CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021771
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein flightless-1 homolog 
Protein Synonyms/Alias
  
Gene Name
 Flii 
Gene Synonyms/Alias
 Fli1; Fliih 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
21DLSGNDFKGGYFPENacetylation[1]
21DLSGNDFKGGYFPENubiquitination[2]
458DVAQEKNKNQEESIDacetylation[3]
730PPQPKLYKVGLGLGYubiquitination[2]
832GTEAQVFKAKFKNWDubiquitination[2]
836QVFKAKFKNWDDVLTubiquitination[2]
862QGQGLSGKVKRDTEKubiquitination[2]
1031TQQQENPKFLSHFKRubiquitination[2]
1037PKFLSHFKRKFIIHRubiquitination[2]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] 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]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
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 (By similarity). Essential for early embryonic development. 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 1070 1117 Gelsolin-like 4.
 REPEAT 1178 1220 Gelsolin-like 5.
 REGION 1 427 Interaction with LRRFIP1 and LRRFIP2 (By
 REGION 495 827 Interaction with ACTL6A (By similarity).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 21 21 N6-acetyllysine (By similarity).
 MOD_RES 406 406 Phosphoserine (By similarity).
 MOD_RES 436 436 Phosphoserine; by SGK3.  
Keyword
 Acetylation; Actin-binding; Activator; Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1271 AA 
Protein Sequence
MEATGVLPFV RGVDLSGNDF KGGYFPENVK AMTSLRWLKL NRTGLCYLPE ELAALQKLEH 60
LSVSHNHLTT LHGELSSLPS LRAIVARANS LKNSGVPDDI FKLDDLSVLD LSHNQLTECP 120
RELENAKNML VLNLSHNGID SIPNQLFINL TDLLYLDLSE NRLESLPPQM RRLVHLQTLV 180
LNGNPLLHAQ LRQLPAMMAL QTLHLRNTQR TQSNLPTSLE GLSNLSDVDL SCNDLTRVPE 240
CLYTLPSLRR LNLSSNQIAE LSLCIDQWVH LETLNLSRNQ LTSLPSAICK LTKLKKLYLN 300
SNKLDFDGLP SGIGKLTSLE EFMAANNNLE LIPESLCRCP KLKKLVLNKN RLVTLPEAIH 360
FLTEIQVLDV RENPSLVMPP KPADRTAEWY NIDFSLQNQL RLAGASPATV AAAAAVGSGS 420
KDPLARKMRL RRRKDSAQDV QAKQVLKGMS DVAQEKNKNQ EESIDARAPG GKVRRWDQGL 480
EKPRLDYSEF FTEDVGQLPG LTIWQIENFV PVLVEEAFHG KFYEADCYIV LKTFLDDSGS 540
LNWEIYYWIG GEATLDKKAC SAIHAVNLRN YLGAECRTVR EEMGDESEEF LQVFDNDISY 600
IEGGTASGFY TVEDTHYVTR MYRVYGKKNI KLEPVPLKGS SLDPRFVFLL DQGLDIYVWR 660
GAQATLSNTT KARLFAEKIN KNERKGKAEI TLLVQGQEPP GFWDVLGGEP SEIKNHVPDD 720
FWPPQPKLYK VGLGLGYLEL PQINYKLSVE HKKRPKVELM PGMRLLQSLL DTRCVYILDC 780
WSDVFIWLGR KSPRLVRAAA LKLGQELCGM LHRPRHTVVS RSLEGTEAQV FKAKFKNWDD 840
VLTVDYTRNA EAVLQGQGLS GKVKRDTEKT DQMKADLTAL FLPRQPPMPL AEAEQLMEEW 900
NEDLDGMEGF VLEGRKFTRL PEEEFGHFYT QDCYVFLCRY WVPVEYEEEE KTEDKEGKAS 960
AEAREGEEAA AEAEEKQPEE DFQCIVYFWQ GREASNMGWL TFTFSLQKKF ESLFPGKLEV 1020
VRMTQQQENP KFLSHFKRKF IIHRGKRKVT QGTLQPTLYQ IRTNGSALCT RCIQINTDSS 1080
LLNSEFCFIL KVPFESEDNQ GIVYAWVGRA SDPDEAKLAE DILNTMFDAS YSKQVINEGE 1140
EPENFFWVGI GAQKPYDDDA EYMKHTRLFR CSNEKGYFAV TEKCSDFCQD DLADDDIMLL 1200
DNGQEVYMWV GTQTSQVEIK LSLKACQVYI QHTRSKEHER PRRLRLVRKG NEQRAFTRCF 1260
HAWSTFRQAP A 1271 
Gene Ontology
 GO:0005813; C:centrosome; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0030036; P:actin cytoskeleton organization; TAS:MGI.
 GO:0051014; P:actin filament severing; TAS:MGI.
 GO:0007275; P:multicellular organismal development; IMP:MGI.
 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.
 IPR007122; Villin/Gelsolin. 
Pfam
 PF00626; Gelsolin
 PF00560; LRR_1
 PF12799; LRR_4 
SMART
 SM00262; GEL 
PROSITE
 PS51450; LRR 
PRINTS
 PR00597; GELSOLIN.