FNBP1_HUMAN
ID FNBP1_HUMAN Reviewed; 617 AA.
AC Q96RU3; B7ZL12; E9PGQ4; O60301; Q3MIN8; Q5TC87; Q5TC88; Q6P658; Q7LGG2;
AC Q9H8H8; Q9NWD1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Formin-binding protein 1;
DE AltName: Full=Formin-binding protein 17;
DE Short=hFBP17;
GN Name=FNBP1; Synonyms=FBP17, KIAA0554;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SNX2, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH
RP KMT2A/MLL1.
RX PubMed=11438682; DOI=10.1073/pnas.121433898;
RA Fuchs U., Rehkamp G.F., Haas O.A., Slany R., Koenig M., Bojesen S.,
RA Bohle R.M., Damm-Welk C., Ludwig W.-D., Harbott J., Borkhardt A.;
RT "The human formin-binding protein 17 (FBP17) interacts with sorting nexin,
RT SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8756-8761(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 36-617 (ISOFORM 2), AND VARIANT ASN-490.
RC TISSUE=Embryo, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-409 (ISOFORM 4).
RC TISSUE=Liver, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH ARHGAP17.
RX PubMed=11431473; DOI=10.1074/jbc.m103540200;
RA Richnau N., Aspenstroem P.;
RT "Rich, a rho GTPase-activating protein domain-containing protein involved
RT in signaling by Cdc42 and Rac1.";
RL J. Biol. Chem. 276:35060-35070(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH FASLG.
RX PubMed=12023017; DOI=10.1016/s0014-5793(02)02709-6;
RA Ghadimi M.P., Sanzenbacher R., Thiede B., Wenzel J., Jing Q., Plomann M.,
RA Borkhardt A., Kabelitz D., Janssen O.;
RT "Identification of interaction partners of the cytosolic polyproline region
RT of CD95 ligand (CD178).";
RL FEBS Lett. 519:50-58(2002).
RN [8]
RP INTERACTION WITH SNX2 AND TNKS, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-515; ASP-519 AND 515-ARG--GLY-520.
RX PubMed=14596906; DOI=10.1016/s0014-5793(03)01063-9;
RA Fuchs U., Rehkamp G.F., Slany R., Follo M., Borkhardt A.;
RT "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to
RT tankyrase, a protein involved in telomere maintenance.";
RL FEBS Lett. 554:10-16(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DNM1; DNM2 AND DNM3,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF PRO-602.
RX PubMed=15252009; DOI=10.1074/jbc.m404899200;
RA Kamioka Y., Fukuhara S., Sawa H., Nagashima K., Masuda M., Matsuda M.,
RA Mochizuki N.;
RT "A novel dynamin-associating molecule, formin-binding protein 17, induces
RT tubular membrane invaginations and participates in endocytosis.";
RL J. Biol. Chem. 279:40091-40099(2004).
RN [11]
RP INTERACTION WITH AKAP9, AND SUBCELLULAR LOCATION.
RX PubMed=15047863; DOI=10.1091/mbc.e03-10-0757;
RA Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M.,
RA Goldenring J.R.;
RT "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi
RT apparatus.";
RL Mol. Biol. Cell 15:2771-2781(2004).
RN [12]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DNM1 AND WASL, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LEU-7.
RX PubMed=16326391; DOI=10.1016/j.devcel.2005.11.005;
RA Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P.;
RT "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane
RT invagination by BAR and F-BAR proteins.";
RL Dev. Cell 9:791-804(2005).
RN [13]
RP FUNCTION, INTERACTION WITH FASLG, AND SUBCELLULAR LOCATION.
RX PubMed=16318909; DOI=10.1016/j.cellsig.2005.10.015;
RA Qian J., Chen W., Lettau M., Podda G., Zoernig M., Kabelitz D., Janssen O.;
RT "Regulation of FasL expression: a SH3 domain containing protein family
RT involved in the lysosomal association of FasL.";
RL Cell. Signal. 18:1327-1337(2006).
RN [14]
RP INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2.
RX PubMed=16630611; DOI=10.1016/j.yexcr.2006.03.013;
RA Aspenstroem P., Richnau N., Johansson A.-S.;
RT "The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA
RT and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin
RT dynamics.";
RL Exp. Cell Res. 312:2180-2194(2006).
RN [15]
RP FUNCTION, INTERACTION WITH DNM2 AND WASL, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-33; ARG-35; 51-LYS-LYS-52 AND 113-ARG-LYS-114.
RX PubMed=16418535; DOI=10.1083/jcb.200508091;
RA Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T.;
RT "Coordination between the actin cytoskeleton and membrane deformation by a
RT novel membrane tubulation domain of PCH proteins is involved in
RT endocytosis.";
RL J. Cell Biol. 172:269-279(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-349 AND
RP SER-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-110, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-359, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-299, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-359, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-300, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, DOMAIN F-BAR, COILED-COIL DOMAIN, AND MUTAGENESIS OF
RP LYS-33; THR-165; LYS-166; ASP-168 AND PRO-210.
RX PubMed=17512409; DOI=10.1016/j.cell.2007.03.040;
RA Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K.,
RA Akasaka R., Nishino Y., Toyama M., Chen L., Liu Z.-J., Wang B.C.,
RA Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M.,
RA Nagayama K., Takenawa T., Yokoyama S.;
RT "Curved EFC/F-BAR-domain dimers are joined end to end into a filament for
RT membrane invagination in endocytosis.";
RL Cell 129:761-772(2007).
CC -!- FUNCTION: May act as a link between RND2 signaling and regulation of
CC the actin cytoskeleton (By similarity). Required to coordinate membrane
CC tubulation with reorganization of the actin cytoskeleton during the
CC late stage of clathrin-mediated endocytosis. Binds to lipids such as
CC phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and
CC promotes membrane invagination and the formation of tubules. Also
CC enhances actin polymerization via the recruitment of WASL/N-WASP, which
CC in turn activates the Arp2/3 complex. Actin polymerization may promote
CC the fission of membrane tubules to form endocytic vesicles. May be
CC required for the lysosomal retention of FASLG/FASL. {ECO:0000250,
CC ECO:0000269|PubMed:15252009, ECO:0000269|PubMed:16318909,
CC ECO:0000269|PubMed:16326391, ECO:0000269|PubMed:16418535,
CC ECO:0000269|PubMed:17512409}.
CC -!- SUBUNIT: Interacts specifically with GTP-bound RND2 and CDC42.
CC Interacts with PDE6G and microtubules (By similarity). Homodimerizes,
CC the dimers can polymerize end-to-end to form filamentous structures.
CC Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2,
CC DNM3, FASLG/FASL, SNX2 and WASL/N-WASP. May interact with TNKS.
CC {ECO:0000250, ECO:0000269|PubMed:11431473, ECO:0000269|PubMed:11438682,
CC ECO:0000269|PubMed:12023017, ECO:0000269|PubMed:14596906,
CC ECO:0000269|PubMed:15047863, ECO:0000269|PubMed:15252009,
CC ECO:0000269|PubMed:16318909, ECO:0000269|PubMed:16326391,
CC ECO:0000269|PubMed:16418535, ECO:0000269|PubMed:16630611,
CC ECO:0000269|PubMed:17512409}.
CC -!- INTERACTION:
CC Q96RU3; Q05193: DNM1; NbExp=5; IntAct=EBI-1111248, EBI-713135;
CC Q96RU3; P48023: FASLG; NbExp=4; IntAct=EBI-1111248, EBI-495538;
CC Q96RU3; Q96RU3: FNBP1; NbExp=3; IntAct=EBI-1111248, EBI-1111248;
CC Q96RU3; O95166: GABARAP; NbExp=2; IntAct=EBI-1111248, EBI-712001;
CC Q96RU3; O60749: SNX2; NbExp=4; IntAct=EBI-1111248, EBI-1046690;
CC Q96RU3; O95271: TNKS; NbExp=4; IntAct=EBI-1111248, EBI-1105254;
CC Q96RU3; P97573: Inpp5d; Xeno; NbExp=2; IntAct=EBI-1111248, EBI-8008869;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm,
CC cell cortex. Lysosome. Cytoplasmic vesicle. Cell membrane; Peripheral
CC membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit.
CC Note=Enriched in cortical regions coincident with F-actin. Also
CC localizes to endocytic vesicles and lysosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96RU3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RU3-2; Sequence=VSP_021695, VSP_021696;
CC Name=3;
CC IsoId=Q96RU3-3; Sequence=VSP_021694, VSP_021696;
CC Name=4;
CC IsoId=Q96RU3-4; Sequence=VSP_021693;
CC Name=5;
CC IsoId=Q96RU3-5; Sequence=VSP_021695;
CC -!- TISSUE SPECIFICITY: Very highly expressed in the epithelial cells of
CC the gastrointestinal tract, respiratory, reproductive and urinary
CC systems. Also highly expressed in brown adipose tissue, cardiomyocytes,
CC enteric ganglia and glucagon producing cells of the pancreas. Expressed
CC in germ cells of the testis and all regions of the brain.
CC {ECO:0000269|PubMed:11438682, ECO:0000269|PubMed:15252009}.
CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its
CC concave surface. The end-to-end polymerization of dimers of these
CC domains provides a curved surface that fits best membranes with around
CC 600 A diameter, and may drive tubulation.
CC {ECO:0000269|PubMed:17512409}.
CC -!- DISEASE: Note=A chromosomal aberration involving FNBP1 is found in
CC acute leukemias. Translocation t(9;11)(q34;q23) with KMT2A/MLL1. The
CC relatively low incidence of the KMT2A/MLL1-FNBP1 fusion protein in
CC acute leukemia may reflect the marginal capacity of this fusion protein
CC to induce cellular transformation.
CC -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH62463.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAK49824.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA25480.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91451.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FBP17ID353.html";
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DR EMBL; AF265550; AAK49824.1; ALT_INIT; mRNA.
DR EMBL; AB011126; BAA25480.1; ALT_INIT; mRNA.
DR EMBL; AK000975; BAA91451.1; ALT_INIT; mRNA.
DR EMBL; AK023681; BAB14638.1; -; mRNA.
DR EMBL; AL136141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062463; AAH62463.1; ALT_SEQ; mRNA.
DR EMBL; BC101755; AAI01756.1; -; mRNA.
DR EMBL; BC143513; AAI43514.1; -; mRNA.
DR CCDS; CCDS48040.1; -. [Q96RU3-1]
DR CCDS; CCDS87699.1; -. [Q96RU3-3]
DR RefSeq; NP_055848.1; NM_015033.2. [Q96RU3-1]
DR RefSeq; XP_005251880.1; XM_005251823.2. [Q96RU3-2]
DR RefSeq; XP_005251881.1; XM_005251824.2. [Q96RU3-5]
DR RefSeq; XP_005251886.1; XM_005251829.2.
DR PDB; 2EFL; X-ray; 2.61 A; A=1-300.
DR PDBsum; 2EFL; -.
DR AlphaFoldDB; Q96RU3; -.
DR SMR; Q96RU3; -.
DR BioGRID; 116686; 54.
DR DIP; DIP-35355N; -.
DR ELM; Q96RU3; -.
DR IntAct; Q96RU3; 32.
DR MINT; Q96RU3; -.
DR STRING; 9606.ENSP00000413625; -.
DR iPTMnet; Q96RU3; -.
DR MetOSite; Q96RU3; -.
DR PhosphoSitePlus; Q96RU3; -.
DR BioMuta; FNBP1; -.
DR DMDM; 118572321; -.
DR EPD; Q96RU3; -.
DR jPOST; Q96RU3; -.
DR MassIVE; Q96RU3; -.
DR MaxQB; Q96RU3; -.
DR PaxDb; Q96RU3; -.
DR PeptideAtlas; Q96RU3; -.
DR PRIDE; Q96RU3; -.
DR ProteomicsDB; 20367; -.
DR ProteomicsDB; 78035; -. [Q96RU3-1]
DR ProteomicsDB; 78036; -. [Q96RU3-2]
DR ProteomicsDB; 78037; -. [Q96RU3-3]
DR ProteomicsDB; 78038; -. [Q96RU3-4]
DR Antibodypedia; 31452; 197 antibodies from 31 providers.
DR DNASU; 23048; -.
DR Ensembl; ENST00000355681.3; ENSP00000347907.3; ENSG00000187239.17. [Q96RU3-3]
DR Ensembl; ENST00000420781.5; ENSP00000407548.2; ENSG00000187239.17. [Q96RU3-5]
DR Ensembl; ENST00000446176.7; ENSP00000413625.1; ENSG00000187239.17. [Q96RU3-1]
DR GeneID; 23048; -.
DR KEGG; hsa:23048; -.
DR MANE-Select; ENST00000446176.7; ENSP00000413625.1; NM_015033.3; NP_055848.1.
DR UCSC; uc004byw.2; human. [Q96RU3-1]
DR CTD; 23048; -.
DR DisGeNET; 23048; -.
DR GeneCards; FNBP1; -.
DR HGNC; HGNC:17069; FNBP1.
DR HPA; ENSG00000187239; Low tissue specificity.
DR MIM; 606191; gene.
DR neXtProt; NX_Q96RU3; -.
DR OpenTargets; ENSG00000187239; -.
DR PharmGKB; PA128394597; -.
DR VEuPathDB; HostDB:ENSG00000187239; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000183047; -.
DR InParanoid; Q96RU3; -.
DR OMA; EFMISKP; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; Q96RU3; -.
DR TreeFam; TF351162; -.
DR PathwayCommons; Q96RU3; -.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q96RU3; -.
DR BioGRID-ORCS; 23048; 19 hits in 1075 CRISPR screens.
DR ChiTaRS; FNBP1; human.
DR EvolutionaryTrace; Q96RU3; -.
DR GeneWiki; FNBP1; -.
DR GenomeRNAi; 23048; -.
DR Pharos; Q96RU3; Tbio.
DR PRO; PR:Q96RU3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96RU3; protein.
DR Bgee; ENSG00000187239; Expressed in corpus callosum and 209 other tissues.
DR ExpressionAtlas; Q96RU3; baseline and differential.
DR Genevisible; Q96RU3; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07676; F-BAR_FBP17; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028532; FNBP1/FBP17.
DR InterPro; IPR037449; FNBP1_F-BAR.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF13; PTHR15735:SF13; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Chromosomal rearrangement; Coated pit; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Lipid-binding; Lysosome;
KW Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..617
FT /note="Formin-binding protein 1"
FT /id="PRO_0000261430"
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 404..481
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 550..611
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..335
FT /note="Interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 1..79
FT /note="Required for self-association and induction of
FT membrane tubulation"
FT REGION 251..617
FT /note="Required for self-association and induction of
FT membrane tubulation"
FT REGION 280..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..552
FT /note="Interaction with RND2"
FT /evidence="ECO:0000250"
FT REGION 486..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..617
FT /note="Interaction with PDE6G"
FT /evidence="ECO:0000250"
FT REGION 514..617
FT /note="Required for interaction with TNKS"
FT /evidence="ECO:0000269|PubMed:14596906"
FT REGION 535..617
FT /note="Interaction with DNM1 and DNM3"
FT /evidence="ECO:0000269|PubMed:15252009"
FT REGION 550..617
FT /note="Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2"
FT /evidence="ECO:0000269|PubMed:11431473,
FT ECO:0000269|PubMed:16630611"
FT REGION 553..610
FT /note="Interaction with FASLG"
FT REGION 553..609
FT /note="Interaction with DNM2 and WASL"
FT COILED 67..259
FT /evidence="ECO:0000269|PubMed:17512409"
FT COILED 398..490
FT /evidence="ECO:0000250"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 166
FT /note="Mediates end-to-end attachment of dimers"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TY0"
FT MOD_RES 500
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80TY0"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R511"
FT VAR_SEQ 329..394
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021693"
FT VAR_SEQ 330..358
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021694"
FT VAR_SEQ 391..395
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_021695"
FT VAR_SEQ 616..617
FT /note="DS -> GAKTYI (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021696"
FT VARIANT 490
FT /note="S -> N (in dbSNP:rs1023000)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_029388"
FT MUTAGEN 7
FT /note="L->E: Impairs membrane tubulation but does not
FT affect lipid-binding."
FT /evidence="ECO:0000269|PubMed:16326391"
FT MUTAGEN 33
FT /note="K->E: Abolishes membrane invagination."
FT /evidence="ECO:0000269|PubMed:16418535,
FT ECO:0000269|PubMed:17512409"
FT MUTAGEN 33
FT /note="K->Q: Impairs lipid-binding and induction of
FT membrane tubulation; when associated with Q-35."
FT /evidence="ECO:0000269|PubMed:16418535,
FT ECO:0000269|PubMed:17512409"
FT MUTAGEN 35
FT /note="R->Q: Impairs lipid-binding and induction of
FT membrane tubulation; when associated with Q-33."
FT /evidence="ECO:0000269|PubMed:16418535"
FT MUTAGEN 51..52
FT /note="KK->QQ: Impairs lipid-binding and induction of
FT membrane tubulation."
FT /evidence="ECO:0000269|PubMed:16418535"
FT MUTAGEN 113..114
FT /note="RK->QQ: Impairs lipid-binding and induction of
FT membrane tubulation."
FT /evidence="ECO:0000269|PubMed:16418535"
FT MUTAGEN 165
FT /note="T->A: Abolishes membrane invagination."
FT /evidence="ECO:0000269|PubMed:17512409"
FT MUTAGEN 166
FT /note="K->A: Abolishes membrane invagination."
FT /evidence="ECO:0000269|PubMed:17512409"
FT MUTAGEN 168
FT /note="D->A,N,R: No significant effect."
FT /evidence="ECO:0000269|PubMed:17512409"
FT MUTAGEN 210
FT /note="P->A: Disrupts helix kink and moderately increases
FT diameter of the induced tubular membrane."
FT /evidence="ECO:0000269|PubMed:17512409"
FT MUTAGEN 515..520
FT /note="Missing: Abrogates interaction with TNKS."
FT /evidence="ECO:0000269|PubMed:14596906"
FT MUTAGEN 515
FT /note="R->A: Impairs interaction with TNKS."
FT /evidence="ECO:0000269|PubMed:14596906"
FT MUTAGEN 519
FT /note="D->A: Impairs interaction with TNKS; when associated
FT with A-515."
FT /evidence="ECO:0000269|PubMed:14596906"
FT MUTAGEN 602
FT /note="P->L: Abrogates interaction with DNM1, DNM2 and
FT DNM3."
FT /evidence="ECO:0000269|PubMed:15252009"
FT CONFLICT 388
FT /note="K -> E (in Ref. 3; BAA91451)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:2EFL"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:2EFL"
FT HELIX 11..52
FT /evidence="ECO:0007829|PDB:2EFL"
FT HELIX 68..160
FT /evidence="ECO:0007829|PDB:2EFL"
FT HELIX 166..206
FT /evidence="ECO:0007829|PDB:2EFL"
FT HELIX 208..238
FT /evidence="ECO:0007829|PDB:2EFL"
FT HELIX 241..257
FT /evidence="ECO:0007829|PDB:2EFL"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:2EFL"
SQ SEQUENCE 617 AA; 71307 MW; F06E847C6E631EC3 CRC64;
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK
EEEEYKYTSC KAFISNLNEM NDYAGQHEVI SENMASQIIV DLARYVQELK QERKSNFHDG
RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRH
QMAEDSKADY SSILQKFNHE QHEYYHTHIP NIFQKIQEME ERRIVRMGES MKTYAEVDRQ
VIPIIGKCLD GIVKAAESID QKNDSQLVIE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
SNSRGEGKPD LKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP SAVPNGPQSP
KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG LSLKLGATPE DFSNLPPEQR RKKLQQKVDE
LNKEIQKEMD QRDAITKMKD VYLKNPQMGD PASLDHKLAE VSQNIEKLRV ETQKFEAWLA
EVEGRLPARS EQARRQSGLY DSQNPPTVNN CAQDRESPDG SYTEEQSQES EMKVLATDFD
DEFDDEEPLP AIGTCKALYT FEGQNEGTIS VVEGETLYVI EEDKGDGWTR IRRNEDEEGY
VPTSYVEVCL DKNAKDS
