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Q5T0N5

- FBP1L_HUMAN

UniProt

Q5T0N5 - FBP1L_HUMAN

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Protein

Formin-binding protein 1-like

Gene

FNBP1L

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

Functioni

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei165 – 1651Mediates end-to-end attachment of dimersBy similarity

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. clathrin-mediated endocytosis Source: BHF-UCL
  3. membrane budding Source: BHF-UCL
  4. membrane invagination Source: BHF-UCL
  5. membrane tubulation Source: BHF-UCL
  6. positive regulation of filopodium assembly Source: BHF-UCL
  7. vesicle organization Source: BHF-UCL
  8. vesicle transport along actin filament Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Autophagy, Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-binding protein 1-like
Alternative name(s):
Transducer of Cdc42-dependent actin assembly protein 1
Short name:
Toca-1
Gene namesi
Name:FNBP1L
Synonyms:C1orf39, TOCA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:20851. FNBP1L.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Cytoplasmic vesicle By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic membrane-bounded vesicle Source: BHF-UCL
  3. cytoskeleton Source: UniProtKB-KW
  4. extracellular vesicular exosome Source: UniProt
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi441 – 4433MGD → IST: Impairs interaction with CDC42 and reduces CDC42-induced actin assembly. 1 Publication
Mutagenesisi576 – 5761W → K: Impairs interaction with WASL and reduces CDC42-induced actin assembly. 1 Publication

Organism-specific databases

PharmGKBiPA128394675.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605Formin-binding protein 1-likePRO_0000261434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951Phosphoserine3 Publications
Modified residuei488 – 4881Phosphoserine3 Publications
Modified residuei501 – 5011Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5T0N5.
PaxDbiQ5T0N5.
PRIDEiQ5T0N5.

PTM databases

PhosphoSiteiQ5T0N5.

Expressioni

Gene expression databases

BgeeiQ5T0N5.
CleanExiHS_FNBP1L.
ExpressionAtlasiQ5T0N5. baseline and differential.
GenevestigatoriQ5T0N5.

Interactioni

Subunit structurei

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.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAAM1Q9Y4D12EBI-714058,EBI-2817289

Protein-protein interaction databases

BioGridi120222. 9 interactions.
IntActiQ5T0N5. 6 interactions.
MINTiMINT-1424364.
STRINGi9606.ENSP00000271234.

Structurei

3D structure databases

ProteinModelPortaliQ5T0N5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6565FCHPROSITE-ProRule annotationAdd
BLAST
Repeati409 – 48476REMAdd
BLAST
Domaini538 – 59962SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 287287F-BAR domainBy similarityAdd
BLAST
Regioni245 – 535291Interaction with CDC42Add
BLAST
Regioni522 – 60584Interaction with DNM1Add
BLAST
Regioni541 – 60565Interaction with DAAM1, DIAPH1 and DIAPH2Add
BLAST
Regioni541 – 59757Interaction with DNM2 and WASLAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili66 – 258193By similarityAdd
BLAST
Coiled coili392 – 48493By similarityAdd
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 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.
HOGENOMiHOG000231767.
HOVERGENiHBG002489.
InParanoidiQ5T0N5.
OrthoDBiEOG780RQK.
PhylomeDBiQ5T0N5.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
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.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5T0N5-1) [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 FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV
60 70 80 90 100
KKYCPKRSSK DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE
110 120 130 140 150
LMRYAHDLKT ERKMHLQEGR KAQQYLDMCW KQMDNSKKKF ERECREAEKA
160 170 180 190 200
QQSYERLDND TNATKADVEK AKQQLNLRTH MADENKNEYA AQLQNFNGEQ
210 220 230 240 250
HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV IPIISKCLEG
260 270 280 290 300
MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS
310 320 330 340 350
ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS
360 370 380 390 400
QFLTFSIEPV HYCMNEIKTG KPRIPSFRSL KRGWSVKMGP ALEDFSHLPP
410 420 430 440 450
EQRRKKLQQR IDELNRELQK ESDQKDALNK MKDVYEKNPQ MGDPGSLQPK
460 470 480 490 500
LAETMNNIDR LRMEIHKNEA WLSEVEGKTG GRGDRRHSSD INHLVTQGRE
510 520 530 540 550
SPEGSYTDDA NQEVRGPPQQ HGHHNEFDDE FEDDDPLPAI GHCKAIYPFD
560 570 580 590 600
GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TSYIDVTLEK

NSKGS

Note: Gene prediction based on EST data.

Length:605
Mass (Da):70,065
Last modified:July 9, 2014 - v3
Checksum:i1D9237185C3006ED
GO
Isoform 2 (identifier: Q5T0N5-2) [UniParc]FASTAAdd to Basket

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

Note: Gene prediction based on EST data.

Show »
Length:600
Mass (Da):69,434
Checksum:i1C2DDFB3A3A5F0B3
GO
Isoform 3 (identifier: Q5T0N5-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:547
Mass (Da):63,572
Checksum:i416101498FF99567
GO
Isoform 4 (identifier: Q5T0N5-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:551
Mass (Da):64,033
Checksum:iB14EB59CE9010149
GO
Isoform 5 (identifier: Q5T0N5-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:604
Mass (Da):69,894
Checksum:i8C72A845744DDFB3
GO

Sequence cautioni

The sequence BAA91051.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei331 – 38858Missing in isoform 3 and isoform 4. 3 PublicationsVSP_021709Add
BLAST
Alternative sequencei384 – 3885Missing in isoform 2 and isoform 5. CuratedVSP_021710
Alternative sequencei605 – 6051S → AVTYI in isoform 4 and isoform 5. 1 PublicationVSP_021711

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY514449 mRNA. Translation: AAR98814.1.
AC095034 Genomic DNA. No translation available.
AL109613 Genomic DNA. No translation available.
AL512651 Genomic DNA. No translation available.
BC062477 mRNA. Translation: AAH62477.1.
BC074891 mRNA. Translation: AAH74891.1.
BC074892 mRNA. Translation: AAH74892.1.
AK000282 mRNA. Translation: BAA91051.1. Different initiation.
CCDSiCCDS53343.1. [Q5T0N5-1]
CCDS53344.1. [Q5T0N5-4]
CCDS60192.1. [Q5T0N5-3]
RefSeqiNP_001020119.1. NM_001024948.2. [Q5T0N5-4]
NP_001157945.1. NM_001164473.2. [Q5T0N5-1]
NP_060207.2. NM_017737.4. [Q5T0N5-3]
UniGeneiHs.134060.

Genome annotation databases

EnsembliENST00000260506; ENSP00000260506; ENSG00000137942. [Q5T0N5-4]
ENST00000271234; ENSP00000271234; ENSG00000137942. [Q5T0N5-1]
ENST00000370253; ENSP00000359275; ENSG00000137942. [Q5T0N5-3]
GeneIDi54874.
KEGGihsa:54874.
UCSCiuc001dpv.3. human. [Q5T0N5-3]
uc001dpw.3. human. [Q5T0N5-4]

Polymorphism databases

DMDMi118572313.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY514449 mRNA. Translation: AAR98814.1 .
AC095034 Genomic DNA. No translation available.
AL109613 Genomic DNA. No translation available.
AL512651 Genomic DNA. No translation available.
BC062477 mRNA. Translation: AAH62477.1 .
BC074891 mRNA. Translation: AAH74891.1 .
BC074892 mRNA. Translation: AAH74892.1 .
AK000282 mRNA. Translation: BAA91051.1 . Different initiation.
CCDSi CCDS53343.1. [Q5T0N5-1 ]
CCDS53344.1. [Q5T0N5-4 ]
CCDS60192.1. [Q5T0N5-3 ]
RefSeqi NP_001020119.1. NM_001024948.2. [Q5T0N5-4 ]
NP_001157945.1. NM_001164473.2. [Q5T0N5-1 ]
NP_060207.2. NM_017737.4. [Q5T0N5-3 ]
UniGenei Hs.134060.

3D structure databases

ProteinModelPortali Q5T0N5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120222. 9 interactions.
IntActi Q5T0N5. 6 interactions.
MINTi MINT-1424364.
STRINGi 9606.ENSP00000271234.

PTM databases

PhosphoSitei Q5T0N5.

Polymorphism databases

DMDMi 118572313.

Proteomic databases

MaxQBi Q5T0N5.
PaxDbi Q5T0N5.
PRIDEi Q5T0N5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260506 ; ENSP00000260506 ; ENSG00000137942 . [Q5T0N5-4 ]
ENST00000271234 ; ENSP00000271234 ; ENSG00000137942 . [Q5T0N5-1 ]
ENST00000370253 ; ENSP00000359275 ; ENSG00000137942 . [Q5T0N5-3 ]
GeneIDi 54874.
KEGGi hsa:54874.
UCSCi uc001dpv.3. human. [Q5T0N5-3 ]
uc001dpw.3. human. [Q5T0N5-4 ]

Organism-specific databases

CTDi 54874.
GeneCardsi GC01P093913.
HGNCi HGNC:20851. FNBP1L.
MIMi 608848. gene.
neXtProti NX_Q5T0N5.
PharmGKBi PA128394675.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG323796.
GeneTreei ENSGT00510000046403.
HOGENOMi HOG000231767.
HOVERGENi HBG002489.
InParanoidi Q5T0N5.
OrthoDBi EOG780RQK.
PhylomeDBi Q5T0N5.

Miscellaneous databases

GeneWikii FNBP1L.
GenomeRNAii 54874.
NextBioi 35537384.
PROi Q5T0N5.
SOURCEi Search...

Gene expression databases

Bgeei Q5T0N5.
CleanExi HS_FNBP1L.
ExpressionAtlasi Q5T0N5. baseline and differential.
Genevestigatori Q5T0N5.

Family and domain databases

InterProi IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00611. FCH. 1 hit.
PF00018. SH3_1. 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. "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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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.
  12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFBP1L_HUMAN
AccessioniPrimary (citable) accession number: Q5T0N5
Secondary accession number(s): J3QSS4
, Q5T0N6, Q6B097, Q6P653, Q6R4Q4, Q9NXG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 9, 2014
Last modified: October 29, 2014
This is version 101 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3