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Protein

Cytoplasmic FMR1-interacting protein 2

Gene

Cyfip2

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

Functioni

Involved in T-cell adhesion and p53-dependent induction of apoptosis (By similarity). Does not bind RNA.By similarity1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell adhesion

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 2
Alternative name(s):
p53-inducible protein 121
Gene namesi
Name:Cyfip2Imported
Synonyms:Kiaa1168Imported, Pir121Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1924134. Cyfip2.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus By similarity
  • Cytoplasmperinuclear region 1 Publication
  • Cell junctionsynapsesynaptosome 1 Publication

  • Note: Highly expressed in the perinuclear region and enriched in synaptosomes (PubMed:11438699).1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus, Synapse, Synaptosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12531253Cytoplasmic FMR1-interacting protein 2PRO_0000279710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1037 – 10371N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ5SQX6.
MaxQBiQ5SQX6.
PaxDbiQ5SQX6.
PeptideAtlasiQ5SQX6.
PRIDEiQ5SQX6.

PTM databases

iPTMnetiQ5SQX6.
PhosphoSiteiQ5SQX6.

Expressioni

Tissue specificityi

Expressed in hippocampus (at protein level).1 Publication

Gene expression databases

BgeeiQ5SQX6.
CleanExiMM_CYFIP2.
ExpressionAtlasiQ5SQX6. baseline and differential.
GenevisibleiQ5SQX6. MM.

Interactioni

Subunit structurei

Component of the WAVE1 complex composed of ABI2, CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Interacts with FMR1, FXR1 AND FXR2 (PubMed:11438699). Interacts with FMR1; the interaction occurs in a RNA-dependent manner (By similarity). Interacts with RAC1 (activated form) which causes the complex to dissociate, releasing activated WASF1 (By similarity). The complex can also be activated by NCK1 (By similarity). Interacts with SHANK3; the interaction mediates the association of SHANK3 with the WAVE1 complex (PubMed:24153177).By similarity2 Publications

Protein-protein interaction databases

BioGridi218375. 1 interaction.
DIPiDIP-32111N.
IntActiQ5SQX6. 5 interactions.
STRINGi10090.ENSMUSP00000090853.

Structurei

3D structure databases

ProteinModelPortaliQ5SQX6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CYFIP family.Sequence analysis

Phylogenomic databases

eggNOGiKOG3534. Eukaryota.
ENOG410XPKW. LUCA.
GeneTreeiENSGT00500000044831.
HOVERGENiHBG053209.
InParanoidiQ5SQX6.
KOiK05749.
OMAiATNRFVK.
OrthoDBiEOG7ZSHS2.
PhylomeDBiQ5SQX6.
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.

Sequencei

Sequence statusi: Complete.

Q5SQX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTHVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSIMYQA NFDTNFEDRN
60 70 80 90 100
AFVTGIARYI EQATVHSSMN EMLEEGHDYA VMLYTWRSCS RAIPQVKCNE
110 120 130 140 150
QPNRVEIYEK TVEVLEPEVT KLMKFMYFQR KAIERFCSEV KRLCHAERRK
160 170 180 190 200
DFVSEAYLLT LGKFINMFAV LDELKNMKCS VKNDHSAYKR AAQFLRKMAD
210 220 230 240 250
PQSIQESQNL SMFLANHNRI TQCLHQQLEV IPGYEELLAD IVNICVDYYE
260 270 280 290 300
NKMYLTPSEK HMLLKVMGFG LYLMDGNVSN IYKLDAKKRI NLSKIDKFFK
310 320 330 340 350
QLQVVPLFGD MQIELARYIK TSAHYEENKS KWTCTQSSIS PQYNICEQMV
360 370 380 390 400
QIRDDHIRFI SELARYSNSE VVTGSGLDSQ KSDEEYRELF DLALRGLQLL
410 420 430 440 450
SKWSAHVMEV YSWKLVHPTD KFCNKDCPGT AEEYERATRY NYTSEEKFAF
460 470 480 490 500
VEVIAMIKGL QVLMGRMESV FNQAIRNTIY AALQDFAQVT LREPLRQAVR
510 520 530 540 550
KKKNVLISVL QAIRKTICDW EGGREPPNDP CLRGEKDPKG GFDIKVPRRA
560 570 580 590 600
VGPSSTQLYM VRTMLESLIA DKSGSKKTLR SSLDGPIVLA IEDFHKQSFF
610 620 630 640 650
FTHLLNISEA LQQCCDLSQL WFREFFLELT MGRRIQFPIE MSMPWILTDH
660 670 680 690 700
ILETKEPSMM EYVLYPLDLY NDSAYYALTK FKKQFLYDEI EAEVNLCFDQ
710 720 730 740 750
FVYKLADQIF AYYKAMAGSV LLDKRFRAEC KNYGVIIPYP PSNRYETLLK
760 770 780 790 800
QRHVQLLGRS IDLNRLITQR ISAAMYKSLD QAISRFESED LTSIVELEWL
810 820 830 840 850
LEINRLTHRL LCKHMTLDSF DAMFREANHN VSAPYGRITL HVFWELNFDF
860 870 880 890 900
LPNYCYNGST NRFVRTAIPF TQEPQRDKPA NVQPYYLYGS KPLNIAYSHI
910 920 930 940 950
YSSYRNFVGP PHFKTICRLL GYQGIAVVME ELLKIVKSLL QGTILQYVKT
960 970 980 990 1000
LIEVMPKICR LPRHEYGSPG ILEFFHHQLK DIIEYAELKT DVFQSLREVG
1010 1020 1030 1040 1050
NAILFCLLIE QALSQEEVCD LLHAAPFQNI LPRVYIKEGE RLEVRMKRLE
1060 1070 1080 1090 1100
AKYAPLHLVP LIERLGTPQQ IAIAREGDLL TKERLCCGLS MFEVILTRIR
1110 1120 1130 1140 1150
SYLQDPIWRG PPPTNGVMHV DECVEFHRLW SAMQFVYCIP VGTNEFTAEQ
1160 1170 1180 1190 1200
CFGDGLNWAG CSIIVLLGQQ RRFDLFDFCY HLLKVQRQDG KDEIIKNVPL
1210 1220 1230 1240 1250
KKMADRIRKY QILNNEVFAI LNKYMKSVET DSSTVEHVRC FQPPIHQSLA

TTC
Length:1,253
Mass (Da):145,659
Last modified:February 1, 2005 - v2
Checksum:i321011BF830F424E
GO

Sequence cautioni

The sequence BAC41472.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761G → V in BAC26942 (PubMed:16141072).Curated
Sequence conflicti229 – 2291E → G in BAE27779 (PubMed:16141072).Curated
Sequence conflicti242 – 2421V → A in BAE27779 (PubMed:16141072).Curated
Sequence conflicti678 – 6781L → P in BAC26942 (PubMed:16141072).Curated
Sequence conflicti1080 – 10801L → P in BAC26942 (PubMed:16141072).Curated

RNA editingi

Edited at position 320.1 Publication
Partially edited. Editing appears to be brain-specific.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti320 – 3201K → E in RNA edited version. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF334144 mRNA. Translation: AAK81821.1.
AB093288 mRNA. Translation: BAC41472.2. Different initiation.
AK030397 mRNA. Translation: BAC26942.1.
AK147224 mRNA. Translation: BAE27779.1.
AK147586 mRNA. Translation: BAE28010.1.
AK147632 mRNA. Translation: BAE28036.1.
AL662806, AL713958 Genomic DNA. Translation: CAI24844.2.
AL713958, AL662806 Genomic DNA. Translation: CAI25371.2.
AF162472 mRNA. Translation: AAD45803.1.
CCDSiCCDS24573.1.
RefSeqiNP_001239388.1. NM_001252459.1.
NP_001239389.1. NM_001252460.1.
NP_598530.2. NM_133769.3.
UniGeneiMm.154358.
Mm.454389.

Genome annotation databases

EnsembliENSMUST00000093165; ENSMUSP00000090853; ENSMUSG00000020340.
ENSMUST00000093166; ENSMUSP00000090854; ENSMUSG00000020340.
ENSMUST00000165599; ENSMUSP00000127586; ENSMUSG00000020340.
GeneIDi76884.
KEGGimmu:76884.
UCSCiuc007iob.2. mouse.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF334144 mRNA. Translation: AAK81821.1.
AB093288 mRNA. Translation: BAC41472.2. Different initiation.
AK030397 mRNA. Translation: BAC26942.1.
AK147224 mRNA. Translation: BAE27779.1.
AK147586 mRNA. Translation: BAE28010.1.
AK147632 mRNA. Translation: BAE28036.1.
AL662806, AL713958 Genomic DNA. Translation: CAI24844.2.
AL713958, AL662806 Genomic DNA. Translation: CAI25371.2.
AF162472 mRNA. Translation: AAD45803.1.
CCDSiCCDS24573.1.
RefSeqiNP_001239388.1. NM_001252459.1.
NP_001239389.1. NM_001252460.1.
NP_598530.2. NM_133769.3.
UniGeneiMm.154358.
Mm.454389.

3D structure databases

ProteinModelPortaliQ5SQX6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218375. 1 interaction.
DIPiDIP-32111N.
IntActiQ5SQX6. 5 interactions.
STRINGi10090.ENSMUSP00000090853.

PTM databases

iPTMnetiQ5SQX6.
PhosphoSiteiQ5SQX6.

Proteomic databases

EPDiQ5SQX6.
MaxQBiQ5SQX6.
PaxDbiQ5SQX6.
PeptideAtlasiQ5SQX6.
PRIDEiQ5SQX6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000093165; ENSMUSP00000090853; ENSMUSG00000020340.
ENSMUST00000093166; ENSMUSP00000090854; ENSMUSG00000020340.
ENSMUST00000165599; ENSMUSP00000127586; ENSMUSG00000020340.
GeneIDi76884.
KEGGimmu:76884.
UCSCiuc007iob.2. mouse.

Organism-specific databases

CTDi26999.
MGIiMGI:1924134. Cyfip2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3534. Eukaryota.
ENOG410XPKW. LUCA.
GeneTreeiENSGT00500000044831.
HOVERGENiHBG053209.
InParanoidiQ5SQX6.
KOiK05749.
OMAiATNRFVK.
OrthoDBiEOG7ZSHS2.
PhylomeDBiQ5SQX6.
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

ChiTaRSiCyfip2. mouse.
PROiQ5SQX6.
SOURCEiSearch...

Gene expression databases

BgeeiQ5SQX6.
CleanExiMM_CYFIP2.
ExpressionAtlasiQ5SQX6. baseline and differential.
GenevisibleiQ5SQX6. 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. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FMR1; FXR1 AND FXR2, SUBCELLULAR LOCATION.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
    DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
    Strain: C57BL/6JImported.
    Tissue: BrainImported, KidneyImported and PituitaryImported.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-367.
  6. Cited for: RNA EDITING OF POSITION 320.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Pancreas and Spleen.
  8. "SHANK3 overexpression causes manic-like behaviour with unique pharmacogenetic properties."
    Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J., Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C., Zoghbi H.Y.
    Nature 503:72-77(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHANK3, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCYFP2_MOUSE
AccessioniPrimary (citable) accession number: Q5SQX6
Secondary accession number(s): Q3UH21
, Q3UHS8, Q8BSW0, Q8CHA9, Q924D3, Q9R181
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: February 1, 2005
Last modified: July 6, 2016
This is version 94 of the entry and version 2 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.