FGF13_HUMAN
ID FGF13_HUMAN Reviewed; 245 AA.
AC Q92913; B1AK18; B7Z4M7; B7Z8N0; D3DWH4; O95830; Q9NZH9; Q9NZI0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Fibroblast growth factor 13 {ECO:0000305};
DE Short=FGF-13;
DE AltName: Full=Fibroblast growth factor homologous factor 2;
DE Short=FHF-2;
GN Name=FGF13 {ECO:0000312|HGNC:HGNC:3670}; Synonyms=FHF2;
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).
RC TISSUE=Retina;
RX PubMed=8790420; DOI=10.1073/pnas.93.18.9850;
RA Smallwood P.M., Munoz-Sanjuan I., Tong P., Macke J.P., Hendry S.H.,
RA Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.;
RT "Fibroblast growth factor (FGF) homologous factors: new members of the FGF
RT family implicated in nervous system development.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9850-9857(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=10071193; DOI=10.1007/s004390050910;
RA Gecz J., Baker E., Donnelly A., Ming J.E., McDonnald-McGinn D.M.,
RA Spinner N.B., Zackai E.H., Sutherland G.R., Mulley J.C.;
RT "Fibroblast growth factor homologous factor 2 (FHF2): gene structure,
RT expression and mapping to the Borjeson-Forssman-Lehmann syndrome region in
RT Xq26 delineated by a duplication breakpoint in a BFLS-like patient.";
RL Hum. Genet. 104:56-63(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-197.
RG NIEHS SNPs program;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Skin;
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 [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), ALTERNATIVE
RP SPLICING, AND SUBCELLULAR LOCATION.
RX PubMed=10644718; DOI=10.1074/jbc.275.4.2589;
RA Munoz-Sanjuan I., Smallwood P.M., Nathans J.;
RT "Isoform diversity among fibroblast growth factor homologous factors is
RT generated by alternative promoter usage and differential splicing.";
RL J. Biol. Chem. 275:2589-2597(2000).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=9232594; DOI=10.1016/s0925-4773(97)00042-7;
RA Hartung H., Feldman B., Lovec H., Coulier F., Birnbaum D., Goldfarb M.;
RT "Murine FGF-12 and FGF-13: expression in embryonic nervous system,
RT connective tissue and heart.";
RL Mech. Dev. 64:31-39(1997).
RN [10]
RP INTERACTION WITH MAPK8IP2.
RX PubMed=11378392; DOI=10.1016/s0960-9822(01)00232-9;
RA Schoorlemmer J., Goldfarb M.;
RT "Fibroblast growth factor homologous factors are intracellular signaling
RT proteins.";
RL Curr. Biol. 11:793-797(2001).
RN [11]
RP FUNCTION IN SCN8A REGULATION, AND INTERACTION WITH SCN8A.
RX PubMed=15282281; DOI=10.1523/jneurosci.1628-04.2004;
RA Wittmack E.K., Rush A.M., Craner M.J., Goldfarb M., Waxman S.G.,
RA Dib-Hajj S.D.;
RT "Fibroblast growth factor homologous factor 2B: association with Nav1.6 and
RT selective colocalization at nodes of Ranvier of dorsal root axons.";
RL J. Neurosci. 24:6765-6775(2004).
RN [12]
RP INTERACTION WITH SCN5A.
RX PubMed=21817159; DOI=10.1161/circresaha.111.247957;
RA Wang C., Hennessey J.A., Kirkton R.D., Wang C., Graham V., Puranam R.S.,
RA Rosenberg P.B., Bursac N., Pitt G.S.;
RT "Fibroblast growth factor homologous factor 13 regulates Na+ channels and
RT conduction velocity in murine hearts.";
RL Circ. Res. 109:775-782(2011).
RN [13]
RP INTERACTION WITH SCN1A; SCN2A; SCN5A AND SCN8A, AND MUTAGENESIS OF PRO-207.
RX PubMed=21566136; DOI=10.1074/jbc.m111.245803;
RA Wang C., Wang C., Hoch E.G., Pitt G.S.;
RT "Identification of novel interaction sites that determine specificity
RT between fibroblast growth factor homologous factors and voltage-gated
RT sodium channels.";
RL J. Biol. Chem. 286:24253-24263(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-245, AND INTERACTION WITH
RP SCN1A; SCN11A; SCN2A AND SCN5A.
RX PubMed=19406745; DOI=10.1074/jbc.m109.001842;
RA Goetz R., Dover K., Laezza F., Shtraizent N., Huang X., Tchetchik D.,
RA Eliseenkova A.V., Xu C.F., Neubert T.A., Ornitz D.M., Goldfarb M.,
RA Mohammadi M.;
RT "Crystal structure of a fibroblast growth factor homologous factor (FHF)
RT defines a conserved surface on FHFs for binding and modulation of voltage-
RT gated sodium channels.";
RL J. Biol. Chem. 284:17883-17896(2009).
RN [16]
RP VARIANTS DEE90 CYS-11; PRO-11 AND THR-14, CHARACTERIZATION OF VARIANTS
RP DEE90 CYS-11 AND THR-14, FUNCTION, AND INTERACTION WITH SCN8A.
RX PubMed=33245860; DOI=10.1016/j.ajhg.2020.10.017;
RG Genomics England Research Consortium;
RA Fry A.E., Marra C., Derrick A.V., Pickrell W.O., Higgins A.T.,
RA Te Water Naude J., McClatchey M.A., Davies S.J., Metcalfe K.A., Tan H.J.,
RA Mohanraj R., Avula S., Williams D., Brady L.I., Mesterman R.,
RA Tarnopolsky M.A., Zhang Y., Yang Y., Wang X., Rees M.I., Goldfarb M.,
RA Chung S.K.;
RT "Missense variants in the N-terminal domain of the A isoform of FHF2/FGF13
RT cause an X-linked developmental and epileptic encephalopathy.";
RL Am. J. Hum. Genet. 108:176-185(2021).
CC -!- FUNCTION: Microtubule-binding protein which directly binds tubulin and
CC is involved in both polymerization and stabilization of microtubules
CC (By similarity). Through its action on microtubules, may participate in
CC the refinement of axons by negatively regulating axonal and leading
CC processes branching (By similarity). Plays a crucial role in neuron
CC polarization and migration in the cerebral cortex and the hippocampus
CC (By similarity). Regulates voltage-gated sodium channels transport and
CC function (PubMed:15282281, PubMed:33245860). May also play a role in
CC MAPK signaling (By similarity). Required for the development of axonal
CC initial segment-targeting inhibitory GABAergic synapses made by
CC chandelier neurons (By similarity). {ECO:0000250|UniProtKB:P70377,
CC ECO:0000269|PubMed:15282281, ECO:0000269|PubMed:33245860}.
CC -!- SUBUNIT: Interacts with SCN8A; regulates SCN8A activity
CC (PubMed:15282281, PubMed:21566136, PubMed:33245860). Interacts with
CC SCN1A; may regulate SCN1A activity (PubMed:19406745, PubMed:21566136).
CC Interacts with SCN5A; the interaction is direct and may regulate SNC5A
CC density at membranes and function (PubMed:21817159). May also interact
CC with SCN2A and SCN11A (PubMed:19406745, PubMed:21566136). Interacts
CC with MAPK8IP2; may regulate the MAPK8IP2 scaffolding activity
CC (PubMed:11378392). {ECO:0000269|PubMed:11378392,
CC ECO:0000269|PubMed:15282281, ECO:0000269|PubMed:19406745,
CC ECO:0000269|PubMed:21566136, ECO:0000269|PubMed:21817159,
CC ECO:0000269|PubMed:33245860}.
CC -!- INTERACTION:
CC Q92913; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-1054883, EBI-742388;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:10644718}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:10644718}. Nucleus {ECO:0000269|PubMed:10644718}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000305|PubMed:10644718}. Nucleus {ECO:0000305|PubMed:10644718}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC {ECO:0000250|UniProtKB:P61329}. Nucleus {ECO:0000250|UniProtKB:P61329}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm
CC {ECO:0000250|UniProtKB:P61329}. Nucleus {ECO:0000250|UniProtKB:P61329}.
CC -!- SUBCELLULAR LOCATION: Cell projection, filopodium
CC {ECO:0000250|UniProtKB:P70377}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P70377}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P70377}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P70377}. Cytoplasm
CC {ECO:0000250|UniProtKB:P70377}. Note=Not secreted. Localizes to the
CC lateral membrane and intercalated disks of myocytes.
CC {ECO:0000250|UniProtKB:P70377}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=FGF13A, 1A, hFHF-2(1S) {ECO:0000303|PubMed:10644718},
CC FGF13S;
CC IsoId=Q92913-1; Sequence=Displayed;
CC Name=2; Synonyms=FGF13B, 1B, hFHF-2(1U) {ECO:0000303|PubMed:10644718},
CC FGF13U;
CC IsoId=Q92913-2; Sequence=VSP_001529;
CC Name=3; Synonyms=hFHF-2(1Y+1V) {ECO:0000303|PubMed:10644718}, FGF13YV;
CC IsoId=Q92913-3; Sequence=VSP_043461;
CC Name=4; Synonyms=hFHF-2(1Z+1Y) {ECO:0000303|PubMed:10644718}, FGF13V;
CC IsoId=Q92913-4; Sequence=VSP_043460;
CC Name=5; Synonyms=hFHF-2(1X+1W+1V) {ECO:0000303|PubMed:10644718},
CC FGF13Y;
CC IsoId=Q92913-5; Sequence=VSP_044129;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Predominantly expressed in
CC the nervous system. {ECO:0000269|PubMed:9232594}.
CC -!- PTM: May be phosphorylated. {ECO:0000250}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 90 (DEE90)
CC [MIM:301058]: A form of epileptic encephalopathy, a heterogeneous group
CC of early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE90 is an X-linked form characterized by onset of
CC refractory seizures in the first days or months of life.
CC {ECO:0000269|PubMed:33245860}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/fgf13/";
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DR EMBL; U66198; AAB18914.1; -; mRNA.
DR EMBL; AF100143; AAD16400.1; -; mRNA.
DR EMBL; AF100144; AAD16401.1; -; mRNA.
DR EMBL; AK297545; BAH12613.1; -; mRNA.
DR EMBL; AK303685; BAH14016.1; -; mRNA.
DR EMBL; AK316170; BAH14541.1; -; mRNA.
DR EMBL; AY672645; AAT70720.1; -; Genomic_DNA.
DR EMBL; AL031386; CAI95616.1; -; Genomic_DNA.
DR EMBL; Z82193; CAI95616.1; JOINED; Genomic_DNA.
DR EMBL; Z82193; CAI95677.1; -; Genomic_DNA.
DR EMBL; AL031386; CAI95677.1; JOINED; Genomic_DNA.
DR EMBL; Z81007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82204; CAI42696.1; -; Genomic_DNA.
DR EMBL; Z83313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL023798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL023800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL034398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL034416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471150; EAW88435.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88438.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88440.1; -; Genomic_DNA.
DR EMBL; BC012347; AAH12347.1; -; mRNA.
DR EMBL; BC034340; AAH34340.1; -; mRNA.
DR EMBL; AF199612; AAF31399.1; -; mRNA.
DR EMBL; AF199613; AAF31400.1; -; mRNA.
DR CCDS; CCDS14664.1; -. [Q92913-2]
DR CCDS; CCDS14665.1; -. [Q92913-1]
DR CCDS; CCDS55511.1; -. [Q92913-5]
DR CCDS; CCDS55512.1; -. [Q92913-4]
DR CCDS; CCDS55513.1; -. [Q92913-3]
DR RefSeq; NP_001132970.1; NM_001139498.1. [Q92913-4]
DR RefSeq; NP_001132972.1; NM_001139500.1. [Q92913-3]
DR RefSeq; NP_001132973.1; NM_001139501.1. [Q92913-5]
DR RefSeq; NP_001132974.1; NM_001139502.1. [Q92913-5]
DR RefSeq; NP_004105.1; NM_004114.3. [Q92913-1]
DR RefSeq; NP_378668.1; NM_033642.2. [Q92913-2]
DR RefSeq; XP_005262456.1; XM_005262399.1. [Q92913-3]
DR PDB; 3HBW; X-ray; 1.90 A; A/B=53-245.
DR PDB; 4DCK; X-ray; 2.20 A; C=63-245.
DR PDB; 4JPZ; X-ray; 3.02 A; A/E=60-245.
DR PDBsum; 3HBW; -.
DR PDBsum; 4DCK; -.
DR PDBsum; 4JPZ; -.
DR AlphaFoldDB; Q92913; -.
DR SMR; Q92913; -.
DR BioGRID; 108549; 178.
DR DIP; DIP-50447N; -.
DR IntAct; Q92913; 5.
DR STRING; 9606.ENSP00000322390; -.
DR iPTMnet; Q92913; -.
DR PhosphoSitePlus; Q92913; -.
DR BioMuta; FGF13; -.
DR DMDM; 2494461; -.
DR EPD; Q92913; -.
DR MassIVE; Q92913; -.
DR PaxDb; Q92913; -.
DR PeptideAtlas; Q92913; -.
DR PRIDE; Q92913; -.
DR ProteomicsDB; 12773; -.
DR ProteomicsDB; 75595; -. [Q92913-1]
DR ProteomicsDB; 75596; -. [Q92913-2]
DR ProteomicsDB; 75597; -. [Q92913-3]
DR ProteomicsDB; 75598; -. [Q92913-4]
DR ABCD; Q92913; 3 sequenced antibodies.
DR Antibodypedia; 468; 618 antibodies from 40 providers.
DR DNASU; 2258; -.
DR Ensembl; ENST00000305414.8; ENSP00000303391.4; ENSG00000129682.16. [Q92913-2]
DR Ensembl; ENST00000315930.11; ENSP00000322390.6; ENSG00000129682.16. [Q92913-1]
DR Ensembl; ENST00000436198.5; ENSP00000396198.2; ENSG00000129682.16. [Q92913-3]
DR Ensembl; ENST00000441825.8; ENSP00000409276.2; ENSG00000129682.16. [Q92913-5]
DR Ensembl; ENST00000626909.2; ENSP00000487411.1; ENSG00000129682.16. [Q92913-4]
DR GeneID; 2258; -.
DR KEGG; hsa:2258; -.
DR MANE-Select; ENST00000315930.11; ENSP00000322390.6; NM_004114.5; NP_004105.1.
DR UCSC; uc004fal.4; human. [Q92913-1]
DR CTD; 2258; -.
DR DisGeNET; 2258; -.
DR GeneCards; FGF13; -.
DR HGNC; HGNC:3670; FGF13.
DR HPA; ENSG00000129682; Tissue enhanced (parathyroid gland, skeletal muscle, tongue).
DR MalaCards; FGF13; -.
DR MIM; 300070; gene.
DR MIM; 301058; phenotype.
DR neXtProt; NX_Q92913; -.
DR OpenTargets; ENSG00000129682; -.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA28109; -.
DR VEuPathDB; HostDB:ENSG00000129682; -.
DR eggNOG; KOG3885; Eukaryota.
DR GeneTree; ENSGT00940000162313; -.
DR HOGENOM; CLU_081609_2_0_1; -.
DR InParanoid; Q92913; -.
DR OMA; LYPSEHF; -.
DR OrthoDB; 1192273at2759; -.
DR PhylomeDB; Q92913; -.
DR TreeFam; TF317805; -.
DR PathwayCommons; Q92913; -.
DR Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
DR SignaLink; Q92913; -.
DR SIGNOR; Q92913; -.
DR BioGRID-ORCS; 2258; 16 hits in 708 CRISPR screens.
DR ChiTaRS; FGF13; human.
DR EvolutionaryTrace; Q92913; -.
DR GeneWiki; FGF13; -.
DR GenomeRNAi; 2258; -.
DR Pharos; Q92913; Tbio.
DR PRO; PR:Q92913; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q92913; protein.
DR Bgee; ENSG00000129682; Expressed in endothelial cell and 194 other tissues.
DR ExpressionAtlas; Q92913; baseline and differential.
DR Genevisible; Q92913; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IPI:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:BHF-UCL.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; TAS:ProtInc.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; IGI:MGI.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0021795; P:cerebral cortex cell migration; ISS:UniProtKB.
DR GO; GO:0045200; P:establishment of neuroblast polarity; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IDA:MGI.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; ISS:BHF-UCL.
DR GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006814; P:sodium ion transport; ISS:BHF-UCL.
DR CDD; cd00058; FGF; 1.
DR DisProt; DP01404; -.
DR InterPro; IPR028279; FGF13.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR PANTHER; PTHR11486:SF145; PTHR11486:SF145; 1.
DR Pfam; PF00167; FGF; 1.
DR PRINTS; PR00263; HBGFFGF.
DR SMART; SM00442; FGF; 1.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00247; HBGF_FGF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Disease variant; Epilepsy; Intellectual disability; Membrane;
KW Microtubule; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..245
FT /note="Fibroblast growth factor 13"
FT /id="PRO_0000147607"
FT REGION 1..62
FT /note="Mediates targeting to the nucleus"
FT /evidence="ECO:0000250"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..201
FT /note="Mediates interaction with sodium channels"
FT REGION 213..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..62
FT /note="MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLF
FT GSKKRRRRRP -> MALLRKSYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10071193"
FT /id="VSP_001529"
FT VAR_SEQ 1..62
FT /note="MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLF
FT GSKKRRRRRP -> MSGKVTKPKEEKDASKVLDDAPPGTQEYIMLRQDSIQSAELKKKE
FT SPFRAKCHEIFCCPLKQVHHKENTEPE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043461"
FT VAR_SEQ 1..62
FT /note="MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLF
FT GSKKRRRRRP -> MSGKVTKPKEEKDASK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043460"
FT VAR_SEQ 1..62
FT /note="MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLF
FT GSKKRRRRRP -> MLRQDSIQSAELKKKESPFRAKCHEIFCCPLKQVHHKENTEPE
FT (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_044129"
FT VARIANT 11
FT /note="R -> C (in DEE90; loss of ability to induce SCN8A
FT long-term inactivation; no effect on pro-excitatory
FT properties; no effect on interaction with SCN8A)"
FT /evidence="ECO:0000269|PubMed:33245860"
FT /id="VAR_085434"
FT VARIANT 11
FT /note="R -> P (in DEE90; loss of ability to induce SCN8A
FT long-term inactivation; no effect on pro-excitatory
FT properties; no effect on interaction with SCN8A; unknown
FT pathological significance)"
FT /evidence="ECO:0000269|PubMed:33245860"
FT /id="VAR_085435"
FT VARIANT 14
FT /note="R -> T (in DEE90; loss of ability to induce SCN8A
FT long-term inactivation; no effect on pro-excitatory
FT properties; no effect on interaction with SCN8A)"
FT /evidence="ECO:0000269|PubMed:33245860"
FT /id="VAR_085436"
FT VARIANT 197
FT /note="K -> Q (in dbSNP:rs17510270)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020945"
FT MUTAGEN 207
FT /note="P->Q: Loss of interaction with SCN1A."
FT /evidence="ECO:0000269|PubMed:21566136"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:3HBW"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4DCK"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3HBW"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3HBW"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3HBW"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:3HBW"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:3HBW"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3HBW"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3HBW"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:3HBW"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:3HBW"
SQ 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
