Q92913 (FGF13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibroblast growth factor 13
Short name=FGF-13

Alternative name(s):
Fibroblast growth factor homologous factor 2
Short name=FHF-2

Gene names

Name:	FGF13
Synonyms:	FHF2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	245 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.11 May regulate voltage-gated sodium channels transport and function. Ref.11 May also play a role in MAPK signaling. Ref.11
Subunit structure	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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Subcellular location	Cell projection › filopodium By similarity. Cell projection › growth cone By similarity. Cell projection › dendrite By similarity. Nucleus Ref.8. Cytoplasm. Note: Not secreted By similarity. Ref.8 Isoform 1: Nucleus › nucleolus Ref.8. Isoform 2: Cytoplasm. Nucleus Ref.8.
Tissue specificity	Ubiquitously expressed. Predominantly expressed in the nervous system. Ref.9
Post-translational modification	May be phosphorylated By similarity.
Sequence similarities	Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
Biological process	Neurogenesis
Cellular component	Cell projection Cytoplasm Microtubule Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from direct assay PubMed 12244047. Source: MGI cell-cell signaling Traceable author statement Ref.1. Source: ProtInc cerebral cortex cell migration Inferred from sequence or structural similarity. Source: UniProtKB establishment of neuroblast polarity Inferred from sequence or structural similarity. Source: UniProtKB hippocampus development Inferred from sequence or structural similarity. Source: UniProtKB learning Inferred from sequence or structural similarity. Source: UniProtKB memory Inferred from sequence or structural similarity. Source: UniProtKB microtubule polymerization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of collateral sprouting Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of microtubule depolymerization Inferred from sequence or structural similarity. Source: UniProtKB neuron migration Inferred from sequence or structural similarity. Source: UniProtKB protein localization to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	axon Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from physical interaction PubMed 12244047. Source: MGI dendrite Inferred from sequence or structural similarity. Source: UniProtKB filopodium Inferred from sequence or structural similarity. Source: UniProtKB growth cone Inferred from sequence or structural similarity. Source: UniProtKB intercalated disc Inferred from sequence or structural similarity. Source: UniProtKB microtubule Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.1. Source: MGI plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	beta-tubulin binding Inferred from sequence or structural similarity. Source: UniProtKB growth factor activity Traceable author statement Ref.1. Source: ProtInc ion channel binding Inferred from sequence or structural similarity. Source: UniProtKB microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB protein kinase activator activity Inferred from genetic interaction PubMed 12244047. Source: MGI sodium channel regulator activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92913-1)

Also known as: FGF13A; 1A; hFHF-2(1S); FGF13S;

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: Q92913-2)

Also known as: FGF13B; 1B; hFHF-2(1U); FGF13U;

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLFGSKKRRRRRP → MALLRKSYS

Isoform 3 (identifier: Q92913-3)

Also known as: hFHF-2(1Y+1V); FGF13YV;

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MAAAIASSLI...GSKKRRRRRP → MSGKVTKPKE...VHHKENTEPE

Isoform 4 (identifier: Q92913-4)

Also known as: hFHF-2(1Z+1Y); FGF13V;

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MAAAIASSLI...GSKKRRRRRP → MSGKVTKPKEEKDASK

Isoform 5 (identifier: Q92913-5)

Also known as: hFHF-2(1X+1W+1V); FGF13Y;

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MAAAIASSLI...GSKKRRRRRP → MLRQDSIQSA...VHHKENTEPE

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 245

245

Fibroblast growth factor 13

PRO_0000147607

Regions

Region

1 – 62

62

Mediates targeting to the nucleus By similarity

Region

67 – 201

135

Mediates interaction with sodium channels

Natural variations

Alternative sequence

1 – 62

62

MAAAI…RRRRP → MALLRKSYS in isoform 2.

VSP_001529

Alternative sequence

1 – 62

62

MAAAI…RRRRP → MSGKVTKPKEEKDASKVLDD APPGTQEYIMLRQDSIQSAE LKKKESPFRAKCHEIFCCPL KQVHHKENTEPE in isoform 3.

VSP_043461

Alternative sequence

1 – 62

62

MAAAI…RRRRP → MSGKVTKPKEEKDASK in isoform 4.

VSP_043460

Alternative sequence

1 – 62

62

MAAAI…RRRRP → MLRQDSIQSAELKKKESPFR AKCHEIFCCPLKQVHHKENT EPE in isoform 5.

VSP_044129

Natural variant

197

1

K → Q. Ref.4
Corresponds to variant rs17510270 [ dbSNP | Ensembl ].

VAR_020945

Experimental info

Mutagenesis

207

1

P → Q: Loss of interaction with SCN1A. Ref.13

Secondary structure

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245

Helix Strand Turn

Details...

Beta strand

66 – 75

10

Turn

76 – 78

3

Beta strand

80 – 83

4

Beta strand

89 – 93

5

Helix

98 – 100

3

Beta strand

102 – 108

7

Beta strand

111 – 116

6

Turn

117 – 119

3

Beta strand

122 – 125

4

Beta strand

131 – 137

7

Helix

139 – 141

3

Beta strand

142 – 148

7

Turn

149 – 151

3

Beta strand

152 – 161

10

Turn

163 – 165

3

Beta strand

168 – 170

3

Beta strand

177 – 179

3

Helix

182 – 184

3

Helix

190 – 192

3

Beta strand

194 – 204

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (FGF13A) (1A) (hFHF-2(1S)) (FGF13S) [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 30FB62C6B2669F29	FASTA	245	27,564
	10 20 30 40 50 60 MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR 70 80 90 100 110 120 RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK 130 140 150 160 170 180 LYLAMNSEGY LYTSELFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM 190 200 210 220 230 240 KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS HNEST
	Isoform 2 (FGF13B) (1B) (hFHF-2(1U)) (FGF13U) [UniParc]. Checksum: 1C5B15BB67B2F232	FASTA	192	21,581
	10 20 30 40 50 60 MALLRKSYSE PQLKGIVTKL YSRQGYHLQL QADGTIDGTK DEDSTYTLFN LIPVGLRVVA 70 80 90 100 110 120 IQGVQTKLYL AMNSEGYLYT SELFTPECKF KESVFENYYV TYSSMIYRQQ QSGRGWYLGL 130 140 150 160 170 180 NKEGEIMKGN HVKKNKPAAH FLPKPLKVAM YKEPSLHDLT EFSRSGSGTP TKSRSVSGVL 190 NGGKSMSHNE ST
	Isoform 3 (hFHF-2(1Y+1V)) (FGF13YV) [UniParc]. Checksum: ADAB4C72927597DC	FASTA	255	28,752
	10 20 30 40 50 60 MSGKVTKPKE EKDASKVLDD APPGTQEYIM LRQDSIQSAE LKKKESPFRA KCHEIFCCPL 70 80 90 100 110 120 KQVHHKENTE PEEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR 130 140 150 160 170 180 VVAIQGVQTK LYLAMNSEGY LYTSELFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY 190 200 210 220 230 240 LGLNKEGEIM KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS 250 GVLNGGKSMS HNEST
	Isoform 4 (hFHF-2(1Z+1Y)) (FGF13V) [UniParc]. Checksum: D73D2E43AAA1414F	FASTA	199	22,275
	10 20 30 40 50 60 MSGKVTKPKE EKDASKEPQL KGIVTKLYSR QGYHLQLQAD GTIDGTKDED STYTLFNLIP 70 80 90 100 110 120 VGLRVVAIQG VQTKLYLAMN SEGYLYTSEL FTPECKFKES VFENYYVTYS SMIYRQQQSG 130 140 150 160 170 180 RGWYLGLNKE GEIMKGNHVK KNKPAAHFLP KPLKVAMYKE PSLHDLTEFS RSGSGTPTKS 190 RSVSGVLNGG KSMSHNEST
	Isoform 5 (hFHF-2(1X+1W+1V)) (FGF13Y) [UniParc]. Checksum: 59444607415A4FD0	FASTA	226	25,607
	10 20 30 40 50 60 MLRQDSIQSA ELKKKESPFR AKCHEIFCCP LKQVHHKENT EPEEPQLKGI VTKLYSRQGY 70 80 90 100 110 120 HLQLQADGTI DGTKDEDSTY TLFNLIPVGL RVVAIQGVQT KLYLAMNSEG YLYTSELFTP 130 140 150 160 170 180 ECKFKESVFE NYYVTYSSMI YRQQQSGRGW YLGLNKEGEI MKGNHVKKNK PAAHFLPKPL 190 200 210 220 KVAMYKEPSL HDLTEFSRSG SGTPTKSRSV SGVLNGGKSM SHNEST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fibroblast growth factor (FGF) homologous factors: new members of the FGF family implicated in nervous system development." 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. Proc. Natl. Acad. Sci. U.S.A. 93:9850-9857(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Retina.
[2]	"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." 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. Hum. Genet. 104:56-63(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Brain.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). Tissue: Brain and Kidney.
[4]	NIEHS SNPs program Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-197.
[5]	"The DNA sequence of the human X chromosome." 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. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung and Skin.
[8]	"Isoform diversity among fibroblast growth factor homologous factors is generated by alternative promoter usage and differential splicing." Munoz-Sanjuan I., Smallwood P.M., Nathans J. J. Biol. Chem. 275:2589-2597(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
[9]	"Murine FGF-12 and FGF-13: expression in embryonic nervous system, connective tissue and heart." Hartung H., Feldman B., Lovec H., Coulier F., Birnbaum D., Goldfarb M. Mech. Dev. 64:31-39(1997) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"Fibroblast growth factor homologous factors are intracellular signaling proteins." Schoorlemmer J., Goldfarb M. Curr. Biol. 11:793-797(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPK8IP2.
[11]	"Fibroblast growth factor homologous factor 2B: association with Nav1.6 and selective colocalization at nodes of Ranvier of dorsal root axons." Wittmack E.K., Rush A.M., Craner M.J., Goldfarb M., Waxman S.G., Dib-Hajj S.D. J. Neurosci. 24:6765-6775(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN SCN8A REGULATION, INTERACTION WITH SCN8A.
[12]	"Fibroblast growth factor homologous factor 13 regulates Na+ channels and conduction velocity in murine hearts." Wang C., Hennessey J.A., Kirkton R.D., Wang C., Graham V., Puranam R.S., Rosenberg P.B., Bursac N., Pitt G.S. Circ. Res. 109:775-782(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCN5A.
[13]	"Identification of novel interaction sites that determine specificity between fibroblast growth factor homologous factors and voltage-gated sodium channels." Wang C., Wang C., Hoch E.G., Pitt G.S. J. Biol. Chem. 286:24253-24263(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCN1A; SCN2A; SCN5A AND SCN8A, MUTAGENESIS OF PRO-207.
[14]	"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." 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. J. Biol. Chem. 284:17883-17896(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-245, INTERACTION WITH SCN1A; SCN11A; SCN2A AND SCN5A.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U66198 mRNA. Translation: AAB18914.1.
AF100143 mRNA. Translation: AAD16400.1.
AF100144 mRNA. Translation: AAD16401.1.
AK297545 mRNA. Translation: BAH12613.1.
AK303685 mRNA. Translation: BAH14016.1.
AK316170 mRNA. Translation: BAH14541.1.
AY672645 Genomic DNA. Translation: AAT70720.1.
AL031386, Z82193 Genomic DNA. Translation: CAI95616.1.
Z82193, AL031386 Genomic DNA. Translation: CAI95677.1.
Z81007 Genomic DNA. No translation available.
Z82204 Genomic DNA. Translation: CAI42696.1.
Z83313 Genomic DNA. No translation available.
AL023798 Genomic DNA. No translation available.
AL023800 Genomic DNA. No translation available.
AL034398 Genomic DNA. No translation available.
AL034416 Genomic DNA. No translation available.
CH471150 Genomic DNA. Translation: EAW88435.1.
CH471150 Genomic DNA. Translation: EAW88438.1.
CH471150 Genomic DNA. Translation: EAW88440.1.
BC012347 mRNA. Translation: AAH12347.1.
BC034340 mRNA. Translation: AAH34340.1.
AF199612 mRNA. Translation: AAF31399.1.
AF199613 mRNA. Translation: AAF31400.1.

IPI

IPI00024251.
IPI00066574.
IPI00552653.
IPI00915279.
IPI00915358.

RefSeq

NP_001132970.1. NM_001139498.1.
NP_001132972.1. NM_001139500.1.
NP_001132973.1. NM_001139501.1.
NP_001132974.1. NM_001139502.1.
NP_004105.1. NM_004114.3.
NP_378668.1. NM_033642.2.

UniGene

Hs.6540.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HBW	X-ray	1.90	A/B	53-245	[»]
4DCK	X-ray	2.20	C	63-245	[»]

ProteinModelPortal

Q92913.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-50447N.

IntAct

Q92913. 1 interaction.

STRING

9606.ENSP00000322390.

PTM databases

PhosphoSite

Q92913.

Polymorphism databases

DMDM

2494461.

Proteomic databases

PaxDb

Q92913.

PRIDE

Q92913.

Protocols and materials databases

DNASU

2258.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000305414; ENSP00000303391; ENSG00000129682.
ENST00000315930; ENSP00000322390; ENSG00000129682.
ENST00000370603; ENSP00000359635; ENSG00000129682.
ENST00000421460; ENSP00000388688; ENSG00000129682.
ENST00000441825; ENSP00000409276; ENSG00000129682.
ENST00000541469; ENSP00000437903; ENSG00000129682.

GeneID

2258.

KEGG

hsa:2258.

UCSC

uc004fam.3. human.
uc004fan.3. human.

Organism-specific databases

CTD

2258.

GeneCards

GC0XM137713.

HGNC

HGNC:3670. FGF13.

HPA

HPA002809.

MIM

300070. gene.

neXtProt

NX_Q92913.

PharmGKB

PA28109.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG308177.

HOGENOM

HOG000290676.

HOVERGEN

HBG007580.

KO

K04358.

OMA

EEDSTYT.

OrthoDB

EOG4VQ9Q2.

PhylomeDB

Q92913.

Gene expression databases

ArrayExpress

Q92913.

Bgee

Q92913.

CleanEx

HS_FGF13.

Genevestigator

Q92913.

GermOnline

ENSG00000129682. Homo sapiens.

Family and domain databases

InterPro

IPR008996. Cytokine_IL1-like.
IPR002209. GF_heparin-bd.
IPR002348. IL1_HBGF.
[Graphical view]

PANTHER

PTHR11486. PTHR11486. 1 hit.

Pfam

PF00167. FGF. 1 hit.
[Graphical view]

PRINTS

PR00263. HBGFFGF.
PR00262. IL1HBGF.

SMART

SM00442. FGF. 1 hit.
[Graphical view]

SUPFAM

SSF50353. Cytok_IL1_like. 1 hit.

PROSITE

PS00247. HBGF_FGF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FGF13. human.

EvolutionaryTrace

Q92913.

GenomeRNAi

2258.

NextBio

9149.

SOURCE

Search...

Entry information

Entry name

FGF13_HUMAN

Accession

Primary (citable) accession number: Q92913
Secondary accession number(s): B1AK18 , B7Z4M7, B7Z8N0, D3DWH4, O95830, Q9NZH9, Q9NZI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.