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Fibroblast growth factor 13 (FGF-13) (Fibroblast growth factor homologous factor 2) (FHF-2)

 FGF13_HUMAN             Reviewed;         245 AA.
Q92913; B1AK18; B7Z4M7; B7Z8N0; D3DWH4; O95830; Q9NZH9; Q9NZI0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 164.
RecName: Full=Fibroblast growth factor 13;
Short=FGF-13;
AltName: Full=Fibroblast growth factor homologous factor 2;
Short=FHF-2;
Name=FGF13; Synonyms=FHF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Retina;
PubMed=8790420; DOI=10.1073/pnas.93.18.9850;
Smallwood P.M., Munoz-Sanjuan I., Tong P., Macke J.P., Hendry S.H.,
Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.;
"Fibroblast growth factor (FGF) homologous factors: new members of the
FGF family implicated in nervous system development.";
Proc. Natl. Acad. Sci. U.S.A. 93:9850-9857(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=10071193; DOI=10.1007/s004390050910;
Gecz J., Baker E., Donnelly A., Ming J.E., McDonnald-McGinn D.M.,
Spinner N.B., Zackai E.H., Sutherland G.R., Mulley J.C.;
"Fibroblast growth factor homologous factor 2 (FHF2): gene structure,
expression and mapping to the Borjeson-Forssman-Lehmann syndrome
region in Xq26 delineated by a duplication breakpoint in a BFLS-like
patient.";
Hum. Genet. 104:56-63(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Brain, and Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-197.
NIEHS SNPs program;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), ALTERNATIVE
SPLICING, AND SUBCELLULAR LOCATION.
PubMed=10644718; DOI=10.1074/jbc.275.4.2589;
Munoz-Sanjuan I., Smallwood P.M., Nathans J.;
"Isoform diversity among fibroblast growth factor homologous factors
is generated by alternative promoter usage and differential
splicing.";
J. Biol. Chem. 275:2589-2597(2000).
[9]
TISSUE SPECIFICITY.
PubMed=9232594; DOI=10.1016/S0925-4773(97)00042-7;
Hartung H., Feldman B., Lovec H., Coulier F., Birnbaum D.,
Goldfarb M.;
"Murine FGF-12 and FGF-13: expression in embryonic nervous system,
connective tissue and heart.";
Mech. Dev. 64:31-39(1997).
[10]
INTERACTION WITH MAPK8IP2.
PubMed=11378392; DOI=10.1016/S0960-9822(01)00232-9;
Schoorlemmer J., Goldfarb M.;
"Fibroblast growth factor homologous factors are intracellular
signaling proteins.";
Curr. Biol. 11:793-797(2001).
[11]
FUNCTION IN SCN8A REGULATION, AND INTERACTION WITH SCN8A.
PubMed=15282281; DOI=10.1523/JNEUROSCI.1628-04.2004;
Wittmack E.K., Rush A.M., Craner M.J., Goldfarb M., Waxman S.G.,
Dib-Hajj S.D.;
"Fibroblast growth factor homologous factor 2B: association with
Nav1.6 and selective colocalization at nodes of Ranvier of dorsal root
axons.";
J. Neurosci. 24:6765-6775(2004).
[12]
INTERACTION WITH SCN5A.
PubMed=21817159; DOI=10.1161/CIRCRESAHA.111.247957;
Wang C., Hennessey J.A., Kirkton R.D., Wang C., Graham V.,
Puranam R.S., Rosenberg P.B., Bursac N., Pitt G.S.;
"Fibroblast growth factor homologous factor 13 regulates Na+ channels
and conduction velocity in murine hearts.";
Circ. Res. 109:775-782(2011).
[13]
INTERACTION WITH SCN1A; SCN2A; SCN5A AND SCN8A, AND MUTAGENESIS OF
PRO-207.
PubMed=21566136; DOI=10.1074/jbc.M111.245803;
Wang C., Wang C., Hoch E.G., Pitt G.S.;
"Identification of novel interaction sites that determine specificity
between fibroblast growth factor homologous factors and voltage-gated
sodium channels.";
J. Biol. Chem. 286:24253-24263(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-245, AND INTERACTION WITH
SCN1A; SCN11A; SCN2A AND SCN5A.
PubMed=19406745; DOI=10.1074/jbc.M109.001842;
Goetz R., Dover K., Laezza F., Shtraizent N., Huang X., Tchetchik D.,
Eliseenkova A.V., Xu C.F., Neubert T.A., Ornitz D.M., Goldfarb M.,
Mohammadi M.;
"Crystal structure of a fibroblast growth factor homologous factor
(FHF) defines a conserved surface on FHFs for binding and modulation
of voltage-gated sodium channels.";
J. Biol. Chem. 284:17883-17896(2009).
-!- FUNCTION: Microtubule-binding protein which directly binds tubulin
and is involved in both polymerization and stabilization of
microtubules. Through its action on microtubules, may participate
to the refinement of axons by negatively regulating axonal and
leading processes branching. Plays a crucial role in neuron
polarization and migration in the cerebral cortex and the
hippocampus. {ECO:0000269|PubMed:15282281}.
-!- FUNCTION: May regulate voltage-gated sodium channels transport and
function. {ECO:0000269|PubMed:15282281}.
-!- FUNCTION: May also play a role in MAPK signaling.
{ECO:0000269|PubMed:15282281}.
-!- SUBUNIT: Interacts with SCN8A; may regulate SCN8A activity.
Interacts with SCN1A; may regulate SCN1A activity. Interacts with
SCN5A; the interaction is direct and may regulate SNC5A density at
membranes and function. May also interact with SCN2A and SCN11A.
Interacts with MAPK8IP2; may regulate the MAPK8IP2 scaffolding
activity. {ECO:0000269|PubMed:11378392,
ECO:0000269|PubMed:15282281, ECO:0000269|PubMed:19406745,
ECO:0000269|PubMed:21566136, ECO:0000269|PubMed:21817159}.
-!- SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000250}.
Cell projection, growth cone {ECO:0000250}. Cell projection,
dendrite {ECO:0000250}. Nucleus {ECO:0000269|PubMed:10644718}.
Cytoplasm {ECO:0000269|PubMed:10644718}. Note=Not secreted.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=FGF13A, 1A, hFHF-2(1S), FGF13S;
IsoId=Q92913-1; Sequence=Displayed;
Name=2; Synonyms=FGF13B, 1B, hFHF-2(1U), FGF13U;
IsoId=Q92913-2; Sequence=VSP_001529;
Name=3; Synonyms=hFHF-2(1Y+1V), FGF13YV;
IsoId=Q92913-3; Sequence=VSP_043461;
Name=4; Synonyms=hFHF-2(1Z+1Y), FGF13V;
IsoId=Q92913-4; Sequence=VSP_043460;
Name=5; Synonyms=hFHF-2(1X+1W+1V), FGF13Y;
IsoId=Q92913-5; Sequence=VSP_044129;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Predominantly
expressed in the nervous system. {ECO:0000269|PubMed:9232594}.
-!- PTM: May be phosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the heparin-binding growth factors family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fgf13/";
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EMBL; U66198; AAB18914.1; -; mRNA.
EMBL; AF100143; AAD16400.1; -; mRNA.
EMBL; AF100144; AAD16401.1; -; mRNA.
EMBL; AK297545; BAH12613.1; -; mRNA.
EMBL; AK303685; BAH14016.1; -; mRNA.
EMBL; AK316170; BAH14541.1; -; mRNA.
EMBL; AY672645; AAT70720.1; -; Genomic_DNA.
EMBL; AL031386; CAI95616.1; -; Genomic_DNA.
EMBL; Z82193; CAI95616.1; JOINED; Genomic_DNA.
EMBL; Z82193; CAI95677.1; -; Genomic_DNA.
EMBL; AL031386; CAI95677.1; JOINED; Genomic_DNA.
EMBL; Z81007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z82204; CAI42696.1; -; Genomic_DNA.
EMBL; Z83313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL023798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL023800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL034398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL034416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471150; EAW88435.1; -; Genomic_DNA.
EMBL; CH471150; EAW88438.1; -; Genomic_DNA.
EMBL; CH471150; EAW88440.1; -; Genomic_DNA.
EMBL; BC012347; AAH12347.1; -; mRNA.
EMBL; BC034340; AAH34340.1; -; mRNA.
EMBL; AF199612; AAF31399.1; -; mRNA.
EMBL; AF199613; AAF31400.1; -; mRNA.
CCDS; CCDS14664.1; -. [Q92913-2]
CCDS; CCDS14665.1; -. [Q92913-1]
CCDS; CCDS55511.1; -. [Q92913-5]
CCDS; CCDS55512.1; -. [Q92913-4]
CCDS; CCDS55513.1; -. [Q92913-3]
RefSeq; NP_001132970.1; NM_001139498.1. [Q92913-4]
RefSeq; NP_001132972.1; NM_001139500.1. [Q92913-3]
RefSeq; NP_001132973.1; NM_001139501.1. [Q92913-5]
RefSeq; NP_001132974.1; NM_001139502.1. [Q92913-5]
RefSeq; NP_004105.1; NM_004114.3. [Q92913-1]
RefSeq; NP_378668.1; NM_033642.2. [Q92913-2]
RefSeq; XP_005262456.1; XM_005262399.1. [Q92913-3]
UniGene; Hs.6540; -.
PDB; 3HBW; X-ray; 1.90 A; A/B=53-245.
PDB; 4DCK; X-ray; 2.20 A; C=63-245.
PDB; 4JPZ; X-ray; 3.02 A; A/E=60-245.
PDBsum; 3HBW; -.
PDBsum; 4DCK; -.
PDBsum; 4JPZ; -.
ProteinModelPortal; Q92913; -.
SMR; Q92913; -.
BioGrid; 108549; 4.
DIP; DIP-50447N; -.
IntAct; Q92913; 5.
STRING; 9606.ENSP00000359635; -.
iPTMnet; Q92913; -.
PhosphoSitePlus; Q92913; -.
BioMuta; FGF13; -.
DMDM; 2494461; -.
PaxDb; Q92913; -.
PeptideAtlas; Q92913; -.
PRIDE; Q92913; -.
DNASU; 2258; -.
Ensembl; ENST00000305414; ENSP00000303391; ENSG00000129682. [Q92913-2]
Ensembl; ENST00000315930; ENSP00000322390; ENSG00000129682. [Q92913-1]
Ensembl; ENST00000436198; ENSP00000396198; ENSG00000129682. [Q92913-3]
Ensembl; ENST00000441825; ENSP00000409276; ENSG00000129682. [Q92913-5]
Ensembl; ENST00000626909; ENSP00000487411; ENSG00000129682. [Q92913-4]
GeneID; 2258; -.
KEGG; hsa:2258; -.
UCSC; uc004fal.4; human. [Q92913-1]
CTD; 2258; -.
DisGeNET; 2258; -.
EuPathDB; HostDB:ENSG00000129682.13; -.
GeneCards; FGF13; -.
HGNC; HGNC:3670; FGF13.
HPA; HPA002809; -.
MIM; 300070; gene.
neXtProt; NX_Q92913; -.
OpenTargets; ENSG00000129682; -.
PharmGKB; PA28109; -.
eggNOG; KOG3885; Eukaryota.
eggNOG; ENOG4111IPH; LUCA.
GeneTree; ENSGT00760000118859; -.
HOGENOM; HOG000290676; -.
HOVERGEN; HBG007580; -.
InParanoid; Q92913; -.
KO; K04358; -.
OMA; KSNACRC; -.
OrthoDB; EOG091G0NAY; -.
PhylomeDB; Q92913; -.
TreeFam; TF317805; -.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
SIGNOR; Q92913; -.
ChiTaRS; FGF13; human.
EvolutionaryTrace; Q92913; -.
GeneWiki; FGF13; -.
GenomeRNAi; 2258; -.
PRO; PR:Q92913; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000129682; -.
CleanEx; HS_FGF13; -.
ExpressionAtlas; Q92913; baseline and differential.
Genevisible; Q92913; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IPI:MGI.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:InterPro.
GO; GO:0030175; C:filopodium; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; ISS:BHF-UCL.
GO; GO:0005874; C:microtubule; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
GO; GO:0008083; F:growth factor activity; TAS:ProtInc.
GO; GO:0044325; F:ion channel binding; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0030295; F:protein kinase activator activity; IGI:MGI.
GO; GO:0017080; F:sodium channel regulator activity; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0021795; P:cerebral cortex cell migration; ISS:UniProtKB.
GO; GO:0045200; P:establishment of neuroblast polarity; ISS:UniProtKB.
GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
GO; GO:0007612; P:learning; ISS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IDA:MGI.
GO; GO:0007613; P:memory; ISS:UniProtKB.
GO; GO:0046785; P:microtubule polymerization; ISS:UniProtKB.
GO; GO:0048671; P:negative regulation of collateral sprouting; ISS:UniProtKB.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; ISS:BHF-UCL.
GO; GO:1990834; P:response to odorant; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006814; P:sodium ion transport; ISS:BHF-UCL.
CDD; cd00058; FGF; 1.
InterPro; IPR028279; FGF13.
InterPro; IPR002209; Fibroblast_GF_fam.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR11486; PTHR11486; 1.
PANTHER; PTHR11486:SF77; PTHR11486:SF77; 1.
Pfam; PF00167; FGF; 1.
PRINTS; PR00263; HBGFFGF.
SMART; SM00442; FGF; 1.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS00247; HBGF_FGF; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection;
Complete proteome; Cytoplasm; Microtubule; Neurogenesis; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 245 Fibroblast growth factor 13.
/FTId=PRO_0000147607.
REGION 1 62 Mediates targeting to the nucleus.
{ECO:0000250}.
REGION 67 201 Mediates interaction with sodium
channels.
MOD_RES 208 208 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 62 MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKN
KLNVFSRVKLFGSKKRRRRRP -> MALLRKSYS (in
isoform 2).
{ECO:0000303|PubMed:10071193}.
/FTId=VSP_001529.
VAR_SEQ 1 62 MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKN
KLNVFSRVKLFGSKKRRRRRP -> MSGKVTKPKEEKDASK
VLDDAPPGTQEYIMLRQDSIQSAELKKKESPFRAKCHEIFC
CPLKQVHHKENTEPE (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043461.
VAR_SEQ 1 62 MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKN
KLNVFSRVKLFGSKKRRRRRP -> MSGKVTKPKEEKDASK
(in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043460.
VAR_SEQ 1 62 MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKN
KLNVFSRVKLFGSKKRRRRRP -> MLRQDSIQSAELKKKE
SPFRAKCHEIFCCPLKQVHHKENTEPE (in isoform
5). {ECO:0000305}.
/FTId=VSP_044129.
VARIANT 197 197 K -> Q (in dbSNP:rs17510270).
{ECO:0000269|Ref.4}.
/FTId=VAR_020945.
MUTAGEN 207 207 P->Q: Loss of interaction with SCN1A.
{ECO:0000269|PubMed:21566136}.
STRAND 66 75 {ECO:0000244|PDB:3HBW}.
TURN 76 78 {ECO:0000244|PDB:4DCK}.
STRAND 80 83 {ECO:0000244|PDB:3HBW}.
STRAND 89 93 {ECO:0000244|PDB:3HBW}.
HELIX 98 100 {ECO:0000244|PDB:3HBW}.
STRAND 102 108 {ECO:0000244|PDB:3HBW}.
STRAND 111 116 {ECO:0000244|PDB:3HBW}.
TURN 117 119 {ECO:0000244|PDB:3HBW}.
STRAND 122 125 {ECO:0000244|PDB:3HBW}.
STRAND 131 137 {ECO:0000244|PDB:3HBW}.
HELIX 139 141 {ECO:0000244|PDB:3HBW}.
STRAND 142 148 {ECO:0000244|PDB:3HBW}.
TURN 149 151 {ECO:0000244|PDB:3HBW}.
STRAND 152 161 {ECO:0000244|PDB:3HBW}.
TURN 163 165 {ECO:0000244|PDB:3HBW}.
STRAND 168 170 {ECO:0000244|PDB:3HBW}.
STRAND 177 179 {ECO:0000244|PDB:3HBW}.
HELIX 182 184 {ECO:0000244|PDB:3HBW}.
HELIX 190 192 {ECO:0000244|PDB:3HBW}.
STRAND 194 204 {ECO:0000244|PDB:3HBW}.
SEQUENCE 245 AA; 27564 MW; 30FB62C6B2669F29 CRC64;
MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR
RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK
LYLAMNSEGY LYTSELFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM
KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS
HNEST


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