflict1741D → H in AAA37679. Ref.8
Sequence conflict1741D → H in ABI54133. Ref.13
Sequence conflict1801R → S in BAE24257. Ref.2
Sequence conflict2071E → D in CAA26571. Ref.1
Sequence conflict2071E → D in AAA37678. Ref.7
Sequence conflict2071E → D in AAA37679. Ref.8
Sequence conflict3471Q → H in CAA26571. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GFAP alpha) [UniParc].

Last modified May 1, 2007. Version 4.
Checksum: C0FB500AE1588377

FASTA43049,900
        10         20         30         40         50         60 
MERRRITSAR RSYASETVVR GLGPSRQLGT MPRFSLSRMT PPLPARVDFS LAGALNAGFK 

        70         80         90        100        110        120 
ETRASERAEM MELNDRFASY IEKVRFLEQQ NKALAAELNQ LRAKEPTKLA DVYQAELREL 

       130        140        150        160        170        180 
RLRLDQLTAN SARLEVERDN FAQDLGTLRQ KLQDETNLRL EAENNLAAYR QEADEATLAR 

       190        200        210        220        230        240 
VDLERKVESL EEEIQFLRKI YEEEVRELRE QLAQQQVHVE MDVAKPDLTA ALREIRTQYE 

       250        260        270        280        290        300 
AVATSNMQET EEWYRSKFAD LTDAASRNAE LLRQAKHEAN DYRRQLQALT CDLESLRGTN 

       310        320        330        340        350        360 
ESLERQMREQ EERHARESAS YQEALARLEE EGQSLKEEMA RHLQEYQDLL NVKLALDIEI 

       370        380        390        400        410        420 
ATYRKLLEGE ENRITIPVQT FSNLQIRETS LDTKSVSEGH LKRNIVVKTV EMRDGEVIKD 

       430 
SKQEHKDVVM 

« Hide

Isoform 2 (GFAP epsilon) [UniParc].

Checksum: 778B9A6A8FDBA6D3
Show »

FASTA42849,365

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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
CCDSCCDS25507.1. [P03995-1]
CCDS48950.1. [P03995-2]
PIRVEMSGF. B60052.
RefSeqNP_001124492.1. NM_001131020.1. [P03995-2]
NP_034407.2. NM_010277.3. [P03995-1]
UniGeneMm.1239.

3D structure databases

ProteinModelPortalP03995.
SMRP03995. Positions 62-200, 226-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199899. 5 interactions.
DIPDIP-1084N.
IntActP03995. 4 interactions.
MINTMINT-4095997.

PTM databases

PhosphoSiteP03995.

2D gel databases

UCD-2DPAGEP03995.

Proteomic databases

MaxQBP03995.
PaxDbP03995.
PRIDEP03995.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067444; ENSMUSP00000064691; ENSMUSG00000020932. [P03995-1]
ENSMUST00000077902; ENSMUSP00000077061; ENSMUSG00000020932. [P03995-2]
GeneID14580.
KEGGmmu:14580.
UCSCuc007lsw.2. mouse. [P03995-1]
uc007lsx.2. mouse. [P03995-2]

Organism-specific databases

CTD2670.
MGIMGI:95697. Gfap.

Phylogenomic databases

eggNOGNOG259463.
GeneTreeENSGT00750000117235.
HOVERGENHBG013015.
InParanoidB2RTI7.
KOK05640.
OMAASSNMQE.
OrthoDBEOG7FV3Q8.
PhylomeDBP03995.
TreeFamTF330122.

Gene expression databases

ArrayExpressP03995.
BgeeP03995.
CleanExMM_GFAP.
GenevestigatorP03995.

Family and domain databases

InterProIPR027701. GFAP.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF41. PTHR23239:SF41. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio286306.
PROP03995.
SOURCESearch...

Entry information

Entry nameGFAP_MOUSE
AccessionPrimary (citable) accession number: P03995
Secondary accession number(s): A1E2H7 expand/collapse secondary AC list , A2AH87, B2RTI7, Q09J71, Q3USS4, Q496R4, Q496S3, Q7TQ30, Q80VX6, Q925K2, Q925K3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 131 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot