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Cytoplasmic FMR1-interacting protein 1 (Specifically Rac1-associated protein 1) (Sra-1) (p140sra-1)

 CYFP1_HUMAN             Reviewed;        1253 AA.
Q7L576; A8K6D9; Q14467; Q5IED0; Q6ZSX1; Q9BSD9; Q9BVC7;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 132.
RecName: Full=Cytoplasmic FMR1-interacting protein 1;
AltName: Full=Specifically Rac1-associated protein 1;
Short=Sra-1;
AltName: Full=p140sra-1;
Name=CYFIP1 {ECO:0000312|HGNC:HGNC:13759};
Synonyms=KIAA0068 {ECO:0000312|EMBL:BAA07552.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAW51476.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT SER-820.
Jiang Y.-H., Beaudet A.L.;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000305, ECO:0000312|EMBL:BAA07552.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow {ECO:0000269|PubMed:7584044};
PubMed=7584044; DOI=10.1093/dnares/1.5.223;
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. II.
The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 1:223-229(1994).
[3] {ECO:0000305, ECO:0000312|EMBL:BAC86825.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
SER-820.
TISSUE=Brain {ECO:0000312|EMBL:BAC86825.1}, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4] {ECO:0000305, ECO:0000312|EMBL:AAW51476.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5] {ECO:0000305, ECO:0000312|EMBL:AAH05097.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain {ECO:0000312|EMBL:AAH05097.1}, and
Placenta {ECO:0000312|EMBL:AAH01306.2};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6] {ECO:0000305, ECO:0000312|EMBL:AAW51476.1}
PROTEIN SEQUENCE OF 50-58; 111-130; 151-163; 366-377; 441-448;
505-515; 564-573; 754-760; 815-826; 867-877; 1054-1076; 1211-1224 AND
1228-1240, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma, and Hepatoma;
Bienvenut W.V., Claeys D., Boldt K., von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[7] {ECO:0000305}
FUNCTION.
PubMed=9417078; DOI=10.1074/jbc.273.1.291;
Kobayashi K., Kuroda S., Fukata M., Nakamura T., Nagase T., Nomura N.,
Matsuura Y., Yoshida-Kubomura N., Iwamatsu A., Kaibuchi K.;
"p140Sra-1 (specifically Rac1-associated protein) is a novel specific
target for Rac1 small GTPase.";
J. Biol. Chem. 273:291-295(1998).
[8] {ECO:0000305}
FUNCTION, AND INTERACTION WITH DPYSL2.
PubMed=16260607; DOI=10.1128/MCB.25.22.9920-9935.2005;
Kawano Y., Yoshimura T., Tsuboi D., Kawabata S., Kaneko-Kawano T.,
Shirataki H., Takenawa T., Kaibuchi K.;
"CRMP-2 is involved in kinesin-1-dependent transport of the Sra-
1/WAVE1 complex and axon formation.";
Mol. Cell. Biol. 25:9920-9935(2005).
[9]
IDENTIFICATION IN THE WAVE2 COMPLEX.
PubMed=16417406; DOI=10.1371/journal.pbio.0040038;
Weiner O.D., Rentel M.C., Ott A., Brown G.E., Jedrychowski M.,
Yaffe M.B., Gygi S.P., Cantley L.C., Bourne H.R., Kirschner M.W.;
"Hem-1 complexes are essential for Rac activation, actin
polymerization, and myosin regulation during neutrophil chemotaxis.";
PLoS Biol. 4:E38-E38(2006).
[10]
FUNCTION.
PubMed=19524508; DOI=10.1016/j.cell.2009.04.013;
Silva J.M., Ezhkova E., Silva J., Heart S., Castillo M., Campos Y.,
Castro V., Bonilla F., Cordon-Cardo C., Muthuswamy S.K., Powers S.,
Fuchs E., Hannon G.J.;
"Cyfip1 is a putative invasion suppressor in epithelial cancers.";
Cell 137:1047-1061(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583 AND THR-1234, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, FUNCTION,
INTERACTION WITH RAC1, MUTAGENESIS OF CYS-179; ARG-190; GLU-434;
PHE-626; MET-632; LEU-697; TYR-704; LEU-841 AND 844-PHE-TRP-845, AND
SUBUNIT.
PubMed=21107423; DOI=10.1038/nature09623;
Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M.,
Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.;
"Structure and control of the actin regulatory WAVE complex.";
Nature 468:533-538(2010).
-!- FUNCTION: Component of the CYFIP1-EIF4E-FMR1 complex which binds
to the mRNA cap and mediates translational repression. In the
CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E
and FMR1. Promotes the translation repression activity of FMR1 in
brain probably by mediating its association with EIF4E and mRNA
(By similarity). Regulates formation of membrane ruffles and
lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but
not to RNA. Part of the WAVE complex that regulates actin filament
reorganization via its interaction with the Arp2/3 complex. Actin
remodeling activity is regulated by RAC1. Regulator of epithelial
morphogenesis. As component of the WAVE1 complex, required for
BDNF-NTRK2 endocytic trafficking and signaling from early
endosomes (By similarity). May act as an invasion suppressor in
cancers. {ECO:0000250|UniProtKB:Q7TMB8,
ECO:0000269|PubMed:16260607, ECO:0000269|PubMed:19524508,
ECO:0000269|PubMed:21107423, ECO:0000269|PubMed:9417078}.
-!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1
or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a
heterodimer containing NCKAP1 and CYFIP1 interacts with a
heterotrimer formed by WAVE1, ABI2 and BRK1. Component of the
CYFIP1-EIF4E-FMR1 complex which is composed of CYFIP, EIF4E and
FMR1. Interacts with FMR1 but does not bind to related proteins
FXR1 or FXR2. Interaction with EIF4E stimulates FMR1 binding.
Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1,
NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2
(PubMed:16417406). Interacts with the active GTP-bound form of
RAC1. Interacts through its C-terminus with the C-terminus of
DPYSL2/CRMP2 which is necessary for DPYSL2-induced axon outgrowth.
Interacts with NYAP1, NYAP2 and MYO16. Interacts with TMEM108 (via
N-terminus); the interaction associates TMEM108 with the WAVE1
complex (By similarity). {ECO:0000250|UniProtKB:Q7TMB8,
ECO:0000269|PubMed:16260607, ECO:0000269|PubMed:16417406,
ECO:0000269|PubMed:21107423}.
-!- INTERACTION:
P63073:Eif4e (xeno); NbExp=2; IntAct=EBI-1048143, EBI-2000006;
Q06787:FMR1; NbExp=4; IntAct=EBI-1048143, EBI-366305;
Q9Y2A7:NCKAP1; NbExp=5; IntAct=EBI-1048143, EBI-389845;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7TMB8}.
Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TMB8}. Cell
projection, lamellipodium {ECO:0000250|UniProtKB:Q7TMB8}. Cell
projection, ruffle {ECO:0000250|UniProtKB:Q7TMB8}. Cell junction,
synapse, synaptosome {ECO:0000250|UniProtKB:Q7TMB8}. Note=Highly
expressed in the perinuclear region (By similarity). Enriched in
synaptosomes (By similarity). Also enriched in membrane ruffles
and at the tips of lamellipodia (By similarity).
{ECO:0000250|UniProtKB:Q7TMB8}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=3;
IsoId=Q7L576-1; Sequence=Displayed;
Name=2; Synonyms=4;
IsoId=Q7L576-2; Sequence=VSP_052346, VSP_052347;
Name=3; Synonyms=5;
IsoId=Q7L576-3; Sequence=VSP_052345;
-!- MISCELLANEOUS: Breakpoint hotspot for the Prader-Willi/Angelman
syndromes and may be implicated in autism. Commonly altered in
tumors.
-!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=BAA07552.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY763577; AAW51476.1; -; mRNA.
EMBL; AY763578; AAW51477.1; -; mRNA.
EMBL; AY763579; AAW51478.1; -; mRNA.
EMBL; AY763580; AAW51479.1; -; mRNA.
EMBL; D38549; BAA07552.1; ALT_INIT; mRNA.
EMBL; AK127094; BAC86825.1; -; mRNA.
EMBL; AK291604; BAF84293.1; -; mRNA.
EMBL; CH471258; EAW65555.1; -; Genomic_DNA.
EMBL; BC001306; AAH01306.2; -; mRNA.
EMBL; BC005097; AAH05097.1; -; mRNA.
CCDS; CCDS73695.1; -. [Q7L576-2]
CCDS; CCDS73696.1; -. [Q7L576-1]
RefSeq; NP_001028200.1; NM_001033028.1. [Q7L576-2]
RefSeq; NP_001274739.1; NM_001287810.2. [Q7L576-1]
RefSeq; NP_001311049.1; NM_001324120.1. [Q7L576-1]
RefSeq; NP_001311052.1; NM_001324123.1. [Q7L576-1]
RefSeq; NP_055423.1; NM_014608.4. [Q7L576-1]
UniGene; Hs.26704; -.
PDB; 3P8C; X-ray; 2.29 A; A=1-1253.
PDB; 4N78; X-ray; 2.43 A; A=1-1253.
PDBsum; 3P8C; -.
PDBsum; 4N78; -.
ProteinModelPortal; Q7L576; -.
SMR; Q7L576; -.
BioGrid; 116800; 69.
CORUM; Q7L576; -.
DIP; DIP-38873N; -.
IntAct; Q7L576; 49.
MINT; Q7L576; -.
STRING; 9606.ENSP00000324549; -.
iPTMnet; Q7L576; -.
PhosphoSitePlus; Q7L576; -.
SwissPalm; Q7L576; -.
BioMuta; CYFIP1; -.
DMDM; 74738589; -.
EPD; Q7L576; -.
MaxQB; Q7L576; -.
PaxDb; Q7L576; -.
PeptideAtlas; Q7L576; -.
PRIDE; Q7L576; -.
DNASU; 23191; -.
Ensembl; ENST00000610365; ENSP00000478779; ENSG00000273749. [Q7L576-1]
Ensembl; ENST00000617556; ENSP00000480525; ENSG00000273749. [Q7L576-2]
Ensembl; ENST00000617928; ENSP00000481038; ENSG00000273749. [Q7L576-1]
GeneID; 23191; -.
KEGG; hsa:23191; -.
UCSC; uc001yus.5; human. [Q7L576-1]
CTD; 23191; -.
DisGeNET; 23191; -.
EuPathDB; HostDB:ENSG00000273749.4; -.
GeneCards; CYFIP1; -.
HGNC; HGNC:13759; CYFIP1.
HPA; HPA068106; -.
MIM; 606322; gene.
neXtProt; NX_Q7L576; -.
OpenTargets; ENSG00000273749; -.
Orphanet; 72; Angelman syndrome.
PharmGKB; PA38367; -.
eggNOG; KOG3534; Eukaryota.
eggNOG; ENOG410XPKW; LUCA.
GeneTree; ENSGT00500000044831; -.
HOGENOM; HOG000272573; -.
HOVERGEN; HBG053209; -.
InParanoid; Q7L576; -.
KO; K05749; -.
OMA; NDIVQYP; -.
OrthoDB; EOG091G0105; -.
PhylomeDB; Q7L576; -.
TreeFam; TF312925; -.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; Q7L576; -.
ChiTaRS; CYFIP1; human.
EvolutionaryTrace; Q7L576; -.
GeneWiki; CYFIP1; -.
GenomeRNAi; 23191; -.
PRO; PR:Q7L576; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000273749; -.
CleanEx; HS_CYFIP1; -.
ExpressionAtlas; Q7L576; baseline and differential.
Genevisible; Q7L576; HS.
GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
GO; GO:0090724; C:central region of growth cone; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0044294; C:dendritic growth cone; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0090725; C:peripheral region of growth cone; IEA:Ensembl.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0031209; C:SCAR complex; IMP:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IEA:Ensembl.
GO; GO:0048675; P:axon extension; IMP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0050890; P:cognition; IMP:UniProtKB.
GO; GO:0097484; P:dendrite extension; IEA:Ensembl.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
GO; GO:0099563; P:modification of synaptic structure; IEA:Ensembl.
GO; GO:1903422; P:negative regulation of synaptic vesicle recycling; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IMP:UniProtKB.
GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
GO; GO:1900006; P:positive regulation of dendrite development; IEA:Ensembl.
GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
GO; GO:1900029; P:positive regulation of ruffle assembly; IEA:Ensembl.
GO; GO:0016601; P:Rac protein signal transduction; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0031529; P:ruffle organization; ISS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
InterPro; IPR008081; Cytoplasmic_FMR1-int.
InterPro; IPR009828; DUF1394.
PANTHER; PTHR12195; PTHR12195; 1.
Pfam; PF07159; DUF1394; 1.
Pfam; PF05994; FragX_IP; 1.
PIRSF; PIRSF008153; FMR1_interacting; 1.
PRINTS; PR01698; CYTOFMRPINTP.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Cell junction;
Cell projection; Cell shape; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; Direct protein sequencing;
Neurogenesis; Phosphoprotein; Polymorphism; Reference proteome;
Synapse; Synaptosome.
CHAIN 1 1253 Cytoplasmic FMR1-interacting protein 1.
/FTId=PRO_0000279706.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1234 1234 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 806 Missing (in isoform 3).
{ECO:0000303|Ref.1}.
/FTId=VSP_052345.
VAR_SEQ 1 431 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.1}.
/FTId=VSP_052346.
VAR_SEQ 432 557 AEEYERATRYNYTSEEKFALVEVIAMIKGLQVLMGRMESVF
NHAIRHTVYAALQDFSQVTLREPLRQAIKKKKNVIQSVLQA
IRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGP
SST -> MAESLGSAELLRQLKSLGMERLLHAVNTFLRQSC
TYLPLLTFGGKTSFVSLDVYGTEANCSATSCSFPKAAATWP
RRQAPGPLGELVRGPPDQGVAEQSFSHGLFEFGITNVPCIF
SPPQMFPWII (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.1}.
/FTId=VSP_052347.
VARIANT 532 532 A -> P (in dbSNP:rs34683919).
/FTId=VAR_053849.
VARIANT 820 820 G -> D (in dbSNP:rs17137190).
/FTId=VAR_053850.
VARIANT 820 820 G -> S (in dbSNP:rs7170637).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.1}.
/FTId=VAR_053851.
MUTAGEN 179 179 C->R: Reduced interaction with RAC1.
{ECO:0000269|PubMed:21107423}.
MUTAGEN 190 190 R->D: Reduced interaction with RAC1.
{ECO:0000269|PubMed:21107423}.
MUTAGEN 434 434 E->K: Reduced interaction with RAC1; when
associated with A-626.
{ECO:0000269|PubMed:21107423}.
MUTAGEN 626 626 F->A: Reduced interaction with RAC1; when
associated with K-434.
{ECO:0000269|PubMed:21107423}.
MUTAGEN 632 632 M->D: Reduced interaction with RAC1.
{ECO:0000269|PubMed:21107423}.
MUTAGEN 697 697 L->D: Constitutive induction of the
formation of actin filaments; when
associated with D-704.
{ECO:0000269|PubMed:21107423}.
MUTAGEN 704 704 Y->D: Constitutive induction of the
formation of actin filaments; when
associated with D-697.
{ECO:0000269|PubMed:21107423}.
MUTAGEN 841 841 L->A: Constitutive induction of the
formation of actin filaments; when
associated with 844-A-A-845.
{ECO:0000269|PubMed:21107423}.
MUTAGEN 844 845 FW->AA: Constitutive induction of the
formation of actin filaments; when
associated with A-841.
{ECO:0000269|PubMed:21107423}.
CONFLICT 583 583 S -> N (in Ref. 1; AAW51478 and 3;
BAC86825). {ECO:0000305}.
CONFLICT 898 898 Y -> H (in Ref. 1; AAW51478 and 3;
BAC86825). {ECO:0000305}.
CONFLICT 930 930 M -> R (in Ref. 1; AAW51478 and 3;
BAC86825). {ECO:0000305}.
CONFLICT 1176 1176 V -> A (in Ref. 1; AAW51479).
{ECO:0000305}.
HELIX 7 17 {ECO:0000244|PDB:3P8C}.
HELIX 59 84 {ECO:0000244|PDB:3P8C}.
HELIX 90 92 {ECO:0000244|PDB:3P8C}.
HELIX 104 143 {ECO:0000244|PDB:3P8C}.
HELIX 148 150 {ECO:0000244|PDB:3P8C}.
HELIX 155 177 {ECO:0000244|PDB:3P8C}.
HELIX 179 193 {ECO:0000244|PDB:3P8C}.
TURN 194 196 {ECO:0000244|PDB:3P8C}.
HELIX 201 215 {ECO:0000244|PDB:3P8C}.
HELIX 219 229 {ECO:0000244|PDB:3P8C}.
HELIX 234 250 {ECO:0000244|PDB:3P8C}.
HELIX 257 274 {ECO:0000244|PDB:3P8C}.
STRAND 275 278 {ECO:0000244|PDB:3P8C}.
HELIX 281 286 {ECO:0000244|PDB:3P8C}.
HELIX 292 301 {ECO:0000244|PDB:3P8C}.
STRAND 304 308 {ECO:0000244|PDB:3P8C}.
STRAND 311 314 {ECO:0000244|PDB:3P8C}.
HELIX 316 320 {ECO:0000244|PDB:3P8C}.
TURN 323 325 {ECO:0000244|PDB:3P8C}.
HELIX 326 331 {ECO:0000244|PDB:3P8C}.
HELIX 346 365 {ECO:0000244|PDB:3P8C}.
HELIX 384 417 {ECO:0000244|PDB:3P8C}.
TURN 422 424 {ECO:0000244|PDB:3P8C}.
HELIX 434 438 {ECO:0000244|PDB:3P8C}.
HELIX 440 442 {ECO:0000244|PDB:3P8C}.
HELIX 445 467 {ECO:0000244|PDB:3P8C}.
HELIX 469 489 {ECO:0000244|PDB:3P8C}.
TURN 490 492 {ECO:0000244|PDB:3P8C}.
HELIX 493 501 {ECO:0000244|PDB:3P8C}.
HELIX 505 518 {ECO:0000244|PDB:3P8C}.
STRAND 522 525 {ECO:0000244|PDB:3P8C}.
HELIX 531 534 {ECO:0000244|PDB:3P8C}.
HELIX 556 570 {ECO:0000244|PDB:3P8C}.
TURN 580 583 {ECO:0000244|PDB:3P8C}.
HELIX 586 598 {ECO:0000244|PDB:3P8C}.
HELIX 599 601 {ECO:0000244|PDB:3P8C}.
HELIX 602 606 {ECO:0000244|PDB:3P8C}.
HELIX 608 615 {ECO:0000244|PDB:3P8C}.
HELIX 619 621 {ECO:0000244|PDB:3P8C}.
HELIX 625 630 {ECO:0000244|PDB:3P8C}.
TURN 631 633 {ECO:0000244|PDB:3P8C}.
HELIX 640 642 {ECO:0000244|PDB:3P8C}.
HELIX 644 655 {ECO:0000244|PDB:3P8C}.
HELIX 658 660 {ECO:0000244|PDB:3P8C}.
TURN 661 663 {ECO:0000244|PDB:3P8C}.
HELIX 664 668 {ECO:0000244|PDB:3P8C}.
HELIX 670 680 {ECO:0000244|PDB:3P8C}.
HELIX 685 721 {ECO:0000244|PDB:3P8C}.
HELIX 725 733 {ECO:0000244|PDB:3P8C}.
HELIX 747 750 {ECO:0000244|PDB:3P8C}.
STRAND 755 757 {ECO:0000244|PDB:3P8C}.
STRAND 760 762 {ECO:0000244|PDB:3P8C}.
HELIX 764 788 {ECO:0000244|PDB:3P8C}.
HELIX 792 794 {ECO:0000244|PDB:3P8C}.
HELIX 795 813 {ECO:0000244|PDB:3P8C}.
HELIX 821 828 {ECO:0000244|PDB:3P8C}.
STRAND 832 836 {ECO:0000244|PDB:3P8C}.
HELIX 838 849 {ECO:0000244|PDB:3P8C}.
HELIX 851 854 {ECO:0000244|PDB:3P8C}.
STRAND 855 858 {ECO:0000244|PDB:3P8C}.
TURN 859 862 {ECO:0000244|PDB:3P8C}.
STRAND 863 866 {ECO:0000244|PDB:3P8C}.
HELIX 869 871 {ECO:0000244|PDB:3P8C}.
HELIX 885 887 {ECO:0000244|PDB:3P8C}.
HELIX 892 901 {ECO:0000244|PDB:3P8C}.
HELIX 902 906 {ECO:0000244|PDB:3P8C}.
HELIX 911 942 {ECO:0000244|PDB:3P8C}.
HELIX 944 955 {ECO:0000244|PDB:3P8C}.
HELIX 965 967 {ECO:0000244|PDB:3P8C}.
HELIX 969 979 {ECO:0000244|PDB:3P8C}.
HELIX 981 984 {ECO:0000244|PDB:3P8C}.
TURN 987 992 {ECO:0000244|PDB:3P8C}.
HELIX 993 1025 {ECO:0000244|PDB:3P8C}.
HELIX 1026 1029 {ECO:0000244|PDB:3P8C}.
HELIX 1043 1053 {ECO:0000244|PDB:3P8C}.
HELIX 1055 1057 {ECO:0000244|PDB:3P8C}.
HELIX 1059 1066 {ECO:0000244|PDB:3P8C}.
HELIX 1069 1083 {ECO:0000244|PDB:3P8C}.
HELIX 1086 1088 {ECO:0000244|PDB:3P8C}.
STRAND 1090 1092 {ECO:0000244|PDB:3P8C}.
HELIX 1093 1101 {ECO:0000244|PDB:3P8C}.
TURN 1107 1110 {ECO:0000244|PDB:3P8C}.
STRAND 1121 1123 {ECO:0000244|PDB:3P8C}.
HELIX 1127 1139 {ECO:0000244|PDB:3P8C}.
HELIX 1149 1153 {ECO:0000244|PDB:3P8C}.
HELIX 1156 1167 {ECO:0000244|PDB:3P8C}.
HELIX 1171 1177 {ECO:0000244|PDB:3P8C}.
HELIX 1179 1190 {ECO:0000244|PDB:3P8C}.
HELIX 1201 1225 {ECO:0000244|PDB:3P8C}.
SEQUENCE 1253 AA; 145182 MW; D8F45E13207BEF16 CRC64;
MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN AFVTGIARYI
EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT
KLMNFMYFQR NAIERFCGEV RRLCHAERRK DFVSEAYLIT LGKFINMFAV LDELKNMKCS
VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD
IVNLCVDYYE NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK
QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCTSSGSS PQYNICEQMI QIREDHMRFI
SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL LSQWSAHVME VYSWKLVHPT
DKYSNKDCPD SAEEYERATR YNYTSEEKFA LVEVIAMIKG LQVLMGRMES VFNHAIRHTV
YAALQDFSQV TLREPLRQAI KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK
SGFDIKVPRR AVGPSSTQLY MVRTMLESLI ADKSGSKKTL RSSLEGPTIL DIEKFHRESF
FYTHLINFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD HILETKEASM
MEYVLYSLDL YNDSAHYALT RFNKQFLYDE IEAEVNLCFD QFVYKLADQI FAYYKVMAGS
LLLDKRLRSE CKNQGATIHL PPSNRYETLL KQRHVQLLGR SIDLNRLITQ RVSAAMYKSL
ELAIGRFESE DLTSIVELDG LLEINRMTHK LLSRYLTLDG FDAMFREANH NVSAPYGRIT
LHVFWELNYD FLPNYCYNGS TNRFVRTVLP FSQEFQRDKQ PNAQPQYLHG SKALNLAYSS
IYGSYRNFVG PPHFQVICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK TLMEVMPKIC
RLPRHEYGSP GILEFFHHQL KDIVEYAELK TVCFQNLREV GNAILFCLLI EQSLSLEEVC
DLLHAAPFQN ILPRVHVKEG ERLDAKMKRL ESKYAPLHLV PLIERLGTPQ QIAIAREGDL
LTKERLCCGL SMFEVILTRI RSFLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI
PVGTHEFTVE QCFGDGLHWA GCMIIVLLGQ QRRFAVLDFC YHLLKVQKHD GKDEIIKNVP
LKKMVERIRK FQILNDEIIT ILDKYLKSGD GEGTPVEHVR CFQPPIHQSL ASS


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