CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011979
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein flightless-1 homolog 
Protein Synonyms/Alias
  
Gene Name
 FLII 
Gene Synonyms/Alias
 FLIL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21DLSGNDFKGGYFPENacetylation[1]
21DLSGNDFKGGYFPENubiquitination[2, 3, 4, 5]
30GYFPENVKAMTSLRWubiquitination[5]
39MTSLRWLKLNRTGLCubiquitination[4]
92VARANSLKNSGVPDDubiquitination[2, 5]
290SLPSAICKLSKLKKLubiquitination[4]
293SAICKLSKLKKLYLNubiquitination[4]
303KLYLNSNKLDFDGLPubiquitination[2, 3, 4, 5]
421AAAGSGPKDPMARKMubiquitination[4]
447DQAKQVLKGMSDVAQubiquitination[2, 3, 4]
459VAQEKNKKQEESADAubiquitination[4]
482RWDQGLEKPRLDYSEubiquitination[2, 4]
638KLEPVPLKGTSLDPRubiquitination[4]
671ATLSSTTKARLFAEKubiquitination[2, 3, 6]
678KARLFAEKINKNERKubiquitination[4]
730PPQPKLYKVGLGLGYubiquitination[4, 7]
746ELPQINYKLSVEHKQubiquitination[2, 4, 5, 6, 7]
752YKLSVEHKQRPKVELubiquitination[4, 6]
756VEHKQRPKVELMPRMubiquitination[4, 7]
802LVRAAALKLGQELCGubiquitination[4, 6]
832GTEAQVFKAKFKNWDubiquitination[2, 4, 5, 6, 7, 8, 9]
834EAQVFKAKFKNWDDVubiquitination[7]
836QVFKAKFKNWDDVLTubiquitination[2, 4, 5, 6, 7, 8, 9]
862QSPGLSGKVKRDAEKubiquitination[2, 3, 5, 6]
864PGLSGKVKRDAEKKDubiquitination[4]
874AEKKDQMKADLTALFubiquitination[2, 3, 4, 5, 6]
962KEEKAEGKEGEEATAubiquitination[2, 6]
974ATAEAEEKQPEEDFQubiquitination[6]
1015FESLFPGKLEVVRMTubiquitination[4]
1029TQQQENPKFLSHFKRubiquitination[2, 4, 8, 9]
1035PKFLSHFKRKFIIHRubiquitination[4, 8, 9, 10]
1046IIHRGKRKAVQGAQQubiquitination[4]
1115ASDPDEAKLAEDILNubiquitination[5]
1173LFRCSNEKGYFAVTEubiquitination[4]
1222VEIKLSLKACQVYIQubiquitination[6]
Reference
 [1] 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]
 [2] 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]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 May play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors (NR) and acts in cooperation with NCOA2 and CARM1. Involved in estrogen hormone signaling. Involved in early embryonic development (By similarity). May play a role in regulation of cytoskeletal rearrangements involved in cytokinesis and cell migration, by inhibiting Rac1-dependent paxillin phosphorylation. 
Sequence Annotation
 REPEAT 7 32 LRR 1.
 REPEAT 33 55 LRR 2.
 REPEAT 56 78 LRR 3.
 REPEAT 80 103 LRR 4.
 REPEAT 104 126 LRR 5.
 REPEAT 127 149 LRR 6.
 REPEAT 150 173 LRR 7.
 REPEAT 175 196 LRR 8.
 REPEAT 197 222 LRR 9.
 REPEAT 223 245 LRR 10.
 REPEAT 247 268 LRR 11.
 REPEAT 269 291 LRR 12.
 REPEAT 293 316 LRR 13.
 REPEAT 318 339 LRR 14.
 REPEAT 340 363 LRR 15.
 REPEAT 501 559 Gelsolin-like 1.
 REPEAT 640 670 Gelsolin-like 2.
 REPEAT 755 798 Gelsolin-like 3.
 REPEAT 1068 1115 Gelsolin-like 4.
 REPEAT 1176 1218 Gelsolin-like 5.
 REGION 1 427 Interaction with LRRFIP1 and LRRFIP2.
 REGION 495 827 Interaction with ACTL6A.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 21 21 N6-acetyllysine.
 MOD_RES 406 406 Phosphoserine.
 MOD_RES 436 436 Phosphoserine; by SGK3.
 MOD_RES 818 818 Phosphothreonine; by SGK3.
 MOD_RES 856 856 Phosphoserine.  
Keyword
 Acetylation; Actin-binding; Activator; Alternative splicing; Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Direct protein sequencing; Leucine-rich repeat; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1269 AA 
Protein Sequence
MEATGVLPFV RGVDLSGNDF KGGYFPENVK AMTSLRWLKL NRTGLCYLPE ELAALQKLEH 60
LSVSHNNLTT LHGELSSLPS LRAIVARANS LKNSGVPDDI FKLDDLSVLD LSHNQLTECP 120
RELENAKNML VLNLSHNSID TIPNQLFINL TDLLYLDLSE NRLESLPPQM RRLVHLQTLV 180
LNGNPLLHAQ LRQLPAMTAL QTLHLRSTQR TQSNLPTSLE GLSNLADVDL SCNDLTRVPE 240
CLYTLPSLRR LNLSSNQITE LSLCIDQWVH VETLNLSRNQ LTSLPSAICK LSKLKKLYLN 300
SNKLDFDGLP SGIGKLTNLE EFMAANNNLE LVPESLCRCP KLRKLVLNKN HLVTLPEAIH 360
FLTEIEVLDV RENPNLVMPP KPADRAAEWY NIDFSLQNQL RLAGASPATV AAAAAAGSGP 420
KDPMARKMRL RRRKDSAQDD QAKQVLKGMS DVAQEKNKKQ EESADARAPS GKVRRWDQGL 480
EKPRLDYSEF FTEDVGQLPG LTIWQIENFV PVLVEEAFHG KFYEADCYIV LKTFLDDSGS 540
LNWEIYYWIG GEATLDKKAC SAIHAVNLRN YLGAECRTVR EEMGDESEEF LQVFDNDISY 600
IEGGTASGFY TVEDTHYVTR MYRVYGKKNI KLEPVPLKGT SLDPRFVFLL DRGLDIYVWR 660
GAQATLSSTT KARLFAEKIN KNERKGKAEI TLLVQGQELP EFWEALGGEP SEIKKHVPED 720
FWPPQPKLYK VGLGLGYLEL PQINYKLSVE HKQRPKVELM PRMRLLQSLL DTRCVYILDC 780
WSDVFIWLGR KSPRLVRAAA LKLGQELCGM LHRPRHATVS RSLEGTEAQV FKAKFKNWDD 840
VLTVDYTRNA EAVLQSPGLS GKVKRDAEKK DQMKADLTAL FLPRQPPMSL AEAEQLMEEW 900
NEDLDGMEGF VLEGKKFARL PEEEFGHFYT QDCYVFLCRY WVPVEYEEEE KKEDKEEKAE 960
GKEGEEATAE AEEKQPEEDF QCIVYFWQGR EASNMGWLTF TFSLQKKFES LFPGKLEVVR 1020
MTQQQENPKF LSHFKRKFII HRGKRKAVQG AQQPSLYQIR TNGSALCTRC IQINTDSSLL 1080
NSEFCFILKV PFESEDNQGI VYAWVGRASD PDEAKLAEDI LNTMFDTSYS KQVINEGEEP 1140
ENFFWVGIGA QKPYDDDAEY MKHTRLFRCS NEKGYFAVTE KCSDFCQDDL ADDDIMLLDN 1200
GQEVYMWVGT QTSQVEIKLS LKACQVYIQH MRSKEHERPR RLRLVRKGNE QHAFTRCFHA 1260
WSAFCKALA 1269 
Gene Ontology
 GO:0005813; C:centrosome; IDA:HPA.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003779; F:actin binding; TAS:ProtInc.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:0006936; P:muscle contraction; TAS:ProtInc.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR007123; Gelsolin_dom.
 IPR001611; Leu-rich_rpt.
 IPR025875; Leu-rich_rpt_4.
 IPR003591; Leu-rich_rpt_typical-subtyp.
 IPR007122; Villin/Gelsolin. 
Pfam
 PF00626; Gelsolin
 PF00560; LRR_1
 PF12799; LRR_4 
SMART
 SM00262; GEL
 SM00369; LRR_TYP 
PROSITE
 PS51450; LRR 
PRINTS
 PR00597; GELSOLIN.