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P14136 (GFAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glial fibrillary acidic protein

Short name=GFAP
Gene names
Name:GFAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length432 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 By similarity. Isoform 3 interacts with PSEN1 (via N-terminus). Ref.16

Subcellular location

Cytoplasm. Note: Associated with intermediate filaments. Ref.16

Tissue specificity

Expressed in cells lacking fibronectin. Ref.3

Post-translational modification

Phosphorylated by PKN1. Ref.18 Ref.19 Ref.20

Involvement in disease

Alexander disease (ALEXD) [MIM:203450]: A rare disorder of the central nervous system. The most common form affects infants and young children, and is characterized by progressive failure of central myelination, usually leading to death within the first decade. Infants with Alexander disease develop a leukodystrophy with macrocephaly, seizures, and psychomotor retardation. Patients with juvenile or adult forms typically experience ataxia, bulbar signs and spasticity, and a more slowly progressive course. Histologically, Alexander disease is characterized by Rosenthal fibers, homogeneous eosinophilic inclusions in astrocytes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27

Sequence similarities

Belongs to the intermediate filament family.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

astrocyte development

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

intermediate filament organization

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

neuron projection regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of Schwann cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of neurotransmitter uptake

Inferred from electronic annotation. Source: Ensembl

response to wounding

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentastrocyte projection

Inferred from electronic annotation. Source: Ensembl

cell body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 12355421. Source: MGI

cytosol

Traceable author statement. Source: Reactome

intermediate filament

Traceable author statement Ref.1. Source: ProtInc

membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionstructural constituent of cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoforms differ in the C-terminal region which is encoded by alternative exons.
Isoform 1 (identifier: P14136-1)

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: P14136-2)

The sequence of this isoform differs from the canonical sequence as follows:
     391-432: ETSLDTKSVS...ESKQEHKDVM → GQYSRASWEG...LGAFVTLQRS
Note: No experimental confirmation available.
Isoform 3 (identifier: P14136-3)

Also known as: GFAP epsilon;

The sequence of this isoform differs from the canonical sequence as follows:
     391-432: ETSLDTKSVS...ESKQEHKDVM → GGKSTKDGEN...IVNGTPPARG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Glial fibrillary acidic protein
PRO_0000063805

Regions

Region1 – 7272Head
Region73 – 377305Rod
Region73 – 10432Coil 1A
Region105 – 11511Linker 1
Region116 – 21499Coil 1B
Region215 – 23016Linker 12
Region231 – 25222Coil 2A
Region253 – 2564Linker 2
Region257 – 377121Coil 2B
Region378 – 43255Tail

Amino acid modifications

Modified residue71Phosphothreonine; by AURKB and ROCK1 Ref.19 Ref.20
Modified residue131Phosphoserine; by AURKB and ROCK1 Ref.19 Ref.20
Modified residue301Citrulline
Modified residue361Citrulline
Modified residue381Phosphoserine; by AURKB and ROCK1 Ref.19 Ref.20
Modified residue1101Phosphothreonine By similarity
Modified residue2701Citrulline
Modified residue3831Phosphothreonine By similarity
Modified residue4061Citrulline
Modified residue4161Citrulline

Natural variations

Alternative sequence391 – 43242ETSLD…HKDVM → GQYSRASWEGHWSPAPSSRA CRLLQTGTEDQGKGIQLSLG AFVTLQRS in isoform 2.
VSP_017051
Alternative sequence391 – 43242ETSLD…HKDVM → GGKSTKDGENHKVTRYLKSL TIRVIPIQAHQIVNGTPPAR G in isoform 3.
VSP_017052
Natural variant471P → L in ALEXD; unknown pathological significance. Ref.22
Corresponds to variant rs57474185 [ dbSNP | Ensembl ].
VAR_017464
Natural variant761L → F in ALEXD. Ref.23
Corresponds to variant rs57120761 [ dbSNP | Ensembl ].
VAR_017465
Natural variant771N → Y in ALEXD. Ref.23
Corresponds to variant rs58732244 [ dbSNP | Ensembl ].
VAR_017466
Natural variant781D → E in ALEXD; adult form. Ref.26
VAR_017477
Natural variant791R → C in ALEXD. Ref.22
Corresponds to variant rs59793293 [ dbSNP | Ensembl ].
VAR_017467
Natural variant791R → H in ALEXD. Ref.22 Ref.23
Corresponds to variant rs59285727 [ dbSNP | Ensembl ].
VAR_017468
Natural variant881R → C in ALEXD. Ref.23
Corresponds to variant rs61622935 [ dbSNP | Ensembl ].
VAR_017469
Natural variant881R → S in ALEXD. Ref.23
VAR_017470
Natural variant2231E → Q in ALEXD; adult form. Ref.27
Corresponds to variant rs56679084 [ dbSNP | Ensembl ].
VAR_017478
Natural variant2391R → C in ALEXD. Ref.22 Ref.23
Corresponds to variant rs58064122 [ dbSNP | Ensembl ].
VAR_017471
Natural variant2391R → H in ALEXD. Ref.22 Ref.23
Corresponds to variant rs59565950 [ dbSNP | Ensembl ].
VAR_017472
Natural variant2441A → V in ALEXD. Ref.24
Corresponds to variant rs61497286 [ dbSNP | Ensembl ].
VAR_017473
Natural variant2581R → P in ALEXD. Ref.22
Corresponds to variant rs61726468 [ dbSNP | Ensembl ].
VAR_017474
Natural variant2951D → N. Ref.5 Ref.22
Corresponds to variant rs1126642 [ dbSNP | Ensembl ].
VAR_017479
Natural variant3621E → D in ALEXD. Ref.25
Corresponds to variant rs28932768 [ dbSNP | Ensembl ].
VAR_017475
Natural variant4161R → W in ALEXD. Ref.22
VAR_017476
Isoform 3:
Natural variant4261T → A.
Natural variant4261T → V.

Experimental info

Sequence conflict1211R → P in CAB61354. Ref.9
Sequence conflict1461Q → H Ref.3
Sequence conflict1511V → L Ref.3
Sequence conflict1551Missing in CAB61354. Ref.9
Sequence conflict1581E → G in AAL16662. Ref.6
Sequence conflict1601N → K Ref.3
Sequence conflict1661E → D Ref.3
Sequence conflict1741Q → QQ in CAB61354. Ref.9
Sequence conflict2581R → H Ref.3
Sequence conflict3261E → V in BAD96403. Ref.8
Sequence conflict3341E → D Ref.3

Sequences

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

Last modified January 1, 1990. Version 1.
Checksum: E6C3B3454C3F1250

FASTA43249,880
        10         20         30         40         50         60 
MERRRITSAA RRSYVSSGEM MVGGLAPGRR LGPGTRLSLA RMPPPLPTRV DFSLAGALNA 

        70         80         90        100        110        120 
GFKETRASER AEMMELNDRF ASYIEKVRFL EQQNKALAAE LNQLRAKEPT KLADVYQAEL 

       130        140        150        160        170        180 
RELRLRLDQL TANSARLEVE RDNLAQDLAT VRQKLQDETN LRLEAENNLA AYRQEADEAT 

       190        200        210        220        230        240 
LARLDLERKI ESLEEEIRFL RKIHEEEVRE LQEQLARQQV HVELDVAKPD LTAALKEIRT 

       250        260        270        280        290        300 
QYEAMASSNM HEAEEWYRSK FADLTDAAAR NAELLRQAKH EANDYRRQLQ SLTCDLESLR 

       310        320        330        340        350        360 
GTNESLERQM REQEERHVRE AASYQEALAR LEEEGQSLKD EMARHLQEYQ DLLNVKLALD 

       370        380        390        400        410        420 
IEIATYRKLL EGEENRITIP VQTFSNLQIR ETSLDTKSVS EGHLKRNIVV KTVEMRDGEV 

       430 
IKESKQEHKD VM 

« Hide

Isoform 2 [UniParc].

Checksum: 05F98D5333D60FE4
Show »

FASTA43850,289
Isoform 3 (GFAP epsilon) [UniParc].

Checksum: 5D716D21A95240D6
Show »

FASTA43149,508

References

« Hide 'large scale' references
[1]"Molecular cloning and primary structure of human glial fibrillary acidic protein."
Reeves S.A., Helman L.J., Allison A., Israel M.A.
Proc. Natl. Acad. Sci. U.S.A. 86:5178-5182(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Human glial fibrillary acidic protein: complementary DNA cloning, chromosome localization, and messenger RNA expression in human glioma cell lines of various phenotypes."
Bongcam-Rudloff E., Nister M., Betsholtz C., Wang J.-L., Stenman G., Huebner K., Croce C.M., Westermark B.
Cancer Res. 51:1553-1560(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[4]"Human glial fibrillary acidic protein (GFAP): molecular cloning of the complete cDNA sequence and chromosomal localization (chromosome 17) of the GFAP gene."
Kumanishi T., Usui H., Ichikawa T., Nishiyama A., Katagiri T., Abe S., Yoshida Y., Washiyama K., Kuwano R., Sakimura K.
Acta Neuropathol. 83:569-578(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Determination of the gene structure of human GFAP and absence of coding region mutations associated with frontotemporal dementia with parkinsonism linked to chromosome 17."
Isaacs A., Baker M., Wavrant-De Vrieze F., Hutton M.
Genomics 51:152-154(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-295.
[6]Han C., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Brain and Thalamus.
[8]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[9]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Kidney.
[10]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"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.
[13]"An RNA polymerase II promoter containing sequences upstream and downstream from the RNA startpoint that direct initiation of transcription from the same site."
Nakatani Y., Brenner M., Freese E.
Proc. Natl. Acad. Sci. U.S.A. 87:4289-4293(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-76.
[14]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 13-29; 50-63; 96-105; 112-121; 163-173; 189-198; 261-270; 288-300; 331-367 AND 377-390, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[15]"Changes in brain gene expression shared by scrapie and Alzheimer disease."
Duguid J.R., Bohmont C.W., Liu N.G., Tourtellotte W.W.
Proc. Natl. Acad. Sci. U.S.A. 86:7260-7264(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 352-417.
[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: NUCLEOTIDE SEQUENCE [MRNA] OF 391-432 (ISOFORM 3), SUBCELLULAR LOCATION, INTERACTION WITH PSEN1.
Tissue: Fetal brain.
[17]"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: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-432 (ISOFORM 3), VARIANTS.
Tissue: Blood.
[18]"Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN."
Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y., Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.
Biochem. Biophys. Res. Commun. 234:621-625(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[19]"Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase."
Kosako H., Amano M., Yanagida M., Tanabe K., Nishi Y., Kaibuchi K., Inagaki M.
J. Biol. Chem. 272:10333-10336(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-7; SER-13 AND SER-38.
[20]"Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinatedly with Rho-kinase."
Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K., Inagaki M.
Mol. Biol. Cell 14:1489-1500(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-7; SER-13 AND SER-38.
[21]"Identification and Characterization of citrulline-modified brain proteins by combining HCD and CID fragmentation."
Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.
Proteomics 13:2682-2691(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-30; ARG-36; ARG-270; ARG-406 AND ARG-416.
[22]"Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease."
Brenner M., Johnson A.B., Boespflug-Tanguy O., Rodriguez D., Goldman J.E., Messing A.
Nat. Genet. 27:117-120(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALEXD LEU-47; CYS-79; HIS-79; CYS-239; HIS-239; PRO-258 AND TRP-416, VARIANT ASN-295.
[23]"Infantile Alexander disease: spectrum of GFAP mutations and genotype-phenotype correlation."
Rodriguez D., Gauthier F., Bertini E., Bugiani M., Brenner M., N'guyen S., Goizet C., Gelot A., Surtees R., Pedespan J.M., Hernandorena X., Troncoso M., Uziel G., Messing A., Ponsot G., Pham-Dinh D., Dautigny A., Boespflug-Tanguy O.
Am. J. Hum. Genet. 69:1134-1140(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALEXD PHE-76; TYR-77; HIS-79; CYS-88; SER-88; CYS-239 AND HIS-239.
[24]"A novel mutation in glial fibrillary acidic protein gene in a patient with Alexander disease."
Aoki Y., Haginoya K., Munakata M., Yokoyama H., Nishio T., Togashi N., Ito T., Suzuki Y., Kure S., Iinuma K., Brenner M., Matsubara Y.
Neurosci. Lett. 312:71-74(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALEXD VAL-244.
[25]"Juvenile Alexander disease with a novel mutation in glial fibrillary acidic protein gene."
Sawaishi Y., Yano T., Takaku I., Takada G.
Neurology 58:1541-1543(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALEXD ASP-362.
[26]"Adult Alexander disease with autosomal dominant transmission: a distinct entity caused by mutation in the glial fibrillary acid protein gene."
Stumpf E., Masson H., Duquette A., Berthelet F., McNabb J., Lortie A., Lesage J., Montplaisir J., Brais B., Cossette P.
Arch. Neurol. 60:1307-1312(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALEXD GLU-78.
[27]"A novel GFAP mutation and disseminated white matter lesions: adult Alexander disease?"
Brockmann K., Meins M., Taubert A., Trappe R., Grond M., Hanefeld F.
Eur. Neurol. 50:100-105(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALEXD GLN-223.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04569 mRNA. Translation: AAA52528.1.
S40719 mRNA. Translation: AAB22581.1.
AF419299 mRNA. Translation: AAL16662.1.
AK128790 mRNA. Translation: BAC87610.1.
AK222683 mRNA. Translation: BAD96403.1.
AK315398 mRNA. Translation: BAG37791.1.
AL133013 Transcribed RNA. Translation: CAB61354.2.
AC015936 Genomic DNA. No translation available.
CH471178 Genomic DNA. Translation: EAW51570.1.
CH471178 Genomic DNA. Translation: EAW51571.1.
BC013596 mRNA. Translation: AAH13596.1.
BC041765 mRNA. Translation: AAH41765.1.
BC062609 mRNA. Translation: AAH62609.1.
M26638 mRNA. Translation: AAA52529.1.
AJ306447 mRNA. Translation: CAC69881.1.
AY142187 Genomic DNA. Translation: AAN87903.1.
AY142188 Genomic DNA. Translation: AAN87904.1.
AY142191 Genomic DNA. Translation: AAN87907.1.
PIRA32936.
T42645.
RefSeqNP_001124491.1. NM_001131019.2.
NP_001229305.1. NM_001242376.1.
NP_002046.1. NM_002055.4.
UniGeneHs.514227.

3D structure databases

ProteinModelPortalP14136.
SMRP14136. Positions 65-204, 229-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108938. 55 interactions.
IntActP14136. 27 interactions.
MINTMINT-1450103.

PTM databases

PhosphoSiteP14136.

Polymorphism databases

DMDM121135.

2D gel databases

REPRODUCTION-2DPAGEP14136.
UCD-2DPAGEP14136.

Proteomic databases

PaxDbP14136.
PeptideAtlasP14136.
PRIDEP14136.

Protocols and materials databases

DNASU2670.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253408; ENSP00000253408; ENSG00000131095. [P14136-1]
ENST00000435360; ENSP00000403962; ENSG00000131095. [P14136-3]
ENST00000586793; ENSP00000468500; ENSG00000131095. [P14136-2]
GeneID2670.
KEGGhsa:2670.
UCSCuc002ihq.3. human. [P14136-1]
uc021tyh.1. human. [P14136-2]

Organism-specific databases

CTD2670.
GeneCardsGC17M042982.
HGNCHGNC:4235. GFAP.
HPACAB000039.
HPA056030.
MIM137780. gene.
203450. phenotype.
neXtProtNX_P14136.
Orphanet363717. Alexander disease type I.
363722. Alexander disease type II.
PharmGKBPA28647.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259463.
HOVERGENHBG013015.
InParanoidP14136.
KOK05640.
OMAASSNMQE.
OrthoDBEOG7FV3Q8.
PhylomeDBP14136.
TreeFamTF330122.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP14136.
BgeeP14136.
GenevestigatorP14136.

Family and domain databases

InterProIPR027701. GFAP.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF26. PTHR23239:SF26. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGFAP. human.
GeneWikiGlial_fibrillary_acidic_protein.
GenomeRNAi2670.
NextBio10538.
PMAP-CutDBP14136.
PROP14136.
SOURCESearch...

Entry information

Entry nameGFAP_HUMAN
AccessionPrimary (citable) accession number: P14136
Secondary accession number(s): B2RD44 expand/collapse secondary AC list , D3DX59, E9PAX3, Q53H98, Q5D055, Q6ZQS3, Q7Z5J6, Q7Z5J7, Q96KS4, Q96P18, Q9UFD0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM