CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016985
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Formin-like protein 3 
Protein Synonyms/Alias
 Formin homology 2 domain-containing protein 3; WW domain-binding protein 3; WBP-3 
Gene Name
 FMNL3 
Gene Synonyms/Alias
 FHOD3; KIAA2014; WBP3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
358GLEEFLQKSRHTESEubiquitination[1]
645LLEANRAKNLAITLRubiquitination[2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. 
Sequence Annotation
 DOMAIN 26 472 GBD/FH3.
 DOMAIN 561 951 FH2.
 DOMAIN 986 1018 DAD.
 MOD_RES 174 174 Phosphoserine.
 LIPID 2 2 N-myristoyl glycine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Lipoprotein; Myristate; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1028 AA 
Protein Sequence
MGNLESAEGV PGEPPSVPLL LPPGKMPMPE PCELEERFAL VLSSMNLPPD KARLLRQYDN 60
EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPSVTRKKFR RRVQESTKVL RELEISLRTN 120
HIGWVREFLN DENKGLDVLV DYLSFAQCSV MFDFEGLESG DDGAFDKLRS WSRSIEDLQP 180
PSALSAPFTN 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 KETYENTSHQ VHTLRRLIKE KEEAFQRRCH LEPNVRGLES 480
VDSEALARVG PAELSEGMPP SDLDLLAPAP PPEEVLPLPP PPAPPLPPPP PPLPDKCPPA 540
PPLPGAAPSV VLTVGLSAIR IKKPIKTKFR LPVFNWTALK PNQISGTVFS ELDDEKILED 600
LDLDKFEELF KTKAQGPALD LICSKNKTAQ KAASKVTLLE ANRAKNLAIT LRKAGRSAEE 660
ICRAIHTFDL QTLPVDFVEC LMRFLPTEAE VKLLRQYERE RQPLEELAAE DRFMLLFSKV 720
ERLTQRMAGM AFLGNFQDNL QMLTPQLNAI IAASASVKSS QKLKQMLEII LALGNYMNSS 780
KRGAVYGFKL QSLDLLLDTK STDRKMTLLH FIALTVKEKY PDLANFWHEL 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; IDA:UniProtKB.
 GO:0032794; F:GTPase activating protein binding; ISS:UniProtKB.
 GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
 GO:0016477; P:cell migration; IMP:UniProtKB.
 GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
 GO:0008360; P:regulation of cell shape; IMP: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