CYFP1_MOUSE - dbPTM
CYFP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYFP1_MOUSE
UniProt AC Q7TMB8
Protein Name Cytoplasmic FMR1-interacting protein 1
Gene Name Cyfip1 {ECO:0000312|EMBL:AAH54429.1, ECO:0000312|MGI:MGI:1338801}
Organism Mus musculus (Mouse).
Sequence Length 1253
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region . Cell projection, lamellipodium . Cell projection, ruffle . Cell junction, synapse, synaptosome . Highly expressed in the perinuclear region (PubMed:11438699). Enriched in synaptosomes (PubMed:11438699). Als
Protein Description 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. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes. [PubMed: 27605705]
Protein Sequence MAAQVTLEDALSNVDLLEELPLPDQQPCIEPPPSSLLYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGQEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMNFMYFQRNAIERFCGEVRRLCHAERRKDFVSEAYLITLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNKITQSLQQQLEVISGYEELLADIVNLCVDYYENRMYLTPSEKHMLLKVMGFGLYLMDGSVSNIYKLDAKKRINLSKIDKYFKQLQVVPLFGDMQIELARYIKTSAHYEENKSRWTCASSSSSPQYNICEQMIQIREDHMRFISELARYSNSEVVTGSGRQEAQKTDAEYRKLFDLALQGLQLLSQWSAHVMEVYSWKLVHPTDKYSNKDCPDNAEEYERATRYNYTTEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTVYAALQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFSETLQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTKFNKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVMAGSLLLDKRLRSECKNQGATIHLPPSNRYETLLKQRHVQLLGRSIDLNRLITQRVSAAMYKSLELAIGRFESEDLTSVVELDGLLEINRMTHKLLSRYLTLDSFDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTVLPFSQEFQRDKQPNAQPQYLHGSKALNLAYSSIYGSYRNFVGPPHFQVICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKICRLPRHEYGSPGILEFFHHQLKDIVEYAELKTVCFQNLREVGNAVLFCLLIEQSLSLEEVCDLLHAAPFQNILPRIHVKEGERVDAKMKRLESKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRTFLDDPIWRGPLPSNGVMHVDECVEFHRLWSAMQFVYCIPVGTHEFTVEQCFGDGLHWAGCMIIVLLGQQRRFAVLDFCYHLLKVQKHDGKDEIIKNVPLKKMVERIRKFQILNDEIITILDKYLKSGDGESTPVEHVRCFQPPIHQSLASS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
79PhosphorylationMLEEGQEYAVMLYTW
HHHHHHHHHHHHHHH
9.16-
97UbiquitinationSRAIPQVKCNEQPNR
HCCCCCCCCCCCCCC
26.54-
108PhosphorylationQPNRVEIYEKTVEVL
CCCCEEEEEHHHHHH
9.6222817900
197 (in isoform 2)Ubiquitination-40.3622790023
197UbiquitinationRAAQFLRKMADPQSI
HHHHHHHHHCCHHHH
40.3622790023
277PhosphorylationGLYLMDGSVSNIYKL
EEEEECCCCCCEEEC
20.3625338131
322PhosphorylationLARYIKTSAHYEENK
HHHHHHHHHCCCCCC
14.19-
346GlutathionylationSSPQYNICEQMIQIR
CCCCCCHHHHHHHHH
2.3724333276
366PhosphorylationFISELARYSNSEVVT
HHHHHHHHCCCCCCC
13.44-
367PhosphorylationISELARYSNSEVVTG
HHHHHHHCCCCCCCC
28.46-
420PhosphorylationSWKLVHPTDKYSNKD
HEEEECCCCCCCCCC
30.19-
426 (in isoform 2)Ubiquitination-55.5622790023
426UbiquitinationPTDKYSNKDCPDNAE
CCCCCCCCCCCCCHH
55.5622790023
560PhosphorylationGPSSTQLYMVRTMLE
CCCHHHHHHHHHHHH
5.4629514104
579PhosphorylationDKSGSKKTLRSSLEG
CCCCCCCHHHHHCCC
31.0123984901
582PhosphorylationGSKKTLRSSLEGPTI
CCCCHHHHHCCCCEE
42.2429472430
583PhosphorylationSKKTLRSSLEGPTIL
CCCHHHHHCCCCEEE
24.8123984901
748PhosphorylationPPSNRYETLLKQRHV
CCCCHHHHHHHHHHH
28.58-
751UbiquitinationNRYETLLKQRHVQLL
CHHHHHHHHHHHHHH
48.69-
808PhosphorylationLLEINRMTHKLLSRY
HHHHHHHHHHHHHHH
16.7822982522
872PhosphorylationVRTVLPFSQEFQRDK
EEHHHCCCHHHHHCC
27.1928507225
887PhosphorylationQPNAQPQYLHGSKAL
CCCCCCCHHCHHHHH
13.8325777480
891PhosphorylationQPQYLHGSKALNLAY
CCCHHCHHHHHHHHH
12.1925777480
935AcetylationVVMEELLKVVKSLLQ
HHHHHHHHHHHHHHH
58.577624067
967PhosphorylationCRLPRHEYGSPGILE
HCCCCHHHCCCCHHH
19.4425367039
969PhosphorylationLPRHEYGSPGILEFF
CCCHHHCCCCHHHHH
21.0325367039
1051 (in isoform 2)Ubiquitination-49.57-
1052PhosphorylationAKMKRLESKYAPLHL
HHHHHHHHHCCCHHH
35.24-
1053UbiquitinationKMKRLESKYAPLHLV
HHHHHHHHCCCHHHH
35.7422790023
1053 (in isoform 2)Ubiquitination-35.7422790023
1054PhosphorylationMKRLESKYAPLHLVP
HHHHHHHCCCHHHHH
23.8029514104
1068PhosphorylationPLIERLGTPQQIAIA
HHHHHHCCHHHHHHH
23.6326824392
1197AcetylationDGKDEIIKNVPLKKM
CCCCCHHHCCCHHHH
58.51-
1233PhosphorylationLKSGDGESTPVEHVR
HHCCCCCCCCCHHEE
43.4724719451
1234PhosphorylationKSGDGESTPVEHVRC
HCCCCCCCCCHHEEE
27.3530635358

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CYFP1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYFP1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CYFP1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AAK1_MOUSEAak1physical
28671696
ABI1_MOUSEAbi1physical
28671696
ACTB_MOUSEActbphysical
28671696
AGAP2_MOUSEAgap2physical
28671696
ANK2_MOUSEAnk2physical
28671696
ANR17_MOUSEAnkrd17physical
28671696
AP1B1_MOUSEAp1b1physical
28671696
AP1S1_MOUSEAp1s1physical
28671696
AP2A1_MOUSEAp2a1physical
28671696
AP2B1_MOUSEAp2b1physical
28671696
ARF3_MOUSEArf3physical
28671696
ARHG2_MOUSEArhgef2physical
28671696
ARPC4_MOUSEArpc4physical
28671696
BAIP2_MOUSEBaiap2physical
28671696
KCC2A_MOUSECamk2aphysical
28671696
KCC2B_MOUSECamk2bphysical
28671696
CAMKV_MOUSECamkvphysical
28671696
CAZA2_MOUSECapza2physical
28671696
TCPG_MOUSECct3physical
28671696
CNTP1_MOUSECntnap1physical
28671696
DPYL1_MOUSECrmp1physical
28671696
CUL3_MOUSECul3physical
28671696
CYFP2_MOUSECyfip2physical
28671696
DREB_MOUSEDbn1physical
28671696
DCLK1_MOUSEDclk1physical
28671696
DCTN1_MOUSEDctn1physical
28671696
DLG2_MOUSEDlg2physical
28671696
DLG4_MOUSEDlg4physical
28671696
AUXI_MOUSEDnajc6physical
28671696
DYN1_MOUSEDnm1physical
28671696
DNM1L_MOUSEDnm1lphysical
28671696
DYN2_MOUSEDnm2physical
28671696
DYN3_MOUSEDnm3physical
28671696
DPYL2_MOUSEDpysl2physical
28671696
DEST_MOUSEDstnphysical
28671696
DYHC1_MOUSEDync1h1physical
28671696
EF1A2_MOUSEEef1a2physical
28671696
E41L1_MOUSEEpb4.1l1physical
28671696
E41L3_MOUSEEpb4.1l3physical
28671696
ERC2_MOUSEErc2physical
28671696
ERF1_MOUSEEtf1physical
28671696
FARP1_MOUSEFarp1physical
28671696
URP2_MOUSEFermt3physical
28671696
GLNA_MOUSEGlulphysical
28671696
GOGA2_MOUSEGolga2physical
28671696
NMDE1_MOUSEGrin2aphysical
28671696
GRM3_MOUSEGrm3physical
28671696
GSK3B_MOUSEGsk3bphysical
28671696
IMDH2_MOUSEImpdh2physical
28671696
IPO4_MOUSEIpo4physical
28671696
IQEC1_MOUSEIqsec1physical
28671696
KCNB1_MOUSEKcnb1physical
28671696
KIF2A_MOUSEKif2aphysical
28671696
LRC24_MOUSELrrc24physical
28671696
MATR3_MOUSEMatr3physical
28671696
MFN2_MOUSEMfn2physical
28671696
MYO5A_MOUSEMyo5aphysical
28671696
NCAN_MOUSENcanphysical
28671696
NCDN_MOUSENcdnphysical
28671696
NCKP1_MOUSENckap1physical
28671696
NFH_MOUSENefhphysical
28671696
NFL_MOUSENeflphysical
28671696
NFM_MOUSENefmphysical
28671696
PSA_MOUSENpeppsphysical
28671696
NSF_MOUSENsfphysical
28671696
NTRK2_MOUSENtrk2physical
28671696
NUMBL_MOUSENumblphysical
28671696
NYAP2_MOUSENyap2physical
28671696
OPA1_MOUSEOpa1physical
28671696
P2RX7_MOUSEP2rx7physical
28671696
PDC6I_MOUSEPdcd6ipphysical
28671696
PDE4A_MOUSEPde4aphysical
28671696
PHAR1_MOUSEPhactr1physical
28671696
PICAL_MOUSEPicalmphysical
28671696
PP1G_MOUSEPpp1ccphysical
28671696
PPCEL_MOUSEPreplphysical
28671696
KPCB_MOUSEPrkcbphysical
28671696
KPCE_MOUSEPrkcephysical
28671696
KPCG_MOUSEPrkcgphysical
28671696
PROX1_MOUSEProx1physical
28671696
PTN9_MOUSEPtpn9physical
28671696
RAC1_MOUSERac1physical
28671696
RPGF2_MOUSERapgef2physical
28671696
RHEB_MOUSERhebphysical
28671696
RHOC_MOUSERhocphysical
28671696
RL27_MOUSERpl27physical
28671696
KS6B1_MOUSERps6kb1physical
28671696
RTN1_MOUSERtn1physical
28671696
MTMR5_MOUSESbf1physical
28671696
SGIP1_MOUSESgip1physical
28671696
SHAN1_MOUSEShank1physical
28671696
SHAN3_MOUSEShank3physical
28671696
S4A8_MOUSESlc4a8physical
28671696
AP180_MOUSESnap91physical
28671696
SPTB2_MOUSESptbn1physical
28671696
SYGP1_MOUSESyngap1physical
28671696
TPD54_MOUSETpd52l2physical
28671696
TPPC3_MOUSETrappc3physical
28671696
TRIM3_MOUSETrim3physical
28671696
TRPC4_MOUSETrpc4physical
28671696
UBA6_MOUSEUba6physical
28671696
UBE2O_MOUSEUbe2ophysical
28671696
WASF1_MOUSEWasf1physical
28671696

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CYFP1_MOUSE

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Related Literatures of Post-Translational Modification

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