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O35601 (FYB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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Names and origin

Protein namesRecommended name:
FYN-binding protein
Alternative name(s):
Adhesion and degranulation promoting adaptor protein
Short name=ADAP
FYB-120/130
Short name=p120/p130
FYN-T-binding protein
SLAP-130
SLP-76-associated phosphoprotein
Gene names
Name:Fyb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length819 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton By similarity. Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. Modulates the expression of interleukin-2 (IL-2). Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2. Ref.1 Ref.2 Ref.5

Subunit structure

Interacts with FYN, LCP2, SKAP1 and SKAP2. Part of a complex consisting of SKAP2, FYB and PTPNS1. Part of a complex consisting of SKAP2, FYB and LILRB3. Interacts with FASLG. Interacts with EVL By similarity. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Expressed in hematopoietic tissues such as myeloid and T-cells, spleen and thymus. Not expressed in B-cells, nor in non-lymphoid tissues. FYB-130 is preferentially expressed in mature T-cells compared to FYB-120, whereas thymocytes showed a greater relative amount of FYB-120.

Post-translational modification

T-cell receptor ligation leads to increased tyrosine phosphorylation.

Disruption phenotype

Slight defects in platelet function. Ref.5

Sequence similarities

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform FYB-130 (identifier: O35601-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform FYB-120 (identifier: O35601-2)

The sequence of this isoform differs from the canonical sequence as follows:
     627-672: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 819818FYN-binding protein
PRO_0000087397

Regions

Domain699 – 75658SH3
Coiled coil448 – 49548 Potential
Motif479 – 49315Nuclear localization signal Potential
Motif584 – 5874SH2-binding; to LCP2
Motif615 – 6184SH2-binding; to FYN
Motif710 – 73627Nuclear localization signal Potential
Compositional bias343 – 3486Poly-Pro
Compositional bias381 – 3855Poly-Pro
Compositional bias606 – 6094Poly-Pro
Compositional bias622 – 6254Poly-Asp
Compositional bias696 – 6994Poly-Pro

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue31N6-acetyllysine By similarity
Modified residue281Phosphoserine Ref.7
Modified residue461Phosphoserine By similarity
Modified residue1141Phosphoserine Ref.8
Modified residue4451Phosphoserine By similarity
Modified residue5591Phosphotyrosine Ref.6 Ref.9
Modified residue5611Phosphoserine Ref.6 Ref.9
Modified residue6871Phosphotyrosine By similarity

Natural variations

Alternative sequence627 – 67246Missing in isoform FYB-120.
VSP_004261

Sequences

Sequence LengthMass (Da)Tools
Isoform FYB-130 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 6222CC7EF1CA2BBD

FASTA81990,055
        10         20         30         40         50         60 
MAKFNTGSNP TEEAATSSRP FKVAGQSSPS GIQSRKNLFD NQGNASPPAG PSSMPKFGTT 

        70         80         90        100        110        120 
KPPLAAKPTY EEKPEKEPKP PFLKPTGGSP RFGTQPNSVS RDPEVKVGFL KPVSPKPTSL 

       130        140        150        160        170        180 
TKEDSKPVVL RPPGNKLHNL NQESDLKTPG PKPGPAPPVP ENELKPGFSK VAGAKSKFMP 

       190        200        210        220        230        240 
AAQDTDSKPR FPRHTFGQKP SLSTEDSQEE NTSKNVPVQK GSPVQLGAKS KGAPFKPPKE 

       250        260        270        280        290        300 
DPEDKDHGAP SSPFPGVVLK PAASRGSPGL SKNFEEKKED RKTDLAKNIF LNKLNQEEPA 

       310        320        330        340        350        360 
RFPKAPSKLT AGTPWGQSQE KEGDKNSATP KQKALPPLSV LGPPPPKPNR PPNVDLTRFR 

       370        380        390        400        410        420 
KADSANSATK SQTPYSTTSL PPPPPTHPAS QPPLPASHPA HPPVPSLPPR NIKPPLDLKH 

       430        440        450        460        470        480 
PINDENQDGV MHSDGTGNLE EEQESEGETY EDIDSSKERD KKREKEEKKR LELERKEQKE 

       490        500        510        520        530        540 
REKKEQELKK KFKLTGPIQV IHHAKACCDV KGGKNELSFK QGEDIEIIRI TDNPEGKWLG 

       550        560        570        580        590        600 
RTARGSYGYI KTTAVEIDYD SLKRKKNSLN AVPPRLVEDD QDVYDDVAEQ DAPNSHGQSG 

       610        620        630        640        650        660 
SGGMFPPPPT DDEIYDGIEE EDDDDGSVPQ VDEKTNAWSW GILKMLKGKD DRKKSIREKP 

       670        680        690        700        710        720 
KVSESDNNEG SSLPSQHKQL DVGEEVYDDV DASDFPPPPA EMSQGMSVGR AKTEEKDPKK 

       730        740        750        760        770        780 
LKKQEKEEKD LRKKFKYDGE IRVLYSTKVA SSLTSKKWGA RDLQIKPGES LEVIQSTDDT 

       790        800        810 
KVLCRNEEGK YGYVLRSYLV DNDGEIYDDI ADGCIYDND

« Hide

Isoform FYB-120 [UniParc].

Checksum: A3EC5C9AA7124B69
Show »

FASTA77384,870

References

« Hide 'large scale' references
[1]"Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production."
da Silva A.J., Li Z., de Vera C., Canto E., Findell P., Rudd C.E.
Proc. Natl. Acad. Sci. U.S.A. 94:7493-7498(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-120), INTERACTION WITH FYN AND LCP2, FUNCTION.
Tissue: T-cell lymphoma.
[2]"Novel isoform of lymphoid adaptor FYN-T-binding protein (FYB-130) interacts with SLP-76 and up-regulates interleukin 2 production."
Veale M., Raab M., Li Z., da Silva A.J., Kraeft S.-K., Weremowicz S., Morton C.C., Rudd C.E.
J. Biol. Chem. 274:28427-28435(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-130), INTERACTION WITH FYN AND LCP2, FUNCTION.
Tissue: Hybridoma.
[3]"SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages."
Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E., Schraven B., Neel B.G.
Curr. Biol. 9:927-930(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP2, IDENTIFICATION IN A COMPLEX WITH SKAP2 AND PTPNS1.
[4]"The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages."
Black D.S., Marie-Cardine A., Schraven B., Bliska J.B.
Cell. Microbiol. 2:401-414(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP2, IDENTIFICATION IN A COMPLEX WITH SKAP2 AND PTPNS1, IDENTIFICATION IN A COMPLEX WITH SKAP2 AND LILRB3.
[5]"ADAP is required for normal alphaIIb-beta3 activation by VWF/GP Ib-IX-V and other agonists."
Kasirer-Friede A., Moran B., Nagrampa-Orje J., Swanson K., Ruggeri Z.M., Schraven B., Neel B.G., Koretzky G., Shattil S.J.
Blood 109:1018-1025(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP2, FUNCTION, DISRUPTION PHENOTYPE.
[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 TYR-559 AND SER-561, MASS SPECTROMETRY.
Tissue: Mast cell.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY.
Tissue: Liver.
[8]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY.
Tissue: Melanoma.
[9]"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 TYR-559 AND SER-561, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF001863 mRNA. Translation: AAB62227.1.
AF061744 mRNA. Translation: AAD03267.1.
IPIIPI00226593.
IPI00626627.
RefSeqNP_035945.1. NM_011815.4.
UniGeneMm.170905.

3D structure databases

ProteinModelPortalO35601.
SMRO35601. Positions 494-567, 725-801.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-244320.
STRING10090.ENSMUSP00000087947.

PTM databases

PhosphoSiteO35601.

Proteomic databases

PaxDbO35601.
PRIDEO35601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090461; ENSMUSP00000087947; ENSMUSG00000022148.
GeneID23880.
KEGGmmu:23880.
UCSCuc007vdk.1. mouse.

Organism-specific databases

CTD2533.
MGIMGI:1346327. Fyb.

Phylogenomic databases

eggNOGNOG18948.
GeneTreeENSGT00530000063460.
HOGENOMHOG000008686.
HOVERGENHBG005774.
InParanoidO35601.
OMAACCDVKG.
OrthoDBEOG4VMFF3.

Enzyme and pathway databases

ReactomeREACT_107772. Immune System.

Gene expression databases

ArrayExpressO35601.
BgeeO35601.
CleanExMM_FYB.
GenevestigatorO35601.
GermOnlineENSMUSG00000022148. Mus musculus.

Family and domain databases

InterProIPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SH3. 2 hits.
PROSITEPS50002. SH3. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio303607.
PMAP-CutDBO35601.
SOURCESearch...

Entry information

Entry nameFYB_MOUSE
AccessionPrimary (citable) accession number: O35601
Secondary accession number(s): Q9Z2H3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: December 1, 2000
Last modified: April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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