Q8WU20 (FRS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

FRS2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	508 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Membrane
Coding sequence diversity	Polymorphism
PTM	Lipoprotein Myristate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Traceable author statement Ref.1. Source: UniProtKB activation of MAPK activity Inferred from electronic annotation. Source: Compara activation of MAPKK activity Traceable author statement. Source: Reactome anterior/posterior axis specification, embryo Inferred from electronic annotation. Source: Compara fibroblast growth factor receptor signaling pathway Traceable author statement Ref.1. Source: UniProtKB forebrain development Inferred from electronic annotation. Source: Compara gastrulation with mouth forming second Inferred from electronic annotation. Source: Compara insulin receptor signaling pathway Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome neuroblast proliferation Inferred from electronic annotation. Source: Compara optic placode formation involved in camera-type eye formation Inferred from electronic annotation. Source: Compara organ induction Inferred from electronic annotation. Source: Compara prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Inferred from electronic annotation. Source: Compara regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara transmembrane receptor protein tyrosine phosphatase signaling pathway Traceable author statement Ref.1. Source: UniProtKB ventricular septum development Inferred from electronic annotation. Source: Compara
Cellular_component	endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell endosome Traceable author statement. Source: Reactome integral to plasma membrane Traceable author statement Ref.1. Source: UniProtKB
Molecular_function	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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 508

508

Fibroblast growth factor receptor substrate 2

PRO_0000087344

Regions

Domain

13 – 115

103

IRS-type PTB

Amino acid modifications

Modified residue

169

1

Phosphoserine By similarity

Modified residue

172

1

Phosphoserine By similarity

Modified residue

196

1

Phosphotyrosine; by FGFR1 By similarity

Modified residue

211

1

Phosphoserine By similarity

Modified residue

221

1

Phosphoserine Ref.1 Ref.7 Ref.11

Modified residue

288

1

Phosphothreonine By similarity

Modified residue

306

1

Phosphotyrosine; by FGFR1 By similarity

Modified residue

349

1

Phosphotyrosine; by FGFR1 By similarity

Modified residue

392

1

Phosphotyrosine; by FGFR1 By similarity

Modified residue

436

1

Phosphotyrosine; by FGFR1 By similarity

Modified residue

471

1

Phosphotyrosine; by FGFR1 By similarity

Lipidation

2

1

N-myristoyl glycine Ref.1 Ref.7

Natural variations

Natural variant

303

1

K → N.
Corresponds to variant rs12580717 [ dbSNP | Ensembl ].

VAR_046966

Natural variant

449

1

N → D.
Corresponds to variant rs35232109 [ dbSNP | Ensembl ].

VAR_046967

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

508

Helix Strand Turn

Details...

Beta strand

20 – 26

7

Beta strand

36 – 40

5

Beta strand

45 – 49

5

Turn

50 – 52

3

Beta strand

53 – 57

5

Beta strand

62 – 67

6

Beta strand

69 – 76

8

Beta strand

84 – 90

7

Helix

94 – 107

14

Sequences

	Sequence		Length	Mass (Da)
	Q8WU20 [UniParc]. Last modified October 14, 2008. Version 4. Checksum: 833714EE12097C75	FASTA	508	57,029
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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.

IPI

IPI00107698.

RefSeq

NP_001036020.1. NM_001042555.1.
NP_006645.3. NM_006654.3.

UniGene

Hs.593446.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XR0	NMR	-	B	11-136	[»]

ProteinModelPortal

Q8WU20.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8WU20. 2 interactions.

STRING

9606.ENSP00000299293.

PTM databases

PhosphoSite

Q8WU20.

Polymorphism databases

DMDM

209572769.

Proteomic databases

PaxDb

Q8WU20.

PRIDE

Q8WU20.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299293; ENSP00000299293; ENSG00000166225.
ENST00000397997; ENSP00000381083; ENSG00000166225.
ENST00000549921; ENSP00000450048; ENSG00000166225.
ENST00000550389; ENSP00000447241; ENSG00000166225.

GeneID

10818.

KEGG

hsa:10818.

UCSC

uc001suy.3. human.

Organism-specific databases

CTD

10818.

GeneCards

GC12P069864.

HGNC

HGNC:16971. FRS2.

HPA

CAB010347.

MIM

607743. gene.

neXtProt

NX_Q8WU20.

PharmGKB

PA134850063.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG316561.

HOGENOM

HOG000290694.

HOVERGEN

HBG062705.

InParanoid

Q8WU20.

KO

K12461.

OMA

RKNRASV.

OrthoDB

EOG4M398C.

PhylomeDB

Q8WU20.

Enzyme and pathway databases

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q8WU20.

Bgee

Q8WU20.

CleanEx

HS_FRS2.

Genevestigator

Q8WU20.

GermOnline

ENSG00000166225. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
[Graphical view]

Pfam

PF02174. IRS. 1 hit.
[Graphical view]

SMART

SM00310. PTBI. 1 hit.
[Graphical view]

PROSITE

PS51064. IRS_PTB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FRS2. human.

EvolutionaryTrace

Q8WU20.

GenomeRNAi

10818.

NextBio

41095.

SOURCE

Search...

Entry information

Entry name

FRS2_HUMAN

Accession

Primary (citable) accession number: Q8WU20
Secondary accession number(s): B0LPF2 , B2R684, O43558, Q7LDQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	October 14, 2008
Last modified:	May 1, 2013
This is version 100 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.