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Protein

Cytoplasmic FMR1-interacting protein 1

Gene

Cyfip1

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

Functioni

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. May act as an invasion suppressor in cancers.By similarity4 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • profilin binding Source: MGI
  • protein complex binding Source: MGI
  • Rac GTPase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell shape, Differentiation, Neurogenesis

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5663213. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic FMR1-interacting protein 1
Alternative name(s):
Specifically Rac1-associated protein 1
Short name:
Sra-1
Gene namesi
Name:Cyfip1Imported
Synonyms:Kiaa0068Imported, ShycImported, Sra1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1338801. Cyfip1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • lamellipodium Source: MGI
  • mRNA cap binding complex Source: UniProtKB
  • neuron projection Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • ruffle Source: UniProtKB
  • SCAR complex Source: MGI
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

Mice display greatly reduced lamellipodium formation in response to growth factor stimulation or aluminum fluoride treatment. Abnormal epithelial morphogenesis in vitro, and cooperation with oncogenic Ras to produce invasive carcinomas in vivo.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi724 – 7241D → A: EIF4E-binding reduced by 20%; when associated with A-726. 1 Publication
Mutagenesisi724 – 7241D → K: EIF4E-binding reduced by 60%; when associated with E-725, E-726 and K-730. 1 Publication
Mutagenesisi725 – 7251K → E: EIF4E-binding reduced by 70%. EIF4E-binding reduced by 60%; when associated with K-724, E-726 and K-730. 1 Publication
Mutagenesisi726 – 7261R → A: EIF4E-binding reduced by 20%; when associated with A-724. 1 Publication
Mutagenesisi726 – 7261R → E: EIF4E-binding reduced by 60%; when associated with K-724, E-725 and K-730. 1 Publication
Mutagenesisi730 – 7301E → K: EIF4E-binding reduced by 60%; when associated with K-724, E-725 and E-726. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12531253Cytoplasmic FMR1-interacting protein 1PRO_0000279707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei583 – 5831PhosphoserineBy similarity
Modified residuei1234 – 12341PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7TMB8.
MaxQBiQ7TMB8.
PaxDbiQ7TMB8.
PeptideAtlasiQ7TMB8.
PRIDEiQ7TMB8.

PTM databases

iPTMnetiQ7TMB8.
PhosphoSiteiQ7TMB8.
SwissPalmiQ7TMB8.

Expressioni

Tissue specificityi

Highly expressed in embryonic and adult developing nervous system.1 Publication

Gene expression databases

BgeeiQ7TMB8.
CleanExiMM_CYFIP1.
MM_SRA1.
ExpressionAtlasiQ7TMB8. baseline and differential.
GenevisibleiQ7TMB8. MM.

Interactioni

Subunit structurei

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 and WASF2/WAVE2. 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 MYO16.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Eif4eP630735EBI-772928,EBI-2000006

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • profilin binding Source: MGI
  • protein complex binding Source: MGI
  • Rac GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi203226. 4 interactions.
IntActiQ7TMB8. 13 interactions.
MINTiMINT-203655.
STRINGi10090.ENSMUSP00000032629.

Structurei

3D structure databases

ProteinModelPortaliQ7TMB8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni724 – 7329EIF4E-binding

Sequence similaritiesi

Belongs to the CYFIP family.Sequence analysis

Phylogenomic databases

eggNOGiKOG3534. Eukaryota.
ENOG410XPKW. LUCA.
GeneTreeiENSGT00500000044831.
HOVERGENiHBG053209.
InParanoidiQ7TMB8.
KOiK05749.
OMAiLTSIMEL.
OrthoDBiEOG7ZSHS2.
PhylomeDBiQ7TMB8.
TreeFamiTF312925.

Family and domain databases

InterProiIPR008081. Cytoplasmic_FMR1-int.
IPR009828. DUF1394.
[Graphical view]
PANTHERiPTHR12195. PTHR12195. 1 hit.
PfamiPF07159. DUF1394. 1 hit.
PF05994. FragX_IP. 1 hit.
[Graphical view]
PIRSFiPIRSF008153. FMR1_interacting. 1 hit.
PRINTSiPR01698. CYTOFMRPINTP.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q7TMB8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN
60 70 80 90 100
AFVTGIARYI EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE
110 120 130 140 150
QPNRVEIYEK TVEVLEPEVT KLMNFMYFQR NAIERFCGEV RRLCHAERRK
160 170 180 190 200
DFVSEAYLIT LGKFINMFAV LDELKNMKCS VKNDHSAYKR AAQFLRKMAD
210 220 230 240 250
PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD IVNLCVDYYE
260 270 280 290 300
NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK
310 320 330 340 350
QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCASSSSS PQYNICEQMI
360 370 380 390 400
QIREDHMRFI SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL
410 420 430 440 450
LSQWSAHVME VYSWKLVHPT DKYSNKDCPD NAEEYERATR YNYTTEEKFA
460 470 480 490 500
LVEVIAMIKG LQVLMGRMES VFNHAIRHTV YAALQDFSQV TLREPLRQAI
510 520 530 540 550
KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK SGFDIKVPRR
560 570 580 590 600
AVGPSSTQLY MVRTMLESLI ADKSGSKKTL RSSLEGPTIL DIEKFHRESF
610 620 630 640 650
FYTHLINFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD
660 670 680 690 700
HILETKEASM MEYVLYSLDL YNDSAHYALT KFNKQFLYDE IEAEVNLCFD
710 720 730 740 750
QFVYKLADQI FAYYKVMAGS LLLDKRLRSE CKNQGATIHL PPSNRYETLL
760 770 780 790 800
KQRHVQLLGR SIDLNRLITQ RVSAAMYKSL ELAIGRFESE DLTSVVELDG
810 820 830 840 850
LLEINRMTHK LLSRYLTLDS FDAMFREANH NVSAPYGRIT LHVFWELNYD
860 870 880 890 900
FLPNYCYNGS TNRFVRTVLP FSQEFQRDKQ PNAQPQYLHG SKALNLAYSS
910 920 930 940 950
IYGSYRNFVG PPHFQVICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK
960 970 980 990 1000
TLMEVMPKIC RLPRHEYGSP GILEFFHHQL KDIVEYAELK TVCFQNLREV
1010 1020 1030 1040 1050
GNAVLFCLLI EQSLSLEEVC DLLHAAPFQN ILPRIHVKEG ERVDAKMKRL
1060 1070 1080 1090 1100
ESKYAPLHLV PLIERLGTPQ QIAIAREGDL LTKERLCCGL SMFEVILTRI
1110 1120 1130 1140 1150
RTFLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI PVGTHEFTVE
1160 1170 1180 1190 1200
QCFGDGLHWA GCMIIVLLGQ QRRFAVLDFC YHLLKVQKHD GKDEIIKNVP
1210 1220 1230 1240 1250
LKKMVERIRK FQILNDEIIT ILDKYLKSGD GESTPVEHVR CFQPPIHQSL

ASS
Length:1,253
Mass (Da):145,241
Last modified:October 1, 2003 - v1
Checksum:i793986FB417CF19B
GO
Isoform 21 Publication (identifier: Q7TMB8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     570-609: IADKSGSKKT...FFYTHLINFS → SSAELLRQLK...YTYPPLLTFG

Show »
Length:1,251
Mass (Da):144,977
Checksum:i1661EC8DF4A36400
GO

Sequence cautioni

The sequence BAD90235.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691A → G in AAC25773 (PubMed:9756361).Curated
Sequence conflicti342 – 3421Q → H in AAH47135 (PubMed:15489334).Curated
Sequence conflicti408 – 4081V → A in AAC25773 (PubMed:9756361).Curated
Sequence conflicti561 – 5611M → L in AAH52713 (PubMed:15489334).Curated
Sequence conflicti566 – 5661L → A in AAH52713 (PubMed:15489334).Curated
Sequence conflicti984 – 9841V → A in AAC25773 (PubMed:9756361).Curated
Sequence conflicti1079 – 10791D → H in AAC25773 (PubMed:9756361).Curated
Sequence conflicti1222 – 12221L → Q in BAC26130 (PubMed:16141072).Curated
Sequence conflicti1233 – 12331S → T in AAC25773 (PubMed:9756361).Curated
Sequence conflicti1238 – 12381H → Y in BAE27303 (PubMed:16141072).Curated
Sequence conflicti1238 – 12381H → Y in BAE31312 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei570 – 60940IADKS…LINFS → SSAELLRQLKSLGMERLLHV VNAFLRQSYTYPPLLTFG in isoform 2. 1 PublicationVSP_052348Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072697 mRNA. Translation: AAC25773.1.
AJ567911 mRNA. Translation: CAD99196.1.
AK028811 mRNA. Translation: BAC26130.1.
AK146613 mRNA. Translation: BAE27303.1.
AK152558 mRNA. Translation: BAE31312.1.
AK157773 mRNA. Translation: BAE34191.1.
AK220320 mRNA. Translation: BAD90235.1. Different initiation.
BC002174 mRNA. Translation: AAH02174.1.
BC047135 mRNA. Translation: AAH47135.2.
BC052713 mRNA. Translation: AAH52713.1.
BC054429 mRNA. Translation: AAH54429.1.
CCDSiCCDS21315.1. [Q7TMB8-1]
CCDS52262.1. [Q7TMB8-2]
PIRiT14349.
RefSeqiNP_001158133.1. NM_001164661.1. [Q7TMB8-1]
NP_001158134.1. NM_001164662.1.
NP_035500.2. NM_011370.3. [Q7TMB8-1]
XP_006540792.1. XM_006540729.1. [Q7TMB8-1]
UniGeneiMm.333893.
Mm.37249.

Genome annotation databases

EnsembliENSMUST00000032629; ENSMUSP00000032629; ENSMUSG00000030447. [Q7TMB8-1]
ENSMUST00000163845; ENSMUSP00000127717; ENSMUSG00000030447. [Q7TMB8-1]
GeneIDi20430.
KEGGimmu:20430.
UCSCiuc009hdk.2. mouse. [Q7TMB8-1]
uc009hdn.2. mouse. [Q7TMB8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072697 mRNA. Translation: AAC25773.1.
AJ567911 mRNA. Translation: CAD99196.1.
AK028811 mRNA. Translation: BAC26130.1.
AK146613 mRNA. Translation: BAE27303.1.
AK152558 mRNA. Translation: BAE31312.1.
AK157773 mRNA. Translation: BAE34191.1.
AK220320 mRNA. Translation: BAD90235.1. Different initiation.
BC002174 mRNA. Translation: AAH02174.1.
BC047135 mRNA. Translation: AAH47135.2.
BC052713 mRNA. Translation: AAH52713.1.
BC054429 mRNA. Translation: AAH54429.1.
CCDSiCCDS21315.1. [Q7TMB8-1]
CCDS52262.1. [Q7TMB8-2]
PIRiT14349.
RefSeqiNP_001158133.1. NM_001164661.1. [Q7TMB8-1]
NP_001158134.1. NM_001164662.1.
NP_035500.2. NM_011370.3. [Q7TMB8-1]
XP_006540792.1. XM_006540729.1. [Q7TMB8-1]
UniGeneiMm.333893.
Mm.37249.

3D structure databases

ProteinModelPortaliQ7TMB8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203226. 4 interactions.
IntActiQ7TMB8. 13 interactions.
MINTiMINT-203655.
STRINGi10090.ENSMUSP00000032629.

PTM databases

iPTMnetiQ7TMB8.
PhosphoSiteiQ7TMB8.
SwissPalmiQ7TMB8.

Proteomic databases

EPDiQ7TMB8.
MaxQBiQ7TMB8.
PaxDbiQ7TMB8.
PeptideAtlasiQ7TMB8.
PRIDEiQ7TMB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032629; ENSMUSP00000032629; ENSMUSG00000030447. [Q7TMB8-1]
ENSMUST00000163845; ENSMUSP00000127717; ENSMUSG00000030447. [Q7TMB8-1]
GeneIDi20430.
KEGGimmu:20430.
UCSCiuc009hdk.2. mouse. [Q7TMB8-1]
uc009hdn.2. mouse. [Q7TMB8-2]

Organism-specific databases

CTDi23191.
MGIiMGI:1338801. Cyfip1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3534. Eukaryota.
ENOG410XPKW. LUCA.
GeneTreeiENSGT00500000044831.
HOVERGENiHBG053209.
InParanoidiQ7TMB8.
KOiK05749.
OMAiLTSIMEL.
OrthoDBiEOG7ZSHS2.
PhylomeDBiQ7TMB8.
TreeFamiTF312925.

Enzyme and pathway databases

ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5663213. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

ChiTaRSiCyfip1. mouse.
PROiQ7TMB8.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TMB8.
CleanExiMM_CYFIP1.
MM_SRA1.
ExpressionAtlasiQ7TMB8. baseline and differential.
GenevisibleiQ7TMB8. MM.

Family and domain databases

InterProiIPR008081. Cytoplasmic_FMR1-int.
IPR009828. DUF1394.
[Graphical view]
PANTHERiPTHR12195. PTHR12195. 1 hit.
PfamiPF07159. DUF1394. 1 hit.
PF05994. FragX_IP. 1 hit.
[Graphical view]
PIRSFiPIRSF008153. FMR1_interacting. 1 hit.
PRINTSiPR01698. CYTOFMRPINTP.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of shyc, a novel gene expressed in the murine developing and adult nervous system."
    Koester F., Schinke B., Niemann S., Hermans-Borgmeyer I.
    Neurosci. Lett. 252:69-71(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: C57BL/6JImported.
    Tissue: BrainImported.
  2. "Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia formation."
    Steffen A., Rottner K., Ehinger J., Innocenti M., Scita G., Wehland J., Stradal T.E.B.
    EMBO J. 23:749-759(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COMPONENT OF WAVE2 COMPLEX, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: C57BL/6JImported.
    Tissue: BrainImported.
  3. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6JImported.
    Tissue: AmnionImported, Bone marrow macrophage, EmbryoImported and SkinImported.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal brainImported.
  5. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6JImported and FVB/NImported.
    Tissue: BrainImported, Mammary glandImported and Olfactory epithelium.
  6. "A highly conserved protein family interacting with the fragile X mental retardation protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P."
    Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.
    Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FMR1, SUBCELLULAR LOCATION.
  7. "The fragile X syndrome protein represses activity-dependent translation through CYFIP1, a new 4E-BP."
    Napoli I., Mercaldo V., Boyl P.P., Eleuteri B., Zalfa F., De Rubeis S., Di Marino D., Mohr E., Massimi M., Falconi M., Witke W., Costa-Mattioli M., Sonenberg N., Achsel T., Bagni C.
    Cell 134:1042-1054(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF4E AND FMR1, MUTAGENESIS OF ASP-724; LYS-725; ARG-726 AND GLU-730.
  8. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling in neurons."
    Yokoyama K., Tezuka T., Kotani M., Nakazawa T., Hoshina N., Shimoda Y., Kakuta S., Sudo K., Watanabe K., Iwakura Y., Yamamoto T.
    EMBO J. 30:4739-4754(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NYAP1; NYAP2 AND MYO16.

Entry informationi

Entry nameiCYFP1_MOUSE
AccessioniPrimary (citable) accession number: Q7TMB8
Secondary accession number(s): O88558
, Q3U7Q7, Q5DU50, Q7TSZ5, Q80VN6, Q8CE85, Q99LY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 1, 2003
Last modified: July 6, 2016
This is version 110 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

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 one 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.