Reviewed, UniProtKB/Swiss-Prot P14136 (GFAP_HUMAN)

Names and origin

Protein names

Recommended name:
    Glial fibrillary acidic protein
      Short name=GFAP

Gene names

Name:

GFAP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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).
Subcellular location	Cytoplasm. Note: Associated with intermediate filaments. Ref.15
Tissue specificity	Expressed in cells lacking fibronectin. Ref.3
Involvement in disease	Defects in GFAP are a cause of Alexander disease (ALEXD) [MIM:203450]. Alexander disease is a rare disorder of the central nervous system. It is a progressive leukoencephalopathy whose hallmark is the widespread accumulation of Rosenthal fibers which are cytoplasmic inclusions in astrocytes. The most common form affects infants and young children, and is characterized by progressive failure of central myelination, usually leading to death usually within the first decade. Infants with Alexander disease develop a leukoencephalopathy 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. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23
Sequence similarities	Belongs to the intermediate filament family.

Ontologies

Keywords
Cellular component	Cytoplasm Intermediate filament
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell intermediate filament Ref.1 Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from sequence or structural similarity. Source: UniProtKB structural constituent of cytoskeleton Ref.1 Traceable author statement. 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...IVNGVPPARG
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Natural variant	426	1	V → A
	Natural variant	426	1	V → T

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 432	432	Glial fibrillary acidic protein		PRO_0000063805
Regions
	Region	1 – 72	72	Head
	Region	73 – 377	305	Rod
	Region	73 – 104	32	Coil 1A
	Region	105 – 115	11	Linker 1
	Region	116 – 214	99	Coil 1B
	Region	215 – 230	16	Linker 12
	Region	231 – 252	22	Coil 2A
	Region	253 – 256	4	Linker 2
	Region	257 – 377	121	Coil 2B
	Region	378 – 432	55	Tail
Amino acid modifications
	Modified residue	110	1	Phosphothreonine By similarity
	Modified residue	383	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	391 – 432	42	ETSLD…HKDVM → GQYSRASWEGHWSPAPSSRA CRLLQTGTEDQGKGIQLSLG AFVTLQRS in isoform 2.		VSP_017051
	Alternative sequence	391 – 432	42	ETSLD…HKDVM → GGKSTKDGENHKVTRYLKSL TIRVIPIQAHQIVNGVPPAR G in isoform 3.		VSP_017052
	Natural variant	47	1	P → L in ALEXD; could be a polymorphism. Ref.18		VAR_017464
	Natural variant	76	1	L → F in ALEXD. Ref.19		VAR_017465
	Natural variant	77	1	N → Y in ALEXD. Ref.19		VAR_017466
	Natural variant	78	1	D → E in ALEXD; adult form. Ref.22		VAR_017477
	Natural variant	79	1	R → C in ALEXD. Ref.18		VAR_017467
	Natural variant	79	1	R → H in ALEXD. Ref.18 Ref.19		VAR_017468
	Natural variant	88	1	R → C in ALEXD. Ref.19		VAR_017469
	Natural variant	88	1	R → S in ALEXD. Ref.19		VAR_017470
	Natural variant	223	1	E → Q in ALEXD; adult form. Ref.23		VAR_017478
	Natural variant	239	1	R → C in ALEXD. Ref.18 Ref.19		VAR_017471
	Natural variant	239	1	R → H in ALEXD. Ref.18 Ref.19		VAR_017472
	Natural variant	244	1	A → V in ALEXD. Ref.20		VAR_017473
	Natural variant	258	1	R → P in ALEXD. Ref.18		VAR_017474
	Natural variant	295	1	D → N: dbSNP rs1126642. Ref.18 Ref.5		VAR_017479
	Natural variant	362	1	E → D in ALEXD. Ref.21		VAR_017475
	Natural variant	416	1	R → W in ALEXD. Ref.18		VAR_017476
Experimental info
	Sequence conflict	121	1	R → P in CAB61354. Ref.9
	Sequence conflict	146	1	Q → H Ref.3
	Sequence conflict	151	1	V → L Ref.3
	Sequence conflict	155	1	Missing in CAB61354. Ref.9
	Sequence conflict	158	1	E → G in AAL16662. Ref.6
	Sequence conflict	160	1	N → K Ref.3
	Sequence conflict	166	1	E → D Ref.3
	Sequence conflict	174	1	Q → QQ in CAB61354. Ref.9
	Sequence conflict	258	1	R → H Ref.3
	Sequence conflict	326	1	E → V in BAD96403. Ref.8
	Sequence conflict	334	1	E → D Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (GFAP alpha) [UniParc]. Last modified January 1, 1990. Version 1. Checksum: E6C3B3454C3F1250	FASTA	432	49,880
	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
	Isoform 2. Checksum: 05F98D5333D60FE4	FASTA	438	50,289
	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 GQYSRASWEG HWSPAPSSRA CRLLQTGTED 430 QGKGIQLSLG AFVTLQRS
	Isoform 3 (GFAP epsilon). Checksum: 5D716D21A95120D6	FASTA	431	49,506
	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 GGKSTKDGEN HKVTRYLKSL TIRVIPIQAH 430 QIVNGVPPAR G

References

	« Hide 'large scale' referencesShow '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: 2740350] [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: 2163003] [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: 1847665] [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: 1636374] [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: 9693047] [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. , 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: 14702039] [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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Kidney.
[10]	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. , 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].
[11]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[12]	"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: 2349237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-76.
[13]	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, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[14]	"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: 2780570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 352-417.
[15]	"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: 12058025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 391-432 (ISOFORM 3), SUBCELLULAR LOCATION, INTERACTION WITH PSEN1. Tissue: Fetal brain.
[16]	"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: 12837269] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-432 (ISOFORM 3), VARIANTS. Tissue: Blood.
[17]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[18]	"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: 11138011] [Abstract] Cited for: VARIANTS ALEXD LEU-47; CYS-79; HIS-79; CYS-239; HIS-239; PRO-258 AND TRP-416, VARIANT ASN-295.
[19]	"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: 11567214] [Abstract] Cited for: VARIANTS ALEXD PHE-76; TYR-77; HIS-79; CYS-88; SER-88; CYS-239 AND HIS-239.
[20]	"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: 11595337] [Abstract] Cited for: VARIANT ALEXD VAL-244.
[21]	"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: 12034796] [Abstract] Cited for: VARIANT ALEXD ASP-362.
[22]	"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: 12975300] [Abstract] Cited for: VARIANT ALEXD GLU-78.
[23]	"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: 12944715] [Abstract] Cited for: VARIANT ALEXD GLN-223.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

Wikipedia

GFAP entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. CH471178 Genomic DNA. Translation: EAW51570.1. 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.
IPI	IPI00025363. IPI00383815. IPI00443478.
PIR	A32936. T42645.
RefSeq	NP_001124491.1. NP_002046.1.
UniGene	Hs.514227
3D structure databases
HSSP	HSSP built from PDB template 1GK4 based on UniProtKB P08670.
SMR	P14136. Positions 294-372.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14136. 14 interactions.
STRING	P14136.
PTM databases
PhosphoSite	P14136.
2-D gel databases
HSC-2DPAGE	P14136.
REPRODUCTION-2DPAGE	P14136.
Proteomic databases
PeptideAtlas	P14136.
PRIDE	P14136.
Genome annotation databases
Ensembl	ENST00000253408; ENSP00000253408; ENSG00000131095; Homo sapiens. [Genome view] ENST00000376990; ENSP00000366189; ENSG00000131095; Homo sapiens. [Genome view] ENST00000421021; ENSP00000408009; ENSG00000131095; Homo sapiens. [Genome view] ENST00000435360; ENSP00000403962; ENSG00000131095; Homo sapiens. [Genome view]
GeneID	2670.
KEGG	hsa:2670.
UCSC	uc002ihq.1. human. uc002ihr.1. human.
Organism-specific databases
CTD	2670.
GeneCards	GC17M040338.
H-InvDB	HIX0013889.
HGNC	HGNC:4235. GFAP.
HPA	CAB000039.
MIM	137780. gene. 203450. phenotype.
Orphanet	58. Alexander disease.
PharmGKB	PA28647.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P14136.
OMA	NLATYRQ.
Gene expression databases
ArrayExpress	P14136.
Bgee	P14136.
Genevestigator	P14136.
GermOnline	ENSG00000131095. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR006821. Intermed_filament_DNA_bd. IPR018039. Intermediate_filament_CS. [Graphical view]
PANTHER	PTHR23239. IF. 1 hit.
Pfam	PF00038. Filament. 1 hit. PF04732. Filament_head. 1 hit. [Graphical view]
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	10538.
PMAP-CutDB	P14136.
SOURCE	Search...

Entry information

Entry name

GFAP_HUMAN

Accession

Primary (citable) accession number: P14136
Secondary accession number(s): B2RD44 , 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:	November 3, 2009
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.