Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00750
Entry Name
UniProt Accession
Theoretical PI
6.98
Molecular Weight
123320.8
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Formin-like protein 2
Protein Synonyms/Alias
Formin homology 2 domain-containing protein 2;
Gene Name
FMNL2
Gene Synonyms/Alias
FHOD2; KIAA1902;
Created Date
29-MAY-2007
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNAGSMDS
[1][2]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Suzuki T, Moriya K, Nagatoshi K, Ota Y, Ezure T, Ando E, Tsunasawa S, UtsumiT. Strategy for comprehensive identification of human N-myristoylated proteinsusing an insect cell-free protein synthesis system. Proteomics. 2010May;10(9):1780-93. doi: 10.1002/pmic.200900783.[PMID:20213681]
[2] Moriya K, Yamamoto T, Takamitsu E, Matsunaga Y, Kimoto M, Fukushige D, Kimoto C, Suzuki T, Utsumi T. Protein N-myristoylation is required for cellularmorphological changes induced by two formin family proteins, FMNL2 and FMNL3.Biosci Biotechnol Biochem. 2012;76(6):1201-9. Epub 2012 Jun 7.[PMID:22790947]
Functional Description
Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics.
Sequence Annotation
Domain: 23 469 GBD/FH3.
Domain: 616 1007 FH2.
Domain: 1040 1079 DAD.
Protein Length
1086 AA.
Protein Sequence
(Canonical)
MGNAGSMDSQ QTDFRAHNVP LKLPMPEPGE LEERFAIVLN AMNLPPDKAR LLRQYDNEKK  60
WELICDQERF QVKNPPHTYI QKLKGYLDPA VTRKKFRRRV QESTQVLREL EISLRTNHIG  120
WVREFLNEEN KGLDVLVEYL SFAQYAVTFD FESVESTVES SVDKSKPWSR SIEDLHRGSN  180
LPSPVGNSVS RSGRHSALRY NTLPSRRTLK NSRLVSKKDD VHVCIMCLRA IMNYQYGFNM  240
VMSHPHAVNE IALSLNNKNP RTKALVLELL AAVCLVRGGH EIILSAFDNF KEVCGEKQRF  300
EKLMEHFRNE DNNIDFMVAS MQFINIVVHS VEDMNFRVHL QYEFTKLGLD EYLDKLKHTE  360
SDKLQVQIQA YLDNVFDVGA LLEDAETKNA ALERVEELEE NISHLSEKLQ DTENEAMSKI  420
VELEKQLMQR NKELDVVREI YKDANTQVHT LRKMVKEKEE AIQRQSTLEK KIHELEKQGT  480
IKIQKKGDGD IAILPVVASG TLSMGSEVVA GNSVGPTMGA ASSGPLPPPP PPLPPSSDTP  540
ETVQNGPVTP PMPPPPPPPP PPPPPPPPPP PPPLPGPAAE TVPAPPLAPP LPSAPPLPGT  600
SSPTVVFNSG LAAVKIKKPI KTKFRMPVFN WVALKPNQIN GTVFNEIDDE RILEDLNVDE  660
FEEIFKTKAQ GPAIDLSSSK QKIPQKGSNK VTLLEANRAK NLAITLRKAG KTADEICKAI  720
HVFDLKTLPV DFVECLMRFL PTENEVKVLR LYERERKPLE NLSDEDRFMM QFSKIERLMQ  780
KMTIMAFIGN FAESIQMLTP QLHAIIAASV SIKSSQKLKK ILEIILALGN YMNSSKRGAV  840
YGFKLQSLDL LLDTKSTDRK QTLLHYISNV VKEKYHQVSL FYNELHYVEK AAAVSLENVL  900
LDVKELQRGM DLTKREYTMH DHNTLLKEFI LNNEGKLKKL QDDAKIAQDA FDDVVKYFGE  960
NPKTTPPSVF FPVFVRFVKA YKQAEEENEL RKKQEQALME KLLEQEALME QQDPKSPSHK  1020
SKRQQQELIA ELRRRQVKDN RHVYEGKDGA IEDIITVLKT VPFTARTAKR GSRFFCEPVL  1080
TEEYHY                                                             1086
FASTA
(Canonical)
>LipidDB-9606-00750|Q96PY5
MGNAGSMDSQQTDFRAHNVPLKLPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKK
WELICDQERFQVKNPPHTYIQKLKGYLDPAVTRKKFRRRVQESTQVLRELEISLRTNHIG
WVREFLNEENKGLDVLVEYLSFAQYAVTFDFESVESTVESSVDKSKPWSRSIEDLHRGSN
LPSPVGNSVSRSGRHSALRYNTLPSRRTLKNSRLVSKKDDVHVCIMCLRAIMNYQYGFNM
VMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHEIILSAFDNFKEVCGEKQRF
EKLMEHFRNEDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKLKHTE
SDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKI
VELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQGT
IKIQKKGDGDIAILPVVASGTLSMGSEVVAGNSVGPTMGAASSGPLPPPPPPLPPSSDTP
ETVQNGPVTPPMPPPPPPPPPPPPPPPPPPPPPLPGPAAETVPAPPLAPPLPSAPPLPGT
SSPTVVFNSGLAAVKIKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDE
FEEIFKTKAQGPAIDLSSSKQKIPQKGSNKVTLLEANRAKNLAITLRKAGKTADEICKAI
HVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERKPLENLSDEDRFMMQFSKIERLMQ
KMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNSSKRGAV
YGFKLQSLDLLLDTKSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVL
LDVKELQRGMDLTKREYTMHDHNTLLKEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGE
NPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQEALMEQQDPKSPSHK
SKRQQQELIAELRRRQVKDNRHVYEGKDGAIEDIITVLKTVPFTARTAKRGSRFFCEPVL
TEEYHY
Gene Ontology
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB
GO:0007010; P:cytoskeleton organization; IMP:UniProtKB
GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB
Interpro
InterPro; IPR016024; ARM-type_fold
InterPro; IPR014767; Diaphanous_autoregulatory
InterPro; IPR015425; FH2_Formin
InterPro; IPR010472; FH3_dom
InterPro; IPR027656; FMNL2
InterPro; IPR010473; GTPase-bd
InterPro; IPR014768; GTPase-bd/formin_homology_3
InterPro; IPR017987; Wilms_tumour
Pfam
Pfam; PF06367; Drf_FH3;
Pfam; PF06371; Drf_GBD;
Pfam; PF02181; FH2;
SMART
SMART; SM00498; FH2;
PROSITE
PROSITE; PS51231; DAD;
PROSITE; PS51444; FH2;
PROSITE; PS51232; GBD_FH3;
PRINTS
PRINTS; PR00049; WILMSTUMOUR;