Q96RU3 (FNBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Formin-binding protein 1

Alternative name(s):
Formin-binding protein 17
Short name=hFBP17

Gene names

Name:	FNBP1
Synonyms:	FBP17, KIAA0554

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	617 AA.
Sequence status	Complete.
Protein existence	Evidence 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.24
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.24
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cytoplasm › cell cortex. Lysosome. Cytoplasmic vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membrane › clathrin-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.24
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.24
Involvement in disease	A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-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.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Coated pit Cytoplasm Cytoplasmic vesicle Cytoskeleton Lysosome Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-1111248,EBI-1111248
DNM1	Q05193	5	EBI-1111248,EBI-713135
GABARAP	O95166	2	EBI-1111248,EBI-712001
SNX2	O60749	4	EBI-1111248,EBI-1046690
TNKS	O95271	4	EBI-1111248,EBI-1105254

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 617

617

Formin-binding protein 1

PRO_0000261430

Regions

Domain

1 – 65

65

FCH

Repeat

416 – 491

76

REM

Domain

550 – 611

62

SH3

Region

1 – 335

335

Interaction with microtubules By similarity

Region

1 – 288

288

F-BAR domain

Region

1 – 79

79

Required for self-association and induction of membrane tubulation

Region

251 – 617

367

Required for self-association and induction of membrane tubulation

Region

400 – 552

153

Interaction with RND2 By similarity

Region

495 – 617

123

Interaction with PDE6G By similarity

Region

514 – 617

104

Required for interaction with TNKS

Region

535 – 617

83

Interaction with DNM1 and DNM3

Region

550 – 617

68

Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2

Region

553 – 610

58

Interaction with FASLG

Region

553 – 609

57

Interaction with DNM2 and WASL

Coiled coil

67 – 259

193

Ref.24

Coiled coil

398 – 490

93

By similarity

Compositional bias

340 – 345

6

Poly-Pro

Sites

Site

166

1

Mediates end-to-end attachment of dimers

Amino acid modifications

Modified residue

66

1

N6-acetyllysine Ref.20

Modified residue

110

1

N6-acetyllysine Ref.20

Modified residue

294

1

Phosphothreonine By similarity

Modified residue

296

1

Phosphoserine Ref.16 Ref.18 Ref.21 Ref.23

Modified residue

299

1

Phosphoserine Ref.18 Ref.23

Modified residue

349

1

Phosphoserine Ref.18

Modified residue

359

1

Phosphoserine Ref.18 Ref.19 Ref.21

Modified residue

497

1

Phosphoserine By similarity

Modified residue

500

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

329 – 394

66

Missing in isoform 4.

VSP_021693

Alternative sequence

330 – 358

29

Missing in isoform 3.

VSP_021694

Alternative sequence

391 – 395

5

Missing in isoform 2.

VSP_021695

Alternative sequence

616 – 617

2

DS → GAKTYI in isoform 2 and isoform 3.

VSP_021696

Natural variant

490

1

S → N. Ref.3
Corresponds to variant rs1023000 [ dbSNP | Ensembl ].

VAR_029388

Experimental info

Mutagenesis

7

1

L → E: Impairs membrane tubulation but does not affect lipid-binding. Ref.12

Mutagenesis

33

1

K → E: Abolishes membrane invagination. Ref.15 Ref.24

Mutagenesis

33

1

K → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-35. Ref.15 Ref.24

Mutagenesis

35

1

R → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-33. Ref.15

Mutagenesis

51 – 52

2

KK → QQ: Impairs lipid-binding and induction of membrane tubulation.

Mutagenesis

113 – 114

2

RK → QQ: Impairs lipid-binding and induction of membrane tubulation.

Mutagenesis

165

1

T → A: Abolishes membrane invagination. Ref.24

Mutagenesis

166

1

K → A: Abolishes membrane invagination. Ref.24

Mutagenesis

168

1

D → A, N or R: No significant effect. Ref.24

Mutagenesis

210

1

P → A: Disrupts helix kink and moderately increases diameter of the induced tubular membrane. Ref.24

Mutagenesis

515 – 520

6

Missing: Abrogates interaction with TNKS. Ref.8

Mutagenesis

515

1

R → A: Impairs interaction with TNKS. Ref.8

Mutagenesis

519

1

D → A: Impairs interaction with TNKS; when associated with A-515. Ref.8

Mutagenesis

602

1

P → L: Abrogates interaction with DNM1, DNM2 and DNM3. Ref.10

Sequence conflict

388

1

K → E in BAA91451. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

617

Helix Strand Turn

Details...

Helix

3 – 6

4

Turn

7 – 9

3

Helix

11 – 52

42

Helix

68 – 160

93

Helix

166 – 206

41

Helix

208 – 238

31

Helix

241 – 257

17

Helix

261 – 272

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: F06E847C6E631EC3	FASTA	617	71,307
	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
	Isoform 2 [UniParc]. Checksum: E82282A5164793B3	FASTA	616	71,184
	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 GATPEDFSNL PPEQRRKKLQ QKVDELNKEI 430 440 450 460 470 480 QKEMDQRDAI TKMKDVYLKN PQMGDPASLD HKLAEVSQNI EKLRVETQKF EAWLAEVEGR 490 500 510 520 530 540 LPARSEQARR QSGLYDSQNP PTVNNCAQDR ESPDGSYTEE QSQESEMKVL ATDFDDEFDD 550 560 570 580 590 600 EEPLPAIGTC KALYTFEGQN EGTISVVEGE TLYVIEEDKG DGWTRIRRNE DEEGYVPTSY 610 VEVCLDKNAK GAKTYI
	Isoform 3 [UniParc]. Checksum: 0CB6B44D9E174667	FASTA	592	68,883
	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 LWPFIKKNKS PKQQKEPLSH RFNEFMTSKP KIHCFRSLKR 370 380 390 400 410 420 GLSLKLGATP EDFSNLPPEQ RRKKLQQKVD ELNKEIQKEM DQRDAITKMK DVYLKNPQMG 430 440 450 460 470 480 DPASLDHKLA EVSQNIEKLR VETQKFEAWL AEVEGRLPAR SEQARRQSGL YDSQNPPTVN 490 500 510 520 530 540 NCAQDRESPD GSYTEEQSQE SEMKVLATDF DDEFDDEEPL PAIGTCKALY TFEGQNEGTI 550 560 570 580 590 SVVEGETLYV IEEDKGDGWT RIRRNEDEEG YVPTSYVEVC LDKNAKGAKT YI
	Isoform 4 [UniParc]. Checksum: BA7F73CA1A28A467	FASTA	551	64,056
	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 LWPFIKKNLG ATPEDFSNLP PEQRRKKLQQ KVDELNKEIQ 370 380 390 400 410 420 KEMDQRDAIT KMKDVYLKNP QMGDPASLDH KLAEVSQNIE KLRVETQKFE AWLAEVEGRL 430 440 450 460 470 480 PARSEQARRQ SGLYDSQNPP TVNNCAQDRE SPDGSYTEEQ SQESEMKVLA TDFDDEFDDE 490 500 510 520 530 540 EPLPAIGTCK ALYTFEGQNE GTISVVEGET LYVIEEDKGD GWTRIRRNED EEGYVPTSYV 550 EVCLDKNAKD S

References

	« Hide 'large scale' referencesShow '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 MLL.
[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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"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, MASS SPECTROMETRY.
[21]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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].
[23]	"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, MASS SPECTROMETRY.
[24]	"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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00102670.
IPI00647034.
IPI00807407.
IPI00807625.

RefSeq

NP_055848.1. NM_015033.2.

UniGene

Hs.189409.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EFL	X-ray	2.61	A	1-300	[»]

ProteinModelPortal

Q96RU3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96RU3. 13 interactions.

PTM databases

PhosphoSite

Q96RU3.

Polymorphism databases

DMDM

118572321.

Proteomic databases

PaxDb

Q96RU3.

PRIDE

Q96RU3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355681; ENSP00000347907; ENSG00000187239.
ENST00000372416; ENSP00000361493; ENSG00000187239.
ENST00000446176; ENSP00000413625; ENSG00000187239.

GeneID

23048.

KEGG

hsa:23048.

UCSC

uc004byw.1. human.
uc004byx.1. human.
uc004byz.1. human.

Organism-specific databases

CTD

23048.

GeneCards

GC09M132649.

HGNC

HGNC:17069. FNBP1.

HPA

HPA019691.
HPA022119.

MIM

606191. gene.

neXtProt

NX_Q96RU3.

PharmGKB

PA128394597.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG323796.

HOVERGEN

HBG002489.

Gene expression databases

ArrayExpress

Q96RU3.

Bgee

Q96RU3.

Genevestigator

Q96RU3.

GermOnline

ENSG00000187239. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

InterPro

IPR001060. FCH_dom.
IPR014729. Rossmann-like_a/b/a_fold.
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. human.

EvolutionaryTrace

Q96RU3.

GenomeRNAi

23048.

NextBio

44088.

PMAP-CutDB

Q96RU3.

SOURCE

Search...

Entry information

Entry name

FNBP1_HUMAN

Accession

Primary (citable) accession number: Q96RU3
Secondary accession number(s): O60301 , 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:	May 1, 2013
This is version 94 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.