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P03995

- GFAP_MOUSE

UniProt

P03995 - GFAP_MOUSE

Protein

Glial fibrillary acidic protein

Gene

Gfap

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 4 (01 May 2007)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. structural constituent of cytoskeleton Source: Ensembl
    3. structural molecule activity Source: MGI

    GO - Biological processi

    1. astrocyte development Source: MGI
    2. Bergmann glial cell differentiation Source: MGI
    3. extracellular matrix organization Source: MGI
    4. intermediate filament-based process Source: MGI
    5. intermediate filament organization Source: MGI
    6. long-term synaptic potentiation Source: MGI
    7. negative regulation of neuron projection development Source: MGI
    8. neuron projection regeneration Source: MGI
    9. positive regulation of Schwann cell proliferation Source: MGI
    10. regulation of neurotransmitter uptake Source: MGI
    11. response to wounding Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_198574. Nuclear signaling by ERBB4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glial fibrillary acidic protein
    Short name:
    GFAP
    Gene namesi
    Name:Gfap
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:95697. Gfap.

    Subcellular locationi

    Cytoplasm By similarity
    Note: Associated with intermediate filaments.By similarity

    GO - Cellular componenti

    1. astrocyte projection Source: MGI
    2. cell body Source: MGI
    3. cell projection Source: MGI
    4. cytoplasm Source: MGI
    5. intermediate filament Source: MGI
    6. membrane Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Intermediate filament

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Glial fibrillary acidic proteinPRO_0000063806Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei7 – 71Phosphothreonine; by AURKB and ROCK1By similarity
    Modified residuei12 – 121Phosphoserine; by AURKB and ROCK1By similarity
    Modified residuei33 – 331CitrullineBy similarity
    Modified residuei35 – 351Phosphoserine; by AURKB and ROCK1By similarity
    Modified residuei40 – 401Phosphothreonine1 Publication
    Modified residuei107 – 1071PhosphothreonineBy similarity
    Modified residuei267 – 2671CitrullineBy similarity
    Modified residuei380 – 3801PhosphothreonineBy similarity
    Modified residuei403 – 4031CitrullineBy similarity
    Modified residuei413 – 4131CitrullineBy similarity

    Post-translational modificationi

    Phosphorylated by PKN1.By similarity

    Keywords - PTMi

    Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiP03995.
    PaxDbiP03995.
    PRIDEiP03995.

    2D gel databases

    UCD-2DPAGEP03995.

    PTM databases

    PhosphoSiteiP03995.

    Expressioni

    Tissue specificityi

    Brain; isoform 2 expressed at 20-fold lower level than isoform 1.1 Publication

    Gene expression databases

    ArrayExpressiP03995.
    BgeeiP03995.
    CleanExiMM_GFAP.
    GenevestigatoriP03995.

    Interactioni

    Subunit structurei

    Interacts with SYNM.1 Publication

    Protein-protein interaction databases

    BioGridi199899. 5 interactions.
    DIPiDIP-1084N.
    IntActiP03995. 4 interactions.
    MINTiMINT-4095997.

    Structurei

    3D structure databases

    ProteinModelPortaliP03995.
    SMRiP03995. Positions 62-200, 226-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 6969HeadAdd
    BLAST
    Regioni70 – 374305RodAdd
    BLAST
    Regioni70 – 10132Coil 1AAdd
    BLAST
    Regioni102 – 11211Linker 1Add
    BLAST
    Regioni113 – 21199Coil 1BAdd
    BLAST
    Regioni212 – 22716Linker 12Add
    BLAST
    Regioni228 – 24922Coil 2AAdd
    BLAST
    Regioni250 – 2534Linker 2
    Regioni254 – 374121Coil 2BAdd
    BLAST
    Regioni375 – 43056TailAdd
    BLAST

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG259463.
    GeneTreeiENSGT00750000117235.
    HOVERGENiHBG013015.
    InParanoidiB2RTI7.
    KOiK05640.
    OMAiASSNMQE.
    OrthoDBiEOG7FV3Q8.
    PhylomeDBiP03995.
    TreeFamiTF330122.

    Family and domain databases

    InterProiIPR027701. GFAP.
    IPR001664. IF.
    IPR006821. Intermed_filament_DNA-bd.
    IPR018039. Intermediate_filament_CS.
    [Graphical view]
    PANTHERiPTHR23239. PTHR23239. 1 hit.
    PTHR23239:SF41. PTHR23239:SF41. 1 hit.
    PfamiPF00038. Filament. 1 hit.
    PF04732. Filament_head. 1 hit.
    [Graphical view]
    PROSITEiPS00226. IF. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P03995-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MERRRITSAR RSYASETVVR GLGPSRQLGT MPRFSLSRMT PPLPARVDFS    50
    LAGALNAGFK ETRASERAEM MELNDRFASY IEKVRFLEQQ NKALAAELNQ 100
    LRAKEPTKLA DVYQAELREL RLRLDQLTAN SARLEVERDN FAQDLGTLRQ 150
    KLQDETNLRL EAENNLAAYR QEADEATLAR VDLERKVESL EEEIQFLRKI 200
    YEEEVRELRE QLAQQQVHVE MDVAKPDLTA ALREIRTQYE AVATSNMQET 250
    EEWYRSKFAD LTDAASRNAE LLRQAKHEAN DYRRQLQALT CDLESLRGTN 300
    ESLERQMREQ EERHARESAS YQEALARLEE EGQSLKEEMA RHLQEYQDLL 350
    NVKLALDIEI ATYRKLLEGE ENRITIPVQT FSNLQIRETS LDTKSVSEGH 400
    LKRNIVVKTV EMRDGEVIKD SKQEHKDVVM 430
    Length:430
    Mass (Da):49,900
    Last modified:May 1, 2007 - v4
    Checksum:iC0FB500AE1588377
    GO
    Isoform 2 (identifier: P03995-2) [UniParc]FASTAAdd to Basket

    Also known as: GFAP epsilon

    The sequence of this isoform differs from the canonical sequence as follows:
         388-430: ETSLDTKSVS...SKQEHKDVVM → GGKSTKEGEG...IENGALPALP

    Show »
    Length:428
    Mass (Da):49,365
    Checksum:i778B9A6A8FDBA6D3
    GO

    Sequence cautioni

    The sequence CAA26571.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti141 – 1411F → L in AAP33501. 1 PublicationCurated
    Sequence conflicti141 – 1411F → L in AAK56091. (PubMed:11471062)Curated
    Sequence conflicti174 – 1741D → H in CAA26571. (PubMed:2994002)Curated
    Sequence conflicti174 – 1741D → H in AAA37678. (PubMed:6585825)Curated
    Sequence conflicti174 – 1741D → H in AAA37679. (PubMed:3866511)Curated
    Sequence conflicti174 – 1741D → H in ABI54133. 1 PublicationCurated
    Sequence conflicti180 – 1801R → S in BAE24257. (PubMed:16141072)Curated
    Sequence conflicti207 – 2071E → D in CAA26571. (PubMed:2994002)Curated
    Sequence conflicti207 – 2071E → D in AAA37678. (PubMed:6585825)Curated
    Sequence conflicti207 – 2071E → D in AAA37679. (PubMed:3866511)Curated
    Sequence conflicti347 – 3471Q → H in CAA26571. (PubMed:2994002)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei388 – 43043ETSLD…KDVVM → GGKSTKEGEGQKVTRPLKRL TIQVVPIQAHQIENGALPAL P in isoform 2. 1 PublicationVSP_017053Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS25507.1. [P03995-1]
    CCDS48950.1. [P03995-2]
    PIRiB60052. VEMSGF.
    RefSeqiNP_001124492.1. NM_001131020.1. [P03995-2]
    NP_034407.2. NM_010277.3. [P03995-1]
    UniGeneiMm.1239.

    Genome annotation databases

    EnsembliENSMUST00000067444; ENSMUSP00000064691; ENSMUSG00000020932. [P03995-1]
    ENSMUST00000077902; ENSMUSP00000077061; ENSMUSG00000020932. [P03995-2]
    GeneIDi14580.
    KEGGimmu:14580.
    UCSCiuc007lsw.2. mouse. [P03995-1]
    uc007lsx.2. mouse. [P03995-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS25507.1. [P03995-1 ]
    CCDS48950.1. [P03995-2 ]
    PIRi B60052. VEMSGF.
    RefSeqi NP_001124492.1. NM_001131020.1. [P03995-2 ]
    NP_034407.2. NM_010277.3. [P03995-1 ]
    UniGenei Mm.1239.

    3D structure databases

    ProteinModelPortali P03995.
    SMRi P03995. Positions 62-200, 226-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199899. 5 interactions.
    DIPi DIP-1084N.
    IntActi P03995. 4 interactions.
    MINTi MINT-4095997.

    PTM databases

    PhosphoSitei P03995.

    2D gel databases

    UCD-2DPAGE P03995.

    Proteomic databases

    MaxQBi P03995.
    PaxDbi P03995.
    PRIDEi P03995.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067444 ; ENSMUSP00000064691 ; ENSMUSG00000020932 . [P03995-1 ]
    ENSMUST00000077902 ; ENSMUSP00000077061 ; ENSMUSG00000020932 . [P03995-2 ]
    GeneIDi 14580.
    KEGGi mmu:14580.
    UCSCi uc007lsw.2. mouse. [P03995-1 ]
    uc007lsx.2. mouse. [P03995-2 ]

    Organism-specific databases

    CTDi 2670.
    MGIi MGI:95697. Gfap.

    Phylogenomic databases

    eggNOGi NOG259463.
    GeneTreei ENSGT00750000117235.
    HOVERGENi HBG013015.
    InParanoidi B2RTI7.
    KOi K05640.
    OMAi ASSNMQE.
    OrthoDBi EOG7FV3Q8.
    PhylomeDBi P03995.
    TreeFami TF330122.

    Enzyme and pathway databases

    Reactomei REACT_198574. Nuclear signaling by ERBB4.

    Miscellaneous databases

    NextBioi 286306.
    PROi P03995.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P03995.
    Bgeei P03995.
    CleanExi MM_GFAP.
    Genevestigatori P03995.

    Family and domain databases

    InterProi IPR027701. GFAP.
    IPR001664. IF.
    IPR006821. Intermed_filament_DNA-bd.
    IPR018039. Intermediate_filament_CS.
    [Graphical view ]
    PANTHERi PTHR23239. PTHR23239. 1 hit.
    PTHR23239:SF41. PTHR23239:SF41. 1 hit.
    Pfami PF00038. Filament. 1 hit.
    PF04732. Filament_head. 1 hit.
    [Graphical view ]
    PROSITEi PS00226. IF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiGFAP_MOUSE
    AccessioniPrimary (citable) accession number: P03995
    Secondary accession number(s): A1E2H7
    , A2AH87, B2RTI7, Q09J71, Q3USS4, Q496R4, Q496S3, Q7TQ30, Q80VX6, Q925K2, Q925K3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 1986
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 133 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3