Q80TY0 (FNBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Formin-binding protein 1

Alternative name(s):
Formin-binding protein 17

Gene names

Name:	Fnbp1
Synonyms:	Fbp17, Kiaa0554

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	616 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 act as a link between RND2 signaling and regulation of the actin cytoskeleton. May be required for the lysosomal retention of FASLG/FASL By similarity.
Subunit structure	Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts specifically with GTP-bound RND2 and CDC42. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, microtubules, PDE6G, SNX2 and WASL/N-WASP. May interact with TNKS By similarity.
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity. Cytoplasm › cell cortex By similarity. Lysosome By similarity. Cytoplasmic vesicle By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Membrane › clathrin-coated pit By similarity. Note: Enriched in cortical regions coincident with F-actin By similarity. Also localizes to endocytic vesicles and lysosomes By similarity.
Tissue specificity	Expressed in brain and testis. Ref.5
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 By similarity.
Sequence similarities	Belongs to the FNBP1 family. Contains 1 FCH domain. Contains 1 REM (Hr1) repeat. Contains 1 SH3 domain.
Sequence caution	The sequence BAC65590.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE33974.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Coated pit Cytoplasm Cytoplasmic vesicle Cytoskeleton Lysosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q80TY0-1)

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: Q80TY0-2)

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

Isoform 3 (identifier: Q80TY0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     329-394: Missing.
     515-515: E → ES

Isoform 4 (identifier: Q80TY0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     329-338: Missing.
     390-394: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q80TY0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     329-338: LMSLLTSPHQ → VLAIWTLRGL
     339-616: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 616	616	Formin-binding protein 1		PRO_0000261431
Regions
	Domain	1 – 65	65	FCH
	Repeat	415 – 490	76	REM
	Domain	549 – 610	62	SH3
	Region	1 – 334	334	Interaction with microtubules By similarity
	Region	1 – 288	288	F-BAR domain By similarity
	Region	1 – 79	79	Required for self-association and induction of membrane tubulation By similarity
	Region	251 – 616	366	Required for self-association and induction of membrane tubulation By similarity
	Region	399 – 551	153	Interaction with RND2 By similarity
	Region	494 – 616	123	Interaction with PDE6G By similarity
	Region	513 – 616	104	Required for interaction with TNKS By similarity
	Region	534 – 616	83	Interaction with DNM1 and DNM3 By similarity
	Region	549 – 616	68	Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2 By similarity
	Region	552 – 609	58	Interaction with FASLG By similarity
	Region	552 – 608	57	Interaction with DNM2 and WASL By similarity
	Coiled coil	67 – 259	193	By similarity
	Coiled coil	398 – 490	93	By similarity
	Compositional bias	336 – 365	30	Pro-rich
Sites
	Site	166	1	Mediates end-to-end attachment of dimers By similarity
Amino acid modifications
	Modified residue	66	1	N6-acetyllysine By similarity
	Modified residue	110	1	N6-acetyllysine By similarity
	Modified residue	294	1	Phosphothreonine Ref.8
	Modified residue	296	1	Phosphoserine Ref.6 Ref.9
	Modified residue	299	1	Phosphoserine Ref.6
	Modified residue	348	1	Phosphoserine By similarity
	Modified residue	358	1	Phosphoserine By similarity
	Modified residue	496	1	Phosphoserine Ref.7 Ref.8
	Modified residue	499	1	Phosphotyrosine Ref.7
Natural variations
	Alternative sequence	1 – 79	79	Missing in isoform 4.		VSP_021697
	Alternative sequence	329 – 394	66	Missing in isoform 2 and isoform 3.		VSP_021698
	Alternative sequence	329 – 338	10	Missing in isoform 4.		VSP_021699
	Alternative sequence	329 – 338	10	LMSLLTSPHQ → VLAIWTLRGL in isoform 5.		VSP_021700
	Alternative sequence	339 – 616	278	Missing in isoform 5.		VSP_021701
	Alternative sequence	390 – 394	5	Missing in isoform 4.		VSP_021702
	Alternative sequence	515	1	E → ES in isoform 3.		VSP_021703

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 947BFCFCCA4BD1E2	FASTA	616	71,344
	10 20 30 40 50 60 MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK 70 80 90 100 110 120 EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV DLMRYVQELK QERKSNFHDG 130 140 150 160 170 180 RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRQ 190 200 210 220 230 240 QMAEDSKADY SLILQRFNQE QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ 250 260 270 280 290 300 VIPIIGKCLD GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 310 320 330 340 350 360 SSSKEGKPEL RFGGKSRGKL WPFIKKNKLM SLLTSPHQPP PPPPASASPS AVPNGPQSPK 370 380 390 400 410 420 QPKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED FSNFPPEQRR KKLQQKVDDL 430 440 450 460 470 480 NREIQKETDQ RDAITKMKDV YLKNPQMGDP ASLDQKLTEV TQNIEKLRLE AQKFEAWLAE 490 500 510 520 530 540 VEGRLPARSE QARRQSGLYD GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLAPDFDD 550 560 570 580 590 600 EFDDEEPLPA IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV 610 PTSYVEVYLD KNAKGS
	Isoform 2 [UniParc]. Checksum: AA80F83DEBE4AC5B	FASTA	550	64,139
	10 20 30 40 50 60 MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK 70 80 90 100 110 120 EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV DLMRYVQELK QERKSNFHDG 130 140 150 160 170 180 RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRQ 190 200 210 220 230 240 QMAEDSKADY SLILQRFNQE QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ 250 260 270 280 290 300 VIPIIGKCLD GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 310 320 330 340 350 360 SSSKEGKPEL RFGGKSRGKL WPFIKKNKGV TPEDFSNFPP EQRRKKLQQK VDDLNREIQK 370 380 390 400 410 420 ETDQRDAITK MKDVYLKNPQ MGDPASLDQK LTEVTQNIEK LRLEAQKFEA WLAEVEGRLP 430 440 450 460 470 480 ARSEQARRQS GLYDGQTHQT VTNCAQDRES PDGSYTEEQS QESEHKVLAP DFDDEFDDEE 490 500 510 520 530 540 PLPAIGTCKA LYTFEGQNEG TISVVEGETL SVIEEDKGDG WTRIRRNEDE EGYVPTSYVE 550 VYLDKNAKGS
	Isoform 3 [UniParc]. Checksum: E73927365F88D8C2	FASTA	551	64,226
	10 20 30 40 50 60 MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK 70 80 90 100 110 120 EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV DLMRYVQELK QERKSNFHDG 130 140 150 160 170 180 RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRQ 190 200 210 220 230 240 QMAEDSKADY SLILQRFNQE QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ 250 260 270 280 290 300 VIPIIGKCLD GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 310 320 330 340 350 360 SSSKEGKPEL RFGGKSRGKL WPFIKKNKGV TPEDFSNFPP EQRRKKLQQK VDDLNREIQK 370 380 390 400 410 420 ETDQRDAITK MKDVYLKNPQ MGDPASLDQK LTEVTQNIEK LRLEAQKFEA WLAEVEGRLP 430 440 450 460 470 480 ARSEQARRQS GLYDGQTHQT VTNCAQDRES SPDGSYTEEQ SQESEHKVLA PDFDDEFDDE 490 500 510 520 530 540 EPLPAIGTCK ALYTFEGQNE GTISVVEGET LSVIEEDKGD GWTRIRRNED EEGYVPTSYV 550 EVYLDKNAKG S
	Isoform 4 [UniParc]. Checksum: 482B1709BE440057	FASTA	522	60,086
	10 20 30 40 50 60 MNDYAGQHEV ISENMTSQIT VDLMRYVQEL KQERKSNFHD GRKAQQHIET CWKQLESSKR 70 80 90 100 110 120 RFERDCKEAD RAQQYFEKMD ADINVTKADV EKARQQAQIR QQMAEDSKAD YSLILQRFNQ 130 140 150 160 170 180 EQWEYYHTHI PNIFQKIQEM EERRIVRIGE SMKTYAEVDR QVIPIIGKCL DGIVKAAESI 190 200 210 220 230 240 DQKNDSQLVV EAYKSGFEPP GDIEFEDYTQ PMKRTVSDNS LSSSKEGKPE LRFGGKSRGK 250 260 270 280 290 300 LWPFIKKNKP PPPPPASASP SAVPNGPQSP KQPKEPLSHR FNEFMTSKPK IHCFRSLKRG 310 320 330 340 350 360 GVTPEDFSNF PPEQRRKKLQ QKVDDLNREI QKETDQRDAI TKMKDVYLKN PQMGDPASLD 370 380 390 400 410 420 QKLTEVTQNI EKLRLEAQKF EAWLAEVEGR LPARSEQARR QSGLYDGQTH QTVTNCAQDR 430 440 450 460 470 480 ESPDGSYTEE QSQESEHKVL APDFDDEFDD EEPLPAIGTC KALYTFEGQN EGTISVVEGE 490 500 510 520 TLSVIEEDKG DGWTRIRRNE DEEGYVPTSY VEVYLDKNAK GS
	Isoform 5 [UniParc]. Checksum: F83CA4FE103657D2	FASTA	338	39,972
	10 20 30 40 50 60 MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK 70 80 90 100 110 120 EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV DLMRYVQELK QERKSNFHDG 130 140 150 160 170 180 RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRQ 190 200 210 220 230 240 QMAEDSKADY SLILQRFNQE QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ 250 260 270 280 290 300 VIPIIGKCLD GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 310 320 330 SSSKEGKPEL RFGGKSRGKL WPFIKKNKVL AIWTLRGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H. DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-616 (ISOFORM 5). Strain: C57BL/6J and NOD. Tissue: Dendritic cell, Embryo, Kidney and Spleen.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"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 5). Strain: FVB/N. Tissue: Mammary gland.
[5]	"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: TISSUE SPECIFICITY.
[6]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-299, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND TYR-499, MASS SPECTROMETRY. Tissue: Mast cell.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294 AND SER-496, MASS SPECTROMETRY. Tissue: Melanoma.
[9]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK122308 mRNA. Translation: BAC65590.1. Different initiation. AK052652 mRNA. Translation: BAC35082.1. AK143512 mRNA. Translation: BAE25408.1. AK157135 mRNA. Translation: BAE33974.1. Different initiation. AK170497 mRNA. Translation: BAE41836.1. AK172100 mRNA. Translation: BAE42825.1. AL844546 Genomic DNA. Translation: CAM18436.1. AL844546 Genomic DNA. Translation: CAM18442.1. BC003867 mRNA. Translation: AAH03867.1.
IPI	IPI00116278. IPI00719992. IPI00755941. IPI00808090. IPI00876259.
RefSeq	NP_001033789.1. NM_001038700.2. NP_001171119.1. NM_001177648.1. NP_001171120.1. NM_001177649.1. NP_001171121.1. NM_001177650.1. NP_062279.1. NM_019406.3.
UniGene	Mm.440993. Mm.52297.
3D structure databases
HSSP	HSSP built from PDB template 2CT4 based on UniProtKB Q15642.
ProteinModelPortal	Q80TY0.
SMR	Q80TY0. Positions 1-288, 399-485, 554-607.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q80TY0. 1 interaction.
STRING	10090.ENSMUSP00000109183.
PTM databases
PhosphoSite	Q80TY0.
Proteomic databases
PaxDb	Q80TY0.
PRIDE	Q80TY0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000113552; ENSMUSP00000109181; ENSMUSG00000075415. ENSMUST00000113559; ENSMUSP00000109189; ENSMUSG00000075415. ENSMUST00000113560; ENSMUSP00000109190; ENSMUSG00000075415. ENSMUST00000113562; ENSMUSP00000109192; ENSMUSG00000075415. ENSMUST00000113564; ENSMUSP00000109194; ENSMUSG00000075415.
GeneID	14269.
KEGG	mmu:14269.
UCSC	uc008jdh.1. mouse. uc008jdi.2. mouse. uc008jdj.2. mouse. uc008jdk.2. mouse. uc008jdm.2. mouse.
Organism-specific databases
CTD	23048.
MGI	MGI:109606. Fnbp1.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG323796.
GeneTree	ENSGT00510000046403.
HOVERGEN	HBG002489.
OMA	LDKNAKG.
OrthoDB	EOG40S0FF.
Gene expression databases
ArrayExpress	Q80TY0.
Bgee	Q80TY0.
CleanEx	MM_FNBP1.
Genevestigator	Q80TY0.
GermOnline	ENSMUSG00000075415. Mus musculus.
Family and domain databases
InterPro	IPR001060. FCH_dom. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00611. FCH. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
SMART	SM00055. FCH. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50133. FCH. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FNBP1. mouse.
NextBio	285633.
SOURCE	Search...

Entry information

Entry name

FNBP1_MOUSE

Accession

Primary (citable) accession number: Q80TY0
Secondary accession number(s): A2AQ40 , A2AQ46, Q3TA45, Q3TCW9, Q3U081, Q3UPI7, Q8C727, Q99L37

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 28, 2006
Last modified:	May 1, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program