[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1073/pnas.86.13.5178; PubMed=2740350 [NCBI, ExPASy, EBI, Israel, Japan] Reeves S.A., Helman L.J., Allison A., Israel M.A.; "Molecular cloning and primary structure of human glial fibrillary acidic protein."; Proc. Natl. Acad. Sci. U.S.A. 86:5178-5182(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1016/0169-328X(90)90078-R; PubMed=2163003 [NCBI, ExPASy, EBI, Israel, Japan] Brenner M., Lampel K., Nakatani Y., Mill J., Banner C., Mearow K., Dohadwala M., Lipsky R., Freese E.; "Characterization of human cDNA and genomic clones for glial fibrillary acidic protein."; Brain Res. Mol. Brain Res. 7:277-286(1990).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. PubMed=1847665 [NCBI, ExPASy, EBI, Israel, Japan] Bongcam-Rudloff E., Nister M., Betsholtz C., Wang J.-L., Stenman G., Huebner K., Croce C.M., Westermark B.; "Human glial fibrillary acidic protein: complementary DNA cloning, chromosome localization, and messenger RNA expression in human glioma cell lines of various phenotypes."; Cancer Res. 51:1553-1560(1991).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1007/BF00299404; PubMed=1636374 [NCBI, ExPASy, EBI, Israel, Japan] Kumanishi T., Usui H., Ichikawa T., Nishiyama A., Katagiri T., Abe S., Yoshida Y., Washiyama K., Kuwano R., Sakimura K.; "Human glial fibrillary acidic protein (GFAP): molecular cloning of the complete cDNA sequence and chromosomal localization (chromosome 17) of the GFAP gene."; Acta Neuropathol. 83:569-578(1992).
[5]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-295. DOI=10.1006/geno.1998.5360; PubMed=9693047 [NCBI, ExPASy, EBI, Israel, Japan] Isaacs A., Baker M., Wavrant-De Vrieze F., Hutton M.; "Determination of the gene structure of human GFAP and absence of coding region mutations associated with frontotemporal dementia with parkinsonism linked to chromosome 17."; Genomics 51:152-154(1998).
[6]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Han C., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.; Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). TISSUE=Brain; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Brain; 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.
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Kidney; DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan] Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.; "The full-ORF clone resource of the German cDNA consortium."; BMC Genomics 8:399-399(2007).
[10]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[11]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-76. DOI=10.1073/pnas.87.11.4289; PubMed=2349237 [NCBI, ExPASy, EBI, Israel, Japan] Nakatani Y., Brenner M., Freese E.; "An RNA polymerase II promoter containing sequences upstream and downstream from the RNA startpoint that direct initiation of transcription from the same site."; Proc. Natl. Acad. Sci. U.S.A. 87:4289-4293(1990).
[12]	PROTEIN SEQUENCE OF 13-29; 50-63; 96-105; 112-121; 163-173; 189-198; 261-270; 288-300; 331-367 AND 377-390, AND MASS SPECTROMETRY. TISSUE=Fetal brain cortex; Lubec G., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[13]	NUCLEOTIDE SEQUENCE [MRNA] OF 352-417. DOI=10.1073/pnas.86.18.7260; PubMed=2780570 [NCBI, ExPASy, EBI, Israel, Japan] Duguid J.R., Bohmont C.W., Liu N.G., Tourtellotte W.W.; "Changes in brain gene expression shared by scrapie and Alzheimer disease."; Proc. Natl. Acad. Sci. U.S.A. 86:7260-7264(1989).
[14]	NUCLEOTIDE SEQUENCE [MRNA] OF 391-432 (ISOFORM 3), SUBCELLULAR LOCATION, AND INTERACTION WITH PSEN1. TISSUE=Fetal brain; DOI=10.1074/jbc.M112121200; PubMed=12058025 [NCBI, ExPASy, EBI, Israel, Japan] Nielsen A.L., Holm I.E., Johansen M., Bonven B., Jorgensen P., Jorgensen A.L.; "A new splice variant of glial fibrillary acidic protein GFAPepsilon, interacts with the presenilin proteins."; J. Biol. Chem. 277:29983-29991(2002).
[15]	PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-432 (ISOFORM 3), AND VARIANTS. TISSUE=Blood; DOI=10.1016/S0888-7543(03)00106-X; PubMed=12837269 [NCBI, ExPASy, EBI, Israel, Japan] Singh R., Nielsen A.L., Johansen M.G., Jorgensen A.L.; "Genetic polymorphism and sequence evolution of an alternatively spliced exon of the glial fibrillary acidic protein gene, GFAP."; Genomics 82:185-193(2003).
[16]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[17]	VARIANTS ALEXD LEU-47; CYS-79; HIS-79; CYS-239; HIS-239; PRO-258 AND TRP-416, AND VARIANT ASN-295. DOI=10.1038/83679; PubMed=11138011 [NCBI, ExPASy, EBI, Israel, Japan] Brenner M., Johnson A.B., Boespflug-Tanguy O., Rodriguez D., Goldman J.E., Messing A.; "Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease."; Nat. Genet. 27:117-120(2001).
[18]	VARIANTS ALEXD PHE-76; TYR-77; HIS-79; CYS-88; SER-88; CYS-239 AND HIS-239. DOI=10.1086/323799; PubMed=11567214 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Infantile Alexander disease: spectrum of GFAP mutations and genotype-phenotype correlation."; Am. J. Hum. Genet. 69:1134-1140(2001).
[19]	VARIANT ALEXD VAL-244. DOI=10.1016/S0304-3940(01)02139-5; PubMed=11595337 [NCBI, ExPASy, EBI, Israel, Japan] Aoki Y., Haginoya K., Munakata M., Yokoyama H., Nishio T., Togashi N., Ito T., Suzuki Y., Kure S., Iinuma K., Brenner M., Matsubara Y.; "A novel mutation in glial fibrillary acidic protein gene in a patient with Alexander disease."; Neurosci. Lett. 312:71-74(2001).
[20]	VARIANT ALEXD ASP-362. PubMed=12034796 [NCBI, ExPASy, EBI, Israel, Japan] Sawaishi Y., Yano T., Takaku I., Takada G.; "Juvenile Alexander disease with a novel mutation in glial fibrillary acidic protein gene."; Neurology 58:1541-1543(2002).
[21]	VARIANT ALEXD GLU-78. DOI=10.1001/archneur.60.9.1307; PubMed=12975300 [NCBI, ExPASy, EBI, Israel, Japan] Stumpf E., Masson H., Duquette A., Berthelet F., McNabb J., Lortie A., Lesage J., Montplaisir J., Brais B., Cossette P.; "Adult Alexander disease with autosomal dominant transmission: a distinct entity caused by mutation in the glial fibrillary acid protein gene."; Arch. Neurol. 60:1307-1312(2003).
[22]	VARIANT ALEXD GLN-223. DOI=10.1159/000072507; PubMed=12944715 [NCBI, ExPASy, EBI, Israel, Japan] Brockmann K., Meins M., Taubert A., Trappe R., Grond M., Hanefeld F.; "A novel GFAP mutation and disseminated white matter lesions: adult Alexander disease?"; Eur. Neurol. 50:100-105(2003).

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: Interacts with SYNM (By similarity). Isoform 3 interacts with PSEN1 (via N-terminus).
SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with intermediate filaments.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing. Isoforms differ in the C-terminal region which is encoded by alternative exons.

Name	1
Synonyms	GFAP alpha
Isoform ID	P14136-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P14136-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_017051.

Name	3
Synonyms	GFAP epsilon
Isoform ID	P14136-3
Note: Variant in position: 426:V->A,T.
Features which should be applied to build the isoform sequence: VSP_017052.

TISSUE SPECIFICITY: Expressed in cells lacking fibronectin.
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.
SIMILARITY: Belongs to the intermediate filament family.
WEB RESOURCE: Name=Human Intermediate Filament Mutation Database; URL="http://www.interfil.org";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=GFAP";.
WEB RESOURCE: Name=Wikipedia; Note=GFAP entry; URL="http://en.wikipedia.org/wiki/Glial_fibrillary_acidic_protein";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J04569; AAA52528.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S40719; AAB22581.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF419299; AAL16662.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK128790; BAC87610.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222683; BAD96403.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133013; CAB61354.2; -; Transcribed_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013596; AAH13596.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC041765; AAH41765.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062609; AAH62609.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26638; AAA52529.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ306447; CAC69881.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY142187; AAN87903.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY142188; AAN87904.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY142191; AAN87907.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00025363; -.
IPI00383815; -.
IPI00443478; -.

PIR

A32936; A32936.
T42645; T42645.

RefSeq

NP_001124491.1; -.
NP_002046.1; -.

UniGene

Hs.514227

3D structure databases

HSSP

P08670; 1GK4. [HSSP ENTRY / PDB]

SMR

P14136; 294-372.

ModBase

P14136.

Protein-protein interaction databases

IntAct

P14136; 14.

PTM databases

PhosphoSite

P14136; -.

2D gel databases

HSC-2DPAGE

P14136; -.

REPRODUCTION-2DPAGE

P14136; -.

Organism-specific databases

GC17M040338; -.

HIX0013889; -.

HGNC:4235; GFAP.

CAB000039; -.

137780; gene. [NCBI / EBI]
203450; phenotype. [NCBI / EBI]

Orphanet

58; Alexander disease.

PharmGKB

PA28647; -.

Gene expression databases

ArrayExpress

P14136; -.

Bgee

P14136; -.

GermOnline

ENSG00000131095; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005882;	Cellular component: intermediate filament (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005200;	Molecular function: structural constituent of cytoskeleton (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR016044; F.
IPR001664; IF.
IPR006821; Intermed_filament_DNA_bd.
IPR018039; Intermediate_filament_CS.
Graphical view of domain structure.

PANTHER

PTHR23239; IF; 1.

Pfam

PF00038; Filament; 1.
PF04732; Filament_head; 1.
Pfam graphical view of domain structure.

PROSITE

PS00226; IF; 1.

Proteomic databases

PeptideAtlas

P14136; -.

PRIDE

P14136; -.

Genome annotation databases

Ensembl

ENSG00000131095; Homo sapiens. [Contig view]

GeneID

2670; -.

KEGG

hsa:2670; -.

Phylogenomic databases

HOVERGEN

P14136; -.

OMA

P14136; NLATYRQ.

Other

10538; -.

P14136; -.

GFAP; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Coiled coil; Cytoplasm; Direct protein sequencing; Disease mutation; Intermediate filament; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 432`	`432`	`Glial fibrillary acidic protein.`	`PRO_0000063805`
`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.`
`MOD_RES`	`110 110`		`Phosphothreonine (By similarity).`
`MOD_RES`	`383 383`		`Phosphothreonine (By similarity).`
`VAR_SEQ`	`391 432`		`ETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQE` `HKDVM -> GQYSRASWEGHWSPAPSSRACRLLQTGTEDQGKGIQLSLG` `AFVTLQRS (in isoform 2).`	`VSP_017051`
`VAR_SEQ`	`391 432`		`ETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQE` `HKDVM -> GGKSTKDGENHKVTRYLKSLTIRVIPIQAHQIVNGV` `PPARG (in isoform 3).`	`VSP_017052`
`VARIANT`	`47 47`	`1`	`P -> L (in ALEXD; could be a polymorphism).`	`VAR_017464`
`VARIANT`	`76 76`	`1`	`L -> F (in ALEXD).`	`VAR_017465`
`VARIANT`	`77 77`	`1`	`N -> Y (in ALEXD).`	`VAR_017466`
`VARIANT`	`78 78`	`1`	`D -> E (in ALEXD; adult form).`	`VAR_017477`
`VARIANT`	`79 79`	`1`	`R -> C (in ALEXD).`	`VAR_017467`
`VARIANT`	`79 79`	`1`	`R -> H (in ALEXD).`	`VAR_017468`
`VARIANT`	`88 88`	`1`	`R -> C (in ALEXD).`	`VAR_017469`
`VARIANT`	`88 88`	`1`	`R -> S (in ALEXD).`	`VAR_017470`
`VARIANT`	`223 223`	`1`	`E -> Q (in ALEXD; adult form).`	`VAR_017478`
`VARIANT`	`239 239`	`1`	`R -> C (in ALEXD).`	`VAR_017471`
`VARIANT`	`239 239`	`1`	`R -> H (in ALEXD).`	`VAR_017472`
`VARIANT`	`244 244`	`1`	`A -> V (in ALEXD).`	`VAR_017473`
`VARIANT`	`258 258`	`1`	`R -> P (in ALEXD).`	`VAR_017474`
`VARIANT`	`295 295`	`1`	`D -> N (in dbSNP:rs1126642 [NCBI]).`	`VAR_017479`
`VARIANT`	`362 362`	`1`	`E -> D (in ALEXD).`	`VAR_017475 [3D]`
`VARIANT`	`416 416`	`1`	`R -> W (in ALEXD).`	`VAR_017476`
`CONFLICT`	`121 121`		`R -> P (in Ref. 9; CAB61354).`
`CONFLICT`	`146 146`		`Q -> H (in Ref. 3).`
`CONFLICT`	`151 151`		`V -> L (in Ref. 3).`
`CONFLICT`	`155 155`		`Missing (in Ref. 9; CAB61354).`
`CONFLICT`	`158 158`		`E -> G (in Ref. 6; AAL16662).`
`CONFLICT`	`160 160`		`N -> K (in Ref. 3).`
`CONFLICT`	`166 166`		`E -> D (in Ref. 3).`
`CONFLICT`	`174 174`		`Q -> QQ (in Ref. 9; CAB61354).`
`CONFLICT`	`258 258`		`R -> H (in Ref. 3).`
`CONFLICT`	`326 326`		`E -> V (in Ref. 8; BAD96403).`
`CONFLICT`	`334 334`		`E -> D (in Ref. 3).`

Sequence information

Length: 432 AA [This is the length of the unprocessed precursor]

Molecular weight: 49880 Da [This is the MW of the unprocessed precursor]

CRC64: E6C3B3454C3F1250 [This is a checksum on the sequence]

        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

P14136 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools