CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001606
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Formin-like protein 1 
Protein Synonyms/Alias
 CLL-associated antigen KW-13; Leukocyte formin 
Gene Name
 FMNL1 
Gene Synonyms/Alias
 C17orf1; C17orf1B; FMNL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
111WMSNLGFKRRVQESTubiquitination[1]
Reference
 [1] 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] 
Functional Description
 May play a role in the control of cell motility and survival of macrophages (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. 
Sequence Annotation
 DOMAIN 27 468 GBD/FH3.
 DOMAIN 632 1023 FH2.
 DOMAIN 1059 1090 DAD.
 MOD_RES 7 7 Phosphoserine.
 MOD_RES 184 184 Phosphoserine.
 MOD_RES 624 624 Phosphoserine.
 LIPID 2 2 N-myristoyl glycine.  
Keyword
 Alternative splicing; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1100 AA 
Protein Sequence
MGNAAGSAEQ PAGPAAPPPK QPAPPKQPMP AAGELEERFN RALNCMNLPP DKVQLLSQYD 60
NEKKWELICD QERFQVKNPP AAYIQKLKSY VDTGGVSRKV AADWMSNLGF KRRVQESTQV 120
LRELETSLRT NHIGWVQEFL NEENRGLDVL LEYLAFAQCS VTYDMESTDN GASNSEKNKP 180
LEQSVEDLSK GPPSSVPKSR HLTIKLTPAH SRKALRNSRI VSQKDDVHVC IMCLRAIMNY 240
QSGFSLVMNH PACVNEIALS LNNKNPRTKA LVLELLAAVC LVRGGHDIIL AAFDNFKEVC 300
GEQHRFEKLM EYFRNEDSNI DFMVACMQFI NIVVHSVENM NFRVFLQYEF THLGLDLYLE 360
RLRLTESDKL QVQIQAYLDN IFDVGALLED TETKNAVLEH MEELQEQVAL LTERLRDAEN 420
ESMAKIAELE KQLSQARKEL ETLRERFSES TAMGPSRRPP EPEKAPPAAP TRPSALELKV 480
EELEEKGLIR ILRGPGDAVS IEILPVAVAT PSGGDAPTPG VPTGSPSPDL APAAEPAPGA 540
APPPPPPLPG LPSPQEAPPS APPQAPPLPG SPEPPPAPPL PGDLPPPPPP PPPPPGTDGP 600
VPPPPPPPPP PPGGPPDALG RRDSELGPGV KAKKPIQTKF RMPLLNWVAL KPSQITGTVF 660
TELNDEKVLQ ELDMSDFEEQ FKTKSQGPSL DLSALKSKAA QKAPSKATLI EANRAKNLAI 720
TLRKGNLGAE RICQAIEAYD LQALGLDFLE LLMRFLPTEY ERSLITRFER EQRPMEELSE 780
EDRFMLCFSR IPRLPERMTT LTFLGNFPDT AQLLMPQLNA IIAASMSIKS SDKLRQILEI 840
VLAFGNYMNS SKRGAAYGFR LQSLDALLEM KSTDRKQTLL HYLVKVIAEK YPQLTGFHSD 900
LHFLDKAGSV SLDSVLADVR SLQRGLELTQ REFVRQDDCM VLKEFLRANS PTMDKLLADS 960
KTAQEAFESV VEYFGENPKT TSPGLFFSLF SRFIKAYKKA EQEVEQWKKE AAAQEAGADT 1020
PGKGEPPAPK SPPKARRPQM DLISELKRRQ QKEPLIYESD RDGAIEDIIT DLRNQPYIRA 1080
DTGRRSARRR PPGPPLQVTS DLSL 1104 
Gene Ontology
 GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0051015; F:actin filament binding; ISS:UniProtKB.
 GO:0032794; F:GTPase activating protein binding; IDA:UniProtKB.
 GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
 GO:0051014; P:actin filament severing; ISS:UniProtKB.
 GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
 GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
 GO:0006929; P:substrate-dependent cell migration; IEA:Compara. 
Interpro
 IPR003104; Actin-bd_FH2/DRF_autoreg.
 IPR016024; ARM-type_fold.
 IPR014767; Diaphanous_autoregulatory.
 IPR010472; Drf_FH3.
 IPR010473; Drf_GTPase-bd.
 IPR015425; FH2_actin-bd.
 IPR014768; GTPase-bd/formin_homology_3. 
Pfam
 PF06367; Drf_FH3
 PF06371; Drf_GBD
 PF02181; FH2 
SMART
 SM00498; FH2 
PROSITE
 PS51231; DAD
 PS51444; FH2
 PS51232; GBD_FH3 
PRINTS