CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013901
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
97SRAIPQVKCNEQPNRubiquitination[1]
197RAAQFLRKMADPQSIubiquitination[1]
294KKRINLSKIDKFFKQacetylation[2]
545PKGGFDIKVPRRAVGubiquitination[1]
750NRYETLLKQRHVQLLubiquitination[1]
777RISAAMYKSLDQAISubiquitination[1]
1037ILPRVYIKEGERLEVubiquitination[1]
1052RMKRLEAKYAPLHLVubiquitination[1]
1209KMADRIRKYQILNNEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Involved in T-cell adhesion and p53-dependent induction of apoptosis (By similarity). Does not bind RNA. 
Sequence Annotation
 MOD_RES 108 108 Phosphotyrosine.
 MOD_RES 1037 1037 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Apoptosis; Cell adhesion; Cell junction; Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome; RNA editing; Synapse; Synaptosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1253 AA 
Protein Sequence
MTTHVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSIMYQA NFDTNFEDRN AFVTGIARYI 60
EQATVHSSMN EMLEEGHDYA 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 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:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0043005; C:neuron projection; ISS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
 GO:0045202; C:synapse; ISA:MGI.
 GO:0006915; P:apoptotic process; ISS:UniProtKB.
 GO:0016337; P:cell-cell adhesion; ISS:UniProtKB. 
Interpro
 IPR008081; Cytoplasmic_FMR1-int.
 IPR016536; Cytoplasmic_FMR1-int_sub. 
Pfam
 PF05994; FragX_IP 
SMART
  
PROSITE
  
PRINTS
 PR01698; CYTOFMRPINTP.