ID GFAP_HUMAN Reviewed; 432 AA. AC P14136; A7REI1; B2RD44; D3DX59; E9PAX3; Q53H98; Q5D055; Q6ZQS3; Q7Z5J6; AC Q7Z5J7; Q96KS4; Q96P18; Q9UFD0; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 27-MAR-2024, entry version 235. DE RecName: Full=Glial fibrillary acidic protein; DE Short=GFAP; GN Name=GFAP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2740350; DOI=10.1073/pnas.86.13.5178; RA Reeves S.A., Helman L.J., Allison A., Israel M.A.; RT "Molecular cloning and primary structure of human glial fibrillary acidic RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5178-5182(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2163003; DOI=10.1016/0169-328x(90)90078-r; RA Brenner M., Lampel K., Nakatani Y., Mill J., Banner C., Mearow K., RA Dohadwala M., Lipsky R., Freese E.; RT "Characterization of human cDNA and genomic clones for glial fibrillary RT acidic protein."; RL Brain Res. Mol. Brain Res. 7:277-286(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=1847665; RA Bongcam-Rudloff E., Nister M., Betsholtz C., Wang J.-L., Stenman G., RA Huebner K., Croce C.M., Westermark B.; RT "Human glial fibrillary acidic protein: complementary DNA cloning, RT chromosome localization, and messenger RNA expression in human glioma cell RT lines of various phenotypes."; RL Cancer Res. 51:1553-1560(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1636374; DOI=10.1007/bf00299404; RA Kumanishi T., Usui H., Ichikawa T., Nishiyama A., Katagiri T., Abe S., RA Yoshida Y., Washiyama K., Kuwano R., Sakimura K.; RT "Human glial fibrillary acidic protein (GFAP): molecular cloning of the RT complete cDNA sequence and chromosomal localization (chromosome 17) of the RT GFAP gene."; RL Acta Neuropathol. 83:569-578(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-295. RX PubMed=9693047; DOI=10.1006/geno.1998.5360; RA Isaacs A., Baker M., Wavrant-De Vrieze F., Hutton M.; RT "Determination of the gene structure of human GFAP and absence of coding RT region mutations associated with frontotemporal dementia with parkinsonism RT linked to chromosome 17."; RL Genomics 51:152-154(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Han C., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Kidney; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-76. RX PubMed=2349237; DOI=10.1073/pnas.87.11.4289; RA Nakatani Y., Brenner M., Freese E.; RT "An RNA polymerase II promoter containing sequences upstream and downstream RT from the RNA startpoint that direct initiation of transcription from the RT same site."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4289-4293(1990). RN [14] RP PROTEIN SEQUENCE OF 13-29; 50-63; 96-105; 112-121; 163-173; 189-198; RP 261-270; 288-300; 331-367 AND 377-390, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 352-417. RX PubMed=2780570; DOI=10.1073/pnas.86.18.7260; RA Duguid J.R., Bohmont C.W., Liu N.G., Tourtellotte W.W.; RT "Changes in brain gene expression shared by scrapie and Alzheimer RT disease."; RL Proc. Natl. Acad. Sci. U.S.A. 86:7260-7264(1989). RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] OF 377-432 (ISOFORM 3). RX PubMed=17203480; DOI=10.1002/glia.20475; RA Blechingberg J., Holm I.E., Nielsen K.B., Jensen T.H., Joergensen A.L., RA Nielsen A.L.; RT "Identification and characterization of GFAPkappa, a novel glial fibrillary RT acidic protein isoform."; RL Glia 55:497-507(2007). RN [17] RP NUCLEOTIDE SEQUENCE [MRNA] OF 391-432 (ISOFORM 2), SUBCELLULAR LOCATION, RP AND INTERACTION WITH PSEN1. RC TISSUE=Fetal brain; RX PubMed=12058025; DOI=10.1074/jbc.m112121200; RA Nielsen A.L., Holm I.E., Johansen M., Bonven B., Jorgensen P., RA Jorgensen A.L.; RT "A new splice variant of glial fibrillary acidic protein GFAPepsilon, RT interacts with the presenilin proteins."; RL J. Biol. Chem. 277:29983-29991(2002). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-432 (ISOFORM 2), AND VARIANTS. RC TISSUE=Blood; RX PubMed=12837269; DOI=10.1016/s0888-7543(03)00106-x; RA Singh R., Nielsen A.L., Johansen M.G., Jorgensen A.L.; RT "Genetic polymorphism and sequence evolution of an alternatively spliced RT exon of the glial fibrillary acidic protein gene, GFAP."; RL Genomics 82:185-193(2003). RN [19] RP PHOSPHORYLATION. RX PubMed=9175763; DOI=10.1006/bbrc.1997.6669; RA Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y., RA Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.; RT "Domain-specific phosphorylation of vimentin and glial fibrillary acidic RT protein by PKN."; RL Biochem. Biophys. Res. Commun. 234:621-625(1997). RN [20] RP PHOSPHORYLATION AT THR-7; SER-13 AND SER-38. RX PubMed=9099667; DOI=10.1074/jbc.272.16.10333; RA Kosako H., Amano M., Yanagida M., Tanabe K., Nishi Y., Kaibuchi K., RA Inagaki M.; RT "Phosphorylation of glial fibrillary acidic protein at the same sites by RT cleavage furrow kinase and Rho-associated kinase."; RL J. Biol. Chem. 272:10333-10336(1997). RN [21] RP PHOSPHORYLATION AT THR-7; SER-13 AND SER-38. RX PubMed=12686604; DOI=10.1091/mbc.e02-09-0612; RA Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K., RA Inagaki M.; RT "Functional significance of the specific sites phosphorylated in desmin at RT cleavage furrow: Aurora-B may phosphorylate and regulate type III RT intermediate filaments during cytokinesis coordinatedly with Rho-kinase."; RL Mol. Biol. Cell 14:1489-1500(2003). RN [22] RP CITRULLINATION AT ARG-30; ARG-36; ARG-270; ARG-406 AND ARG-416. RX PubMed=23828821; DOI=10.1002/pmic.201300064; RA Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.; RT "Identification and Characterization of citrulline-modified brain proteins RT by combining HCD and CID fragmentation."; RL Proteomics 13:2682-2691(2013). RN [23] RP INVOLVEMENT IN ALXDRD, VARIANTS ALXDRD CYS-79; HIS-79; CYS-239; HIS-239; RP PRO-258 AND TRP-416, AND VARIANTS LEU-47 AND ASN-295. RX PubMed=11138011; DOI=10.1038/83679; RA Brenner M., Johnson A.B., Boespflug-Tanguy O., Rodriguez D., Goldman J.E., RA Messing A.; RT "Mutations in GFAP, encoding glial fibrillary acidic protein, are RT associated with Alexander disease."; RL Nat. Genet. 27:117-120(2001). RN [24] RP VARIANTS ALXDRD PHE-76; TYR-77; HIS-79; CYS-88; SER-88; CYS-239 AND RP HIS-239. RX PubMed=11567214; DOI=10.1086/323799; RA Rodriguez D., Gauthier F., Bertini E., Bugiani M., Brenner M., N'guyen S., RA Goizet C., Gelot A., Surtees R., Pedespan J.M., Hernandorena X., RA Troncoso M., Uziel G., Messing A., Ponsot G., Pham-Dinh D., Dautigny A., RA Boespflug-Tanguy O.; RT "Infantile Alexander disease: spectrum of GFAP mutations and genotype- RT phenotype correlation."; RL Am. J. Hum. Genet. 69:1134-1140(2001). RN [25] RP VARIANT ALXDRD VAL-244. RX PubMed=11595337; DOI=10.1016/s0304-3940(01)02139-5; RA Aoki Y., Haginoya K., Munakata M., Yokoyama H., Nishio T., Togashi N., RA Ito T., Suzuki Y., Kure S., Iinuma K., Brenner M., Matsubara Y.; RT "A novel mutation in glial fibrillary acidic protein gene in a patient with RT Alexander disease."; RL Neurosci. Lett. 312:71-74(2001). RN [26] RP VARIANTS ALXDRD ARG-73; GLY-79; CYS-79; HIS-79; CYS-88; CYS-239; ASP-242; RP LYS-373 AND TRP-416. RX PubMed=12034785; DOI=10.1212/wnl.58.10.1494; RA Gorospe J.R., Naidu S., Johnson A.B., Puri V., Raymond G.V., Jenkins S.D., RA Pedersen R.C., Lewis D., Knowles P., Fernandez R., De Vivo D., RA van der Knaap M.S., Messing A., Brenner M., Hoffman E.P.; RT "Molecular findings in symptomatic and pre-symptomatic Alexander disease RT patients."; RL Neurology 58:1494-1500(2002). RN [27] RP VARIANT ALXDRD ASP-362. RX PubMed=12034796; DOI=10.1212/wnl.58.10.1541; RA Sawaishi Y., Yano T., Takaku I., Takada G.; RT "Juvenile Alexander disease with a novel mutation in glial fibrillary RT acidic protein gene."; RL Neurology 58:1541-1543(2002). RN [28] RP VARIANT ALXDRD GLU-78. RX PubMed=12975300; DOI=10.1001/archneur.60.9.1307; RA Stumpf E., Masson H., Duquette A., Berthelet F., McNabb J., Lortie A., RA Lesage J., Montplaisir J., Brais B., Cossette P.; RT "Adult Alexander disease with autosomal dominant transmission: a distinct RT entity caused by mutation in the glial fibrillary acid protein gene."; RL Arch. Neurol. 60:1307-1312(2003). RN [29] RP VARIANT ALXDRD LEU-79. RX PubMed=12581808; DOI=10.1016/s0387-7604(02)00167-5; RA Shiroma N., Kanazawa N., Kato Z., Shimozawa N., Imamura A., Ito M., RA Ohtani K., Oka A., Wakabayashi K., Iai M., Sugai K., Sasaki M., Kaga M., RA Ohta T., Tsujino S.; RT "Molecular genetic study in Japanese patients with Alexander disease: a RT novel mutation, R79L."; RL Brain Dev. 25:116-121(2003). RN [30] RP VARIANT GLN-223. RX PubMed=12944715; DOI=10.1159/000072507; RA Brockmann K., Meins M., Taubert A., Trappe R., Grond M., Hanefeld F.; RT "A novel GFAP mutation and disseminated white matter lesions: adult RT Alexander disease?"; RL Eur. Neurol. 50:100-105(2003). RN [31] RP VARIANT ALXDRD PRO-90. RX PubMed=15030911; DOI=10.1016/s0387-7604(03)00132-3; RA Suzuki Y., Kanazawa N., Takenaka J., Okumura A., Negoro T., Tsujino S.; RT "A case of infantile Alexander disease with a milder phenotype and a novel RT GFAP mutation, L90P."; RL Brain Dev. 26:206-208(2004). RN [32] RP VARIANTS LEU-47; ILE-115; ASN-157 AND GLN-223, VARIANTS ALXDRD GLN-63; RP THR-73; PHE-76; VAL-76; SER-77; CYS-79; CYS-88; PRO-97; LYS-207; GLN-207; RP LYS-210; PRO-235; CYS-239; HIS-239; PRO-239; VAL-244; GLY-253; GLU-279; RP PRO-352; VAL-359; PRO-364; HIS-366; LYS-373; GLN-373; GLY-374 AND TRP-416, RP CHARACTERIZATION OF VARIANTS ALXDRD GLN-63; LYS-210; VAL-244 AND GLY-253, RP AND CHARACTERIZATION OF VARIANT ILE-115. RX PubMed=15732097; DOI=10.1002/ana.20406; RA Li R., Johnson A.B., Salomons G., Goldman J.E., Naidu S., Quinlan R., RA Cree B., Ruyle S.Z., Banwell B., D'Hooghe M., Siebert J.R., Rolf C.M., RA Cox H., Reddy A., Gutierrez-Solana L.G., Collins A., Weller R.O., RA Messing A., van der Knaap M.S., Brenner M.; RT "Glial fibrillary acidic protein mutations in infantile, juvenile, and RT adult forms of Alexander disease."; RL Ann. Neurol. 57:310-326(2005). RN [33] RP VARIANT ALXDRD LEU-239. RX PubMed=17043438; DOI=10.3346/jkms.2006.21.5.954; RA Lee J.M., Kim A.S., Lee S.J., Cho S.M., Lee D.S., Choi S.M., Kim D.K., RA Ki C.S., Kim J.W.; RT "A case of infantile Alexander disease accompanied by infantile spasms RT diagnosed by DNA analysis."; RL J. Korean Med. Sci. 21:954-957(2006). RN [34] RP VARIANT ALXDRD PRO-267. RX PubMed=17805552; DOI=10.1007/s00401-007-0292-8; RA Hinttala R., Karttunen V., Karttunen A., Herva R., Uusimaa J., Remes A.M.; RT "Alexander disease with occipital predominance and a novel c.799G>C RT mutation in the GFAP gene."; RL Acta Neuropathol. 114:543-545(2007). RN [35] RP VARIANTS ALXDRD TRP-70; GLN-70; LYS-73; SER-77; CYS-79; PRO-79; CYS-88; RP HIS-239; PRO-239; PRO-359 AND TRP-416. RX PubMed=17894839; DOI=10.1111/j.1399-0004.2007.00869.x; RA Caroli F., Biancheri R., Seri M., Rossi A., Pessagno A., Bugiani M., RA Corsolini F., Savasta S., Romano S., Antonelli C., Romano A., Pareyson D., RA Gambero P., Uziel G., Ravazzolo R., Ceccherini I., Filocamo M.; RT "GFAP mutations and polymorphisms in 13 unrelated Italian patients affected RT by Alexander disease."; RL Clin. Genet. 72:427-433(2007). RN [36] RP VARIANT ALXDRD THR-74. RX PubMed=17934883; DOI=10.1007/s00415-007-0557-0; RA Ohnari K., Yamano M., Uozumi T., Hashimoto T., Tsuji S., Nakagawa M.; RT "An adult form of Alexander disease: a novel mutation in glial fibrillary RT acidic protein."; RL J. Neurol. 254:1390-1394(2007). RN [37] RP VARIANTS ALXDRD HIS-83 AND CYS-88. RX PubMed=18079314; DOI=10.1177/0883073807308691; RA Ye W., Qiang G., Jingmin W., Yanling Y., Xiru W., Yuwu J.; RT "Clinical and genetic study in Chinese patients with Alexander disease."; RL J. Child Neurol. 23:173-177(2008). RN [38] RP VARIANTS ALXDRD GLY-330 AND LYS-332. RX PubMed=18004641; DOI=10.1007/s00415-007-0654-0; RA Balbi P., Seri M., Ceccherini I., Uggetti C., Casale R., Fundaro C., RA Caroli F., Santoro L.; RT "Adult-onset Alexander disease: report on a family."; RL J. Neurol. 255:24-30(2008). RN [39] RP VARIANT ALXDRD CYS-257, AND CHARACTERIZATION OF VARIANT ALXDRD CYS-257. RX PubMed=17960815; DOI=10.1002/mds.21774; RA Howard K.L., Hall D.A., Moon M., Agarwal P., Newman E., Brenner M.; RT "Adult-onset Alexander disease with progressive ataxia and palatal RT tremor."; RL Mov. Disord. 23:118-122(2008). RN [40] RP VARIANT ALXDRD PRO-101. RX PubMed=19412928; DOI=10.1002/mds.22556; RA Kaneko H., Hirose M., Katada S., Takahashi T., Naruse S., Tsuchiya M., RA Yoshida T., Nakagawa M., Onodera O., Nishizawa M., Ikeuchi T.; RT "Novel GFAP mutation in patient with adult-onset Alexander disease RT presenting with spastic ataxia."; RL Mov. Disord. 24:1393-1395(2009). RN [41] RP VARIANT ALXDRD LEU-276. RX PubMed=20359319; DOI=10.1186/1471-2377-10-21; RA Namekawa M., Takiyama Y., Honda J., Shimazaki H., Sakoe K., Nakano I.; RT "Adult-onset Alexander disease with typical 'tadpole' brainstem atrophy and RT unusual bilateral basal ganglia involvement: a case report and review of RT the literature."; RL BMC Neurol. 10:21-21(2010). RN [42] RP VARIANTS ALXDRD GLN-66; LYS-72; GLU-86; THR-236; GLN-371; VAL-371 AND RP GLY-376. RX PubMed=21917775; DOI=10.1212/wnl.0b013e3182309f72; RA Prust M., Wang J., Morizono H., Messing A., Brenner M., Gordon E., RA Hartka T., Sokohl A., Schiffmann R., Gordish-Dressman H., Albin R., RA Amartino H., Brockman K., Dinopoulos A., Dotti M.T., Fain D., Fernandez R., RA Ferreira J., Fleming J., Gill D., Griebel M., Heilstedt H., Kaplan P., RA Lewis D., Nakagawa M., Pedersen R., Reddy A., Sawaishi Y., Schneider M., RA Sherr E., Takiyama Y., Wakabayashi K., Gorospe J.R., Vanderver A.; RT "GFAP mutations, age at onset, and clinical subtypes in Alexander RT disease."; RL Neurology 77:1287-1294(2011). RN [43] RP VARIANTS ALXDRD PHE-76; LYS-77; LEU-79; HIS-79; CYS-79; CYS-88; SER-88; RP CYS-239; HIS-239; ASP-373; GLN-374 AND PHE-385. RX PubMed=23364391; DOI=10.1038/jhg.2012.152; RA Zang L., Wang J., Jiang Y., Gu Q., Gao Z., Yang Y., Xiao J., Wu Y.; RT "Follow-up study of 22 Chinese children with Alexander disease and analysis RT of parental origin of de novo GFAP mutations."; RL J. Hum. Genet. 58:183-188(2013). RN [44] RP VARIANT ALXDRD ASN-78. RX PubMed=23743246; DOI=10.1016/j.jns.2013.05.019; RA Wada Y., Yanagihara C., Nishimura Y., Namekawa M.; RT "Familial adult-onset Alexander disease with a novel mutation (D78N) in the RT glial fibrillary acidic protein gene with unusual bilateral basal ganglia RT involvement."; RL J. Neurol. Sci. 331:161-164(2013). RN [45] RP VARIANT ALXDRD TRP-416. RX PubMed=24742911; DOI=10.1016/j.ejpn.2014.03.009; RA Nishri D., Edvardson S., Lev D., Leshinsky-Silver E., Ben-Sira L., RA Henneke M., Lerman-Sagie T., Blumkin L.; RT "Diagnosis by whole exome sequencing of atypical infantile onset Alexander RT disease masquerading as a mitochondrial disorder."; RL Eur. J. Paediatr. Neurol. 18:495-501(2014). CC -!- FUNCTION: GFAP, a class-III intermediate filament, is a cell-specific CC marker that, during the development of the central nervous system, CC distinguishes astrocytes from other glial cells. CC -!- SUBUNIT: Interacts with SYNM. {ECO:0000250|UniProtKB:P03995}. CC -!- SUBUNIT: [Isoform 2]: Interacts with PSEN1 (via N-terminus). CC {ECO:0000269|PubMed:12058025}. CC -!- INTERACTION: CC P14136; Q9NYB9-2: ABI2; NbExp=6; IntAct=EBI-744302, EBI-11096309; CC P14136; Q6H8Q1-8: ABLIM2; NbExp=3; IntAct=EBI-744302, EBI-16436655; CC P14136; P00352: ALDH1A1; NbExp=3; IntAct=EBI-744302, EBI-752170; CC P14136; P63010-2: AP2B1; NbExp=3; IntAct=EBI-744302, EBI-11529439; CC P14136; Q06481-5: APLP2; NbExp=3; IntAct=EBI-744302, EBI-25646567; CC P14136; Q8N6T3-3: ARFGAP1; NbExp=3; IntAct=EBI-744302, EBI-10694449; CC P14136; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-744302, EBI-14199987; CC P14136; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-744302, EBI-9089489; CC P14136; P21281: ATP6V1B2; NbExp=3; IntAct=EBI-744302, EBI-4290814; CC P14136; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-744302, EBI-742750; CC P14136; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-744302, EBI-9092016; CC P14136; O75934: BCAS2; NbExp=3; IntAct=EBI-744302, EBI-1050106; CC P14136; Q13490: BIRC2; NbExp=3; IntAct=EBI-744302, EBI-514538; CC P14136; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-744302, EBI-2837444; CC P14136; Q5SZD1: C6orf141; NbExp=3; IntAct=EBI-744302, EBI-10697767; CC P14136; P62158: CALM3; NbExp=3; IntAct=EBI-744302, EBI-397435; CC P14136; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-744302, EBI-3866279; CC P14136; P29466-3: CASP1; NbExp=3; IntAct=EBI-744302, EBI-12248206; CC P14136; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-744302, EBI-744556; CC P14136; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-744302, EBI-10181422; CC P14136; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-744302, EBI-10961624; CC P14136; P24863: CCNC; NbExp=3; IntAct=EBI-744302, EBI-395261; CC P14136; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-744302, EBI-396137; CC P14136; Q16543: CDC37; NbExp=3; IntAct=EBI-744302, EBI-295634; CC P14136; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-744302, EBI-749051; CC P14136; Q3SX64: CIMAP1D; NbExp=3; IntAct=EBI-744302, EBI-6660184; CC P14136; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-744302, EBI-2872414; CC P14136; Q8WUE5: CT55; NbExp=3; IntAct=EBI-744302, EBI-6873363; CC P14136; P35222: CTNNB1; NbExp=3; IntAct=EBI-744302, EBI-491549; CC P14136; Q2TBE0: CWF19L2; NbExp=6; IntAct=EBI-744302, EBI-5453285; CC P14136; Q9UBU7: DBF4; NbExp=3; IntAct=EBI-744302, EBI-372690; CC P14136; Q5TDH0-2: DDI2; NbExp=3; IntAct=EBI-744302, EBI-25858598; CC P14136; P35638: DDIT3; NbExp=3; IntAct=EBI-744302, EBI-742651; CC P14136; P17661: DES; NbExp=6; IntAct=EBI-744302, EBI-1055572; CC P14136; Q14689-3: DIP2A; NbExp=3; IntAct=EBI-744302, EBI-25858204; CC P14136; Q96EY1-3: DNAJA3; NbExp=3; IntAct=EBI-744302, EBI-11526226; CC P14136; Q92782-2: DPF1; NbExp=3; IntAct=EBI-744302, EBI-23669343; CC P14136; Q6UXG2-3: ELAPOR1; NbExp=3; IntAct=EBI-744302, EBI-12920100; CC P14136; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-744302, EBI-744099; CC P14136; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-744302, EBI-6255981; CC P14136; Q13216-2: ERCC8; NbExp=3; IntAct=EBI-744302, EBI-16466949; CC P14136; Q96DF8: ESS2; NbExp=3; IntAct=EBI-744302, EBI-3928124; CC P14136; Q9UBQ6: EXTL2; NbExp=3; IntAct=EBI-744302, EBI-21506125; CC P14136; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-744302, EBI-742802; CC P14136; O15287: FANCG; NbExp=3; IntAct=EBI-744302, EBI-81610; CC P14136; Q53R41: FASTKD1; NbExp=3; IntAct=EBI-744302, EBI-3957005; CC P14136; Q9Y261-2: FOXA2; NbExp=3; IntAct=EBI-744302, EBI-25830360; CC P14136; P06241-3: FYN; NbExp=3; IntAct=EBI-744302, EBI-10691738; CC P14136; P14136: GFAP; NbExp=7; IntAct=EBI-744302, EBI-744302; CC P14136; Q08379: GOLGA2; NbExp=9; IntAct=EBI-744302, EBI-618309; CC P14136; Q13322-4: GRB10; NbExp=3; IntAct=EBI-744302, EBI-12353035; CC P14136; Q71DI3: H3C15; NbExp=3; IntAct=EBI-744302, EBI-750650; CC P14136; Q8N7T0: hCG_1820408; NbExp=3; IntAct=EBI-744302, EBI-25858908; CC P14136; P61978: HNRNPK; NbExp=3; IntAct=EBI-744302, EBI-304185; CC P14136; P42858: HTT; NbExp=10; IntAct=EBI-744302, EBI-466029; CC P14136; Q12891: HYAL2; NbExp=3; IntAct=EBI-744302, EBI-2806068; CC P14136; Q8NDH6-2: ICA1L; NbExp=3; IntAct=EBI-744302, EBI-12141931; CC P14136; Q8IY31-2: IFT20; NbExp=3; IntAct=EBI-744302, EBI-11742277; CC P14136; Q14005-2: IL16; NbExp=3; IntAct=EBI-744302, EBI-17178971; CC P14136; Q8NA54: IQUB; NbExp=3; IntAct=EBI-744302, EBI-10220600; CC P14136; Q92613: JADE3; NbExp=3; IntAct=EBI-744302, EBI-10278909; CC P14136; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-744302, EBI-1055254; CC P14136; Q6ZU52: KIAA0408; NbExp=5; IntAct=EBI-744302, EBI-739493; CC P14136; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-744302, EBI-10188326; CC P14136; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-744302, EBI-14069005; CC P14136; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-744302, EBI-714379; CC P14136; A1A4E9: KRT13; NbExp=4; IntAct=EBI-744302, EBI-10171552; CC P14136; P13646: KRT13; NbExp=6; IntAct=EBI-744302, EBI-1223876; CC P14136; P19012: KRT15; NbExp=9; IntAct=EBI-744302, EBI-739566; CC P14136; P08727: KRT19; NbExp=9; IntAct=EBI-744302, EBI-742756; CC P14136; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-744302, EBI-3044087; CC P14136; Q15323: KRT31; NbExp=3; IntAct=EBI-744302, EBI-948001; CC P14136; Q14525: KRT33B; NbExp=3; IntAct=EBI-744302, EBI-1049638; CC P14136; Q6A163: KRT39; NbExp=3; IntAct=EBI-744302, EBI-11958242; CC P14136; Q14847-2: LASP1; NbExp=3; IntAct=EBI-744302, EBI-9088686; CC P14136; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-744302, EBI-726510; CC P14136; Q96PV6: LENG8; NbExp=3; IntAct=EBI-744302, EBI-739546; CC P14136; Q8TCE9: LGALS14; NbExp=7; IntAct=EBI-744302, EBI-10274069; CC P14136; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-744302, EBI-9088829; CC P14136; P25791: LMO2; NbExp=3; IntAct=EBI-744302, EBI-739696; CC P14136; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-744302, EBI-739832; CC P14136; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-744302, EBI-2510853; CC P14136; Q14693: LPIN1; NbExp=3; IntAct=EBI-744302, EBI-5278370; CC P14136; Q9BX40-2: LSM14B; NbExp=3; IntAct=EBI-744302, EBI-19133880; CC P14136; Q13387-4: MAPK8IP2; NbExp=3; IntAct=EBI-744302, EBI-12345753; CC P14136; P45984: MAPK9; NbExp=3; IntAct=EBI-744302, EBI-713568; CC P14136; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-744302, EBI-348259; CC P14136; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-744302, EBI-8487781; CC P14136; O94851: MICAL2; NbExp=3; IntAct=EBI-744302, EBI-2804835; CC P14136; A4FUJ8: MKL1; NbExp=3; IntAct=EBI-744302, EBI-21250407; CC P14136; Q15049: MLC1; NbExp=3; IntAct=EBI-744302, EBI-8475277; CC P14136; P00540: MOS; NbExp=3; IntAct=EBI-744302, EBI-1757866; CC P14136; Q9Y3D2: MSRB2; NbExp=3; IntAct=EBI-744302, EBI-9092052; CC P14136; Q9Y483-4: MTF2; NbExp=3; IntAct=EBI-744302, EBI-10698053; CC P14136; A2RUH7: MYBPHL; NbExp=6; IntAct=EBI-744302, EBI-9088235; CC P14136; Q96A32: MYL11; NbExp=3; IntAct=EBI-744302, EBI-1390771; CC P14136; Q6N069-4: NAA16; NbExp=3; IntAct=EBI-744302, EBI-10699337; CC P14136; Q99457: NAP1L3; NbExp=3; IntAct=EBI-744302, EBI-8645631; CC P14136; O76041: NEBL; NbExp=3; IntAct=EBI-744302, EBI-2880203; CC P14136; I6L9F6: NEFL; NbExp=4; IntAct=EBI-744302, EBI-10178578; CC P14136; P07196: NEFL; NbExp=9; IntAct=EBI-744302, EBI-475646; CC P14136; Q9HC98-4: NEK6; NbExp=5; IntAct=EBI-744302, EBI-11750983; CC P14136; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-744302, EBI-10271199; CC P14136; Q12986: NFX1; NbExp=3; IntAct=EBI-744302, EBI-2130062; CC P14136; Q9Y239: NOD1; NbExp=3; IntAct=EBI-744302, EBI-1051262; CC P14136; Q6X4W1-6: NSMF; NbExp=3; IntAct=EBI-744302, EBI-25842707; CC P14136; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-744302, EBI-741158; CC P14136; O43809: NUDT21; NbExp=3; IntAct=EBI-744302, EBI-355720; CC P14136; Q9UBU9: NXF1; NbExp=7; IntAct=EBI-744302, EBI-398874; CC P14136; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-744302, EBI-1058491; CC P14136; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-744302, EBI-25830200; CC P14136; Q16549: PCSK7; NbExp=3; IntAct=EBI-744302, EBI-8059854; CC P14136; O00151: PDLIM1; NbExp=4; IntAct=EBI-744302, EBI-724897; CC P14136; Q96HC4: PDLIM5; NbExp=3; IntAct=EBI-744302, EBI-751267; CC P14136; Q5T2W1: PDZK1; NbExp=4; IntAct=EBI-744302, EBI-349819; CC P14136; P16284: PECAM1; NbExp=3; IntAct=EBI-744302, EBI-716404; CC P14136; O15534: PER1; NbExp=3; IntAct=EBI-744302, EBI-2557276; CC P14136; Q96FX8: PERP; NbExp=3; IntAct=EBI-744302, EBI-17183069; CC P14136; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-744302, EBI-2339674; CC P14136; O75928: PIAS2; NbExp=3; IntAct=EBI-744302, EBI-348555; CC P14136; O75928-2: PIAS2; NbExp=6; IntAct=EBI-744302, EBI-348567; CC P14136; Q8WWB5: PIH1D2; NbExp=4; IntAct=EBI-744302, EBI-10232538; CC P14136; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-744302, EBI-9090282; CC P14136; Q9Y446: PKP3; NbExp=3; IntAct=EBI-744302, EBI-2880227; CC P14136; Q6P1J6-2: PLB1; NbExp=3; IntAct=EBI-744302, EBI-10694821; CC P14136; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-744302, EBI-10171633; CC P14136; P00491: PNP; NbExp=3; IntAct=EBI-744302, EBI-712238; CC P14136; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-744302, EBI-710402; CC P14136; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-744302, EBI-10293968; CC P14136; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-744302, EBI-2557469; CC P14136; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-744302, EBI-25835994; CC P14136; P57729: RAB38; NbExp=3; IntAct=EBI-744302, EBI-6552718; CC P14136; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-744302, EBI-11984839; CC P14136; P20339: RAB5A; NbExp=3; IntAct=EBI-744302, EBI-399437; CC P14136; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-744302, EBI-438710; CC P14136; P50749: RASSF2; NbExp=3; IntAct=EBI-744302, EBI-960081; CC P14136; Q8WWW0-2: RASSF5; NbExp=3; IntAct=EBI-744302, EBI-960502; CC P14136; Q8NHQ8-2: RASSF8; NbExp=3; IntAct=EBI-744302, EBI-10976415; CC P14136; Q8TCX5: RHPN1; NbExp=3; IntAct=EBI-744302, EBI-746325; CC P14136; P35398: RORA; NbExp=3; IntAct=EBI-744302, EBI-748689; CC P14136; Q6ZNE9: RUFY4; NbExp=3; IntAct=EBI-744302, EBI-10181525; CC P14136; Q8N488: RYBP; NbExp=3; IntAct=EBI-744302, EBI-752324; CC P14136; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-744302, EBI-11528848; CC P14136; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-744302, EBI-3957636; CC P14136; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-744302, EBI-25837959; CC P14136; Q96HL8: SH3YL1; NbExp=4; IntAct=EBI-744302, EBI-722667; CC P14136; Q9GZS3: SKIC8; NbExp=3; IntAct=EBI-744302, EBI-358545; CC P14136; O95391: SLU7; NbExp=3; IntAct=EBI-744302, EBI-750559; CC P14136; Q12824: SMARCB1; NbExp=4; IntAct=EBI-744302, EBI-358419; CC P14136; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-744302, EBI-358489; CC P14136; Q96DI7: SNRNP40; NbExp=3; IntAct=EBI-744302, EBI-538492; CC P14136; Q13573: SNW1; NbExp=3; IntAct=EBI-744302, EBI-632715; CC P14136; Q9UM82: SPATA2; NbExp=3; IntAct=EBI-744302, EBI-744066; CC P14136; Q8NHS9: SPATA22; NbExp=3; IntAct=EBI-744302, EBI-7067260; CC P14136; Q8IUW3: SPATA2L; NbExp=3; IntAct=EBI-744302, EBI-2510414; CC P14136; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-744302, EBI-5235340; CC P14136; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-744302, EBI-7082156; CC P14136; Q9NRP7: STK36; NbExp=3; IntAct=EBI-744302, EBI-863797; CC P14136; Q9BR01-2: SULT4A1; NbExp=3; IntAct=EBI-744302, EBI-25831443; CC P14136; Q9H7C4: SYNC; NbExp=3; IntAct=EBI-744302, EBI-11285923; CC P14136; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-744302, EBI-745958; CC P14136; Q8IYX1: TBC1D21; NbExp=6; IntAct=EBI-744302, EBI-12018146; CC P14136; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-744302, EBI-8787464; CC P14136; O15273: TCAP; NbExp=3; IntAct=EBI-744302, EBI-954089; CC P14136; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-744302, EBI-1105213; CC P14136; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-744302, EBI-741515; CC P14136; Q08117: TLE5; NbExp=3; IntAct=EBI-744302, EBI-717810; CC P14136; Q96B77: TMEM186; NbExp=3; IntAct=EBI-744302, EBI-9089409; CC P14136; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-744302, EBI-2505861; CC P14136; O60784-2: TOM1; NbExp=3; IntAct=EBI-744302, EBI-12117154; CC P14136; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-744302, EBI-11952721; CC P14136; P14373: TRIM27; NbExp=6; IntAct=EBI-744302, EBI-719493; CC P14136; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-744302, EBI-11525489; CC P14136; Q99598: TSNAX; NbExp=3; IntAct=EBI-744302, EBI-742638; CC P14136; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-744302, EBI-9088812; CC P14136; P10599: TXN; NbExp=3; IntAct=EBI-744302, EBI-594644; CC P14136; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-744302, EBI-7353612; CC P14136; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-744302, EBI-10180829; CC P14136; O00124: UBXN8; NbExp=3; IntAct=EBI-744302, EBI-1993850; CC P14136; Q14694: USP10; NbExp=3; IntAct=EBI-744302, EBI-2510389; CC P14136; P08670: VIM; NbExp=7; IntAct=EBI-744302, EBI-353844; CC P14136; P58304: VSX2; NbExp=3; IntAct=EBI-744302, EBI-6427899; CC P14136; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-744302, EBI-7705033; CC P14136; O76024: WFS1; NbExp=3; IntAct=EBI-744302, EBI-720609; CC P14136; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-744302, EBI-12040603; CC P14136; P07947: YES1; NbExp=3; IntAct=EBI-744302, EBI-515331; CC P14136; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-744302, EBI-740767; CC P14136; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-744302, EBI-14104088; CC P14136; Q8WW38: ZFPM2; NbExp=3; IntAct=EBI-744302, EBI-947213; CC P14136; Q9H4I2-2: ZHX3; NbExp=3; IntAct=EBI-744302, EBI-10693326; CC P14136; Q9BRR0: ZKSCAN3; NbExp=3; IntAct=EBI-744302, EBI-1965777; CC P14136; Q9Y2L8: ZKSCAN5; NbExp=3; IntAct=EBI-744302, EBI-2876965; CC P14136; P17023: ZNF19; NbExp=3; IntAct=EBI-744302, EBI-12884200; CC P14136; P17024: ZNF20; NbExp=3; IntAct=EBI-744302, EBI-717634; CC P14136; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-744302, EBI-749023; CC P14136; Q9NR11-2: ZNF302; NbExp=3; IntAct=EBI-744302, EBI-12988373; CC P14136; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-744302, EBI-11741890; CC P14136; Q9C0F3: ZNF436; NbExp=3; IntAct=EBI-744302, EBI-8489702; CC P14136; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-744302, EBI-12010736; CC P14136; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-744302, EBI-25831733; CC P14136; O60304: ZNF500; NbExp=3; IntAct=EBI-744302, EBI-18234077; CC P14136; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-744302, EBI-10172590; CC P14136; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-744302, EBI-745520; CC P14136; Q8N720: ZNF655; NbExp=3; IntAct=EBI-744302, EBI-625509; CC P14136; Q6NX45: ZNF774; NbExp=9; IntAct=EBI-744302, EBI-10251462; CC P14136; P10073: ZSCAN22; NbExp=3; IntAct=EBI-744302, EBI-10178224; CC P14136; O15535: ZSCAN9; NbExp=3; IntAct=EBI-744302, EBI-751531; CC P14136; Q86V28; NbExp=3; IntAct=EBI-744302, EBI-10259496; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12058025}. CC Note=Associated with intermediate filaments. CC {ECO:0000269|PubMed:12058025}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Isoforms differ in the C-terminal region which is encoded by CC alternative exons.; CC Name=1; Synonyms=GFAP alpha {ECO:0000303|PubMed:17203480}; CC IsoId=P14136-1; Sequence=Displayed; CC Name=2; Synonyms=GFAP epsilon {ECO:0000303|PubMed:12058025, CC ECO:0000303|PubMed:12837269}; CC IsoId=P14136-3; Sequence=VSP_017052; CC Name=3; Synonyms=GFAP kappa {ECO:0000303|PubMed:17203480}; CC IsoId=P14136-2; Sequence=VSP_017051; CC -!- TISSUE SPECIFICITY: Expressed in cells lacking fibronectin. CC {ECO:0000269|PubMed:1847665}. CC -!- PTM: Phosphorylated by PKN1. {ECO:0000269|PubMed:12686604, CC ECO:0000269|PubMed:9099667, ECO:0000269|PubMed:9175763}. CC -!- DISEASE: Alexander disease (ALXDRD) [MIM:203450]: A rare disorder of CC the central nervous system. The most common form affects infants and CC young children, and is characterized by progressive failure of central CC myelination, usually leading to death within the first decade. Infants CC with Alexander disease develop a leukodystrophy with macrocephaly, CC seizures, and psychomotor retardation. Patients with juvenile or adult CC forms typically experience ataxia, bulbar signs and spasticity, and a CC more slowly progressive course. Histologically, Alexander disease is CC characterized by Rosenthal fibers, homogeneous eosinophilic inclusions CC in astrocytes. {ECO:0000269|PubMed:11138011, CC ECO:0000269|PubMed:11567214, ECO:0000269|PubMed:11595337, CC ECO:0000269|PubMed:12034785, ECO:0000269|PubMed:12034796, CC ECO:0000269|PubMed:12581808, ECO:0000269|PubMed:12944715, CC ECO:0000269|PubMed:12975300, ECO:0000269|PubMed:15030911, CC ECO:0000269|PubMed:15732097, ECO:0000269|PubMed:17043438, CC ECO:0000269|PubMed:17805552, ECO:0000269|PubMed:17894839, CC ECO:0000269|PubMed:17934883, ECO:0000269|PubMed:17960815, CC ECO:0000269|PubMed:18004641, ECO:0000269|PubMed:18079314, CC ECO:0000269|PubMed:19412928, ECO:0000269|PubMed:20359319, CC ECO:0000269|PubMed:21917775, ECO:0000269|PubMed:23364391, CC ECO:0000269|PubMed:23743246, ECO:0000269|PubMed:24742911}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=GFAP entry; CC URL="https://en.wikipedia.org/wiki/Glial_fibrillary_acidic_protein"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04569; AAA52528.1; -; mRNA. DR EMBL; S40719; AAB22581.1; -; mRNA. DR EMBL; AF419299; AAL16662.1; -; mRNA. DR EMBL; AK128790; BAC87610.1; -; mRNA. DR EMBL; AK222683; BAD96403.1; -; mRNA. DR EMBL; AK315398; BAG37791.1; -; mRNA. DR EMBL; AL133013; CAB61354.2; -; Transcribed_RNA. DR EMBL; AC015936; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471178; EAW51570.1; -; Genomic_DNA. DR EMBL; CH471178; EAW51571.1; -; Genomic_DNA. DR EMBL; BC013596; AAH13596.1; -; mRNA. DR EMBL; BC041765; AAH41765.1; -; mRNA. DR EMBL; BC062609; AAH62609.1; -; mRNA. DR EMBL; M26638; AAA52529.1; -; mRNA. DR EMBL; DQ979832; ABL14186.1; -; mRNA. DR EMBL; AJ306447; CAC69881.1; -; mRNA. DR EMBL; AY142187; AAN87903.1; -; Genomic_DNA. DR EMBL; AY142188; AAN87904.1; -; Genomic_DNA. DR EMBL; AY142191; AAN87907.1; -; Genomic_DNA. DR CCDS; CCDS11491.1; -. [P14136-1] DR CCDS; CCDS45708.1; -. [P14136-3] DR CCDS; CCDS59296.1; -. [P14136-2] DR PIR; A32936; A32936. DR PIR; T42645; T42645. DR RefSeq; NP_001124491.1; NM_001131019.2. [P14136-3] DR RefSeq; NP_001229305.1; NM_001242376.1. [P14136-2] DR RefSeq; NP_002046.1; NM_002055.4. [P14136-1] DR PDB; 6A9P; X-ray; 2.51 A; A/B/C/D/E/F/G/H=110-213. DR PDBsum; 6A9P; -. DR AlphaFoldDB; P14136; -. DR SMR; P14136; -. DR BioGRID; 108938; 233. DR IntAct; P14136; 263. DR MINT; P14136; -. DR STRING; 9606.ENSP00000253408; -. DR GlyCosmos; P14136; 1 site, 1 glycan. DR GlyGen; P14136; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P14136; -. DR PhosphoSitePlus; P14136; -. DR SwissPalm; P14136; -. DR BioMuta; GFAP; -. DR DMDM; 121135; -. DR REPRODUCTION-2DPAGE; P14136; -. DR EPD; P14136; -. DR jPOST; P14136; -. DR MassIVE; P14136; -. DR MaxQB; P14136; -. DR PaxDb; 9606-ENSP00000468500; -. DR PeptideAtlas; P14136; -. DR PRIDE; P14136; -. DR ProteomicsDB; 19099; -. DR ProteomicsDB; 53022; -. [P14136-1] DR ProteomicsDB; 53023; -. [P14136-2] DR ProteomicsDB; 53024; -. [P14136-3] DR ABCD; P14136; 10 sequenced antibodies. DR Antibodypedia; 3505; 3579 antibodies from 62 providers. DR DNASU; 2670; -. DR Ensembl; ENST00000435360.8; ENSP00000403962.1; ENSG00000131095.14. [P14136-3] DR Ensembl; ENST00000588735.3; ENSP00000466598.2; ENSG00000131095.14. [P14136-1] DR Ensembl; ENST00000638281.1; ENSP00000491088.1; ENSG00000131095.14. [P14136-2] DR GeneID; 2670; -. DR KEGG; hsa:2670; -. DR MANE-Select; ENST00000588735.3; ENSP00000466598.2; NM_002055.5; NP_002046.1. DR UCSC; uc002ihq.3; human. [P14136-1] DR AGR; HGNC:4235; -. DR CTD; 2670; -. DR DisGeNET; 2670; -. DR GeneCards; GFAP; -. DR GeneReviews; GFAP; -. DR HGNC; HGNC:4235; GFAP. DR HPA; ENSG00000131095; Tissue enriched (brain). DR MalaCards; GFAP; -. DR MIM; 137780; gene. DR MIM; 203450; phenotype. DR neXtProt; NX_P14136; -. DR OpenTargets; ENSG00000131095; -. DR Orphanet; 363717; Alexander disease type I. DR Orphanet; 363722; Alexander disease type II. DR PharmGKB; PA28647; -. DR VEuPathDB; HostDB:ENSG00000131095; -. DR eggNOG; ENOG502RKU6; Eukaryota. DR GeneTree; ENSGT00940000159539; -. DR HOGENOM; CLU_012560_7_4_1; -. DR InParanoid; P14136; -. DR OMA; IMAHQVH; -. DR PhylomeDB; P14136; -. DR TreeFam; TF330122; -. DR PathwayCommons; P14136; -. DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4. DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy. DR SignaLink; P14136; -. DR SIGNOR; P14136; -. DR BioGRID-ORCS; 2670; 7 hits in 1141 CRISPR screens. DR ChiTaRS; GFAP; human. DR GeneWiki; Glial_fibrillary_acidic_protein; -. DR GenomeRNAi; 2670; -. DR Pharos; P14136; Tbio. DR PRO; PR:P14136; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P14136; Protein. DR Bgee; ENSG00000131095; Expressed in dorsal motor nucleus of vagus nerve and 142 other cell types or tissues. DR ExpressionAtlas; P14136; baseline and differential. DR GO; GO:0097450; C:astrocyte end-foot; IEA:Ensembl. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0042995; C:cell projection; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005178; F:integrin binding; IEA:Ensembl. DR GO; GO:0019900; F:kinase binding; IEA:Ensembl. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl. DR GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl. DR GO; GO:0070779; P:D-aspartate import across plasma membrane; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0045109; P:intermediate filament organization; IDA:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl. DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl. DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0031102; P:neuron projection regeneration; IEA:Ensembl. DR GO; GO:0010625; P:positive regulation of Schwann cell proliferation; IEA:Ensembl. DR GO; GO:1904714; P:regulation of chaperone-mediated autophagy; ISS:ParkinsonsUK-UCL. DR GO; GO:0051580; P:regulation of neurotransmitter uptake; IEA:Ensembl. DR GO; GO:0043254; P:regulation of protein-containing complex assembly; TAS:ParkinsonsUK-UCL. DR GO; GO:0014010; P:Schwann cell proliferation; IEA:Ensembl. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR006821; Intermed_filament_DNA-bd. DR PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1. DR PANTHER; PTHR45652:SF9; GLIAL FIBRILLARY ACIDIC PROTEIN; 1. DR Pfam; PF00038; Filament; 1. DR Pfam; PF04732; Filament_head; 1. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR UCD-2DPAGE; P14136; -. DR Genevisible; P14136; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Citrullination; Coiled coil; Cytoplasm; KW Direct protein sequencing; Disease variant; Intermediate filament; KW Leukodystrophy; Methylation; Phosphoprotein; Reference proteome. FT CHAIN 1..432 FT /note="Glial fibrillary acidic protein" FT /id="PRO_0000063805" FT DOMAIN 69..377 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..72 FT /note="Head" FT REGION 73..104 FT /note="Coil 1A" FT REGION 105..115 FT /note="Linker 1" FT REGION 116..214 FT /note="Coil 1B" FT REGION 215..230 FT /note="Linker 12" FT REGION 231..252 FT /note="Coil 2A" FT REGION 253..256 FT /note="Linker 2" FT REGION 257..377 FT /note="Coil 2B" FT REGION 378..432 FT /note="Tail" FT MOD_RES 7 FT /note="Phosphothreonine; by AURKB and ROCK1" FT /evidence="ECO:0000269|PubMed:12686604, FT ECO:0000269|PubMed:9099667" FT MOD_RES 12 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P03995" FT MOD_RES 13 FT /note="Phosphoserine; by AURKB and ROCK1" FT /evidence="ECO:0000269|PubMed:12686604, FT ECO:0000269|PubMed:9099667" FT MOD_RES 30 FT /note="Citrulline" FT /evidence="ECO:0000269|PubMed:23828821" FT MOD_RES 36 FT /note="Citrulline" FT /evidence="ECO:0000269|PubMed:23828821" FT MOD_RES 38 FT /note="Phosphoserine; by AURKB and ROCK1" FT /evidence="ECO:0000269|PubMed:12686604, FT ECO:0000269|PubMed:9099667" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P47819" FT MOD_RES 110 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P47819" FT MOD_RES 150 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P47819" FT MOD_RES 270 FT /note="Citrulline" FT /evidence="ECO:0000269|PubMed:23828821" FT MOD_RES 323 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P47819" FT MOD_RES 383 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P47819" FT MOD_RES 385 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P47819" FT MOD_RES 406 FT /note="Citrulline" FT /evidence="ECO:0000269|PubMed:23828821" FT MOD_RES 416 FT /note="Citrulline" FT /evidence="ECO:0000269|PubMed:23828821" FT VAR_SEQ 391..432 FT /note="ETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVM -> GGKSTK FT DGENHKVTRYLKSLTIRVIPIQAHQIVNGTPPARG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12058025, FT ECO:0000303|PubMed:14702039" FT /id="VSP_017052" FT VAR_SEQ 391..432 FT /note="ETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVM -> GQYSRA FT SWEGHWSPAPSSRACRLLQTGTEDQGKGIQLSLGAFVTLQRS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_017051" FT VARIANT 47 FT /note="P -> L (in dbSNP:rs57474185)" FT /evidence="ECO:0000269|PubMed:11138011, FT ECO:0000269|PubMed:15732097" FT /id="VAR_017464" FT VARIANT 63 FT /note="K -> Q (in ALXDRD; affects intermediate filaments FT formation yielding protein aggregates; dbSNP:rs60095124)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071517" FT VARIANT 66 FT /note="R -> Q (in ALXDRD; dbSNP:rs797044569)" FT /evidence="ECO:0000269|PubMed:21917775" FT /id="VAR_071518" FT VARIANT 70 FT /note="R -> Q (in ALXDRD; dbSNP:rs267607510)" FT /evidence="ECO:0000269|PubMed:17894839" FT /id="VAR_071519" FT VARIANT 70 FT /note="R -> W (in ALXDRD; dbSNP:rs60343255)" FT /evidence="ECO:0000269|PubMed:17894839" FT /id="VAR_071520" FT VARIANT 72 FT /note="E -> K (in ALXDRD; dbSNP:rs267607523)" FT /evidence="ECO:0000269|PubMed:21917775" FT /id="VAR_071521" FT VARIANT 73 FT /note="M -> K (in ALXDRD; dbSNP:rs61060395)" FT /evidence="ECO:0000269|PubMed:17894839" FT /id="VAR_071522" FT VARIANT 73 FT /note="M -> R (in ALXDRD; dbSNP:rs61060395)" FT /evidence="ECO:0000269|PubMed:12034785" FT /id="VAR_071523" FT VARIANT 73 FT /note="M -> T (in ALXDRD; dbSNP:rs61060395)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071524" FT VARIANT 74 FT /note="M -> T (in ALXDRD; dbSNP:rs267607504)" FT /evidence="ECO:0000269|PubMed:17934883" FT /id="VAR_071525" FT VARIANT 76 FT /note="L -> F (in ALXDRD; dbSNP:rs57120761)" FT /evidence="ECO:0000269|PubMed:11567214, FT ECO:0000269|PubMed:15732097, ECO:0000269|PubMed:23364391" FT /id="VAR_017465" FT VARIANT 76 FT /note="L -> V (in ALXDRD; dbSNP:rs57120761)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071526" FT VARIANT 77 FT /note="N -> K (in ALXDRD)" FT /evidence="ECO:0000269|PubMed:23364391" FT /id="VAR_071527" FT VARIANT 77 FT /note="N -> S (in ALXDRD; dbSNP:rs57590980)" FT /evidence="ECO:0000269|PubMed:15732097, FT ECO:0000269|PubMed:17894839" FT /id="VAR_071528" FT VARIANT 77 FT /note="N -> Y (in ALXDRD; dbSNP:rs58732244)" FT /evidence="ECO:0000269|PubMed:11567214" FT /id="VAR_017466" FT VARIANT 78 FT /note="D -> E (in ALXDRD; adult form; dbSNP:rs121909720)" FT /evidence="ECO:0000269|PubMed:12975300" FT /id="VAR_017477" FT VARIANT 78 FT /note="D -> N (in ALXDRD; dbSNP:rs797044571)" FT /evidence="ECO:0000269|PubMed:23743246" FT /id="VAR_071529" FT VARIANT 79 FT /note="R -> C (in ALXDRD; dbSNP:rs59793293)" FT /evidence="ECO:0000269|PubMed:11138011, FT ECO:0000269|PubMed:12034785, ECO:0000269|PubMed:15732097, FT ECO:0000269|PubMed:17894839, ECO:0000269|PubMed:23364391" FT /id="VAR_017467" FT VARIANT 79 FT /note="R -> G (in ALXDRD; dbSNP:rs59793293)" FT /evidence="ECO:0000269|PubMed:12034785" FT /id="VAR_071530" FT VARIANT 79 FT /note="R -> H (in ALXDRD; dbSNP:rs59285727)" FT /evidence="ECO:0000269|PubMed:11138011, FT ECO:0000269|PubMed:11567214, ECO:0000269|PubMed:12034785, FT ECO:0000269|PubMed:23364391" FT /id="VAR_017468" FT VARIANT 79 FT /note="R -> L (in ALXDRD; dbSNP:rs59285727)" FT /evidence="ECO:0000269|PubMed:12581808, FT ECO:0000269|PubMed:23364391" FT /id="VAR_071531" FT VARIANT 79 FT /note="R -> P (in ALXDRD; dbSNP:rs59285727)" FT /evidence="ECO:0000269|PubMed:17894839" FT /id="VAR_071532" FT VARIANT 83 FT /note="Y -> H (in ALXDRD; dbSNP:rs267607506)" FT /evidence="ECO:0000269|PubMed:18079314" FT /id="VAR_071533" FT VARIANT 86 FT /note="K -> E (in ALXDRD; dbSNP:rs797044573)" FT /evidence="ECO:0000269|PubMed:21917775" FT /id="VAR_071534" FT VARIANT 88 FT /note="R -> C (in ALXDRD; dbSNP:rs61622935)" FT /evidence="ECO:0000269|PubMed:11567214, FT ECO:0000269|PubMed:12034785, ECO:0000269|PubMed:15732097, FT ECO:0000269|PubMed:17894839, ECO:0000269|PubMed:18079314, FT ECO:0000269|PubMed:23364391" FT /id="VAR_017469" FT VARIANT 88 FT /note="R -> S (in ALXDRD; dbSNP:rs61622935)" FT /evidence="ECO:0000269|PubMed:11567214, FT ECO:0000269|PubMed:23364391" FT /id="VAR_017470" FT VARIANT 90 FT /note="L -> P (in ALXDRD; dbSNP:rs59661476)" FT /evidence="ECO:0000269|PubMed:15030911" FT /id="VAR_071535" FT VARIANT 97 FT /note="L -> P (in ALXDRD; dbSNP:rs59568967)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071536" FT VARIANT 101 FT /note="L -> P (in ALXDRD; dbSNP:rs267607516)" FT /evidence="ECO:0000269|PubMed:19412928" FT /id="VAR_071537" FT VARIANT 115 FT /note="V -> I (does not affect intermediate filaments FT formation; dbSNP:rs56746197)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071538" FT VARIANT 157 FT /note="D -> N (in dbSNP:rs59291670)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071539" FT VARIANT 207 FT /note="E -> K (in ALXDRD; dbSNP:rs267607500)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071540" FT VARIANT 207 FT /note="E -> Q (in ALXDRD; dbSNP:rs267607500)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071541" FT VARIANT 210 FT /note="E -> K (in ALXDRD; affects intermediate filaments FT formation; dbSNP:rs57661783)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071542" FT VARIANT 223 FT /note="E -> Q (in dbSNP:rs56679084)" FT /evidence="ECO:0000269|PubMed:12944715, FT ECO:0000269|PubMed:15732097" FT /id="VAR_017478" FT VARIANT 235 FT /note="L -> P (in ALXDRD; dbSNP:rs60269890)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071543" FT VARIANT 236 FT /note="K -> T (in ALXDRD; dbSNP:rs267607525)" FT /evidence="ECO:0000269|PubMed:21917775" FT /id="VAR_071544" FT VARIANT 239 FT /note="R -> C (in ALXDRD; dbSNP:rs58064122)" FT /evidence="ECO:0000269|PubMed:11138011, FT ECO:0000269|PubMed:11567214, ECO:0000269|PubMed:12034785, FT ECO:0000269|PubMed:15732097, ECO:0000269|PubMed:23364391" FT /id="VAR_017471" FT VARIANT 239 FT /note="R -> H (in ALXDRD; dbSNP:rs59565950)" FT /evidence="ECO:0000269|PubMed:11138011, FT ECO:0000269|PubMed:11567214, ECO:0000269|PubMed:15732097, FT ECO:0000269|PubMed:17894839, ECO:0000269|PubMed:23364391" FT /id="VAR_017472" FT VARIANT 239 FT /note="R -> L (in ALXDRD; dbSNP:rs59565950)" FT /evidence="ECO:0000269|PubMed:17043438" FT /id="VAR_071545" FT VARIANT 239 FT /note="R -> P (in ALXDRD; dbSNP:rs59565950)" FT /evidence="ECO:0000269|PubMed:15732097, FT ECO:0000269|PubMed:17894839" FT /id="VAR_071546" FT VARIANT 242 FT /note="Y -> D (in ALXDRD; dbSNP:rs60551555)" FT /evidence="ECO:0000269|PubMed:12034785" FT /id="VAR_071547" FT VARIANT 244 FT /note="A -> V (in ALXDRD; uncertain significance; does not FT affect intermediate filaments formation; dbSNP:rs61497286)" FT /evidence="ECO:0000269|PubMed:11595337, FT ECO:0000269|PubMed:15732097" FT /id="VAR_017473" FT VARIANT 253 FT /note="A -> G (in ALXDRD; affects intermediate filaments FT formation yielding protein aggregates; dbSNP:rs61726470)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071548" FT VARIANT 257 FT /note="Y -> C (in ALXDRD; impairs filaments formation; FT dbSNP:rs267607505)" FT /evidence="ECO:0000269|PubMed:17960815" FT /id="VAR_071549" FT VARIANT 258 FT /note="R -> P (in ALXDRD; dbSNP:rs61726468)" FT /evidence="ECO:0000269|PubMed:11138011" FT /id="VAR_017474" FT VARIANT 267 FT /note="A -> P (in ALXDRD; dbSNP:rs797044581)" FT /evidence="ECO:0000269|PubMed:17805552" FT /id="VAR_071550" FT VARIANT 276 FT /note="R -> L (in ALXDRD; dbSNP:rs121909719)" FT /evidence="ECO:0000269|PubMed:20359319" FT /id="VAR_071551" FT VARIANT 279 FT /note="K -> E (in ALXDRD; dbSNP:rs58536923)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071552" FT VARIANT 295 FT /note="D -> N (in dbSNP:rs1126642)" FT /evidence="ECO:0000269|PubMed:11138011, FT ECO:0000269|PubMed:9693047" FT /id="VAR_017479" FT VARIANT 330 FT /note="R -> G (in ALXDRD; associated in cis with K-332; FT dbSNP:rs267607513)" FT /evidence="ECO:0000269|PubMed:18004641" FT /id="VAR_071553" FT VARIANT 332 FT /note="E -> K (in ALXDRD; associated in cis with G-330; FT dbSNP:rs267607514)" FT /evidence="ECO:0000269|PubMed:18004641" FT /id="VAR_071554" FT VARIANT 352 FT /note="L -> P (in ALXDRD; dbSNP:rs28932769)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071555" FT VARIANT 359 FT /note="L -> P (in ALXDRD; dbSNP:rs267607511)" FT /evidence="ECO:0000269|PubMed:17894839" FT /id="VAR_071556" FT VARIANT 359 FT /note="L -> V (in ALXDRD; dbSNP:rs60825166)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071557" FT VARIANT 362 FT /note="E -> D (in ALXDRD; dbSNP:rs121909718)" FT /evidence="ECO:0000269|PubMed:12034796" FT /id="VAR_017475" FT VARIANT 364 FT /note="A -> P (in ALXDRD; dbSNP:rs58645997)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071558" FT VARIANT 366 FT /note="Y -> H (in ALXDRD; dbSNP:rs58008462)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071559" FT VARIANT 371 FT /note="E -> Q (in ALXDRD; dbSNP:rs267607526)" FT /evidence="ECO:0000269|PubMed:21917775" FT /id="VAR_071560" FT VARIANT 371 FT /note="E -> V (in ALXDRD; dbSNP:rs57815192)" FT /evidence="ECO:0000269|PubMed:21917775" FT /id="VAR_071561" FT VARIANT 373 FT /note="E -> D (in ALXDRD)" FT /evidence="ECO:0000269|PubMed:23364391" FT /id="VAR_071562" FT VARIANT 373 FT /note="E -> K (in ALXDRD; dbSNP:rs58075601)" FT /evidence="ECO:0000269|PubMed:12034785, FT ECO:0000269|PubMed:15732097" FT /id="VAR_071563" FT VARIANT 373 FT /note="E -> Q (in ALXDRD; dbSNP:rs58075601)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071564" FT VARIANT 374 FT /note="E -> G (in ALXDRD; dbSNP:rs59628143)" FT /evidence="ECO:0000269|PubMed:15732097" FT /id="VAR_071565" FT VARIANT 374 FT /note="E -> Q (in ALXDRD)" FT /evidence="ECO:0000269|PubMed:23364391" FT /id="VAR_071566" FT VARIANT 376 FT /note="R -> G (in ALXDRD; dbSNP:rs267607512)" FT /evidence="ECO:0000269|PubMed:21917775" FT /id="VAR_071567" FT VARIANT 385 FT /note="S -> F (in ALXDRD; dbSNP:rs797044590)" FT /evidence="ECO:0000269|PubMed:23364391" FT /id="VAR_071568" FT VARIANT 416 FT /note="R -> W (in ALXDRD; dbSNP:rs121909717)" FT /evidence="ECO:0000269|PubMed:11138011, FT ECO:0000269|PubMed:12034785, ECO:0000269|PubMed:15732097, FT ECO:0000269|PubMed:17894839, ECO:0000269|PubMed:24742911" FT /id="VAR_017476" FT CONFLICT 121 FT /note="R -> P (in Ref. 9; CAB61354)" FT /evidence="ECO:0000305" FT CONFLICT 146 FT /note="Q -> H (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 151 FT /note="V -> L (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="Missing (in Ref. 9; CAB61354)" FT /evidence="ECO:0000305" FT CONFLICT 158 FT /note="E -> G (in Ref. 6; AAL16662)" FT /evidence="ECO:0000305" FT CONFLICT 160 FT /note="N -> K (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 166 FT /note="E -> D (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 174 FT /note="Q -> QQ (in Ref. 9; CAB61354)" FT /evidence="ECO:0000305" FT CONFLICT 258 FT /note="R -> H (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 326 FT /note="E -> V (in Ref. 8; BAD96403)" FT /evidence="ECO:0000305" FT CONFLICT 334 FT /note="E -> D (in Ref. 3)" FT /evidence="ECO:0000305" FT HELIX 111..210 FT /evidence="ECO:0007829|PDB:6A9P" FT VARIANT P14136-3:426 FT /note="T -> A (in dbSNP:rs9916491)" FT /evidence="ECO:0000305" FT /id="VAR_082837" FT VARIANT P14136-3:426 FT /note="T -> V (requires 2 nucleotide substitutions; FT dbSNP:rs386797323)" FT /evidence="ECO:0000305" FT /id="VAR_082838" SQ SEQUENCE 432 AA; 49880 MW; E6C3B3454C3F1250 CRC64; MERRRITSAA RRSYVSSGEM MVGGLAPGRR LGPGTRLSLA RMPPPLPTRV DFSLAGALNA GFKETRASER AEMMELNDRF ASYIEKVRFL EQQNKALAAE LNQLRAKEPT KLADVYQAEL RELRLRLDQL TANSARLEVE RDNLAQDLAT VRQKLQDETN LRLEAENNLA AYRQEADEAT LARLDLERKI ESLEEEIRFL RKIHEEEVRE LQEQLARQQV HVELDVAKPD LTAALKEIRT QYEAMASSNM HEAEEWYRSK FADLTDAAAR NAELLRQAKH EANDYRRQLQ SLTCDLESLR GTNESLERQM REQEERHVRE AASYQEALAR LEEEGQSLKD EMARHLQEYQ DLLNVKLALD IEIATYRKLL EGEENRITIP VQTFSNLQIR ETSLDTKSVS EGHLKRNIVV KTVEMRDGEV IKESKQEHKD VM //