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Protein

Fibroblast growth factor 21

Gene

Fgf21

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Activity probably requires the presence of KLB.1 Publication

GO - Biological processi

  1. positive regulation of cell proliferation Source: MGI
  2. positive regulation of ERK1 and ERK2 cascade Source: MGI
  3. positive regulation of glucose import Source: MGI
  4. positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor 21
Short name:
FGF-21
Gene namesi
Name:Fgf21
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1861377. Fgf21.

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 210182Fibroblast growth factor 21PRO_0000008995Add
BLAST

Proteomic databases

PRIDEiQ9JJN1.

Expressioni

Tissue specificityi

Most abundantly expressed in the liver, also expressed in the thymus at lower levels.1 Publication

Gene expression databases

BgeeiQ9JJN1.
CleanExiMM_FGF21.
GenevestigatoriQ9JJN1.

Interactioni

Subunit structurei

Interacts (via C-terminus) with KLB; this interaction is direct. Interacts with FGFR4 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-60919N.
STRINGi10090.ENSMUSP00000033099.

Structurei

3D structure databases

ProteinModelPortaliQ9JJN1.
SMRiQ9JJN1. Positions 61-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG311125.
GeneTreeiENSGT00530000063469.
HOGENOMiHOG000112572.
HOVERGENiHBG051612.
InParanoidiQ9JJN1.
KOiK04358.
OMAiTLYGSLH.
OrthoDBiEOG7X6M1F.
PhylomeDBiQ9JJN1.
TreeFamiTF335872.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028292. FGF21.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF62. PTHR11486:SF62. 1 hit.
PRINTSiPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JJN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEWMRSRVGT LGLWVRLLLA VFLLGVYQAY PIPDSSPLLQ FGGQVRQRYL
60 70 80 90 100
YTDDDQDTEA HLEIREDGTV VGAAHRSPES LLELKALKPG VIQILGVKAS
110 120 130 140 150
RFLCQQPDGA LYGSPHFDPE ACSFRELLLE DGYNVYQSEA HGLPLRLPQK
160 170 180 190 200
DSPNQDATSW GPVRFLPMPG LLHEPQDQAG FLPPEPPDVG SSDPLSMVEP
210
LQGRSPSYAS
Length:210
Mass (Da):23,237
Last modified:October 1, 2000 - v1
Checksum:iAE02AABA6477E6F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025718 mRNA. Translation: BAA99416.1.
AK007574 mRNA. Translation: BAB25115.1.
BC049592 mRNA. Translation: AAH49592.1.
CCDSiCCDS21253.1.
RefSeqiNP_064397.1. NM_020013.4.
UniGeneiMm.143736.

Genome annotation databases

EnsembliENSMUST00000033099; ENSMUSP00000033099; ENSMUSG00000030827.
GeneIDi56636.
KEGGimmu:56636.
UCSCiuc009gwe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025718 mRNA. Translation: BAA99416.1.
AK007574 mRNA. Translation: BAB25115.1.
BC049592 mRNA. Translation: AAH49592.1.
CCDSiCCDS21253.1.
RefSeqiNP_064397.1. NM_020013.4.
UniGeneiMm.143736.

3D structure databases

ProteinModelPortaliQ9JJN1.
SMRiQ9JJN1. Positions 61-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60919N.
STRINGi10090.ENSMUSP00000033099.

Proteomic databases

PRIDEiQ9JJN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033099; ENSMUSP00000033099; ENSMUSG00000030827.
GeneIDi56636.
KEGGimmu:56636.
UCSCiuc009gwe.1. mouse.

Organism-specific databases

CTDi26291.
MGIiMGI:1861377. Fgf21.

Phylogenomic databases

eggNOGiNOG311125.
GeneTreeiENSGT00530000063469.
HOGENOMiHOG000112572.
HOVERGENiHBG051612.
InParanoidiQ9JJN1.
KOiK04358.
OMAiTLYGSLH.
OrthoDBiEOG7X6M1F.
PhylomeDBiQ9JJN1.
TreeFamiTF335872.

Miscellaneous databases

NextBioi313077.
PROiQ9JJN1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJN1.
CleanExiMM_FGF21.
GenevestigatoriQ9JJN1.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028292. FGF21.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF62. PTHR11486:SF62. 1 hit.
PRINTSiPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel FGF, FGF-21, preferentially expressed in the liver."
    Nishimura T., Nakatake Y., Konishi M., Itoh N.
    Biochim. Biophys. Acta 1492:203-206(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. Cited for: FUNCTION.

Entry informationi

Entry nameiFGF21_MOUSE
AccessioniPrimary (citable) accession number: Q9JJN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: February 4, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.