CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015513
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Formin-like protein 3 
Protein Synonyms/Alias
  
Gene Name
 Fmnl3 
Gene Synonyms/Alias
 Kiaa2014 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
358GLEEFLQKSRHTESEubiquitination[1]
692LPTEAEVKLLRQYERubiquitination[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
Functional Description
 Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration (By similarity). 
Sequence Annotation
 DOMAIN 26 472 GBD/FH3.
 DOMAIN 561 951 FH2.
 DOMAIN 986 1018 DAD.
 MOD_RES 174 174 Phosphoserine (By similarity).
 LIPID 2 2 N-myristoyl glycine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Lipoprotein; Myristate; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1028 AA 
Protein Sequence
MGNLESTDGG PGEPPSVPLL LPPGKTPMPE PCELEERFAL VLSSMNLPPD KARLLRQYDN 60
EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPNVTRKKFR RRVQESTKVL RELEISLRTN 120
HIGWVREFLN DENKGLDVLV DYLSFAQCSV MFDFEGLESG DDGAFDKLRS WSRSIEDLQP 180
PNALSAPFTN SLARSARQSV LRYSTLPGRR ALKNSRLVSQ KDDVHVCILC LRAIMNYQYG 240
FNLVMSHPHA VNEIALSLNN KNPRTKALVL ELLAAVCLVR GGHEIILAAF DNFKEVCKEL 300
HRFEKLMEYF RNEDSNIDFM VACMQFINIV VHSVEDMNFR VHLQYEFTKL GLEEFLQKSR 360
HTESEKLQVQ IQAYLDNVFD VGGLLEDAET KNVALEKVEE LEEHVSHLTE KLLDLENENM 420
MRVAELEKQL LQREKELESI KETYENTSNQ VHTLRRLIKE KEEAFQRRCH LEPSARGLES 480
MGGEALARVG PTELTEGIPP SDLDLLAPAP PTEETLPLPP PPAPPLPPPP PPLPDKCPPA 540
PPLPGAAPSV VLTVGLSAIR IKKPIKTKFR LPVFNWTALK PNQINGTVFS ELDDEKILED 600
LDLDRFEELF KTKAQGPALD LICSKNKTAQ KAASKVTLLE ANRAKNLAIT LRKAGRSAEE 660
ICRAIHTFDL QTLPVDFVEC LMRFLPTEAE VKLLRQYERE RQPLEELAAE DRFMLLFSKV 720
ERLTQRMAGM AFLGNFQDNL QMLTPQLNAI IAASASVKSS QKLKQMLEII LALGNYMNSS 780
KRGAVYGFKL QSLDLLLDTK STDRKMTLLH FIALTVKEKY PELANFWQEL HFVEKAAAVS 840
LENVLLDVKE LGRGMELIRR ECSIHDNSVL RNFLSTNEGK LDKLQRDAKT AEEAYNAVVR 900
YFGESPKTTP PSVFFPVFVR FIRSYKEAEQ ENEARKKQEE VMREKQLAQE AKKLDAKTPS 960
QRNKWQQQEL IAELRRRQAK EHRPVYEGKD GTIEDIITVL KSVPFTARTA KRGSRFFCDA 1020
AHHDESNC 1028 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0032794; F:GTPase activating protein binding; IDA:UniProtKB.
 GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
 GO:0016477; P:cell migration; ISS:UniProtKB.
 GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
 GO:0008360; P:regulation of cell shape; ISS:UniProtKB. 
Interpro
 IPR003104; Actin-bd_FH2/DRF_autoreg.
 IPR016024; ARM-type_fold.
 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