Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96RU3 (FNBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formin-binding protein 1
Alternative name(s):
Formin-binding protein 17
Short name=hFBP17
Gene names
Name:FNBP1
Synonyms:FBP17, KIAA0554
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a link between RND2 signaling and regulation of the actin cytoskeleton By similarity. Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated 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. Ref.10 Ref.12 Ref.13 Ref.15 Ref.25

Subunit structure

Interacts specifically with GTP-bound RND2 and CDC42. Interacts with PDE6G and microtubules By similarity. Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, SNX2 and WASL/N-WASP. May interact with TNKS. Ref.1 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.25

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cytoplasmcell cortex. Lysosome. Cytoplasmic vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membraneclathrin-coated pit. Note: Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes. Ref.1 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.25

Tissue specificity

Very highly expressed in the epithelial cells of the gastrointestinal tract, respiratory, reproductive and urinary systems. Also highly expressed in brown adipose tissue, cardiomyocytes, enteric ganglia and glucagon producing cells of the pancreas. Expressed in germ cells of the testis and all regions of the brain. Ref.1 Ref.10

Domain

The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation. Ref.25

Involvement in disease

A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with KMT2A/MLL1. The relatively low incidence of the KMT2A/MLL1-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.

Sequence similarities

Belongs to the FNBP1 family.

Contains 1 FCH domain.

Contains 1 REM (Hr1) repeat.

Contains 1 SH3 domain.

Sequence caution

The sequence AAH62463.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAK49824.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA25480.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA91451.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI12149.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI12150.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI13910.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI13911.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96RU3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96RU3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     391-395: Missing.
     616-617: DS → GAKTYI
Isoform 3 (identifier: Q96RU3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     330-358: Missing.
     616-617: DS → GAKTYI
Isoform 4 (identifier: Q96RU3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     329-394: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 617617Formin-binding protein 1
PRO_0000261430

Regions

Domain1 – 6565FCH
Repeat416 – 49176REM
Domain550 – 61162SH3
Region1 – 335335Interaction with microtubules By similarity
Region1 – 288288F-BAR domain
Region1 – 7979Required for self-association and induction of membrane tubulation
Region251 – 617367Required for self-association and induction of membrane tubulation
Region400 – 552153Interaction with RND2 By similarity
Region495 – 617123Interaction with PDE6G By similarity
Region514 – 617104Required for interaction with TNKS
Region535 – 61783Interaction with DNM1 and DNM3
Region550 – 61768Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2
Region553 – 61058Interaction with FASLG
Region553 – 60957Interaction with DNM2 and WASL
Coiled coil67 – 259193 Ref.25
Coiled coil398 – 49093 By similarity
Compositional bias340 – 3456Poly-Pro

Sites

Site1661Mediates end-to-end attachment of dimers

Amino acid modifications

Modified residue661N6-acetyllysine Ref.21
Modified residue1101N6-acetyllysine Ref.21
Modified residue2961Phosphoserine Ref.16 Ref.18 Ref.22 Ref.24
Modified residue2991Phosphoserine Ref.18 Ref.24
Modified residue3491Phosphoserine Ref.18
Modified residue3591Phosphoserine Ref.18 Ref.20 Ref.22
Modified residue4971Phosphoserine By similarity
Modified residue5001Phosphotyrosine By similarity

Natural variations

Alternative sequence329 – 39466Missing in isoform 4.
VSP_021693
Alternative sequence330 – 35829Missing in isoform 3.
VSP_021694
Alternative sequence391 – 3955Missing in isoform 2.
VSP_021695
Alternative sequence616 – 6172DS → GAKTYI in isoform 2 and isoform 3.
VSP_021696
Natural variant4901S → N. Ref.3
Corresponds to variant rs1023000 [ dbSNP | Ensembl ].
VAR_029388

Experimental info

Mutagenesis71L → E: Impairs membrane tubulation but does not affect lipid-binding. Ref.12
Mutagenesis331K → E: Abolishes membrane invagination. Ref.15 Ref.25
Mutagenesis331K → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-35. Ref.15 Ref.25
Mutagenesis351R → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-33. Ref.15
Mutagenesis51 – 522KK → QQ: Impairs lipid-binding and induction of membrane tubulation.
Mutagenesis113 – 1142RK → QQ: Impairs lipid-binding and induction of membrane tubulation.
Mutagenesis1651T → A: Abolishes membrane invagination. Ref.25
Mutagenesis1661K → A: Abolishes membrane invagination. Ref.25
Mutagenesis1681D → A, N or R: No significant effect. Ref.25
Mutagenesis2101P → A: Disrupts helix kink and moderately increases diameter of the induced tubular membrane. Ref.25
Mutagenesis515 – 5206Missing: Abrogates interaction with TNKS. Ref.8
Mutagenesis5151R → A: Impairs interaction with TNKS. Ref.8
Mutagenesis5191D → A: Impairs interaction with TNKS; when associated with A-515. Ref.8
Mutagenesis6021P → L: Abrogates interaction with DNM1, DNM2 and DNM3. Ref.10
Sequence conflict3881K → E in BAA91451. Ref.3

Secondary structure

................ 617
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: F06E847C6E631EC3

FASTA61771,307
        10         20         30         40         50         60 
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK 

        70         80         90        100        110        120 
EEEEYKYTSC KAFISNLNEM NDYAGQHEVI SENMASQIIV DLARYVQELK QERKSNFHDG 

       130        140        150        160        170        180 
RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRH 

       190        200        210        220        230        240 
QMAEDSKADY SSILQKFNHE QHEYYHTHIP NIFQKIQEME ERRIVRMGES MKTYAEVDRQ 

       250        260        270        280        290        300 
VIPIIGKCLD GIVKAAESID QKNDSQLVIE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 

       310        320        330        340        350        360 
SNSRGEGKPD LKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP SAVPNGPQSP 

       370        380        390        400        410        420 
KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG LSLKLGATPE DFSNLPPEQR RKKLQQKVDE 

       430        440        450        460        470        480 
LNKEIQKEMD QRDAITKMKD VYLKNPQMGD PASLDHKLAE VSQNIEKLRV ETQKFEAWLA 

       490        500        510        520        530        540 
EVEGRLPARS EQARRQSGLY DSQNPPTVNN CAQDRESPDG SYTEEQSQES EMKVLATDFD 

       550        560        570        580        590        600 
DEFDDEEPLP AIGTCKALYT FEGQNEGTIS VVEGETLYVI EEDKGDGWTR IRRNEDEEGY 

       610 
VPTSYVEVCL DKNAKDS 

« Hide

Isoform 2 [UniParc].

Checksum: E82282A5164793B3
Show »

FASTA61671,184
Isoform 3 [UniParc].

Checksum: 0CB6B44D9E174667
Show »

FASTA59268,883
Isoform 4 [UniParc].

Checksum: BA7F73CA1A28A467
Show »

FASTA55164,056

References

« Hide 'large scale' references
[1]"The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia."
Fuchs U., Rehkamp G.F., Haas O.A., Slany R., Koenig M., Bojesen S., Bohle R.M., Damm-Welk C., Ludwig W.-D., Harbott J., Borkhardt A.
Proc. Natl. Acad. Sci. U.S.A. 98:8756-8761(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SNX2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
[2]"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."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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 T.-O., 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-617 (ISOFORM 2), VARIANT ASN-490.
Tissue: Embryo and Placenta.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-409 (ISOFORM 4).
Tissue: Liver and Uterus.
[6]"Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1."
Richnau N., Aspenstroem P.
J. Biol. Chem. 276:35060-35070(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP17.
[7]"Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)."
Ghadimi M.P., Sanzenbacher R., Thiede B., Wenzel J., Jing Q., Plomann M., Borkhardt A., Kabelitz D., Janssen O.
FEBS Lett. 519:50-58(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FASLG.
[8]"The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance."
Fuchs U., Rehkamp G.F., Slany R., Follo M., Borkhardt A.
FEBS Lett. 554:10-16(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX2 AND TNKS, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-515; ASP-519 AND 515-ARG--GLY-520.
[9]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis."
Kamioka Y., Fukuhara S., Sawa H., Nagashima K., Masuda M., Matsuda M., Mochizuki N.
J. Biol. Chem. 279:40091-40099(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DNM1; DNM2 AND DNM3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-602.
[11]"AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus."
Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M., Goldenring J.R.
Mol. Biol. Cell 15:2771-2781(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AKAP9, SUBCELLULAR LOCATION.
[12]"Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins."
Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P.
Dev. Cell 9:791-804(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DNM1 AND WASL, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-7.
[13]"Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL."
Qian J., Chen W., Lettau M., Podda G., Zoernig M., Kabelitz D., Janssen O.
Cell. Signal. 18:1327-1337(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FASLG, SUBCELLULAR LOCATION.
[14]"The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics."
Aspenstroem P., Richnau N., Johansson A.-S.
Exp. Cell Res. 312:2180-2194(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2.
[15]"Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis."
Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T.
J. Cell Biol. 172:269-279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNM2 AND WASL, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-33; ARG-35; 51-LYS-LYS-52 AND 113-ARG-LYS-114.
[16]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-349 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis."
Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L., Liu Z.-J., Wang B.C., Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M. expand/collapse author list , Nagayama K., Takenawa T., Yokoyama S.
Cell 129:761-772(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-300, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN F-BAR, COILED-COIL DOMAIN, MUTAGENESIS OF LYS-33; THR-165; LYS-166; ASP-168 AND PRO-210.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF265550 mRNA. Translation: AAK49824.1. Different initiation.
AB011126 mRNA. Translation: BAA25480.1. Different initiation.
AK000975 mRNA. Translation: BAA91451.1. Different initiation.
AK023681 mRNA. Translation: BAB14638.1.
AL136141, AL158207 Genomic DNA. Translation: CAI12149.1. Sequence problems.
AL136141, AL158207 Genomic DNA. Translation: CAI12150.1. Sequence problems.
AL158207, AL136141 Genomic DNA. Translation: CAI13910.1. Sequence problems.
AL158207, AL136141 Genomic DNA. Translation: CAI13911.1. Sequence problems.
BC062463 mRNA. Translation: AAH62463.1. Sequence problems.
BC101755 mRNA. Translation: AAI01756.1.
CCDSCCDS48040.1. [Q96RU3-1]
RefSeqNP_055848.1. NM_015033.2. [Q96RU3-1]
XP_005251880.1. XM_005251823.1. [Q96RU3-2]
XP_005251886.1. XM_005251829.1. [Q96RU3-3]
UniGeneHs.189409.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EFLX-ray2.61A1-300[»]
ProteinModelPortalQ96RU3.
SMRQ96RU3. Positions 1-288, 400-486, 555-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116686. 19 interactions.
IntActQ96RU3. 17 interactions.
MINTMINT-238223.

PTM databases

PhosphoSiteQ96RU3.

Polymorphism databases

DMDM118572321.

Proteomic databases

MaxQBQ96RU3.
PaxDbQ96RU3.
PRIDEQ96RU3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355681; ENSP00000347907; ENSG00000187239. [Q96RU3-3]
ENST00000446176; ENSP00000413625; ENSG00000187239. [Q96RU3-1]
GeneID23048.
KEGGhsa:23048.
UCSCuc004byw.1. human. [Q96RU3-1]
uc004byx.1. human. [Q96RU3-2]
uc004byz.1. human. [Q96RU3-3]

Organism-specific databases

CTD23048.
GeneCardsGC09M132649.
HGNCHGNC:17069. FNBP1.
HPAHPA019691.
HPA022119.
MIM606191. gene.
neXtProtNX_Q96RU3.
PharmGKBPA128394597.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323796.
HOVERGENHBG002489.
OMAVYIKNPQ.
OrthoDBEOG780RQK.
PhylomeDBQ96RU3.
TreeFamTF351162.

Gene expression databases

ArrayExpressQ96RU3.
BgeeQ96RU3.
GenevestigatorQ96RU3.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR001060. FCH_dom.
IPR028532. FNBP1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR12602:SF21. PTHR12602:SF21. 1 hit.
PfamPF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFNBP1. human.
EvolutionaryTraceQ96RU3.
GeneWikiFNBP1.
GenomeRNAi23048.
NextBio44088.
PMAP-CutDBQ96RU3.
PROQ96RU3.
SOURCESearch...

Entry information

Entry nameFNBP1_HUMAN
AccessionPrimary (citable) accession number: Q96RU3
Secondary accession number(s): O60301 expand/collapse secondary AC list , Q3MIN8, Q5TC87, Q5TC88, Q6P658, Q7LGG2, Q9H8H8, Q9NWD1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM