CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019224
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytoplasmic FMR1-interacting protein 2 
Protein Synonyms/Alias
 p53-inducible protein 121 
Gene Name
 CYFIP2 
Gene Synonyms/Alias
 KIAA1168; PIR121 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
97SRAIPQVKCNEQPNRubiquitination[1]
110NRVEIYEKTVEVLEPubiquitination[1]
121VLEPEVTKLMKFMYFubiquitination[1]
124PEVTKLMKFMYFQRKubiquitination[1]
141ERFCSEVKRLCHAERubiquitination[1]
150LCHAERRKDFVSEAYubiquitination[1]
175FAVLDELKNMKCSVKubiquitination[1]
197RAAQFLRKMADPQSIubiquitination[1]
260MYLTPSEKHMLLKVMubiquitination[1]
294KKRINLSKIDKFFKQubiquitination[1]
297INLSKIDKFFKQLQVubiquitination[1]
320IELARYIKTSAHYEEubiquitination[1]
331HYEENKSKWTCTQSSubiquitination[1]
381GSGLDSQKSDEEYREubiquitination[1]
421KLVHPTDKFCNKDCPubiquitination[1]
425PTDKFCNKDCPGTAEubiquitination[1]
545PKGGFDIKVPRRAVGubiquitination[1, 2]
597LESLIADKSGSKKTLubiquitination[1]
749AGSVLLDKRFRAECKubiquitination[1]
756KRFRAECKNYGVIIPubiquitination[1]
775NRYETLLKQRHVQLLubiquitination[1]
802RISAAMYKSLDQAISubiquitination[1, 3]
838LTHRLLCKHMTLDSFubiquitination[1]
903TQEPQRDKPANVQPYubiquitination[1, 4, 5]
916PYYLYGSKPLNIAYSubiquitination[1]
939FVGPPHFKTICRLLGubiquitination[1]
982TLIEVMPKICRLPRHubiquitination[1]
1062ILPRVYIKEGERLEVacetylation[6]
1062ILPRVYIKEGERLEVubiquitination[1]
1077RMKRLEAKYAPLHLVubiquitination[1, 2, 4, 5]
1107REGDLLTKERLCCGLubiquitination[1]
1216KVQRQDGKDEIIKNVubiquitination[1]
1234KMADRIRKYQILNNEubiquitination[1]
1248EVFAILNKYMKSVETubiquitination[1]
1251AILNKYMKSVETDSSubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Involved in T-cell adhesion and p53/TP53-dependent induction of apoptosis. Does not bind RNA. 
Sequence Annotation
 MOD_RES 108 108 Phosphotyrosine (By similarity).
 MOD_RES 1062 1062 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Apoptosis; Cell adhesion; Cell junction; Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome; RNA editing; Synapse; Synaptosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1278 AA 
Protein Sequence
MTTHVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSIMYQA NFDTNFEDRN AFVTGIARYI 60
EQATVHSSMN EMLEEGHEYA VMLYTWRSCS RAIPQVKCNE 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 VGPSSTQACQ WSPRALFHPT GGTQGRRGCR SLLYMVRTML ESLIADKSGS 600
KKTLRSSLDG PIVLAIEDFH KQSFFFTHLL NISEALQQCC DLSQLWFREF FLELTMGRRI 660
QFPIEMSMPW ILTDHILETK EPSMMEYVLY PLDLYNDSAY YALTKFKKQF LYDEIEAEVN 720
LCFDQFVYKL ADQIFAYYKA MAGSVLLDKR FRAECKNYGV IIPYPPSNRY ETLLKQRHVQ 780
LLGRSIDLNR LITQRISAAM YKSLDQAISR FESEDLTSIV ELEWLLEINR LTHRLLCKHM 840
TLDSFDAMFR EANHNVSAPY GRITLHVFWE LNFDFLPNYC YNGSTNRFVR TAIPFTQEPQ 900
RDKPANVQPY YLYGSKPLNI AYSHIYSSYR NFVGPPHFKT ICRLLGYQGI AVVMEELLKI 960
VKSLLQGTIL QYVKTLIEVM PKICRLPRHE YGSPGILEFF HHQLKDIIEY AELKTDVFQS 1020
LREVGNAILF CLLIEQALSQ EEVCDLLHAA PFQNILPRVY IKEGERLEVR MKRLEAKYAP 1080
LHLVPLIERL GTPQQIAIAR EGDLLTKERL CCGLSMFEVI LTRIRSYLQD PIWRGPPPTN 1140
GVMHVDECVE FHRLWSAMQF VYCIPVGTNE FTAEQCFGDG LNWAGCSIIV LLGQQRRFDL 1200
FDFCYHLLKV QRQDGKDEII KNVPLKKMAD RIRKYQILNN EVFAILNKYM KSVETDSSTV 1260
EHVRCFQPPI HQSLATTC 1278 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0045202; C:synapse; IDA:MGI.
 GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
 GO:0006915; P:apoptotic process; IDA:UniProtKB.
 GO:0016337; P:cell-cell adhesion; IDA:UniProtKB.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL. 
Interpro
 IPR008081; Cytoplasmic_FMR1-int.
 IPR016536; Cytoplasmic_FMR1-int_sub. 
Pfam
 PF05994; FragX_IP 
SMART
  
PROSITE
  
PRINTS
 PR01698; CYTOFMRPINTP.