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Q8WU20 (FRS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibroblast growth factor receptor substrate 2

Short name=FGFR substrate 2
Alternative name(s):
FGFR-signaling adaptor SNT
Suc1-associated neurotrophic factor target 1
Short name=SNT-1
Gene names
Name:FRS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that links activated FGR and NGF receptors to downstream signaling pathways. Plays an important role in the activation of MAP kinases and in the phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, in response to ligand-mediated activation of FGFR1. Modulates signaling via SHC1 by competing for a common binding site on NTRK1. Ref.8 Ref.12

Subunit structure

Part of a complex containing FRS2, GRB2, GAB1, PIK3R1 and SOS1. Part of a complex containing GRB2 and CBL. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Binds RET By similarity. Binds ALK, FGFR1, CKS2, MAPK1/ERK2, MAPK3/ERK1 and SRC. The tyrosine-phosphorylated protein binds the SH2 domains of GRB2 and PTPN11. Interacts with NTRK1, NTRK2 and NTRK3 (phosphorylated upon ligand-binding). Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Subcellular location

Endomembrane system. Note: Cytoplasmic, membrane-bound.

Tissue specificity

Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Ref.7

Post-translational modification

Phosphorylated by ULK2 in vitro By similarity. Phosphorylated on tyrosine residues upon stimulation by NGF or FGF2. Phosphorylated on tyrosine residues by activated ALK and FGFR1. Phosphorylated on tyrosine residues upon activation of FGFR2 and FGFR3. Phosphorylated on threonine residues by MAP kinases; this inhibits tyrosine phosphorylation, and thereby down-regulates FRS2-mediated activation of MAP kinases. Ref.1 Ref.7 Ref.8 Ref.10 Ref.12

Ubiquitinated when tyrosine phosphorylated and in a complex with GRB2. The unphosphorylated form is not subject to ubiquitination By similarity. Ref.1 Ref.7 Ref.8 Ref.10 Ref.12

Sequence similarities

Contains 1 IRS-type PTB domain.

Sequence caution

The sequence AAH21562.1 differs from that shown. Reason: Erroneous termination at position 509. Translated as stop.

The sequence BAG35381.1 differs from that shown. Reason: Erroneous termination at position 509. Translated as stop.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   PTMLipoprotein
Myristate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

G-protein coupled receptor signaling pathway

Traceable author statement Ref.1. Source: UniProtKB

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

activation of MAPKK activity

Traceable author statement. Source: Reactome

anterior/posterior axis specification, embryo

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement Ref.1. Source: UniProtKB

forebrain development

Inferred from electronic annotation. Source: Ensembl

gastrulation with mouth forming second

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

optic placode formation involved in camera-type eye formation

Inferred from electronic annotation. Source: Ensembl

organ induction

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein tyrosine phosphatase signaling pathway

Traceable author statement Ref.1. Source: UniProtKB

ventricular septum development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendosome

Traceable author statement. Source: Reactome

integral component of plasma membrane

Traceable author statement Ref.1. Source: UniProtKB

membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionfibroblast growth factor receptor binding

Inferred from physical interaction Ref.1. Source: MGI

neurotrophin TRKA receptor binding

Inferred from physical interaction Ref.9. Source: UniProtKB

phosphatase activator activity

Traceable author statement Ref.1. Source: UniProtKB

transmembrane receptor protein tyrosine kinase adaptor activity

Traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 508507Fibroblast growth factor receptor substrate 2
PRO_0000087344

Regions

Domain13 – 115103IRS-type PTB

Amino acid modifications

Modified residue1961Phosphotyrosine; by FGFR1 By similarity
Modified residue2111Phosphoserine By similarity
Modified residue2211Phosphoserine Ref.1 Ref.7 Ref.11
Modified residue3061Phosphotyrosine; by FGFR1 By similarity
Modified residue3491Phosphotyrosine; by FGFR1 By similarity
Modified residue3921Phosphotyrosine; by FGFR1 By similarity
Modified residue4361Phosphotyrosine; by FGFR1 By similarity
Modified residue4711Phosphotyrosine; by FGFR1 By similarity
Lipidation21N-myristoyl glycine Ref.1 Ref.7

Natural variations

Natural variant3031K → N.
Corresponds to variant rs12580717 [ dbSNP | Ensembl ].
VAR_046966
Natural variant4491N → D.
Corresponds to variant rs35232109 [ dbSNP | Ensembl ].
VAR_046967

Secondary structure

................. 508
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WU20 [UniParc].

Last modified October 14, 2008. Version 4.
Checksum: 833714EE12097C75

FASTA50857,029
        10         20         30         40         50         60 
MGSCCSCPDK DTVPDNHRNK FKVINVDDDG NELGSGIMEL TDTELILYTR KRDSVKWHYL 

        70         80         90        100        110        120 
CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CARAEELFNM LQEIMQNNSI NVVEEPVVER 

       130        140        150        160        170        180 
NNHQTELEVP RTPRTPTTPG FAAQNLPNGY PRYPSFGDAS SHPSSRHPSV GSARLPSVGE 

       190        200        210        220        230        240 
ESTHPLLVAE EQVHTYVNTT GVQEERKNRT SVHVPLEARV SNAESSTPKE EPSSIEDRDP 

       250        260        270        280        290        300 
QILLEPEGVK FVLGPTPVQK QLMEKEKLEQ LGRDQVSGSG ANNTEWDTGY DSDERRDAPS 

       310        320        330        340        350        360 
VNKLVYENIN GLSIPSASGV RRGRLTSTST SDTQNINNSA QRRTALLNYE NLPSLPPVWE 

       370        380        390        400        410        420 
ARKLSRDEDD NLGPKTPSLN GYHNNLDPMH NYVNTENVTV PASAHKIEYS RRRDCTPTVF 

       430        440        450        460        470        480 
NFDIRRPSLE HRQLNYIQVD LEGGSDSDNP QTPKTPTTPL PQTPTRRTEL YAVIDIERTA 

       490        500 
AMSNLQKALP RDDGTSRKTR HNSTDLPM 

« Hide

References

« Hide 'large scale' references
[1]"Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins."
Xu H., Lee K.W., Goldfarb M.P.
J. Biol. Chem. 273:17987-17990(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FGFR1, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT TYROSINE RESIDUES.
Tissue: Placenta.
[2]"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].
Tissue: Hippocampus.
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Uterus.
[7]"The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation."
Meakin S.O., MacDonald J.I.S., Gryz E.A., Kubu C.J., Verdi J.M.
J. Biol. Chem. 274:9861-9870(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CKS2; GRB2; PTPN11; SRC; NTRK1; NTRK2 AND NTRK3, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT TYROSINE RESIDUES, TISSUE SPECIFICITY.
[8]"EGFR and FGFR signaling through FRS2 is subject to negative feedback control by ERK1/2."
Wu Y., Chen Z., Ullrich A.
Biol. Chem. 384:1215-1226(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY MAPK1/ERK2 AND MAPK3/ERK1, INTERACTION WITH MAPK1/ERK2 AND MAPK3/ERK1, FUNCTION.
[9]"TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma."
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A., Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A., Mackay A.R.
Cancer Cell 6:347-360(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NTRK1.
[10]"ALK activation induces Shc and FRS2 recruitment: Signaling and phenotypic outcomes in PC12 cells differentiation."
Degoutin J., Vigny M., Gouzi J.Y.
FEBS Lett. 581:727-734(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALK, PHOSPHORYLATION.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Nedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and function."
Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F., Dirks P., Ciruna B., Rotin D.
EMBO J. 30:3259-3273(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF AKT1; PLCG1; MAPK1/ERK2, MAPK3/ERK1 AND MAP KINASE SIGNALING, INTERACTION WITH FGFR1, PHOSPHORYLATION.
[13]"Regulation of growth factor signaling by FRS2 family docking/scaffold adaptor proteins."
Gotoh N.
Cancer Sci. 99:1319-1325(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION; SUBUNIT AND PHOSPHORYLATION.
[14]"Fibroblast growth factor signalling: from development to cancer."
Turner N., Grose R.
Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN FGF SIGNALING.
[15]"Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors."
Dhalluin C., Yan K.S., Plotnikova O., Lee K.W., Zeng L., Kuti M., Mujtaba S., Goldfarb M.P., Zhou M.-M.
Mol. Cell 6:921-929(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 11-136 IN COMPLEX WITH FGFR1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF036717 mRNA. Translation: AAB92554.1.
AK312477 mRNA. Translation: BAG35381.1. Sequence problems.
EU332842 Genomic DNA. Translation: ABY87531.1.
AC018921 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97225.1.
BC021562 mRNA. Translation: AAH21562.1. Sequence problems.
RefSeqNP_001036020.1. NM_001042555.2.
NP_001265280.1. NM_001278351.1.
NP_001265282.1. NM_001278353.1.
NP_001265283.1. NM_001278354.1.
NP_001265284.1. NM_001278355.1.
NP_001265285.1. NM_001278356.1.
NP_001265286.1. NM_001278357.1.
NP_006645.3. NM_006654.4.
UniGeneHs.593446.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XR0NMR-B11-136[»]
2MFQNMR-A11-122[»]
ProteinModelPortalQ8WU20.
SMRQ8WU20. Positions 11-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116031. 17 interactions.
IntActQ8WU20. 4 interactions.
MINTMINT-8019836.
STRING9606.ENSP00000299293.

PTM databases

PhosphoSiteQ8WU20.

Polymorphism databases

DMDM209572769.

Proteomic databases

PaxDbQ8WU20.
PRIDEQ8WU20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299293; ENSP00000299293; ENSG00000166225.
ENST00000397997; ENSP00000381083; ENSG00000166225.
ENST00000549921; ENSP00000450048; ENSG00000166225.
ENST00000550389; ENSP00000447241; ENSG00000166225.
GeneID10818.
KEGGhsa:10818.
UCSCuc001suy.3. human.

Organism-specific databases

CTD10818.
GeneCardsGC12P069864.
HGNCHGNC:16971. FRS2.
HPACAB010347.
HPA038323.
MIM607743. gene.
neXtProtNX_Q8WU20.
PharmGKBPA134850063.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316561.
HOGENOMHOG000290694.
HOVERGENHBG062705.
InParanoidQ8WU20.
KOK12461.
OMASTEWDTG.
PhylomeDBQ8WU20.
TreeFamTF324994.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkQ8WU20.

Gene expression databases

ArrayExpressQ8WU20.
BgeeQ8WU20.
CleanExHS_FRS2.
GenevestigatorQ8WU20.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
[Graphical view]
PfamPF02174. IRS. 1 hit.
[Graphical view]
SMARTSM00310. PTBI. 1 hit.
[Graphical view]
PROSITEPS51064. IRS_PTB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFRS2. human.
EvolutionaryTraceQ8WU20.
GeneWikiFRS2.
GenomeRNAi10818.
NextBio41095.
PROQ8WU20.
SOURCESearch...

Entry information

Entry nameFRS2_HUMAN
AccessionPrimary (citable) accession number: Q8WU20
Secondary accession number(s): B0LPF2 expand/collapse secondary AC list , B2R684, O43558, Q7LDQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 14, 2008
Last modified: April 16, 2014
This is version 110 of the entry and version 4 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 12

Human chromosome 12: entries, gene names and cross-references to MIM