CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037158
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Cytoplasmic FMR1-interacting protein 2 
Protein Synonyms/Alias
  
Gene Name
 CYFIP2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
110NRVEIYEKTVEVLEPubiquitination[1, 2]
121VLEPEVTKLMKFMYFubiquitination[2]
124PEVTKLMKFMYFQRKubiquitination[2]
141ERFCSEVKRLCHAERubiquitination[2, 3]
150LCHAERRKDFVSEAYubiquitination[2]
175FAVLDELKNMKCSVKubiquitination[2]
182KNMKCSVKNDHSAYKacetylation[3]
197RAAQFLRKMADPQSIubiquitination[2]
260MYLTPSEKHMLLKVMubiquitination[2]
294KKRINLSKIDKFFKQubiquitination[2, 3]
297INLSKIDKFFKQLQVubiquitination[2]
320IELARYIKTSAHYEEubiquitination[1, 2, 3]
331HYEENKSKWTCTQSSubiquitination[2]
381GSGLDSQKSDEEYREubiquitination[2]
421KLVHPTDKFCNKDCPubiquitination[2, 3]
425PTDKFCNKDCPGTAEubiquitination[2, 3]
539LRGEKDPKGGFDIKVubiquitination[3]
545PKGGFDIKVPRRAVGubiquitination[2, 3, 4]
572LESLIADKSGSKKTLubiquitination[1, 2, 3]
724AGSVLLDKRFRAECKubiquitination[2]
731KRFRAECKNYGVIIPubiquitination[2]
750NRYETLLKQRHVQLLubiquitination[1, 2, 3]
777RISAAMYKSLDQAISubiquitination[1, 2, 3]
813LTHRLLCKHMTLDSFubiquitination[2, 3]
878TQEPQRDKPANVQPYubiquitination[2, 5]
891PYYLYGSKPLNIAYSubiquitination[2]
914FVGPPHFKTICRLLGubiquitination[2, 3]
957TLIEVMPKICRLPRHubiquitination[2]
1037ILPRVYIKEGERLEVubiquitination[2, 3]
1052RMKRLEAKYAPLHLVubiquitination[2, 3, 4, 5]
1082REGDLLTKERLCCGLubiquitination[1, 2, 3, 6]
1191KVQRQDGKDEIIKNVubiquitination[2]
1209KMADRIRKYQILNNEubiquitination[2, 3]
1223EVFAILNKYMKSVETubiquitination[2]
1226AILNKYMKSVETDSSubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1253 AA 
Protein Sequence
MTTHVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSIMYQA NFDTNFEDRN AFVTGIARYI 60
EQATVHSSMN EMLEEGHEYA VMLYTWRSCS RAIPKVKCNE QPNRVEIYEK TVEVLEPEVT 120
KLMKFMYFQR KAIERFCSEV KRLCHAERRK DFVSEAYLLT LGKFINMFAV LDELKNMKCS 180
VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNRI TQCLHQQLEV IPGYEELLAD 240
IVNICVDYYE NKMYLTPSEK HMLLKVMGFG LYLMDGNVSN IYKLDAKKRI NLSKIDKFFK 300
QLQVVPLFGD MQIELARYIK TSAHYEENKS KWTCTQSSIS PQYNICEQMV QIRDDHIRFI 360
SELARYSNSE VVTGSGLDSQ KSDEEYRELF DLALRGLQLL SKWSAHVMEV YSWKLVHPTD 420
KFCNKDCPGT AEEYERATRY NYTSEEKFAF VEVIAMIKGL QVLMGRMESV FNQAIRNTIY 480
AALQDFAQVT LREPLRQAVR KKKNVLISVL QAIRKTICDW EGGREPPNDP CLRGEKDPKG 540
GFDIKVPRRA VGPSSTQLYM VRTMLESLIA DKSGSKKTLR SSLDGPIVLA IEDFHKQSFF 600
FTHLLNISEA LQQCCDLSQL WFREFFLELT MGRRIQFPIE MSMPWILTDH ILETKEPSMM 660
EYVLYPLDLY NDSAYYALTK FKKQFLYDEI EAEVNLCFDQ FVYKLADQIF AYYKAMAGSV 720
LLDKRFRAEC KNYGVIIPYP PSNRYETLLK QRHVQLLGRS IDLNRLITQR ISAAMYKSLD 780
QAISRFESED LTSIVELEWL LEINRLTHRL LCKHMTLDSF DAMFREANHN VSAPYGRITL 840
HVFWELNFDF LPNYCYNGST NRFVRTAIPF TQEPQRDKPA NVQPYYLYGS KPLNIAYSHI 900
YSSYRNFVGP PHFKTICRLL GYQGIAVVME ELLKIVKSLL QGTILQYVKT LIEVMPKICR 960
LPRHEYGSPG ILEFFHHQLK DIIEYAELKT DVFQSLREVG NAILFCLLIE QALSQEEVCD 1020
LLHAAPFQNI LPRVYIKEGE RLEVRMKRLE AKYAPLHLVP LIERLGTPQQ IAIAREGDLL 1080
TKERLCCGLS MFEVILTRIR SYLQDPIWRG PPPTNGVMHV DECVEFHRLW SAMQFVYCIP 1140
VGTNEFTAEQ CFGDGLNWAG CSIIVLLGQQ RRFDLFDFCY HLLKVQRQDG KDEIIKNVPL 1200
KKMADRIRKY QILNNEVFAI LNKYMKSVET DSSTVEHVRC FQPPIHQSLA TTC 1253 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro. 
Interpro
 IPR008081; Cytoplasmic_FMR1-int.
 IPR016536; Cytoplasmic_FMR1-int_sub. 
Pfam
 PF05994; FragX_IP 
SMART
  
PROSITE
  
PRINTS
 PR01698; CYTOFMRPINTP.