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Q92913

- FGF13_HUMAN

UniProt

Q92913 - FGF13_HUMAN

Protein

Fibroblast growth factor 13

Gene

FGF13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    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.1 Publication
    May regulate voltage-gated sodium channels transport and function.1 Publication
    May also play a role in MAPK signaling.1 Publication

    GO - Molecular functioni

    1. beta-tubulin binding Source: UniProtKB
    2. growth factor activity Source: ProtInc
    3. ion channel binding Source: UniProtKB
    4. microtubule binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein kinase activator activity Source: MGI
    7. sodium channel regulator activity Source: UniProtKB

    GO - Biological processi

    1. cell-cell signaling Source: ProtInc
    2. cerebral cortex cell migration Source: UniProtKB
    3. establishment of neuroblast polarity Source: UniProtKB
    4. hippocampus development Source: UniProtKB
    5. learning Source: UniProtKB
    6. MAPK cascade Source: MGI
    7. memory Source: UniProtKB
    8. microtubule polymerization Source: UniProtKB
    9. negative regulation of collateral sprouting Source: UniProtKB
    10. negative regulation of microtubule depolymerization Source: UniProtKB
    11. nervous system development Source: ProtInc
    12. neuron migration Source: UniProtKB
    13. positive regulation of protein kinase activity Source: GOC
    14. protein localization to plasma membrane Source: UniProtKB
    15. signal transduction Source: ProtInc

    Keywords - Biological processi

    Neurogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor 13
    Short name:
    FGF-13
    Alternative name(s):
    Fibroblast growth factor homologous factor 2
    Short name:
    FHF-2
    Gene namesi
    Name:FGF13
    Synonyms:FHF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3670. FGF13.

    Subcellular locationi

    Cell projectionfilopodium By similarity. Cell projectiongrowth cone By similarity. Cell projectiondendrite By similarity. Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Not secreted.By similarity

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. cytoplasm Source: HPA
    3. dendrite Source: UniProtKB
    4. extracellular region Source: InterPro
    5. filopodium Source: UniProtKB
    6. growth cone Source: UniProtKB
    7. intercalated disc Source: UniProtKB
    8. microtubule Source: UniProtKB
    9. neuron projection Source: UniProtKB
    10. nucleolus Source: UniProtKB-SubCell
    11. nucleus Source: MGI
    12. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Microtubule, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi207 – 2071P → Q: Loss of interaction with SCN1A. 1 Publication

    Organism-specific databases

    PharmGKBiPA28109.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 245245Fibroblast growth factor 13PRO_0000147607Add
    BLAST

    Post-translational modificationi

    May be phosphorylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ92913.
    PRIDEiQ92913.

    PTM databases

    PhosphoSiteiQ92913.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Predominantly expressed in the nervous system.1 Publication

    Gene expression databases

    ArrayExpressiQ92913.
    BgeeiQ92913.
    CleanExiHS_FGF13.
    GenevestigatoriQ92913.

    Organism-specific databases

    HPAiHPA002809.

    Interactioni

    Subunit structurei

    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.5 Publications

    Protein-protein interaction databases

    BioGridi108549. 3 interactions.
    DIPiDIP-50447N.
    IntActiQ92913. 1 interaction.
    STRINGi9606.ENSP00000322390.

    Structurei

    Secondary structure

    1
    245
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi66 – 7510
    Turni76 – 783
    Beta strandi80 – 834
    Beta strandi89 – 935
    Helixi98 – 1003
    Beta strandi102 – 1087
    Beta strandi111 – 1166
    Turni117 – 1193
    Beta strandi122 – 1254
    Beta strandi131 – 1377
    Helixi139 – 1413
    Beta strandi142 – 1487
    Turni149 – 1513
    Beta strandi152 – 16110
    Turni163 – 1653
    Beta strandi168 – 1703
    Beta strandi177 – 1793
    Helixi182 – 1843
    Helixi190 – 1923
    Beta strandi194 – 20411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HBWX-ray1.90A/B53-245[»]
    4DCKX-ray2.20C63-245[»]
    4JPZX-ray3.02A/E60-245[»]
    ProteinModelPortaliQ92913.
    SMRiQ92913. Positions 64-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92913.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 6262Mediates targeting to the nucleusBy similarityAdd
    BLAST
    Regioni67 – 201135Mediates interaction with sodium channelsAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG308177.
    HOGENOMiHOG000290676.
    HOVERGENiHBG007580.
    KOiK04358.
    OMAiKSNACRC.
    OrthoDBiEOG7J447D.
    PhylomeDBiQ92913.
    TreeFamiTF317805.

    Family and domain databases

    InterProiIPR008996. Cytokine_IL1-like.
    IPR028279. FGF13.
    IPR002209. Fibroblast_GF_fam.
    IPR028142. IL-1_fam/FGF_fam.
    [Graphical view]
    PANTHERiPTHR11486. PTHR11486. 1 hit.
    PTHR11486:SF77. PTHR11486:SF77. 1 hit.
    PfamiPF00167. FGF. 1 hit.
    [Graphical view]
    PRINTSiPR00263. HBGFFGF.
    PR00262. IL1HBGF.
    SMARTiSM00442. FGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF50353. SSF50353. 1 hit.
    PROSITEiPS00247. HBGF_FGF. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92913-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK    50
    LFGSKKRRRR RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT 100
    LFNLIPVGLR VVAIQGVQTK LYLAMNSEGY LYTSELFTPE CKFKESVFEN 150
    YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM KGNHVKKNKP AAHFLPKPLK 200
    VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS HNEST 245
    Length:245
    Mass (Da):27,564
    Last modified:February 1, 1997 - v1
    Checksum:i30FB62C6B2669F29
    GO
    Isoform 2 (identifier: Q92913-2) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:192
    Mass (Da):21,581
    Checksum:i1C5B15BB67B2F232
    GO
    Isoform 3 (identifier: Q92913-3) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:255
    Mass (Da):28,752
    Checksum:iADAB4C72927597DC
    GO
    Isoform 4 (identifier: Q92913-4) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:199
    Mass (Da):22,275
    Checksum:iD73D2E43AAA1414F
    GO
    Isoform 5 (identifier: Q92913-5) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:226
    Mass (Da):25,607
    Checksum:i59444607415A4FD0
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti197 – 1971K → Q.1 Publication
    Corresponds to variant rs17510270 [ dbSNP | Ensembl ].
    VAR_020945

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6262MAAAI…RRRRP → MALLRKSYS in isoform 2. 1 PublicationVSP_001529Add
    BLAST
    Alternative sequencei1 – 6262MAAAI…RRRRP → MSGKVTKPKEEKDASKVLDD APPGTQEYIMLRQDSIQSAE LKKKESPFRAKCHEIFCCPL KQVHHKENTEPE in isoform 3. 1 PublicationVSP_043461Add
    BLAST
    Alternative sequencei1 – 6262MAAAI…RRRRP → MSGKVTKPKEEKDASK in isoform 4. 1 PublicationVSP_043460Add
    BLAST
    Alternative sequencei1 – 6262MAAAI…RRRRP → MLRQDSIQSAELKKKESPFR AKCHEIFCCPLKQVHHKENT EPE in isoform 5. CuratedVSP_044129Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14664.1. [Q92913-2]
    CCDS14665.1. [Q92913-1]
    CCDS55511.1. [Q92913-5]
    CCDS55512.1. [Q92913-4]
    CCDS55513.1. [Q92913-3]
    RefSeqiNP_001132970.1. NM_001139498.1. [Q92913-4]
    NP_001132972.1. NM_001139500.1. [Q92913-3]
    NP_001132973.1. NM_001139501.1. [Q92913-5]
    NP_001132974.1. NM_001139502.1. [Q92913-5]
    NP_004105.1. NM_004114.3. [Q92913-1]
    NP_378668.1. NM_033642.2. [Q92913-2]
    XP_005262456.1. XM_005262399.1. [Q92913-3]
    UniGeneiHs.6540.

    Genome annotation databases

    EnsembliENST00000305414; ENSP00000303391; ENSG00000129682. [Q92913-2]
    ENST00000315930; ENSP00000322390; ENSG00000129682. [Q92913-1]
    ENST00000421460; ENSP00000388688; ENSG00000129682.
    ENST00000441825; ENSP00000409276; ENSG00000129682. [Q92913-5]
    GeneIDi2258.
    KEGGihsa:2258.
    UCSCiuc004fam.3. human. [Q92913-1]
    uc004fan.3. human. [Q92913-2]
    uc004faq.3. human. [Q92913-3]
    uc004far.3. human. [Q92913-5]
    uc011mwk.2. human. [Q92913-4]

    Polymorphism databases

    DMDMi2494461.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14664.1. [Q92913-2 ]
    CCDS14665.1. [Q92913-1 ]
    CCDS55511.1. [Q92913-5 ]
    CCDS55512.1. [Q92913-4 ]
    CCDS55513.1. [Q92913-3 ]
    RefSeqi NP_001132970.1. NM_001139498.1. [Q92913-4 ]
    NP_001132972.1. NM_001139500.1. [Q92913-3 ]
    NP_001132973.1. NM_001139501.1. [Q92913-5 ]
    NP_001132974.1. NM_001139502.1. [Q92913-5 ]
    NP_004105.1. NM_004114.3. [Q92913-1 ]
    NP_378668.1. NM_033642.2. [Q92913-2 ]
    XP_005262456.1. XM_005262399.1. [Q92913-3 ]
    UniGenei Hs.6540.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HBW X-ray 1.90 A/B 53-245 [» ]
    4DCK X-ray 2.20 C 63-245 [» ]
    4JPZ X-ray 3.02 A/E 60-245 [» ]
    ProteinModelPortali Q92913.
    SMRi Q92913. Positions 64-212.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108549. 3 interactions.
    DIPi DIP-50447N.
    IntActi Q92913. 1 interaction.
    STRINGi 9606.ENSP00000322390.

    PTM databases

    PhosphoSitei Q92913.

    Polymorphism databases

    DMDMi 2494461.

    Proteomic databases

    PaxDbi Q92913.
    PRIDEi Q92913.

    Protocols and materials databases

    DNASUi 2258.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305414 ; ENSP00000303391 ; ENSG00000129682 . [Q92913-2 ]
    ENST00000315930 ; ENSP00000322390 ; ENSG00000129682 . [Q92913-1 ]
    ENST00000421460 ; ENSP00000388688 ; ENSG00000129682 .
    ENST00000441825 ; ENSP00000409276 ; ENSG00000129682 . [Q92913-5 ]
    GeneIDi 2258.
    KEGGi hsa:2258.
    UCSCi uc004fam.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

    CTDi 2258.
    GeneCardsi GC0XM137713.
    HGNCi HGNC:3670. FGF13.
    HPAi HPA002809.
    MIMi 300070. gene.
    neXtProti NX_Q92913.
    PharmGKBi PA28109.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG308177.
    HOGENOMi HOG000290676.
    HOVERGENi HBG007580.
    KOi K04358.
    OMAi KSNACRC.
    OrthoDBi EOG7J447D.
    PhylomeDBi Q92913.
    TreeFami TF317805.

    Miscellaneous databases

    ChiTaRSi FGF13. human.
    EvolutionaryTracei Q92913.
    GeneWikii FGF13.
    GenomeRNAii 2258.
    NextBioi 9149.
    PROi Q92913.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92913.
    Bgeei Q92913.
    CleanExi HS_FGF13.
    Genevestigatori Q92913.

    Family and domain databases

    InterProi IPR008996. Cytokine_IL1-like.
    IPR028279. FGF13.
    IPR002209. Fibroblast_GF_fam.
    IPR028142. IL-1_fam/FGF_fam.
    [Graphical view ]
    PANTHERi PTHR11486. PTHR11486. 1 hit.
    PTHR11486:SF77. PTHR11486:SF77. 1 hit.
    Pfami PF00167. FGF. 1 hit.
    [Graphical view ]
    PRINTSi PR00263. HBGFFGF.
    PR00262. IL1HBGF.
    SMARTi SM00442. FGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50353. SSF50353. 1 hit.
    PROSITEi PS00247. HBGF_FGF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiFGF13_HUMAN
    AccessioniPrimary (citable) accession number: Q92913
    Secondary accession number(s): B1AK18
    , B7Z4M7, B7Z8N0, D3DWH4, O95830, Q9NZH9, Q9NZI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3