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Protein

Formin-binding protein 1

Gene

Fnbp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

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

GO - Molecular functioni

  1. identical protein binding Source: MGI
  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
Gene namesi
Name:Fnbp1
Synonyms:Fbp17, Kiaa0554
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:109606. Fnbp1.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Lysosome By similarity. Cytoplasmic vesicle By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Membraneclathrin-coated pit By similarity
Note: Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes.By similarity

GO - Cellular componenti

  1. cell cortex Source: UniProtKB-SubCell
  2. coated pit Source: UniProtKB-SubCell
  3. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  4. cytoskeleton Source: UniProtKB-SubCell
  5. lysosome Source: UniProtKB-SubCell
  6. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 616616Formin-binding protein 1PRO_0000261431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysineBy similarity
Modified residuei110 – 1101N6-acetyllysineBy similarity
Modified residuei296 – 2961Phosphoserine1 Publication
Modified residuei299 – 2991PhosphoserineBy similarity
Modified residuei348 – 3481PhosphoserineBy similarity
Modified residuei358 – 3581PhosphoserineBy similarity
Modified residuei496 – 4961Phosphoserine1 Publication
Modified residuei499 – 4991Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ80TY0.
PaxDbiQ80TY0.
PRIDEiQ80TY0.

PTM databases

PhosphoSiteiQ80TY0.

Expressioni

Tissue specificityi

Expressed in brain and testis.1 Publication

Gene expression databases

BgeeiQ80TY0.
CleanExiMM_FNBP1.
ExpressionAtlasiQ80TY0. baseline and differential.
GenevestigatoriQ80TY0.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi199720. 1 interaction.
IntActiQ80TY0. 2 interactions.
MINTiMINT-4123990.
STRINGi10090.ENSMUSP00000109183.

Structurei

3D structure databases

ProteinModelPortaliQ80TY0.
SMRiQ80TY0. Positions 1-288, 399-485, 554-607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 264264F-BARPROSITE-ProRule annotationAdd
BLAST
Repeati415 – 49076REMAdd
BLAST
Domaini549 – 61062SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 334334Interaction with microtubulesBy similarityAdd
BLAST
Regioni1 – 7979Required for self-association and induction of membrane tubulationBy similarityAdd
BLAST
Regioni251 – 616366Required for self-association and induction of membrane tubulationBy similarityAdd
BLAST
Regioni399 – 551153Interaction with RND2By similarityAdd
BLAST
Regioni494 – 616123Interaction with PDE6GBy similarityAdd
BLAST
Regioni513 – 616104Required for interaction with TNKSBy similarityAdd
BLAST
Regioni534 – 61683Interaction with DNM1 and DNM3By similarityAdd
BLAST
Regioni549 – 61668Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2By similarityAdd
BLAST
Regioni552 – 60958Interaction with FASLGBy similarityAdd
BLAST
Regioni552 – 60857Interaction with DNM2 and WASLBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili67 – 259193By similarityAdd
BLAST
Coiled coili398 – 49093By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi336 – 36530Pro-richAdd
BLAST

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the FNBP1 family.Curated
Contains 1 F-BAR 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.
InParanoidiQ80TY0.
OMAiVYIKNPQ.
PhylomeDBiQ80TY0.
TreeFamiTF351162.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR028532. FNBP1/FBP17.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR12602:SF21. PTHR12602:SF21. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80TY0-1) [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 EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV
110 120 130 140 150
DLMRYVQELK QERKSNFHDG RKAQQHIETC WKQLESSKRR FERDCKEADR
160 170 180 190 200
AQQYFEKMDA DINVTKADVE KARQQAQIRQ QMAEDSKADY SLILQRFNQE
210 220 230 240 250
QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ VIPIIGKCLD
260 270 280 290 300
GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
310 320 330 340 350
SSSKEGKPEL RFGGKSRGKL WPFIKKNKLM SLLTSPHQPP PPPPASASPS
360 370 380 390 400
AVPNGPQSPK QPKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED
410 420 430 440 450
FSNFPPEQRR KKLQQKVDDL NREIQKETDQ RDAITKMKDV YLKNPQMGDP
460 470 480 490 500
ASLDQKLTEV TQNIEKLRLE AQKFEAWLAE VEGRLPARSE QARRQSGLYD
510 520 530 540 550
GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLAPDFDD EFDDEEPLPA
560 570 580 590 600
IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV
610
PTSYVEVYLD KNAKGS
Length:616
Mass (Da):71,344
Last modified:November 28, 2006 - v2
Checksum:i947BFCFCCA4BD1E2
GO
Isoform 2 (identifier: Q80TY0-2) [UniParc]FASTAAdd to basket

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

Show »
Length:550
Mass (Da):64,139
Checksum:iAA80F83DEBE4AC5B
GO
Isoform 3 (identifier: Q80TY0-3) [UniParc]FASTAAdd to basket

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

Show »
Length:551
Mass (Da):64,226
Checksum:iE73927365F88D8C2
GO
Isoform 4 (identifier: Q80TY0-4) [UniParc]FASTAAdd to basket

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.

Show »
Length:522
Mass (Da):60,086
Checksum:i482B1709BE440057
GO
Isoform 5 (identifier: Q80TY0-5) [UniParc]FASTAAdd to basket

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

Show »
Length:338
Mass (Da):39,972
Checksum:iF83CA4FE103657D2
GO

Sequence cautioni

The sequence BAC65590.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE33974.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7979Missing in isoform 4. 1 PublicationVSP_021697Add
BLAST
Alternative sequencei329 – 39466Missing in isoform 2 and isoform 3. 1 PublicationVSP_021698Add
BLAST
Alternative sequencei329 – 33810Missing in isoform 4. 1 PublicationVSP_021699
Alternative sequencei329 – 33810LMSLLTSPHQ → VLAIWTLRGL in isoform 5. 2 PublicationsVSP_021700
Alternative sequencei339 – 616278Missing in isoform 5. 2 PublicationsVSP_021701Add
BLAST
Alternative sequencei390 – 3945Missing in isoform 4. 1 PublicationVSP_021702
Alternative sequencei515 – 5151E → ES in isoform 3. 1 PublicationVSP_021703

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15894.1. [Q80TY0-5]
CCDS38097.1. [Q80TY0-2]
CCDS50560.1. [Q80TY0-4]
CCDS50561.1. [Q80TY0-1]
CCDS57165.1. [Q80TY0-3]
RefSeqiNP_001033789.1. NM_001038700.2. [Q80TY0-2]
NP_001171119.1. NM_001177648.1. [Q80TY0-1]
NP_001171120.1. NM_001177649.1. [Q80TY0-3]
NP_001171121.1. NM_001177650.1. [Q80TY0-4]
NP_062279.1. NM_019406.3. [Q80TY0-5]
UniGeneiMm.440993.
Mm.52297.

Genome annotation databases

EnsembliENSMUST00000113552; ENSMUSP00000109181; ENSMUSG00000075415. [Q80TY0-5]
ENSMUST00000113559; ENSMUSP00000109189; ENSMUSG00000075415. [Q80TY0-4]
ENSMUST00000113560; ENSMUSP00000109190; ENSMUSG00000075415. [Q80TY0-1]
ENSMUST00000113562; ENSMUSP00000109192; ENSMUSG00000075415. [Q80TY0-2]
ENSMUST00000113564; ENSMUSP00000109194; ENSMUSG00000075415. [Q80TY0-3]
GeneIDi14269.
KEGGimmu:14269.
UCSCiuc008jdh.1. mouse. [Q80TY0-4]
uc008jdi.2. mouse. [Q80TY0-2]
uc008jdj.2. mouse. [Q80TY0-1]
uc008jdk.2. mouse. [Q80TY0-3]
uc008jdm.2. mouse. [Q80TY0-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15894.1. [Q80TY0-5]
CCDS38097.1. [Q80TY0-2]
CCDS50560.1. [Q80TY0-4]
CCDS50561.1. [Q80TY0-1]
CCDS57165.1. [Q80TY0-3]
RefSeqiNP_001033789.1. NM_001038700.2. [Q80TY0-2]
NP_001171119.1. NM_001177648.1. [Q80TY0-1]
NP_001171120.1. NM_001177649.1. [Q80TY0-3]
NP_001171121.1. NM_001177650.1. [Q80TY0-4]
NP_062279.1. NM_019406.3. [Q80TY0-5]
UniGeneiMm.440993.
Mm.52297.

3D structure databases

ProteinModelPortaliQ80TY0.
SMRiQ80TY0. Positions 1-288, 399-485, 554-607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199720. 1 interaction.
IntActiQ80TY0. 2 interactions.
MINTiMINT-4123990.
STRINGi10090.ENSMUSP00000109183.

PTM databases

PhosphoSiteiQ80TY0.

Proteomic databases

MaxQBiQ80TY0.
PaxDbiQ80TY0.
PRIDEiQ80TY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113552; ENSMUSP00000109181; ENSMUSG00000075415. [Q80TY0-5]
ENSMUST00000113559; ENSMUSP00000109189; ENSMUSG00000075415. [Q80TY0-4]
ENSMUST00000113560; ENSMUSP00000109190; ENSMUSG00000075415. [Q80TY0-1]
ENSMUST00000113562; ENSMUSP00000109192; ENSMUSG00000075415. [Q80TY0-2]
ENSMUST00000113564; ENSMUSP00000109194; ENSMUSG00000075415. [Q80TY0-3]
GeneIDi14269.
KEGGimmu:14269.
UCSCiuc008jdh.1. mouse. [Q80TY0-4]
uc008jdi.2. mouse. [Q80TY0-2]
uc008jdj.2. mouse. [Q80TY0-1]
uc008jdk.2. mouse. [Q80TY0-3]
uc008jdm.2. mouse. [Q80TY0-5]

Organism-specific databases

CTDi23048.
MGIiMGI:109606. Fnbp1.
RougeiSearch...

Phylogenomic databases

eggNOGiNOG323796.
GeneTreeiENSGT00510000046403.
HOVERGENiHBG002489.
InParanoidiQ80TY0.
OMAiVYIKNPQ.
PhylomeDBiQ80TY0.
TreeFamiTF351162.

Miscellaneous databases

ChiTaRSiFnbp1. mouse.
NextBioi285633.
PROiQ80TY0.
SOURCEiSearch...

Gene expression databases

BgeeiQ80TY0.
CleanExiMM_FNBP1.
ExpressionAtlasiQ80TY0. baseline and differential.
GenevestigatoriQ80TY0.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR028532. FNBP1/FBP17.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR12602:SF21. PTHR12602:SF21. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  7. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFNBP1_MOUSE
AccessioniPrimary (citable) accession number: Q80TY0
Secondary accession number(s): A2AQ40
, A2AQ46, Q3TA45, Q3TCW9, Q3U081, Q3UPI7, Q8C727, Q99L37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: March 4, 2015
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.