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Q8WU20

- FRS2_HUMAN

UniProt

Q8WU20 - FRS2_HUMAN

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Protein

Fibroblast growth factor receptor substrate 2

Gene

FRS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 NTRK1.2 Publications

GO - Molecular functioni

  1. fibroblast growth factor receptor binding Source: MGI
  2. neurotrophin TRKA receptor binding Source: UniProtKB
  3. phosphatase activator activity Source: UniProtKB
  4. transmembrane receptor protein tyrosine kinase adaptor activity Source: UniProtKB

GO - Biological processi

  1. activation of MAPK activity Source: Ensembl
  2. activation of MAPKK activity Source: Reactome
  3. anterior/posterior axis specification, embryo Source: Ensembl
  4. epidermal growth factor receptor signaling pathway Source: Reactome
  5. Fc-epsilon receptor signaling pathway Source: Reactome
  6. fibroblast growth factor receptor signaling pathway Source: UniProtKB
  7. forebrain development Source: Ensembl
  8. gastrulation with mouth forming second Source: Ensembl
  9. G-protein coupled receptor signaling pathway Source: UniProtKB
  10. innate immune response Source: Reactome
  11. insulin receptor signaling pathway Source: Reactome
  12. lens fiber cell development Source: Ensembl
  13. neuroblast proliferation Source: Ensembl
  14. neurotrophin TRK receptor signaling pathway Source: Reactome
  15. optic placode formation involved in camera-type eye formation Source: Ensembl
  16. organ induction Source: Ensembl
  17. phosphatidylinositol-mediated signaling Source: Reactome
  18. prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: Ensembl
  19. regulation of apoptotic process Source: Ensembl
  20. regulation of epithelial cell proliferation Source: Ensembl
  21. regulation of ERK1 and ERK2 cascade Source: Ensembl
  22. transmembrane receptor protein tyrosine phosphatase signaling pathway Source: UniProtKB
  23. ventricular septum development Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_111184. Negative regulation of FGFR signaling.
REACT_12076. Frs2-mediated activation.
REACT_121398. Signaling by FGFR mutants.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_21247. FRS2-mediated cascade.
REACT_21270. PI-3K cascade.
REACT_75829. PIP3 activates AKT signaling.
REACT_976. PI3K Cascade.
SignaLinkiQ8WU20.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:FRS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:16971. FRS2.

Subcellular locationi

Endomembrane system
Note: Cytoplasmic, membrane-bound.

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. endosome Source: Reactome
  3. integral component of plasma membrane Source: UniProtKB
  4. membrane Source: ProtInc
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134850063.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 508507Fibroblast growth factor receptor substrate 2PRO_0000087344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine2 Publications
Modified residuei196 – 1961Phosphotyrosine; by FGFR1By similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei221 – 2211Phosphoserine1 Publication
Modified residuei306 – 3061Phosphotyrosine; by FGFR1By similarity
Modified residuei349 – 3491Phosphotyrosine; by FGFR1By similarity
Modified residuei392 – 3921Phosphotyrosine; by FGFR1By similarity
Modified residuei436 – 4361Phosphotyrosine; by FGFR1By similarity
Modified residuei471 – 4711Phosphotyrosine; by FGFR1By similarity

Post-translational modificationi

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.By similarity6 Publications
Ubiquitinated when tyrosine phosphorylated and in a complex with GRB2. The unphosphorylated form is not subject to ubiquitination (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8WU20.
PaxDbiQ8WU20.
PRIDEiQ8WU20.

PTM databases

PhosphoSiteiQ8WU20.

Expressioni

Tissue specificityi

Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.1 Publication

Gene expression databases

BgeeiQ8WU20.
CleanExiHS_FRS2.
ExpressionAtlasiQ8WU20. baseline and differential.
GenevestigatoriQ8WU20.

Organism-specific databases

HPAiCAB010347.
HPA038323.

Interactioni

Subunit structurei

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).By similarity7 Publications

Protein-protein interaction databases

BioGridi116031. 17 interactions.
IntActiQ8WU20. 4 interactions.
MINTiMINT-8019836.
STRINGi9606.ENSP00000299293.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni15 – 184Combined sources
Beta strandi20 – 267Combined sources
Beta strandi32 – 343Combined sources
Beta strandi36 – 405Combined sources
Beta strandi45 – 495Combined sources
Turni50 – 523Combined sources
Beta strandi53 – 575Combined sources
Turni59 – 613Combined sources
Beta strandi62 – 676Combined sources
Beta strandi69 – 768Combined sources
Beta strandi84 – 907Combined sources
Helixi94 – 10714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XR0NMR-B11-136[»]
2MFQNMR-A11-122[»]
ProteinModelPortaliQ8WU20.
SMRiQ8WU20. Positions 11-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WU20.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 115103IRS-type PTBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 IRS-type PTB domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG316561.
GeneTreeiENSGT00510000046707.
HOGENOMiHOG000290694.
HOVERGENiHBG062705.
InParanoidiQ8WU20.
KOiK12461.
OMAiTRRRDCT.
PhylomeDBiQ8WU20.
TreeFamiTF324994.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF02174. IRS. 1 hit.
[Graphical view]
SMARTiSM00310. PTBI. 1 hit.
[Graphical view]
PROSITEiPS51064. IRS_PTB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8WU20-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSCCSCPDK DTVPDNHRNK FKVINVDDDG NELGSGIMEL TDTELILYTR
60 70 80 90 100
KRDSVKWHYL CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CARAEELFNM
110 120 130 140 150
LQEIMQNNSI NVVEEPVVER NNHQTELEVP RTPRTPTTPG FAAQNLPNGY
160 170 180 190 200
PRYPSFGDAS SHPSSRHPSV GSARLPSVGE ESTHPLLVAE EQVHTYVNTT
210 220 230 240 250
GVQEERKNRT SVHVPLEARV SNAESSTPKE EPSSIEDRDP QILLEPEGVK
260 270 280 290 300
FVLGPTPVQK QLMEKEKLEQ LGRDQVSGSG ANNTEWDTGY DSDERRDAPS
310 320 330 340 350
VNKLVYENIN GLSIPSASGV RRGRLTSTST SDTQNINNSA QRRTALLNYE
360 370 380 390 400
NLPSLPPVWE ARKLSRDEDD NLGPKTPSLN GYHNNLDPMH NYVNTENVTV
410 420 430 440 450
PASAHKIEYS RRRDCTPTVF NFDIRRPSLE HRQLNYIQVD LEGGSDSDNP
460 470 480 490 500
QTPKTPTTPL PQTPTRRTEL YAVIDIERTA AMSNLQKALP RDDGTSRKTR

HNSTDLPM
Length:508
Mass (Da):57,029
Last modified:October 14, 2008 - v4
Checksum:i833714EE12097C75
GO

Sequence cautioni

The sequence AAH21562.1 differs from that shown. Reason: Erroneous termination at position 509. Translated as stop.Curated
The sequence BAG35381.1 differs from that shown. Reason: Erroneous termination at position 509. Translated as stop.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031K → N.
Corresponds to variant rs12580717 [ dbSNP | Ensembl ].
VAR_046966
Natural varianti449 – 4491N → D.
Corresponds to variant rs35232109 [ dbSNP | Ensembl ].
VAR_046967

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41809.1.
RefSeqiNP_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.
UniGeneiHs.593446.

Genome annotation databases

EnsembliENST00000397997; ENSP00000381083; ENSG00000166225.
ENST00000549921; ENSP00000450048; ENSG00000166225.
ENST00000550389; ENSP00000447241; ENSG00000166225.
GeneIDi10818.
KEGGihsa:10818.
UCSCiuc001suy.3. human.

Polymorphism databases

DMDMi209572769.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS41809.1.
RefSeqi NP_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.
UniGenei Hs.593446.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XR0 NMR - B 11-136 [» ]
2MFQ NMR - A 11-122 [» ]
ProteinModelPortali Q8WU20.
SMRi Q8WU20. Positions 11-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116031. 17 interactions.
IntActi Q8WU20. 4 interactions.
MINTi MINT-8019836.
STRINGi 9606.ENSP00000299293.

PTM databases

PhosphoSitei Q8WU20.

Polymorphism databases

DMDMi 209572769.

Proteomic databases

MaxQBi Q8WU20.
PaxDbi Q8WU20.
PRIDEi Q8WU20.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000397997 ; ENSP00000381083 ; ENSG00000166225 .
ENST00000549921 ; ENSP00000450048 ; ENSG00000166225 .
ENST00000550389 ; ENSP00000447241 ; ENSG00000166225 .
GeneIDi 10818.
KEGGi hsa:10818.
UCSCi uc001suy.3. human.

Organism-specific databases

CTDi 10818.
GeneCardsi GC12P069864.
HGNCi HGNC:16971. FRS2.
HPAi CAB010347.
HPA038323.
MIMi 607743. gene.
neXtProti NX_Q8WU20.
PharmGKBi PA134850063.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316561.
GeneTreei ENSGT00510000046707.
HOGENOMi HOG000290694.
HOVERGENi HBG062705.
InParanoidi Q8WU20.
KOi K12461.
OMAi TRRRDCT.
PhylomeDBi Q8WU20.
TreeFami TF324994.

Enzyme and pathway databases

Reactomei REACT_111184. Negative regulation of FGFR signaling.
REACT_12076. Frs2-mediated activation.
REACT_121398. Signaling by FGFR mutants.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_21247. FRS2-mediated cascade.
REACT_21270. PI-3K cascade.
REACT_75829. PIP3 activates AKT signaling.
REACT_976. PI3K Cascade.
SignaLinki Q8WU20.

Miscellaneous databases

ChiTaRSi FRS2. human.
EvolutionaryTracei Q8WU20.
GeneWikii FRS2.
GenomeRNAii 10818.
NextBioi 41095.
PROi Q8WU20.
SOURCEi Search...

Gene expression databases

Bgeei Q8WU20.
CleanExi HS_FRS2.
ExpressionAtlasi Q8WU20. baseline and differential.
Genevestigatori Q8WU20.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF02174. IRS. 1 hit.
[Graphical view ]
SMARTi SM00310. PTBI. 1 hit.
[Graphical view ]
PROSITEi PS51064. IRS_PTB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiFRS2_HUMAN
AccessioniPrimary (citable) accession number: Q8WU20
Secondary accession number(s): B0LPF2
, B2R684, O43558, Q7LDQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 14, 2008
Last modified: November 26, 2014
This is version 117 of the entry and version 4 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 12
    Human chromosome 12: 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