Q5T0N5 (FBP1L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Formin-binding protein 1-like

Alternative name(s):
Transducer of Cdc42-dependent actin assembly protein 1
Short name=Toca-1

Gene names

Name:	FNBP1L
Synonyms:	C1orf39, TOCA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	605 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 endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens. Ref.1 Ref.5 Ref.10
Subunit structure	Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures By similarity. Interacts with GTP-bound CDC42. Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and WASL/N-WASP. Interacts with ATG3. Ref.1 Ref.5 Ref.6 Ref.7 Ref.10
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton By similarity. Cytoplasm › cell cortex By similarity. Cytoplasmic vesicle By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity Ref.8.
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 BAA91051.1 differs from that shown. Reason: Erroneous initiation. The sequence CAI18954.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI18981.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Autophagy Endocytosis
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	autophagy Inferred from electronic annotation. Source: UniProtKB-KW clathrin-mediated endocytosis Inferred from direct assay PubMed 20730103. Source: BHF-UCL membrane budding Inferred from direct assay PubMed 20730103. Source: BHF-UCL membrane invagination Inferred from direct assay PubMed 20730103. Source: BHF-UCL membrane tubulation Inferred from direct assay PubMed 20730103. Source: BHF-UCL positive regulation of filopodium assembly Inferred from direct assay PubMed 20730103. Source: BHF-UCL vesicle transport along actin filament Inferred from direct assay PubMed 20730103. Source: BHF-UCL
Cellular_component	cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic membrane-bounded vesicle Inferred from direct assay PubMed 20730103. Source: BHF-UCL cytoskeleton 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: Q5T0N5-1)

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.

Note: Gene prediction based on EST data.

Isoform 2 (identifier: Q5T0N5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     384-388: Missing.

Note: Gene prediction based on EST data.

Isoform 3 (identifier: Q5T0N5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     331-388: Missing.

Isoform 4 (identifier: Q5T0N5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     331-388: Missing.
     605-605: S → AVTYI

Note: Gene prediction based on EST data.

Isoform 5 (identifier: Q5T0N5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     384-388: Missing.
     605-605: S → AVTYI

Note: Gene prediction based on EST data. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 605	605	Formin-binding protein 1-like		PRO_0000261434
Regions
	Domain	1 – 65	65	FCH
	Repeat	409 – 484	76	REM
	Domain	538 – 599	62	SH3
	Region	1 – 287	287	F-BAR domain By similarity
	Region	245 – 535	291	Interaction with CDC42
	Region	522 – 605	84	Interaction with DNM1
	Region	541 – 605	65	Interaction with DAAM1, DIAPH1 and DIAPH2
	Region	541 – 597	57	Interaction with DNM2 and WASL
	Coiled coil	66 – 258	193	By similarity
	Coiled coil	392 – 484	93	By similarity
Sites
	Site	165	1	Mediates end-to-end attachment of dimers By similarity
Amino acid modifications
	Modified residue	295	1	Phosphoserine Ref.9 Ref.11 Ref.13
	Modified residue	488	1	Phosphoserine Ref.9 Ref.11 Ref.13
	Modified residue	501	1	Phosphoserine Ref.9 Ref.11 Ref.13
Natural variations
	Alternative sequence	331 – 388	58	Missing in isoform 3 and isoform 4.		VSP_021709
	Alternative sequence	384 – 388	5	Missing in isoform 2 and isoform 5.		VSP_021710
	Alternative sequence	605	1	S → AVTYI in isoform 4 and isoform 5.		VSP_021711
Experimental info
	Mutagenesis	441 – 443	3	MGD → IST: Impairs interaction with CDC42 and reduces CDC42-induced actin assembly. Ref.1
	Mutagenesis	576	1	W → K: Impairs interaction with WASL and reduces CDC42-induced actin assembly. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 9C8576E8FAA3B626	FASTA	605	69,977
	10 20 30 40 50 60 MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK 70 80 90 100 110 120 DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR 130 140 150 160 170 180 KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH 190 200 210 220 230 240 MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV 250 260 270 280 290 300 IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS 310 320 330 340 350 360 ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTFSIEPV 370 380 390 400 410 420 HYCMNEIKTG KPRIPSFRSL KRGVSLIMGP ALEDFSHLPP EQRRKKLQQR IDELNRELQK 430 440 450 460 470 480 ESDQKDALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG 490 500 510 520 530 540 GRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHNEFDDE FEDDDPLPAI 550 560 570 580 590 600 GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TSYIDVTLEK NSKGS
	Isoform 2 [UniParc]. Checksum: 1C2DDFB3A3A5F0B3	FASTA	600	69,434
	10 20 30 40 50 60 MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK 70 80 90 100 110 120 DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR 130 140 150 160 170 180 KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH 190 200 210 220 230 240 MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV 250 260 270 280 290 300 IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS 310 320 330 340 350 360 ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTFSIEPV 370 380 390 400 410 420 HYCMNEIKTG KPRIPSFRSL KRGGPALEDF SHLPPEQRRK KLQQRIDELN RELQKESDQK 430 440 450 460 470 480 DALNKMKDVY EKNPQMGDPG SLQPKLAETM NNIDRLRMEI HKNEAWLSEV EGKTGGRGDR 490 500 510 520 530 540 RHSSDINHLV TQGRESPEGS YTDDANQEVR GPPQQHGHHN EFDDEFEDDD PLPAIGHCKA 550 560 570 580 590 600 IYPFDGHNEG TLAMKEGEVL YIIEEDKGDG WTRARRQNGE EGYVPTSYID VTLEKNSKGS
	Isoform 3 [UniParc]. Checksum: 416101498FF99567	FASTA	547	63,572
	10 20 30 40 50 60 MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK 70 80 90 100 110 120 DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR 130 140 150 160 170 180 KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH 190 200 210 220 230 240 MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV 250 260 270 280 290 300 IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS 310 320 330 340 350 360 ASKQESGKMD AKTTVGKAKG KLWLFGKKPK GPALEDFSHL PPEQRRKKLQ QRIDELNREL 370 380 390 400 410 420 QKESDQKDAL NKMKDVYEKN PQMGDPGSLQ PKLAETMNNI DRLRMEIHKN EAWLSEVEGK 430 440 450 460 470 480 TGGRGDRRHS SDINHLVTQG RESPEGSYTD DANQEVRGPP QQHGHHNEFD DEFEDDDPLP 490 500 510 520 530 540 AIGHCKAIYP FDGHNEGTLA MKEGEVLYII EEDKGDGWTR ARRQNGEEGY VPTSYIDVTL EKNSKGS
	Isoform 4 [UniParc]. Checksum: B14EB59CE9010149	FASTA	551	64,033
	10 20 30 40 50 60 MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK 70 80 90 100 110 120 DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR 130 140 150 160 170 180 KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH 190 200 210 220 230 240 MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV 250 260 270 280 290 300 IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS 310 320 330 340 350 360 ASKQESGKMD AKTTVGKAKG KLWLFGKKPK GPALEDFSHL PPEQRRKKLQ QRIDELNREL 370 380 390 400 410 420 QKESDQKDAL NKMKDVYEKN PQMGDPGSLQ PKLAETMNNI DRLRMEIHKN EAWLSEVEGK 430 440 450 460 470 480 TGGRGDRRHS SDINHLVTQG RESPEGSYTD DANQEVRGPP QQHGHHNEFD DEFEDDDPLP 490 500 510 520 530 540 AIGHCKAIYP FDGHNEGTLA MKEGEVLYII EEDKGDGWTR ARRQNGEEGY VPTSYIDVTL 550 EKNSKGAVTY I
	Isoform 5 [UniParc]. Checksum: 8C72A845744DDFB3	FASTA	604	69,894
	10 20 30 40 50 60 MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK 70 80 90 100 110 120 DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR 130 140 150 160 170 180 KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH 190 200 210 220 230 240 MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV 250 260 270 280 290 300 IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS 310 320 330 340 350 360 ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTFSIEPV 370 380 390 400 410 420 HYCMNEIKTG KPRIPSFRSL KRGGPALEDF SHLPPEQRRK KLQQRIDELN RELQKESDQK 430 440 450 460 470 480 DALNKMKDVY EKNPQMGDPG SLQPKLAETM NNIDRLRMEI HKNEAWLSEV EGKTGGRGDR 490 500 510 520 530 540 RHSSDINHLV TQGRESPEGS YTDDANQEVR GPPQQHGHHN EFDDEFEDDD PLPAIGHCKA 550 560 570 580 590 600 IYPFDGHNEG TLAMKEGEVL YIIEEDKGDG WTRARRQNGE EGYVPTSYID VTLEKNSKGA VTYI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex." Ho H.-Y.H., Rohatgi R., Lebensohn A.M., Ma L., Li J., Gygi S.P., Kirschner M.W. Cell 118:203-216(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH CDC42 AND WASL, MUTAGENESIS OF 441-MET--ASP-443 AND TRP-576. Tissue: Fetal brain.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] OF 134-605 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-605 (ISOFORM 3). Tissue: Lung and Pituitary.
[4]	"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. , 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] OF 200-605 (ISOFORM 3). Tissue: Hepatoma.
[5]	"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, INTERACTION WITH DNM1 AND WASL.
[6]	"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.
[7]	"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: INTERACTION WITH DNM2 AND WASL.
[8]	"Tuba stimulates intracellular N-WASP-dependent actin assembly." Kovacs E.M., Makar R.S., Gertler F.B. J. Cell Sci. 119:2715-2726(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"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-295; SER-488 AND SER-501, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A novel hybrid yeast-human network analysis reveals an essential role for FNBP1L in antibacterial autophagy." Huett A., Ng A., Cao Z., Kuballa P., Komatsu M., Daly M.J., Podolsky D.K., Xavier R.J. J. Immunol. 182:4917-4930(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN AUTOPHAGY, INTERACTION WITH ATG3.
[11]	"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-295; SER-488 AND SER-501, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"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-295; SER-488 AND SER-501, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY514449 mRNA. Translation: AAR98814.1. AL109613, AC095034, AL512651 Genomic DNA. Translation: CAI18952.1. AL109613, AC095034, AL512651 Genomic DNA. Translation: CAI18953.1. AL109613, AC095034, AL512651 Genomic DNA. Translation: CAI18954.1. Sequence problems. AL512651, AC095034, AL109613 Genomic DNA. Translation: CAI18979.1. AL512651, AC095034, AL109613 Genomic DNA. Translation: CAI18980.1. AL512651, AC095034, AL109613 Genomic DNA. Translation: CAI18981.1. Sequence problems. BC062477 mRNA. Translation: AAH62477.1. BC074891 mRNA. Translation: AAH74891.1. BC074892 mRNA. Translation: AAH74892.1. AK000282 mRNA. Translation: BAA91051.1. Different initiation.
IPI	IPI00015580. IPI00028718. IPI00607808. IPI00646028. IPI00937956.
RefSeq	NP_001020119.1. NM_001024948.2. NP_001157945.1. NM_001164473.2. NP_060207.2. NM_017737.4.
UniGene	Hs.134060.
3D structure databases
HSSP	HSSP built from PDB template 2CT4 based on UniProtKB Q15642.
ProteinModelPortal	Q5T0N5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5T0N5. 3 interactions.
MINT	MINT-1424364.
STRING	9606.ENSP00000271234.
PTM databases
PhosphoSite	Q5T0N5.
Polymorphism databases
DMDM	118572313.
Proteomic databases
PaxDb	Q5T0N5.
PRIDE	Q5T0N5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260506; ENSP00000260506; ENSG00000137942. ENST00000370253; ENSP00000359275; ENSG00000137942. ENST00000370256; ENSP00000359278; ENSG00000137942. ENST00000424449; ENSP00000397451; ENSG00000137942.
GeneID	54874.
KEGG	hsa:54874.
UCSC	uc001dpv.3. human. uc001dpw.3. human. uc010otk.2. human.
Organism-specific databases
CTD	54874.
GeneCards	GC01P093913.
HGNC	HGNC:20851. FNBP1L.
MIM	608848. gene.
neXtProt	NX_Q5T0N5.
PharmGKB	PA128394675.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG323796.
HOGENOM	HOG000231767.
HOVERGEN	HBG002489.
Gene expression databases
ArrayExpress	Q5T0N5.
Bgee	Q5T0N5.
CleanEx	HS_FNBP1L.
Genevestigator	Q5T0N5.
GermOnline	ENSG00000137942. Homo sapiens.
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
GenomeRNAi	54874.
NextBio	57799.
SOURCE	Search...

Entry information

Entry name

FBP1L_HUMAN

Accession

Primary (citable) accession number: Q5T0N5
Secondary accession number(s): Q5T0N6 , Q6B097, Q6P653, Q6R4Q4, Q9NXG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 28, 2006
Last modified:	May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.