Hmdb loader
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP08396
Secondary Accession Numbers
  • 14108
Name Formin-binding protein 1
Synonyms
  1. Formin-binding protein 17
  2. hFBP17
Gene Name FNBP1
Protein Type Unknown
Biological Properties
General Function Involved in identical protein binding
Specific Function May act as a link between RND2 signaling and regulation of the actin cytoskeleton. Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Cell membrane
  2. Cytoplasm
  3. Cytoplasm
  4. Cytoplasm
  5. Peripheral membrane protein
  6. Lysosome
  7. Cytoplasmic vesicle
  8. Cytoplasmic side
  9. cytoskeleton
  10. cell cortex
Gene Properties
Chromosome Location Chromosome:9
Locus 9q34
SNPs FNBP1
Gene Sequence
>1854 bp
ATGAGCTGGGGCACCGAGCTCTGGGATCAGTTTGACAACTTAGAAAAACACACACAGTGG
GGAATTGATATTCTTGAGAAATATATCAAGTTTGTGAAAGAAAGGACAGAGATTGAACTC
AGCTATGCAAAGCAACTCAGGAATCTTTCAAAGAAGTACCAACCTAAAAAGAACTCGAAG
GAGGAAGAAGAATACAAGTATACGTCATGTAAAGCTTTCATTTCCAACCTGAACGAAATG
AATGATTACGCAGGGCAGCATGAAGTTATCTCCGAGAACATGGCATCACAGATCATTGTG
GACTTGGCACGCTATGTTCAGGAACTGAAACAGGAGAGGAAATCAAACTTTCACGATGGC
CGTAAAGCACAGCAGCACATCGAGACTTGCTGGAAGCAGCTTGAATCTAGTAAAAGGCGA
TTTGAACGCGATTGCAAAGAGGCGGACAGGGCGCAGCAGTACTTTGAGAAAATGGACGCT
GACATCAATGTCACAAAAGCGGATGTTGAAAAGGCCCGACAACAAGCTCAAATACGTCAC
CAAATGGCAGAGGACAGCAAAGCAGATTACTCATCCATTCTCCAGAAATTCAACCATGAG
CAGCATGAATATTACCATACTCACATCCCCAACATCTTCCAGAAAATACAAGAGATGGAG
GAAAGGAGGATTGTGAGAATGGGAGAGTCCATGAAGACATATGCAGAGGTTGATCGGCAG
GTGATCCCAATCATTGGGAAGTGCCTGGATGGAATAGTAAAAGCAGCCGAATCAATTGAT
CAGAAAAATGATTCACAGCTGGTAATAGAAGCTTATAAATCAGGGTTTGAGCCTCCTGGA
GACATTGAATTTGAGGATTACACTCAGCCAATGAAGCGCACTGTGTCAGATAACAGCCTT
TCAAATTCCAGAGGAGAAGGCAAACCAGACCTCAAATTTGGTGGCAAATCCAAAGGAAAG
TTATGGCCGTTCATCAAAAAAAATAAGCTTATGTCCCTTTTAACATCCCCCCATCAGCCT
CCCCCTCCCCCTCCTGCCTCTGCCTCACCCTCTGCTGTTCCCAACGGCCCCCAGTCTCCC
AAGCAGCAAAAGGAACCCCTCTCCCATCGCTTCAACGAGTTCATGACCTCCAAACCCAAA
ATCCACTGCTTCAGGAGCCTAAAGCGTGGGCTTTCTCTCAAGCTGGGTGCAACACCGGAG
GATTTCAGCAACCTCCCACCTGAACAAAGAAGGAAAAAGCTGCAGCAGAAAGTCGATGAG
TTAAATAAAGAAATTCAGAAGGAGATGGATCAAAGAGATGCCATAACAAAAATGAAAGAT
GTCTACCTAAAGAATCCTCAGATGGGAGACCCAGCCAGTTTGGATCACAAATTAGCAGAA
GTCAGCCAAAATATAGAGAAACTGCGAGTAGAGACCCAGAAATTTGAGGCCTGGCTGGCT
GAGGTTGAAGGCCGGCTCCCAGCACGCAGCGAGCAGGCGCGCCGGCAGAGCGGACTGTAC
GACAGCCAGAACCCACCCACAGTCAACAACTGCGCCCAGGACCGTGAGAGCCCAGATGGC
AGTTACACAGAGGAGCAGAGTCAGGAGAGTGAGATGAAGGTGCTGGCCACGGATTTTGAC
GACGAGTTTGATGATGAGGAGCCCCTCCCTGCCATAGGGACGTGCAAAGCTCTCTACACA
TTTGAAGGTCAGAATGAAGGAACGATTTCCGTAGTTGAAGGAGAAACATTGTATGTCATA
GAGGAAGACAAAGGCGATGGCTGGACCCGCATTCGGAGAAATGAAGATGAAGAGGGTTAT
GTCCCCACTTCATATGTCGAAGTCTGTTTGGACAAAAATGCCAAAGATTCCTAG
Protein Properties
Number of Residues 617
Molecular Weight 71306.3
Theoretical pI 5.44
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Formin-binding protein 1
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSK
EEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDG
RKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRH
QMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQ
VIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSL
SNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSP
KQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDE
LNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLA
EVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFD
DEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGY
VPTSYVEVCLDKNAKDS
GenBank ID Protein 38524622
UniProtKB/Swiss-Prot ID Q96RU3
UniProtKB/Swiss-Prot Entry Name FNBP1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_015033.2
GeneCard ID FNBP1
GenAtlas ID FNBP1
HGNC ID HGNC:17069
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455 ]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  5. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  6. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  9. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  10. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  11. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  12. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed:9628581 ]
  13. Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal Chem. 2004 May 15;76(10):2763-72. [PubMed:15144186 ]
  14. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed:19367720 ]
  15. Larocca MC, Shanks RA, Tian L, Nelson DL, Stewart DM, Goldenring JR: AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus. Mol Biol Cell. 2004 Jun;15(6):2771-81. Epub 2004 Mar 26. [PubMed:15047863 ]
  16. Richnau N, Aspenstrom P: Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1. J Biol Chem. 2001 Sep 14;276(37):35060-70. Epub 2001 Jun 28. [PubMed:11431473 ]
  17. Itoh T, Erdmann KS, Roux A, Habermann B, Werner H, De Camilli P: Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell. 2005 Dec;9(6):791-804. [PubMed:16326391 ]
  18. Qian J, Chen W, Lettau M, Podda G, Zornig M, Kabelitz D, Janssen O: Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL. Cell Signal. 2006 Aug;18(8):1327-37. Epub 2005 Nov 28. [PubMed:16318909 ]
  19. Aspenstrom P, Richnau N, Johansson AS: The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics. Exp Cell Res. 2006 Jul 15;312(12):2180-94. Epub 2006 Apr 21. [PubMed:16630611 ]
  20. Tsujita K, Suetsugu S, Sasaki N, Furutani M, Oikawa T, Takenawa T: Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J Cell Biol. 2006 Jan 16;172(2):269-79. [PubMed:16418535 ]
  21. Fuchs U, Rehkamp G, Haas OA, Slany R, Konig M, Bojesen S, Bohle RM, Damm-Welk C, Ludwig WD, Harbott J, Borkhardt A: The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia. Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8756-61. Epub 2001 Jul 3. [PubMed:11438682 ]
  22. Ghadimi MP, Sanzenbacher R, Thiede B, Wenzel J, Jing Q, Plomann M, Borkhardt A, Kabelitz D, Janssen O: Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178). FEBS Lett. 2002 May 22;519(1-3):50-8. [PubMed:12023017 ]
  23. Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A: The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance. FEBS Lett. 2003 Nov 6;554(1-2):10-6. [PubMed:14596906 ]
  24. Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N: A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J Biol Chem. 2004 Sep 17;279(38):40091-9. Epub 2004 Jul 12. [PubMed:15252009 ]