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Protein

Formin-binding protein 4

Gene

Fnbp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-binding protein 4
Alternative name(s):
Formin-binding protein 30
Gene namesi
Name:Fnbp4
Synonyms:Fbp30, Kiaa1014
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1860513. Fnbp4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10311031Formin-binding protein 4PRO_0000289864Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei120 – 1201PhosphoserineCombined sources
Modified residuei125 – 1251PhosphoserineCombined sources
Modified residuei128 – 1281PhosphoserineCombined sources
Modified residuei176 – 1761PhosphothreonineBy similarity
Modified residuei294 – 2941N6-acetyllysineCombined sources
Cross-linki305 – 305Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki352 – 352Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki352 – 352Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei435 – 4351PhosphoserineCombined sources
Modified residuei440 – 4401PhosphoserineCombined sources
Modified residuei443 – 4431PhosphoserineCombined sources
Modified residuei446 – 4461PhosphoserineCombined sources
Modified residuei450 – 4501PhosphoserineCombined sources
Modified residuei472 – 4721PhosphoserineBy similarity
Modified residuei507 – 5071PhosphoserineCombined sources
Modified residuei516 – 5161PhosphoserineBy similarity
Cross-linki527 – 527Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki527 – 527Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei977 – 9771PhosphoserineBy similarity
Modified residuei978 – 9781PhosphoserineBy similarity
Modified residuei979 – 9791PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6ZQ03.
MaxQBiQ6ZQ03.
PaxDbiQ6ZQ03.
PeptideAtlasiQ6ZQ03.
PRIDEiQ6ZQ03.

PTM databases

iPTMnetiQ6ZQ03.
PhosphoSiteiQ6ZQ03.

Expressioni

Tissue specificityi

Ubiquitous. Highest levels in spleen and thymus.2 Publications

Developmental stagei

First detected at 9 dpc.

Inductioni

Up-regulated by p53.1 Publication

Gene expression databases

BgeeiQ6ZQ03.
CleanExiMM_FNBP4.

Interactioni

Subunit structurei

Binds FMN1. Interacts with the Arg/Gly-rich-flanked Pro-rich regions of KHDRBS1/SAM68. Arginine methylation in these regions has no effect on this binding (By similarity).By similarity

Protein-protein interaction databases

IntActiQ6ZQ03. 2 interactions.
MINTiMINT-125886.
STRINGi10090.ENSMUSP00000013759.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini218 – 25235WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini603 – 63735WW 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi638 – 6425Poly-Glu
Compositional biasi707 – 939233Pro-richAdd
BLAST

Domaini

These WW domains interact with Arg/Gly-rich-flanked Pro-rich domains found in several WW domain-binding proteins (WBPs). The N-terminal WW domain has the greater ligand-binding ability (By similarity).By similarity

Sequence similaritiesi

Contains 2 WW domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IIQY. Eukaryota.
ENOG4111F8J. LUCA.
HOGENOMiHOG000168238.
HOVERGENiHBG066308.
InParanoidiQ6ZQ03.
OrthoDBiEOG75F4GV.
PhylomeDBiQ6ZQ03.
TreeFamiTF331046.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
PfamiPF00397. WW. 2 hits.
[Graphical view]
SMARTiSM00456. WW. 2 hits.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 2 hits.
PROSITEiPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZQ03-1) [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
MMGKKSRAVP GRRPILQLSP PGPRSSTPGR DPDPDPDPEA DSTAAATSQS
60 70 80 90 100
APAAATAAAA TSPAVPASAA PEDSPSEDEQ EVVVEVPNVV QNPPTPVMTT
110 120 130 140 150
RPTAVKATGG LCLLGAYADS DDDESDVSEK TAQSKEANGN QATDIDSTLA
160 170 180 190 200
NFLAEIDAIT APQPAAPVVA SAPPPTPPRP EPKEAATPAL SPTASNGSDT
210 220 230 240 250
AQTPGWHYDT QCSLAGVEIE MGDWQEVWDE NTGCYYYWNT QTNEVTWELP
260 270 280 290 300
QYLATQVQGL QHYQPSSVTG TEAAFVVNTD MYTKERTTAA SSSKSGPVIT
310 320 330 340 350
KREVKKEVNE GIQALSNSEE ERKGVAAALL APLLPEGVKE EEERWRRKVI
360 370 380 390 400
CKEADPVSET KETSTASEET GPSIKPPEVM MDGTEDPSQE ELCSVVQSGE
410 420 430 440 450
SEEEEEEEEQ DTLELELALE RKKAELRALE EGDGSVSGSS PRSDISQPAS
460 470 480 490 500
QDGVRRIMSK RGKWKMFVRA TSPESTSRSS SKTGRDSPEN GETAIGAEDS
510 520 530 540 550
EKIDEISDKE TEVEESSEKI KVQLAPKVEE EQDLKFQIGE LANTLTSKFE
560 570 580 590 600
FLGINRQSIS NFHMLLLQTE TRIADWREGA LNGNYLKRKL QDAAEQLKQY
610 620 630 640 650
EINATPKGWS CHWDRDHRRY FYVNEQSGES QWEFPDGEEE EESQTKEVRD
660 670 680 690 700
ESLPKLTVKD KTCTDPNSTE SSENPTGSLC KESFSGQVSS SLMPLTPFWT
710 720 730 740 750
LLQSNVPVLQ PPLPLEMPPP PPPPPESPPP PPPPPPPPPP LEDGEIQEVE
760 770 780 790 800
MEDEGSEEPP APGTEEDTPL KPSTQTTAVT SQSLVDSTAS SPPSNKAVKR
810 820 830 840 850
KAPEMSTSVV QRSATIGSSP VLYSQSAIAA GHQAVGMAHQ AVGMAHQAVS
860 870 880 890 900
ASHAAAAGVG HQARGMSLQS NYLGLAAAPA LMSYAECSVP IGVTTPSLQP
910 920 930 940 950
AQARGTMAAP AVVEPPPPPP PPPTPTPPPP PPAPKVPPPE KTRKGKKDKA
960 970 980 990 1000
KKSKTKMPSL VKKWQSIQRE LDEEDNSSSS EEDRESTAQK RIEEWKQQQL
1010 1020 1030
VSGLAERNAN FEALPEDWRA RLKRRKMAPS T
Length:1,031
Mass (Da):111,245
Last modified:May 29, 2007 - v2
Checksum:iAC49681858666E69
GO
Isoform 2 (identifier: Q6ZQ03-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     616-622: DHRRYFY → TSGSNYS
     623-1031: Missing.

Note: No experimental confirmation available.
Show »
Length:622
Mass (Da):67,305
Checksum:i0D52293D48C00892
GO
Isoform 3 (identifier: Q6ZQ03-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     616-630: DHRRYFYVNEQSGES → YALFSPSYLSPLTSQ
     631-1031: Missing.

Note: No experimental confirmation available.
Show »
Length:630
Mass (Da):68,264
Checksum:i0B4A8C89AEB06E02
GO

Sequence cautioni

The sequence AAF59410.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC98073.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE37831.1 differs from that shown. Reason: Frameshift at position 612. Curated
The sequence CAM20821.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681S → T (PubMed:10510470).Curated
Sequence conflicti95 – 951T → K (PubMed:10510470).Curated
Sequence conflicti99 – 991T → P (PubMed:10510470).Curated
Sequence conflicti104 – 1041A → T (PubMed:10510470).Curated
Sequence conflicti192 – 1921P → S in BAC98073 (PubMed:14621295).Curated
Sequence conflicti198 – 1981S → T in BAC98073 (PubMed:14621295).Curated
Sequence conflicti646 – 6461K → Q in BAC98073 (PubMed:14621295).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei616 – 63015DHRRY…QSGES → YALFSPSYLSPLTSQ in isoform 3. 1 PublicationVSP_029267Add
BLAST
Alternative sequencei616 – 6227DHRRYFY → TSGSNYS in isoform 2. 1 PublicationVSP_026025
Alternative sequencei623 – 1031409Missing in isoform 2. 1 PublicationVSP_026026Add
BLAST
Alternative sequencei631 – 1031401Missing in isoform 3. 1 PublicationVSP_029268Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40750 mRNA. Translation: AAF59410.1. Different initiation.
AK129263 mRNA. Translation: BAC98073.2. Different initiation.
AK084018 mRNA. Translation: BAC39098.1.
AK164543 mRNA. Translation: BAE37831.1. Frameshift.
AL714026 Genomic DNA. Translation: CAM20821.1. Different initiation.
PIRiS64717.
RefSeqiNP_061298.1. NM_018828.2.
UniGeneiMm.489638.

Genome annotation databases

GeneIDi55935.
KEGGimmu:55935.
UCSCiuc008ktb.1. mouse. [Q6ZQ03-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40750 mRNA. Translation: AAF59410.1. Different initiation.
AK129263 mRNA. Translation: BAC98073.2. Different initiation.
AK084018 mRNA. Translation: BAC39098.1.
AK164543 mRNA. Translation: BAE37831.1. Frameshift.
AL714026 Genomic DNA. Translation: CAM20821.1. Different initiation.
PIRiS64717.
RefSeqiNP_061298.1. NM_018828.2.
UniGeneiMm.489638.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6ZQ03. 2 interactions.
MINTiMINT-125886.
STRINGi10090.ENSMUSP00000013759.

PTM databases

iPTMnetiQ6ZQ03.
PhosphoSiteiQ6ZQ03.

Proteomic databases

EPDiQ6ZQ03.
MaxQBiQ6ZQ03.
PaxDbiQ6ZQ03.
PeptideAtlasiQ6ZQ03.
PRIDEiQ6ZQ03.

Protocols and materials databases

DNASUi55935.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi55935.
KEGGimmu:55935.
UCSCiuc008ktb.1. mouse. [Q6ZQ03-1]

Organism-specific databases

CTDi23360.
MGIiMGI:1860513. Fnbp4.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IIQY. Eukaryota.
ENOG4111F8J. LUCA.
HOGENOMiHOG000168238.
HOVERGENiHBG066308.
InParanoidiQ6ZQ03.
OrthoDBiEOG75F4GV.
PhylomeDBiQ6ZQ03.
TreeFamiTF331046.

Miscellaneous databases

PROiQ6ZQ03.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZQ03.
CleanExiMM_FNBP4.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
PfamiPF00397. WW. 2 hits.
[Graphical view]
SMARTiSM00456. WW. 2 hits.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 2 hits.
PROSITEiPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains."
    Chan D.C., Bedford M.T., Leder P.
    EMBO J. 15:1045-1054(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH FMN1.
    Strain: FVB/NJ.
    Tissue: Limb bud.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH WW DOMAIN-BINDING PROTEINS.
    Strain: FVB/NJ.
    Tissue: Embryo, Fibroblast and Limb bud.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 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., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryonic tail.
  4. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1031 (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Heart and Spinal ganglion.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
    Strain: C57BL/6J.
  6. "WW domain-containing FBP-30 is regulated by p53."
    Depraetere V., Golstein P.
    Cell Death Differ. 6:883-889(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-1031 (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION.
    Strain: C57BL/6J.
    Tissue: Embryo, Placenta, Thymic lymphoma and Thymus.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-125; SER-128; SER-435; SER-440; SER-443; SER-446; SER-450 AND SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiFNBP4_MOUSE
AccessioniPrimary (citable) accession number: Q6ZQ03
Secondary accession number(s): Q3TPA6, Q8BNC8, Q9JHC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: July 6, 2016
This is version 85 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

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 one 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.