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Filamin-B (FLN-B) (ABP-280-like protein) (Actin-binding-like protein) (Beta-filamin)

 FLNB_MOUSE              Reviewed;        2602 AA.
Q80X90; E9QNV9; Q8VHX4; Q8VHX7; Q99KY3;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
08-MAY-2019, entry version 153.
RecName: Full=Filamin-B;
Short=FLN-B;
AltName: Full=ABP-280-like protein;
AltName: Full=Actin-binding-like protein;
AltName: Full=Beta-filamin;
Name=Flnb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1663-1752 AND 2031-2181.
STRAIN=C3H/HeJ;
PubMed=11807098; DOI=10.1083/jcb.200103037;
van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M.,
Takafuta T., Shapiro S.S., Sonnenberg A.;
"Different splice variants of filamin-B affect myogenesis, subcellular
distribution, and determine binding to integrin (beta) subunits.";
J. Cell Biol. 156:361-376(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1884-2602.
STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=12393796; DOI=10.1093/hmg/11.23.2845;
Sheen V.L., Feng Y., Graham D., Takafuta T., Shapiro S.S., Walsh C.A.;
"Filamin A and filamin B are co-expressed within neurons during
periods of neuronal migration and can physically interact.";
Hum. Mol. Genet. 11:2845-2854(2002).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH RFLNA AND RFLNB.
PubMed=21709252; DOI=10.1073/pnas.1104211108;
Gay O., Gilquin B., Nakamura F., Jenkins Z.A., McCartney R.,
Krakow D., Deshiere A., Assard N., Hartwig J.H., Robertson S.P.,
Baudier J.;
"RefilinB (FAM101B) targets filamin A to organize perinuclear actin
networks and regulates nuclear shape.";
Proc. Natl. Acad. Sci. U.S.A. 108:11464-11469(2011).
[8]
INTERACTION WITH MICALL2.
PubMed=23890175; DOI=10.1111/gtc.12078;
Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K.,
Kitamura T., Imoto I., Matsushita N., Sasaki T.;
"Junctional Rab13-binding protein (JRAB) regulates cell spreading via
filamins.";
Genes Cells 18:810-822(2013).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1780, SUCCINYLATION [LARGE
SCALE ANALYSIS] AT LYS-2518 AND LYS-2524, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[10]
INTERACTION WITH RFLNA AND RFLNB.
PubMed=24436304; DOI=10.1093/hmg/ddu007;
Mizuhashi K., Kanamoto T., Moriishi T., Muranishi Y., Miyazaki T.,
Terada K., Omori Y., Ito M., Komori T., Furukawa T.;
"Filamin-interacting proteins, Cfm1 and Cfm2, are essential for the
formation of cartilaginous skeletal elements.";
Hum. Mol. Genet. 23:2953-2967(2014).
-!- FUNCTION: Connects cell membrane constituents to the actin
cytoskeleton. May promote orthogonal branching of actin filaments
and links actin filaments to membrane glycoproteins. Anchors
various transmembrane proteins to the actin cytoskeleton (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with FLNA, FLNC, INPPL1, ITGB1A,
ITGB1D, ITGB3, ITGB6, MYOT, MYOZ1, PSEN1 and PSEN2 (By
similarity). Interacts with MICALL2. Interacts with RFLNA and
RFLNB (PubMed:21709252,PubMed:24436304). {ECO:0000250,
ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm,
cytoskeleton. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250}.
Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in hippocampus, cortex, cerebellar
Purkinje cells and granule cell layers.
{ECO:0000269|PubMed:12393796}.
-!- DEVELOPMENTAL STAGE: Expressed within the ventricular,
periventricular and subventricular zones at 12.5 dpc; olfactory
epithelium, radial glial fibers, cortical plate and lateral
ventricles at 16 dpc; in a lesser degree in lung, renal cortices
and alimentary tract. {ECO:0000269|PubMed:12393796}.
-!- DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24
internally homologous repeats and two hinge regions. Repeat 24 and
the second hinge domain are important for dimer formation. The
first hinge region prevents binding to ITGA and ITGB subunits (By
similarity). {ECO:0000250}.
-!- PTM: ISGylation prevents ability to interact with the upstream
activators of the JNK cascade and inhibits IFNA-induced JNK
signaling. {ECO:0000250}.
-!- PTM: Ubiquitination by a SCF-like complex containing ASB2 isoform
2 leads to proteasomal degradation which promotes muscle
differentiation. {ECO:0000250|UniProtKB:O75369}.
-!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC129222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC140322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF353669; AAL68445.1; -; mRNA.
EMBL; AF353672; AAL68448.1; -; mRNA.
EMBL; BC003959; AAH03959.1; -; mRNA.
EMBL; BC048835; AAH48835.1; -; mRNA.
CCDS; CCDS70540.1; -.
RefSeq; NP_001074896.1; NM_001081427.1.
SMR; Q80X90; -.
BioGrid; 235046; 106.
IntAct; Q80X90; 109.
MINT; Q80X90; -.
STRING; 10090.ENSMUSP00000052020; -.
iPTMnet; Q80X90; -.
PhosphoSitePlus; Q80X90; -.
SwissPalm; Q80X90; -.
EPD; Q80X90; -.
jPOST; Q80X90; -.
MaxQB; Q80X90; -.
PaxDb; Q80X90; -.
PeptideAtlas; Q80X90; -.
PRIDE; Q80X90; -.
Ensembl; ENSMUST00000052678; ENSMUSP00000052020; ENSMUSG00000025278.
GeneID; 286940; -.
KEGG; mmu:286940; -.
UCSC; uc007sek.1; mouse.
CTD; 2317; -.
MGI; MGI:2446089; Flnb.
eggNOG; KOG0518; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00940000156286; -.
HOGENOM; HOG000044235; -.
InParanoid; Q80X90; -.
KO; K04437; -.
OMA; PHENGIH; -.
OrthoDB; 35998at2759; -.
TreeFam; TF313685; -.
Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
PRO; PR:Q80X90; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000025278; Expressed in 302 organ(s), highest expression level in placenta.
Genevisible; Q80X90; MM.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005925; C:focal adhesion; IDA:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0001725; C:stress fiber; IDA:MGI.
GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
GO; GO:0003334; P:keratinocyte development; IMP:MGI.
GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
CDD; cd00014; CH; 2.
Gene3D; 1.10.418.10; -; 2.
Gene3D; 2.60.40.10; -; 24.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR017868; Filamin/ABP280_repeat-like.
InterPro; IPR001298; Filamin/ABP280_rpt.
InterPro; IPR029874; FLNB.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
PANTHER; PTHR38537:SF7; PTHR38537:SF7; 1.
Pfam; PF00307; CH; 2.
Pfam; PF00630; Filamin; 23.
SMART; SM00033; CH; 2.
SMART; SM00557; IG_FLMN; 24.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF81296; SSF81296; 24.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS50194; FILAMIN_REPEAT; 24.
1: Evidence at protein level;
Acetylation; Actin-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Isopeptide bond; Phosphoprotein; Reference proteome;
Repeat; Ubl conjugation.
CHAIN 1 2602 Filamin-B.
/FTId=PRO_0000087299.
DOMAIN 16 122 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 139 242 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REPEAT 249 347 Filamin 1.
REPEAT 349 446 Filamin 2.
REPEAT 447 543 Filamin 3.
REPEAT 544 636 Filamin 4.
REPEAT 640 736 Filamin 5.
REPEAT 737 839 Filamin 6.
REPEAT 840 938 Filamin 7.
REPEAT 939 1034 Filamin 8.
REPEAT 1035 1127 Filamin 9.
REPEAT 1128 1222 Filamin 10.
REPEAT 1223 1322 Filamin 11.
REPEAT 1323 1415 Filamin 12.
REPEAT 1416 1511 Filamin 13.
REPEAT 1512 1608 Filamin 14.
REPEAT 1609 1704 Filamin 15.
REPEAT 1729 1813 Filamin 16.
REPEAT 1816 1908 Filamin 17.
REPEAT 1919 1994 Filamin 18.
REPEAT 1997 2089 Filamin 19.
REPEAT 2091 2185 Filamin 20.
REPEAT 2188 2280 Filamin 21.
REPEAT 2282 2375 Filamin 22.
REPEAT 2379 2471 Filamin 23.
REPEAT 2507 2601 Filamin 24.
REGION 1 239 Actin-binding.
REGION 1705 1728 Hinge 1. {ECO:0000250}.
REGION 2472 2602 Self-association site, tail.
{ECO:0000250}.
REGION 2472 2506 Hinge 2. {ECO:0000250}.
MOD_RES 216 216 Phosphothreonine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 519 519 Phosphothreonine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 681 681 N6-acetyllysine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 730 730 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 932 932 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 983 983 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1307 1307 Phosphothreonine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1316 1316 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1433 1433 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1505 1505 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1602 1602 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 1780 1780 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2083 2083 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2113 2113 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2369 2369 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2465 2465 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2478 2478 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2481 2481 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2492 2492 Phosphoserine.
{ECO:0000250|UniProtKB:O75369}.
MOD_RES 2518 2518 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2524 2524 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2576 2576 N6-acetyllysine.
{ECO:0000250|UniProtKB:O75369}.
CROSSLNK 2468 2468 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000250}.
SEQUENCE 2602 AA; 277825 MW; 41BA737EC52A89DB CRC64;
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK
RMHHKYHQRP TFRQMKLENV SVALEFLDHE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH
YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP
GLCPDWESWD PRKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA
KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK
EEARVTPDSD KNKTYSVEYL PKVTGLHKVI VLFAGQHISK SPFEVNVDKA QGDASKVTAK
GPGLETTGNI ANKPTYFDIY TAGAGVGDIG IEVEDPQGKN SVELLVEDRG NQVYRCVYKP
VQPGPHVVKV SFAGDAIPKS PFGVQIGEAC NPNACRASGR GLQPKGVRIR ETADFKVDTK
AAGSGELGVT VKGPKGLEEL VKQKGFLDGV YSFEYYPSTP GKYSVAVTWG GHHIPKSPFE
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG TLGFAIEGPS QAKIEYDDQN
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GDYNPDLVQA YGPGLEKSGC
TINNPAEFIV DPKDAGSAPL KILAQDGEGQ PIDIQMKSRM DGTYACSYTP LKAIKHTIAV
VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG
IKCDARVLSD DEEDVDFDII HNANDTFTVK YVPPAPGRYT IKVLFASQEI PASPFRVKVD
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV HTKGAGKAPL NVQFSSPLPG EAVKDLDIID
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKIN GLENRVEVGK
DQEFAIDTNG AGGQGKLDVT ILSPSRKVVP CLVAPVAGRE CSTAKFIPRE EGLFAVDVTY
DGHPVPGSPY TVEASLPPDP TKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP
CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG
PGLEHGKVGE PGILCVDCSE AGPGTLGLEA VSDSGAKAEV SIQNNKDGTY AVTYVPLTAG
MYTLTMKYGG ELVPHFPAWV KVEPAIDTSG IKAFGPGIEG KDVFREATTD FTVDSRPLTQ
VGGDHIKAQI TNPSGASTEC FVKDNADGTY QVEYTPFEKG FHVVEVTYDD VPIPNSPFKV
AVTEGCQPSR VHAQGPGLKE AFTNKSNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD
GSCSAEYIPF APGDYDVNIT YGGVHIPGSP FRVPSKDVVD PSKVKIAGPG LSSCVRACIP
QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YIVSVKYADE
EIPRSPFKVK VLPTYDASKV TASGPGLSAY GVPASLPVEF AIDARDAGEG LLAVQITDQE
GKPQRATVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDNIP LSPYRIRATQ TGDASKCLAT
GPGIAPTVKT GEEVGFVVDA KTAGKGKVTC VILTPDGTEA EADVIENEDG TYDIFYTAAK
PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AMEEAPVNAC PPGFRPWVTE EAYVPVSDMN
GLGFKPFDLV IPFAVRKGEI TGTVHMPSGK KATPEIVDNK DGTVTVRYAP TEVGLHEMHI
KYRGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG
PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DNRRCSQVKL
GSAADFLLDI SETDLSTLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK
NGNHVANSPV SIMVVQSEIG DARRAKVYGQ GLSEGRTFEM SDFIVDTRDA GYGGISLAVE
GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVRESIT
RTSRAPAVAT VGSICDLNLK IPEINSSDMS AHVTSPSGHV TEAEIVPMGK NSHCVRFVPQ
EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGI PAEFSIWTRE
AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPDSPYLVPV
IAPSDDARCL TVLSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP
DKYAVRFIPH ENGIHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GAGLETGTTG
IQSEFFINTT QAGPGTLSVT IEGPSKVKMD CQEIPEGYKV MYTPMAPGNY LIGVKYGGPN
HISRSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKSSS DASKVTSKGA
GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGKQQYN VTYVVKERGD
YVLAVKWGEE HIPGSPFHVT VP


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WP731: Sterol regulatory element binding protein related
WP1531: Vitamin D synthesis
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WP2218: sGC
WP1616: ABC transporters
WP1566: Citrate cycle (TCA cycle)
WP346: Protein Modifications
WP1690: Propanoate metabolism
WP931: G Protein Signaling Pathways
WP1650: Fluorobenzoate degradation
WP232: G Protein Signaling Pathways
WP1657: Glycerolipid metabolism
WP1939: Unfolded Protein Response
WP1694: Pyrimidine metabolism
WP1049: G Protein Signaling Pathways
WP1714: Tyrosine metabolism
WP2371: Parkinsons Disease Pathway
WP1663: Homologous recombination
WP1673: Naphthalene and anthracene degradation
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1678: Nucleotide excision repair
WP1644: DNA replication

Related Genes :
[FLNB FLN1L FLN3 TABP TAP] Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)
[FLNA FLN FLN1] Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)
[FLNC ABPL FLN2] Filamin-C (FLN-C) (FLNc) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin)
[Flna Fln Fln1] Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)
[ARHGAP24 FILGAP] Rho GTPase-activating protein 24 (Filamin-A-associated RhoGAP) (FilGAP) (RAC1- and CDC42-specific GTPase-activating protein of 72 kDa) (RC-GAP72) (Rho-type GTPase-activating protein 24) (RhoGAP of 73 kDa) (Sarcoma antigen NY-SAR-88) (p73RhoGAP)
[Dbnl Abp1 Sh3p7] Drebrin-like protein (Actin-binding protein 1) (SH3 domain-containing protein 7)
[abpE-1 abp1-1 DDB_G0273447; abpE-2 abp1-2 DDB_G0273517] Drebrin-like protein (Actin-binding protein 1) (Dabp1) (Actin-binding protein E)
[MACF1 ABP620 ACF7 KIAA0465 KIAA1251] Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha)
[ABP1 YCR088W YCR88W] Actin-binding protein
[Oprm1 Ror-b] Mu-type opioid receptor (M-OR-1) (MOR-1) (Opioid receptor B)
[Abp1 CG10083] Drebrin-like protein (Actin binding protein 1)
[NEBL LNEBL] Nebulette (Actin-binding Z-disk protein)
[GP1BB] Platelet glycoprotein Ib beta chain (GP-Ib beta) (GPIb-beta) (GPIbB) (Antigen CD42b-beta) (CD antigen CD42c)
[ACTN2] Alpha-actinin-2 (Alpha-actinin skeletal muscle isoform 2) (F-actin cross-linking protein)
[Mycbp2 Pam Phr1] E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.-) (Myc-binding protein 2) (Pam/highwire/rpm-1 protein) (Protein Magellan) (Protein associated with Myc)
[RUVBL2 INO80J TIP48 TIP49B CGI-46] RuvB-like 2 (EC 3.6.4.12) (48 kDa TATA box-binding protein-interacting protein) (48 kDa TBP-interacting protein) (51 kDa erythrocyte cytosolic protein) (ECP-51) (INO80 complex subunit J) (Repressing pontin 52) (Reptin 52) (TIP49b) (TIP60-associated protein 54-beta) (TAP54-beta)
[SMARCA4 BAF190A BRG1 SNF2B SNF2L4] Transcription activator BRG1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA4) (BRG1-associated factor 190A) (BAF190A) (Mitotic growth and transcription activator) (Protein BRG-1) (Protein brahma homolog 1) (SNF2-beta) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4)
[MYCBP2 KIAA0916 PAM] E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.-) (Myc-binding protein 2) (Protein associated with Myc)
[mreB envB rodY b3251 JW3220] Cell shape-determining protein MreB (Actin-like MreB protein) (Rod shape-determining protein MreB)
[Igf2bp1 Imp1 Vickz1] Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2 mRNA-binding protein 1) (IMP-1) (B-actin zipcode-binding protein 1) (ZBP1) (rZBP-1) (IGF-II mRNA-binding protein 1) (VICKZ family member 1)
[Ppp1r9b] Neurabin-2 (Neurabin-II) (Neural tissue-specific F-actin-binding protein II) (PP1bp134) (Protein phosphatase 1 regulatory subunit 9B) (Spinophilin) (p130)
[mycbp2] E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.-) (Myc-binding protein 2) (Protein Esrom)
[GP1BA] Platelet glycoprotein Ib alpha chain (GP-Ib alpha) (GPIb-alpha) (GPIbA) (Glycoprotein Ibalpha) (Antigen CD42b-alpha) (CD antigen CD42b) [Cleaved into: Glycocalicin]
[Smarca4 Baf190a Brg1 Snf2b Snf2l4] Transcription activator BRG1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA4) (BRG1-associated factor 190A) (BAF190A) (Protein brahma homolog 1) (SNF2-beta) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4)
[Smarca4 Baf190a Brg1 Snf2b Snf2l4] Transcription activator BRG1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA4) (BRG1-associated factor 190A) (BAF190A) (Protein brahma homolog 1) (SNF2-beta) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4)
[Or22b AN12 DOR22A.2 dor67 Or22A.2 CG4231] Odorant receptor 22b
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[EFB1 TEF5 YAL003W] Elongation factor 1-beta (EF-1-beta) (Eukaryotic elongation factor 1Balpha) (eEF1Balpha) (Translation elongation factor 1B alpha)
[OPRM1 MOR1] Mu-type opioid receptor (M-OR-1) (MOR-1) (Mu opiate receptor) (Mu opioid receptor) (MOP) (hMOP)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

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