CYFP2_HUMAN - dbPTM
CYFP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYFP2_HUMAN
UniProt AC Q96F07
Protein Name Cytoplasmic FMR1-interacting protein 2
Gene Name CYFIP2 {ECO:0000312|EMBL:AAH11762.1}
Organism Homo sapiens (Human).
Sequence Length 1278
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, perinuclear region . Cell junction, synapse, synaptosome . Highly expressed in the perinuclear regionand enriched in synaptosomes (By similarity). Treatment with leptomycin-B triggers translocation to the nucleus (Pub
Protein Description Involved in T-cell adhesion and p53/TP53-dependent induction of apoptosis. Does not bind RNA. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity)..
Protein Sequence MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLTLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLADIVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIKTSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLLSKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIYAALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQACQWSPRALFHPTGGTQGRRGCRSLLYMVRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKAMAGSVLLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAMYKSLDQAISRFESEDLTSIVELEWLLEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYCYNGSTNRFVRTAIPFTQEPQRDKPANVQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKIVKSLLQGTILQYVKTLIEVMPKICRLPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQEEVCDLLHAAPFQNILPRVYIKEGERLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSYLQDPIWRGPPPTNGVMHVDECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDLFDFCYHLLKVQRQDGKDEIIKNVPLKKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC
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
54PhosphorylationEDRNAFVTGIARYIE
HHHHHHHHHHHHHHH		19.2023403867
64PhosphorylationARYIEQATVHSSMNE
HHHHHHHHHCHHHHH		20.6023403867
67PhosphorylationIEQATVHSSMNEMLE
HHHHHHCHHHHHHHH		27.2623403867
79PhosphorylationMLEEGHEYAVMLYTW
HHHHCHHHHHHHHHH		9.9823403867
97UbiquitinationSRAIPQVKCNEQPNR
CCCCCCCCCCCCCCC		26.54-
108PhosphorylationQPNRVEIYEKTVEVL
CCCCEEEEEHHHHHH		9.6219605366
110UbiquitinationNRVEIYEKTVEVLEP
CCEEEEEHHHHHHCH		40.68-
110 (in isoform 1)Ubiquitination-40.6821890473
110 (in isoform 2)Ubiquitination-40.6821890473
121UbiquitinationVLEPEVTKLMKFMYF
HHCHHHHHHHHHHHH		52.32-
124UbiquitinationPEVTKLMKFMYFQRK
HHHHHHHHHHHHHHH		37.10-
141AcetylationERFCSEVKRLCHAER
HHHHHHHHHHHHHHH		35.2825953088
141UbiquitinationERFCSEVKRLCHAER
HHHHHHHHHHHHHHH		35.28-
150UbiquitinationLCHAERRKDFVSEAY
HHHHHHHHCCCCHHH		62.83-
175UbiquitinationFAVLDELKNMKCSVK
HHHHHHHHCCCCCCC		53.61-
180PhosphorylationELKNMKCSVKNDHSA
HHHCCCCCCCCCHHH		30.5225367160
182AcetylationKNMKCSVKNDHSAYK
HCCCCCCCCCHHHHH		40.12-
182UbiquitinationKNMKCSVKNDHSAYK
HCCCCCCCCCHHHHH		40.12-
189AcetylationKNDHSAYKRAAQFLR
CCCHHHHHHHHHHHH		34.9712437991
197AcetylationRAAQFLRKMADPQSI
HHHHHHHHHCCHHHH		40.3612438001
197UbiquitinationRAAQFLRKMADPQSI
HHHHHHHHHCCHHHH		40.36-
254PhosphorylationDYYENKMYLTPSEKH
HHHCCCCCCCHHHHH		14.72-
256PhosphorylationYENKMYLTPSEKHML
HCCCCCCCHHHHHHH		13.79-
260UbiquitinationMYLTPSEKHMLLKVM
CCCCHHHHHHHHHHH		38.36-
279PhosphorylationYLMDGNVSNIYKLDA
EEECCCCCCEEECCH		22.85-
294UbiquitinationKKRINLSKIDKFFKQ
HHCCCHHHHHHHHHH		59.08-
297UbiquitinationINLSKIDKFFKQLQV
CCHHHHHHHHHHCCC		57.06-
320UbiquitinationIELARYIKTSAHYEE
HHHHHHHHHHHCCCC		27.74-
320 (in isoform 1)Ubiquitination-27.7421890473
320 (in isoform 2)Ubiquitination-27.7421890473
322PhosphorylationLARYIKTSAHYEENK
HHHHHHHHHCCCCCC		14.1924719451
325PhosphorylationYIKTSAHYEENKSKW
HHHHHHCCCCCCCCC		25.3428796482
331UbiquitinationHYEENKSKWTCTQSS
CCCCCCCCCEEECCC		48.40-
366PhosphorylationFISELARYSNSEVVT
HHHHHHHHCCCCEEC		13.44-
367PhosphorylationISELARYSNSEVVTG
HHHHHHHCCCCEECC		28.46-
381UbiquitinationGSGLDSQKSDEEYRE
CCCCCCCCCHHHHHH		64.92-
401PhosphorylationLRGLQLLSKWSAHVM
HHHHHHHHHHHHHHH		40.4424719451
419PhosphorylationSWKLVHPTDKFCNKD
HEEEECCCCCCCCCC		36.6224719451
421AcetylationKLVHPTDKFCNKDCP
EEECCCCCCCCCCCC		55.0525953088
421UbiquitinationKLVHPTDKFCNKDCP
EEECCCCCCCCCCCC		55.05-
425UbiquitinationPTDKFCNKDCPGTAE
CCCCCCCCCCCCCHH		62.99-
430PhosphorylationCNKDCPGTAEEYERA
CCCCCCCCHHHHHHH		18.9528796482
434PhosphorylationCPGTAEEYERATRYN
CCCCHHHHHHHHHCC		11.3928796482
438PhosphorylationAEEYERATRYNYTSE
HHHHHHHHHCCCCCH		39.6521945579
440PhosphorylationEYERATRYNYTSEEK
HHHHHHHCCCCCHHH		14.2521945579
442PhosphorylationERATRYNYTSEEKFA
HHHHHCCCCCHHHHH		11.6021945579
443PhosphorylationRATRYNYTSEEKFAF
HHHHCCCCCHHHHHH		26.4821945579
444PhosphorylationATRYNYTSEEKFAFV
HHHCCCCCHHHHHHH		33.1421945579
467SulfoxidationLQVLMGRMESVFNQA
HHHHHHHHHHHHHHH		3.5921406390
469PhosphorylationVLMGRMESVFNQAIR
HHHHHHHHHHHHHHH		23.7522210691
490PhosphorylationLQDFAQVTLREPLRQ
HHHHHHHHCCHHHHH		14.1722210691
508PhosphorylationKKKNVLISVLQAIRK
HHCHHHHHHHHHHHH		16.7721406692
539UbiquitinationLRGEKDPKGGFDIKV
CCCCCCCCCCCCCCC		80.12-
545UbiquitinationPKGGFDIKVPRRAVG
CCCCCCCCCCCCCCC		48.29-
555PhosphorylationRRAVGPSSTQACQWS
CCCCCCCCCCCCCCC		27.8924532841
562PhosphorylationSTQACQWSPRALFHP
CCCCCCCCCCCCCCC		4.4224719451
572 (in isoform 2)Ubiquitination-19.8321890473
573PhosphorylationLFHPTGGTQGRRGCR
CCCCCCCCCCHHHHH		29.2424532841
588PhosphorylationSLLYMVRTMLESLIA
HHHHHHHHHHHHHHC		18.0720068231
592PhosphorylationMVRTMLESLIADKSG
HHHHHHHHHHCCCCC		22.5520068231
597UbiquitinationLESLIADKSGSKKTL
HHHHHCCCCCCCHHH		47.93-
597 (in isoform 1)Ubiquitination-47.9321890473
598PhosphorylationESLIADKSGSKKTLR
HHHHCCCCCCCHHHH		49.1720068231
600PhosphorylationLIADKSGSKKTLRSS
HHCCCCCCCHHHHHH		37.7624719451
603PhosphorylationDKSGSKKTLRSSLDG
CCCCCCHHHHHHCCC		31.01-
606PhosphorylationGSKKTLRSSLDGPIV
CCCHHHHHHCCCCEE		38.0624076635
607PhosphorylationSKKTLRSSLDGPIVL
CCHHHHHHCCCCEEE		24.8527690223
673PhosphorylationMSMPWILTDHILETK
CCCHHHHHHCHHCCC		19.1927067055
679PhosphorylationLTDHILETKEPSMME
HHHCHHCCCCCCCCC		36.9427067055
749UbiquitinationAGSVLLDKRFRAECK
CCCHHHCHHHHHHHH		54.10-
750 (in isoform 2)Ubiquitination-26.4221890473
756UbiquitinationKRFRAECKNYGVIIP
HHHHHHHHCCCEEEE		44.71-
775UbiquitinationNRYETLLKQRHVQLL
HHHHHHHHHHHHHHH		48.6921906983
775 (in isoform 1)Ubiquitination-48.6921890473
777 (in isoform 2)Ubiquitination-30.2921890473
802UbiquitinationRISAAMYKSLDQAIS
HHHHHHHHCHHHHHH		31.3021906983
802 (in isoform 1)Ubiquitination-31.3021890473
838UbiquitinationLTHRLLCKHMTLDSF
HHHHHHHHHCCHHHH		36.06-
857PhosphorylationREANHNVSAPYGRIT
HHHCCCCCCCCCEEE		28.9228152594
860PhosphorylationNHNVSAPYGRITLHV
CCCCCCCCCEEEEEE		20.8228152594
864PhosphorylationSAPYGRITLHVFWEL
CCCCCEEEEEEEEEC		14.9523898821
878 (in isoform 2)Ubiquitination-41.4721890473
879PhosphorylationNFDFLPNYCYNGSTN
CCCCCCCCCCCCCCC		8.3823898821
881PhosphorylationDFLPNYCYNGSTNRF
CCCCCCCCCCCCCCE		16.5223898821
884PhosphorylationPNYCYNGSTNRFVRT
CCCCCCCCCCCEEEE		20.9023898821
885PhosphorylationNYCYNGSTNRFVRTA
CCCCCCCCCCEEEEC		31.6323898821
896PhosphorylationVRTAIPFTQEPQRDK
EEECCCCCCCCCCCC		27.0322210691
903UbiquitinationTQEPQRDKPANVQPY
CCCCCCCCCCCCCCE		48.4921890473
903 (in isoform 1)Ubiquitination-48.4921890473
911PhosphorylationPANVQPYYLYGSKPL
CCCCCCEEEECCCCC		10.5120090780
915PhosphorylationQPYYLYGSKPLNIAY
CCEEEECCCCCCHHH		19.9724719451
916UbiquitinationPYYLYGSKPLNIAYS
CEEEECCCCCCHHHH		49.51-
939UbiquitinationFVGPPHFKTICRLLG
CCCCCHHHHHHHHHC		33.67-
963PhosphorylationELLKIVKSLLQGTIL
HHHHHHHHHHHHHHH		24.3429978859
968PhosphorylationVKSLLQGTILQYVKT
HHHHHHHHHHHHHHH		12.9329978859
972PhosphorylationLQGTILQYVKTLIEV
HHHHHHHHHHHHHHH		10.6429978859
982UbiquitinationTLIEVMPKICRLPRH
HHHHHHHHHHCCCCH		36.02-
991PhosphorylationCRLPRHEYGSPGILE
HCCCCHHHCCCCHHH		19.44-
1020PhosphorylationLKTDVFQSLREVGNA
HCHHHHHHHHHHHHH		20.2324719451
1037AcetylationFCLLIEQALSQEEVC
HHHHHHHHCCHHHHH		9.0819608861
1037UbiquitinationFCLLIEQALSQEEVC
HHHHHHHHCCHHHHH		9.0819608861
1052 (in isoform 2)Ubiquitination-8.1321890473
1062AcetylationILPRVYIKEGERLEV
CCCEEEEECCCCCHH		41.8119608861
1062UbiquitinationILPRVYIKEGERLEV
CCCEEEEECCCCCHH		41.8119608861
1072UbiquitinationERLEVRMKRLEAKYA
CCCHHHHHHHHHHCC		43.18-
1077AcetylationRMKRLEAKYAPLHLV
HHHHHHHHCCCHHHH		32.3525953088
1077UbiquitinationRMKRLEAKYAPLHLV
HHHHHHHHCCCHHHH		32.3521890473
1077 (in isoform 1)Ubiquitination-32.3521890473
1078PhosphorylationMKRLEAKYAPLHLVP
HHHHHHHCCCHHHHH		22.0928152594
1082 (in isoform 2)Ubiquitination-24.5821890473
1092PhosphorylationPLIERLGTPQQIAIA
HHHHHHCCHHHHHHH		23.6325159151
1107UbiquitinationREGDLLTKERLCCGL
HCCCCCCHHHHHHHH		40.58-
1107 (in isoform 1)Ubiquitination-40.5821890473
1216UbiquitinationKVQRQDGKDEIIKNV
HHHHHCCCCHHHHCC		61.55-
1221UbiquitinationDGKDEIIKNVPLKKM
CCCCHHHHCCCHHHH		58.51-
1234UbiquitinationKMADRIRKYQILNNE
HHHHHHHHHHHHCHH		38.85-
1248UbiquitinationEVFAILNKYMKSVET
HHHHHHHHHHHHCCC		43.19-
1249PhosphorylationVFAILNKYMKSVETD
HHHHHHHHHHHCCCC		14.5424719451
1251UbiquitinationAILNKYMKSVETDSS
HHHHHHHHHCCCCCC		48.54-
1258PhosphorylationKSVETDSSTVEHVRC
HHCCCCCCCCCEEEC		39.0024719451
1277O-linked_GlycosylationIHQSLATTC------
CHHHHHCCC------		15.6023301498
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 CYFP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYFP2_HUMAN !!
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 CYFP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FMR1_HUMANFMR1physical
12837692
NCKP1_ARATHGRLphysical
15294869
RAC4_ARATHROP2physical
15294869
PLMN_HUMANPLGphysical
21988832
SMAD4_HUMANSMAD4physical
21988832
ZC12A_HUMANZC3H12Aphysical
21988832
WASF1_HUMANWASF1physical
26344197
WASF2_HUMANWASF2physical
26344197
WASF3_HUMANWASF3physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CYFP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1062, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108, AND MASSSPECTROMETRY.

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