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P03995

- GFAP_MOUSE

UniProt

P03995 - GFAP_MOUSE

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Protein

Glial fibrillary acidic protein

Gene

Gfap

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. structural constituent of cytoskeleton Source: Ensembl
  2. 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
Complete GO annotation...

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 end-foot Source: MGI
  2. astrocyte projection Source: MGI
  3. cell body Source: MGI
  4. cell projection Source: MGI
  5. cytoplasm Source: MGI
  6. intermediate filament Source: MGI
  7. membrane Source: MGI
Complete GO annotation...

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

BgeeiP03995.
CleanExiMM_GFAP.
ExpressionAtlasiP03995. baseline and differential.
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.
GeneTreeiENSGT00760000118905.
HOVERGENiHBG013015.
InParanoidiP03995.
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

        10         20         30         40         50
MERRRITSAR RSYASETVVR GLGPSRQLGT MPRFSLSRMT PPLPARVDFS
60 70 80 90 100
LAGALNAGFK ETRASERAEM MELNDRFASY IEKVRFLEQQ NKALAAELNQ
110 120 130 140 150
LRAKEPTKLA DVYQAELREL RLRLDQLTAN SARLEVERDN FAQDLGTLRQ
160 170 180 190 200
KLQDETNLRL EAENNLAAYR QEADEATLAR VDLERKVESL EEEIQFLRKI
210 220 230 240 250
YEEEVRELRE QLAQQQVHVE MDVAKPDLTA ALREIRTQYE AVATSNMQET
260 270 280 290 300
EEWYRSKFAD LTDAASRNAE LLRQAKHEAN DYRRQLQALT CDLESLRGTN
310 320 330 340 350
ESLERQMREQ EERHARESAS YQEALARLEE EGQSLKEEMA RHLQEYQDLL
360 370 380 390 400
NVKLALDIEI ATYRKLLEGE ENRITIPVQT FSNLQIRETS LDTKSVSEGH
410 420 430
LKRNIVVKTV EMRDGEVIKD SKQEHKDVVM
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000118905.
HOVERGENi HBG013015.
InParanoidi P03995.
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

Bgeei P03995.
CleanExi MM_GFAP.
ExpressionAtlasi P03995. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 134 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