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Q92913 (FGF13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceEvidence 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 projectionfilopodium By similarity. Cell projectiongrowth cone By similarity. Cell projectiondendrite By similarity. Nucleus Ref.8. Cytoplasm. Note: Not secreted By similarity. Ref.8

Isoform 1: Nucleusnucleolus 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 processNeurogenesis
   Cellular componentCell projection
Cytoplasm
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK 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

nervous system development

Traceable author statement Ref.1. Source: ProtInc

neuron migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from genetic interaction PubMed 12244047. Source: GOC

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: InterPro

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

neuron projection

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_functionbeta-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Fibroblast growth factor 13
PRO_0000147607

Regions

Region1 – 6262Mediates targeting to the nucleus By similarity
Region67 – 201135Mediates interaction with sodium channels

Natural variations

Alternative sequence1 – 6262MAAAI…RRRRP → MALLRKSYS in isoform 2.
VSP_001529
Alternative sequence1 – 6262MAAAI…RRRRP → MSGKVTKPKEEKDASKVLDD APPGTQEYIMLRQDSIQSAE LKKKESPFRAKCHEIFCCPL KQVHHKENTEPE in isoform 3.
VSP_043461
Alternative sequence1 – 6262MAAAI…RRRRP → MSGKVTKPKEEKDASK in isoform 4.
VSP_043460
Alternative sequence1 – 6262MAAAI…RRRRP → MLRQDSIQSAELKKKESPFR AKCHEIFCCPLKQVHHKENT EPE in isoform 5.
VSP_044129
Natural variant1971K → Q. Ref.4
Corresponds to variant rs17510270 [ dbSNP | Ensembl ].
VAR_020945

Experimental info

Mutagenesis2071P → Q: Loss of interaction with SCN1A. Ref.13

Secondary structure

.................................... 245
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (FGF13A) (1A) (hFHF-2(1S)) (FGF13S) [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 30FB62C6B2669F29

FASTA24527,564
        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 

« Hide

Isoform 2 (FGF13B) (1B) (hFHF-2(1U)) (FGF13U) [UniParc].

Checksum: 1C5B15BB67B2F232
Show »

FASTA19221,581
Isoform 3 (hFHF-2(1Y+1V)) (FGF13YV) [UniParc].

Checksum: ADAB4C72927597DC
Show »

FASTA25528,752
Isoform 4 (hFHF-2(1Z+1Y)) (FGF13V) [UniParc].

Checksum: D73D2E43AAA1414F
Show »

FASTA19922,275
Isoform 5 (hFHF-2(1X+1W+1V)) (FGF13Y) [UniParc].

Checksum: 59444607415A4FD0
Show »

FASTA22625,607

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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

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.
RefSeqNP_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.
XP_005262456.1. XM_005262399.1.
UniGeneHs.6540.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HBWX-ray1.90A/B53-245[»]
4DCKX-ray2.20C63-245[»]
ProteinModelPortalQ92913.
SMRQ92913. Positions 64-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108549. 3 interactions.
DIPDIP-50447N.
IntActQ92913. 1 interaction.
STRING9606.ENSP00000322390.

PTM databases

PhosphoSiteQ92913.

Polymorphism databases

DMDM2494461.

Proteomic databases

PaxDbQ92913.
PRIDEQ92913.

Protocols and materials databases

DNASU2258.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305414; ENSP00000303391; ENSG00000129682. [Q92913-2]
ENST00000315930; ENSP00000322390; ENSG00000129682. [Q92913-1]
ENST00000370603; ENSP00000359635; ENSG00000129682. [Q92913-3]
ENST00000421460; ENSP00000388688; ENSG00000129682.
ENST00000441825; ENSP00000409276; ENSG00000129682. [Q92913-5]
ENST00000541469; ENSP00000437903; ENSG00000129682. [Q92913-4]
GeneID2258.
KEGGhsa:2258.
UCSCuc004fam.3. human. [Q92913-1]
uc004fan.3. human. [Q92913-2]
uc004faq.3. human. [Q92913-3]
uc004far.3. human. [Q92913-5]
uc011mwk.2. human. [Q92913-4]

Organism-specific databases

CTD2258.
GeneCardsGC0XM137713.
HGNCHGNC:3670. FGF13.
HPAHPA002809.
MIM300070. gene.
neXtProtNX_Q92913.
PharmGKBPA28109.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308177.
HOGENOMHOG000290676.
HOVERGENHBG007580.
KOK04358.
OMAKSNACRC.
OrthoDBEOG7J447D.
PhylomeDBQ92913.
TreeFamTF317805.

Gene expression databases

ArrayExpressQ92913.
BgeeQ92913.
CleanExHS_FGF13.
GenevestigatorQ92913.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR028279. FGF13.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF16. PTHR11486:SF16. 1 hit.
PfamPF00167. FGF. 1 hit.
[Graphical view]
PRINTSPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFGF13. human.
EvolutionaryTraceQ92913.
GeneWikiFGF13.
GenomeRNAi2258.
NextBio9149.
PROQ92913.
SOURCESearch...

Entry information

Entry nameFGF13_HUMAN
AccessionPrimary (citable) accession number: Q92913
Secondary accession number(s): B1AK18 expand/collapse secondary AC list , B7Z4M7, B7Z8N0, D3DWH4, O95830, Q9NZH9, Q9NZI0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM