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Q96RU3

- FNBP1_HUMAN

UniProt

Q96RU3 - FNBP1_HUMAN

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Protein

Formin-binding protein 1

Gene

FNBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei166 – 1661Mediates end-to-end attachment of dimers

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-binding protein 1
Alternative name(s):
Formin-binding protein 17
Short name:
hFBP17
Gene namesi
Name:FNBP1
Synonyms:FBP17, KIAA0554
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:17069. FNBP1.

Subcellular locationi

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.

GO - Cellular componenti

  1. coated pit Source: UniProtKB-KW
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. lysosome Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71L → E: Impairs membrane tubulation but does not affect lipid-binding. 1 Publication
Mutagenesisi33 – 331K → E: Abolishes membrane invagination. 2 Publications
Mutagenesisi33 – 331K → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-35. 2 Publications
Mutagenesisi35 – 351R → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-33. 1 Publication
Mutagenesisi51 – 522KK → QQ: Impairs lipid-binding and induction of membrane tubulation. 1 Publication
Mutagenesisi113 – 1142RK → QQ: Impairs lipid-binding and induction of membrane tubulation. 1 Publication
Mutagenesisi165 – 1651T → A: Abolishes membrane invagination. 1 Publication
Mutagenesisi166 – 1661K → A: Abolishes membrane invagination. 1 Publication
Mutagenesisi168 – 1681D → A, N or R: No significant effect. 1 Publication
Mutagenesisi210 – 2101P → A: Disrupts helix kink and moderately increases diameter of the induced tubular membrane. 1 Publication
Mutagenesisi515 – 5206Missing: Abrogates interaction with TNKS. 1 Publication
Mutagenesisi515 – 5151R → A: Impairs interaction with TNKS. 1 Publication
Mutagenesisi519 – 5191D → A: Impairs interaction with TNKS; when associated with A-515. 1 Publication
Mutagenesisi602 – 6021P → L: Abrogates interaction with DNM1, DNM2 and DNM3. 1 Publication

Organism-specific databases

PharmGKBiPA128394597.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 617617Formin-binding protein 1PRO_0000261430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysine1 Publication
Modified residuei110 – 1101N6-acetyllysine1 Publication
Modified residuei296 – 2961Phosphoserine4 Publications
Modified residuei299 – 2991Phosphoserine2 Publications
Modified residuei349 – 3491Phosphoserine1 Publication
Modified residuei359 – 3591Phosphoserine3 Publications
Modified residuei497 – 4971PhosphoserineBy similarity
Modified residuei500 – 5001PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96RU3.
PaxDbiQ96RU3.
PRIDEiQ96RU3.

PTM databases

PhosphoSiteiQ96RU3.

Miscellaneous databases

PMAP-CutDBQ96RU3.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ96RU3.
ExpressionAtlasiQ96RU3. baseline and differential.
GenevestigatoriQ96RU3.

Organism-specific databases

HPAiHPA019691.
HPA022119.

Interactioni

Subunit structurei

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.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1111248,EBI-1111248
DNM1Q051935EBI-1111248,EBI-713135
FASLGP480234EBI-1111248,EBI-495538
GABARAPO951662EBI-1111248,EBI-712001
SNX2O607494EBI-1111248,EBI-1046690
TNKSO952714EBI-1111248,EBI-1105254

Protein-protein interaction databases

BioGridi116686. 19 interactions.
IntActiQ96RU3. 17 interactions.
MINTiMINT-238223.

Structurei

Secondary structure

1
617
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Turni7 – 93Combined sources
Helixi11 – 5242Combined sources
Helixi68 – 16093Combined sources
Helixi166 – 20641Combined sources
Helixi208 – 23831Combined sources
Helixi241 – 25717Combined sources
Helixi261 – 27212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EFLX-ray2.61A1-300[»]
ProteinModelPortaliQ96RU3.
SMRiQ96RU3. Positions 1-288, 400-486, 555-608.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96RU3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6565FCHPROSITE-ProRule annotationAdd
BLAST
Repeati416 – 49176REMAdd
BLAST
Domaini550 – 61162SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 335335Interaction with microtubulesBy similarityAdd
BLAST
Regioni1 – 288288F-BAR domainAdd
BLAST
Regioni1 – 7979Required for self-association and induction of membrane tubulationAdd
BLAST
Regioni251 – 617367Required for self-association and induction of membrane tubulationAdd
BLAST
Regioni400 – 552153Interaction with RND2By similarityAdd
BLAST
Regioni495 – 617123Interaction with PDE6GBy similarityAdd
BLAST
Regioni514 – 617104Required for interaction with TNKSAdd
BLAST
Regioni535 – 61783Interaction with DNM1 and DNM3Add
BLAST
Regioni550 – 61768Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2Add
BLAST
Regioni553 – 61058Interaction with FASLGAdd
BLAST
Regioni553 – 60957Interaction with DNM2 and WASLAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili67 – 2591931 PublicationAdd
BLAST
Coiled coili398 – 49093By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi340 – 3456Poly-Pro

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the FNBP1 family.Curated
Contains 1 FCH domain.PROSITE-ProRule annotation
Contains 1 REM (Hr1) repeat.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG323796.
GeneTreeiENSGT00510000046403.
HOVERGENiHBG002489.
InParanoidiQ96RU3.
OMAiVYIKNPQ.
OrthoDBiEOG780RQK.
PhylomeDBiQ96RU3.
TreeFamiTF351162.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR001060. FCH_dom.
IPR028532. FNBP1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR12602:SF21. PTHR12602:SF21. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96RU3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS
60 70 80 90 100
KKYQPKKNSK EEEEYKYTSC KAFISNLNEM NDYAGQHEVI SENMASQIIV
110 120 130 140 150
DLARYVQELK QERKSNFHDG RKAQQHIETC WKQLESSKRR FERDCKEADR
160 170 180 190 200
AQQYFEKMDA DINVTKADVE KARQQAQIRH QMAEDSKADY SSILQKFNHE
210 220 230 240 250
QHEYYHTHIP NIFQKIQEME ERRIVRMGES MKTYAEVDRQ VIPIIGKCLD
260 270 280 290 300
GIVKAAESID QKNDSQLVIE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
310 320 330 340 350
SNSRGEGKPD LKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP
360 370 380 390 400
SAVPNGPQSP KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG LSLKLGATPE
410 420 430 440 450
DFSNLPPEQR RKKLQQKVDE LNKEIQKEMD QRDAITKMKD VYLKNPQMGD
460 470 480 490 500
PASLDHKLAE VSQNIEKLRV ETQKFEAWLA EVEGRLPARS EQARRQSGLY
510 520 530 540 550
DSQNPPTVNN CAQDRESPDG SYTEEQSQES EMKVLATDFD DEFDDEEPLP
560 570 580 590 600
AIGTCKALYT FEGQNEGTIS VVEGETLYVI EEDKGDGWTR IRRNEDEEGY
610
VPTSYVEVCL DKNAKDS
Length:617
Mass (Da):71,307
Last modified:November 28, 2006 - v2
Checksum:iF06E847C6E631EC3
GO
Isoform 2 (identifier: Q96RU3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     391-395: Missing.
     616-617: DS → GAKTYI

Show »
Length:616
Mass (Da):71,184
Checksum:iE82282A5164793B3
GO
Isoform 3 (identifier: Q96RU3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     330-358: Missing.
     616-617: DS → GAKTYI

Show »
Length:592
Mass (Da):68,883
Checksum:i0CB6B44D9E174667
GO
Isoform 4 (identifier: Q96RU3-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:551
Mass (Da):64,056
Checksum:iBA7F73CA1A28A467
GO

Sequence cautioni

The sequence AAH62463.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAK49824.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA25480.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA91451.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI12149.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI12150.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI13910.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI13911.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti388 – 3881K → E in BAA91451. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti490 – 4901S → N.1 Publication
Corresponds to variant rs1023000 [ dbSNP | Ensembl ].
VAR_029388

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei329 – 39466Missing in isoform 4. 1 PublicationVSP_021693Add
BLAST
Alternative sequencei330 – 35829Missing in isoform 3. 1 PublicationVSP_021694Add
BLAST
Alternative sequencei391 – 3955Missing in isoform 2. 1 PublicationVSP_021695
Alternative sequencei616 – 6172DS → GAKTYI in isoform 2 and isoform 3. 1 PublicationVSP_021696

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48040.1. [Q96RU3-1]
RefSeqiNP_055848.1. NM_015033.2. [Q96RU3-1]
XP_005251880.1. XM_005251823.1. [Q96RU3-2]
XP_005251886.1. XM_005251829.1. [Q96RU3-3]
UniGeneiHs.189409.

Genome annotation databases

EnsembliENST00000355681; ENSP00000347907; ENSG00000187239. [Q96RU3-3]
ENST00000446176; ENSP00000413625; ENSG00000187239. [Q96RU3-1]
GeneIDi23048.
KEGGihsa:23048.
UCSCiuc004byw.1. human. [Q96RU3-1]
uc004byx.1. human. [Q96RU3-2]
uc004byz.1. human. [Q96RU3-3]

Polymorphism databases

DMDMi118572321.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS48040.1. [Q96RU3-1 ]
RefSeqi NP_055848.1. NM_015033.2. [Q96RU3-1 ]
XP_005251880.1. XM_005251823.1. [Q96RU3-2 ]
XP_005251886.1. XM_005251829.1. [Q96RU3-3 ]
UniGenei Hs.189409.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EFL X-ray 2.61 A 1-300 [» ]
ProteinModelPortali Q96RU3.
SMRi Q96RU3. Positions 1-288, 400-486, 555-608.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116686. 19 interactions.
IntActi Q96RU3. 17 interactions.
MINTi MINT-238223.

PTM databases

PhosphoSitei Q96RU3.

Polymorphism databases

DMDMi 118572321.

Proteomic databases

MaxQBi Q96RU3.
PaxDbi Q96RU3.
PRIDEi Q96RU3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355681 ; ENSP00000347907 ; ENSG00000187239 . [Q96RU3-3 ]
ENST00000446176 ; ENSP00000413625 ; ENSG00000187239 . [Q96RU3-1 ]
GeneIDi 23048.
KEGGi hsa:23048.
UCSCi uc004byw.1. human. [Q96RU3-1 ]
uc004byx.1. human. [Q96RU3-2 ]
uc004byz.1. human. [Q96RU3-3 ]

Organism-specific databases

CTDi 23048.
GeneCardsi GC09M132649.
HGNCi HGNC:17069. FNBP1.
HPAi HPA019691.
HPA022119.
MIMi 606191. gene.
neXtProti NX_Q96RU3.
PharmGKBi PA128394597.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG323796.
GeneTreei ENSGT00510000046403.
HOVERGENi HBG002489.
InParanoidi Q96RU3.
OMAi VYIKNPQ.
OrthoDBi EOG780RQK.
PhylomeDBi Q96RU3.
TreeFami TF351162.

Miscellaneous databases

ChiTaRSi FNBP1. human.
EvolutionaryTracei Q96RU3.
GeneWikii FNBP1.
GenomeRNAii 23048.
NextBioi 44088.
PMAP-CutDB Q96RU3.
PROi Q96RU3.
SOURCEi Search...

Gene expression databases

Bgeei Q96RU3.
ExpressionAtlasi Q96RU3. baseline and differential.
Genevestigatori Q96RU3.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
InterProi IPR001060. FCH_dom.
IPR028532. FNBP1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR12602:SF21. PTHR12602:SF21. 1 hit.
Pfami PF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
SMARTi SM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, 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. 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. 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. 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.

Entry informationi

Entry nameiFNBP1_HUMAN
AccessioniPrimary (citable) accession number: Q96RU3
Secondary accession number(s): O60301
, Q3MIN8, Q5TC87, Q5TC88, Q6P658, Q7LGG2, Q9H8H8, Q9NWD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: November 26, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3