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O15117 (FYB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:SLAP130
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length783 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton. Ref.3 Ref.14 Ref.16

Subunit structure

Part of a complex consisting of SKAP2, FYB and PTPNS1. Part of a complex consisting of SKAP2, FYB and LILRB3 By similarity. Interacts with FYN, LCP2, SKAP1 and SKAP2. Interacts with FASLG. Interacts with EVL. Ref.1 Ref.3 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.18

Subcellular location

Cytoplasm. Nucleus By similarity Ref.10.

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.

Post-translational modification

T-cell receptor ligation leads to increased tyrosine phosphorylation.

Sequence similarities

Contains 1 SH3 domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform FYB-120 (identifier: O15117-1)

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-130 (identifier: O15117-2)

The sequence of this isoform differs from the canonical sequence as follows:
     636-636: G → GSTLQVQEKSNTWSWGILKMLKGKDDRKKSIREKPKVSDSDNNEGSS
Isoform 3 (identifier: O15117-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDGKADVKSLM
     636-636: G → GSTLQVQEKSNTWSWGILKMLKGKDDRKKSIREKPKVSDSDNNEGSS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.20
Chain2 – 783782FYN-binding protein
PRO_0000087396

Regions

Domain514 – 57057SH3
Region348 – 448101Interaction with SKAP1
Coiled coil456 – 50752 Potential
Motif462 – 4654SH2-binding Potential
Motif469 – 50537Nuclear localization signal Potential
Motif595 – 5984SH2-binding; to LCP2
Motif625 – 6284SH2-binding; to FYN
Motif674 – 70027Nuclear localization signal Potential
Compositional bias355 – 3606Poly-Pro
Compositional bias393 – 3975Poly-Pro
Compositional bias617 – 6204Poly-Pro

Amino acid modifications

Modified residue21N-acetylalanine Ref.20
Modified residue31N6-acetyllysine Ref.20
Modified residue281Phosphoserine By similarity
Modified residue461Phosphoserine Ref.17 Ref.19
Modified residue4571Phosphoserine Ref.19
Modified residue5711Phosphotyrosine Ref.19
Modified residue5731Phosphoserine Ref.19
Modified residue6511Phosphotyrosine Ref.19

Natural variations

Alternative sequence11M → MDGKADVKSLM in isoform 3.
VSP_047288
Alternative sequence6361G → GSTLQVQEKSNTWSWGILKM LKGKDDRKKSIREKPKVSDS DNNEGSS in isoform FYB-130 and isoform 3.
VSP_042309
Natural variant511P → L.
Corresponds to variant rs1642515 [ dbSNP | Ensembl ].
VAR_056880
Natural variant3321K → R.
Corresponds to variant rs3749741 [ dbSNP | Ensembl ].
VAR_056881
Natural variant6721V → F. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7 Ref.19
Corresponds to variant rs379707 [ dbSNP | Ensembl ].
VAR_060592

Experimental info

Sequence conflict271N → S in BAF83092. Ref.4
Sequence conflict2731P → L in AAC51300. Ref.2
Sequence conflict2751L → V in AAB62226. Ref.1
Sequence conflict5411R → C in BAF83092. Ref.4
Sequence conflict6741K → E in BAF83092. Ref.4
Sequence conflict7291V → A in BAF83092. Ref.4

Secondary structure

........................... 783
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform FYB-120 [UniParc].

Last modified November 24, 2009. Version 2.
Checksum: 4EE28EF12AA0E457

FASTA78385,387
        10         20         30         40         50         60 
MAKYNTGGNP TEDVSVNSRP FRVTGPNSSS GIQARKNLFN NQGNASPPAG PSNVPKFGSP 

        70         80         90        100        110        120 
KPPVAVKPSS EEKPDKEPKP PFLKPTGAGQ RFGTPASLTT RDPEAKVGFL KPVGPKPINL 

       130        140        150        160        170        180 
PKEDSKPTFP WPPGNKPSLH SVNQDHDLKP LGPKSGPTPP TSENEQKQAF PKLTGVKGKF 

       190        200        210        220        230        240 
MSASQDLEPK PLFPKPAFGQ KPPLSTENSH EDESPMKNVS SSKGSPAPLG VRSKSGPLKP 

       250        260        270        280        290        300 
AREDSENKDH AGEISSLPFP GVVLKPAASR GGPGLSKNGE EKKEDRKIDA AKNTFQSKIN 

       310        320        330        340        350        360 
QEELASGTPP ARFPKAPSKL TVGGPWGQSQ EKEKGDKNSA TPKQKPLPPL FTLGPPPPKP 

       370        380        390        400        410        420 
NRPPNVDLTK FHKTSSGNST SKGQTSYSTT SLPPPPPSHP ASQPPLPASH PSQPPVPSLP 

       430        440        450        460        470        480 
PRNIKPPFDL KSPVNEDNQD GVTHSDGAGN LDEEQDSEGE TYEDIEASKE REKKREKEEK 

       490        500        510        520        530        540 
KRLELEKKEQ KEKEKKEQEI KKKFKLTGPI QVIHLAKACC DVKGGKNELS FKQGEQIEII 

       550        560        570        580        590        600 
RITDNPEGKW LGRTARGSYG YIKTTAVEID YDSLKLKKDS LGAPSRPIED DQEVYDDVAE 

       610        620        630        640        650        660 
QDDISSHSQS GSGGIFPPPP DDDIYDGIEE EDADDGFPAP PKQLDMGDEV YDDVDTSDFP 

       670        680        690        700        710        720 
VSSAEMSQGT NVGKAKTEEK DLKKLKKQEK EEKDFRKKFK YDGEIRVLYS TKVTTSITSK 

       730        740        750        760        770        780 
KWGTRDLQVK PGESLEVIQT TDDTKVLCRN EEGKYGYVLR SYLADNDGEI YDDIADGCIY 


DND 

« Hide

Isoform FYB-130 [UniParc].

Checksum: BDDEE1977674BC65
Show »

FASTA82990,606
Isoform 3 [UniParc].

Checksum: 3EB9A0C1FF816B6B
Show »

FASTA83991,651

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, VARIANT PHE-672.
Tissue: Tonsil.
[2]"Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases."
Musci M.A., Hendricks-Taylor L.R., Motto D.G., Paskind M., Kamens J., Turck C.W., Koretzky G.A.
J. Biol. Chem. 272:11674-11677(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-120), PROTEIN SEQUENCE OF 363-370, VARIANT PHE-672.
[3]"Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton."
Krause M., Sechi A.S., Konradt M., Monner D., Gertler F.B., Wehland J.
J. Cell Biol. 149:181-194(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-130), FUNCTION, INTERACTION WITH EVL, VARIANT PHE-672.
[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. expand/collapse author list , 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] (ISOFORMS FYB-130 AND 3), VARIANT PHE-672.
Tissue: Umbilical cord blood.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 FYB-130), VARIANT PHE-672.
Tissue: Cerebellum.
[8]"SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein SKAP55."
Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.
FEBS Lett. 435:55-60(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP1 AND SKAP2.
[9]"Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130."
Marie-Cardine A., Hendricks-Taylor L.R., Boerth N.J., Zhao H., Schraven B., Koretzky G.A.
J. Biol. Chem. 273:25789-25795(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP1.
[10]"FYB (FYN binding protein) serves as a binding partner for lymphoid protein and FYN kinase substrate SKAP55 and a SKAP55-related protein in T cells."
Liu J., Kang H., Raab M., da Silva A.J., Kraeft S.-K., Rudd C.E.
Proc. Natl. Acad. Sci. U.S.A. 95:8779-8784(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP1 AND SKAP2, SUBCELLULAR LOCATION.
[11]"Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin."
Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A., Schweighoffer E., Tybulewicz V., Bon C., Liu S.K., McGlade C.J., Schraven B., Watson S.P.
J. Biol. Chem. 275:33427-33434(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP2.
[12]"SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55."
Kang H., Freund C., Duke-Cohan J.S., Musacchio A., Wagner G., Rudd C.E.
EMBO J. 19:2889-2899(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP1.
[13]"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.
[14]"Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells."
Huang Y., Norton D.D., Precht P., Martindale J.L., Burkhardt J.K., Wange R.L.
J. Biol. Chem. 280:23576-23583(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP1 AND FYN, FUNCTION.
[15]"Regulation and function of SKAP-55 non-canonical motif binding to the SH3c domain of adhesion and degranulation-promoting adaptor protein."
Duke-Cohan J.S., Kang H., Liu H., Rudd C.E.
J. Biol. Chem. 281:13743-13750(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKAP1.
[16]"The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated integrin activation through plasma membrane targeting of Rap1."
Kliche S., Breitling D., Togni M., Pusch R., Heuer K., Wang X., Freund C., Kasirer-Friede A., Menasche G., Koretzky G.A., Schraven B.
Mol. Cell. Biol. 26:7130-7144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[18]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[19]"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-46; SER-457; TYR-571; SER-573 AND TYR-651, VARIANT [LARGE SCALE ANALYSIS] PHE-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"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 ALA-2 AND LYS-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[21]"Structure of a helically extended SH3 domain of the T cell adapter protein ADAP."
Heuer K., Kofler M., Langdon G., Thiemke K., Freund C.
Structure 12:603-610(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 683-771.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF001862 mRNA. Translation: AAB62226.1.
U93049 mRNA. Translation: AAC51300.1.
AF198052 mRNA. Translation: AAF62400.1.
AK290403 mRNA. Translation: BAF83092.1.
AK297077 mRNA. Translation: BAG59594.1.
AC008964 Genomic DNA. No translation available.
AC010633 Genomic DNA. No translation available.
AC025471 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW55984.1.
BC117449 mRNA. Translation: AAI17450.1.
BC143645 mRNA. Translation: AAI43646.1.
CCDSCCDS47200.1. [O15117-1]
CCDS54848.1. [O15117-2]
CCDS58945.1. [O15117-3]
RefSeqNP_001230022.1. NM_001243093.1. [O15117-3]
NP_001456.3. NM_001465.4. [O15117-2]
NP_955367.1. NM_199335.3. [O15117-1]
XP_006714527.1. XM_006714464.1. [O15117-2]
XP_006714528.1. XM_006714465.1. [O15117-2]
XP_006714529.1. XM_006714466.1. [O15117-2]
UniGeneHs.370503.
Hs.691768.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RI9NMR-A683-771[»]
2GTJNMR-A486-579[»]
2GTONMR-A486-579[»]
ProteinModelPortalO15117.
SMRO15117. Positions 506-579, 689-765.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108809. 12 interactions.
DIPDIP-42204N.
IntActO15117. 26 interactions.
MINTMINT-1176058.
STRING9606.ENSP00000316460.

PTM databases

PhosphoSiteO15117.

2D gel databases

OGPO15117.

Proteomic databases

MaxQBO15117.
PaxDbO15117.
PRIDEO15117.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351578; ENSP00000316460; ENSG00000082074. [O15117-1]
ENST00000505428; ENSP00000427114; ENSG00000082074. [O15117-2]
ENST00000512982; ENSP00000425845; ENSG00000082074. [O15117-2]
ENST00000515010; ENSP00000426346; ENSG00000082074. [O15117-1]
ENST00000540520; ENSP00000442840; ENSG00000082074. [O15117-3]
GeneID2533.
KEGGhsa:2533.
UCSCuc003jls.3. human. [O15117-1]
uc003jlt.3. human. [O15117-2]

Organism-specific databases

CTD2533.
GeneCardsGC05M039112.
H-InvDBHIX0024785.
HGNCHGNC:4036. FYB.
HPACAB025336.
HPA026796.
MIM602731. gene.
neXtProtNX_O15117.
PharmGKBPA28452.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG18948.
HOGENOMHOG000008686.
HOVERGENHBG005774.
KOK17698.
OMAACCDVKG.
OrthoDBEOG70W3CP.
PhylomeDBO15117.
TreeFamTF337003.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_6900. Immune System.
SignaLinkO15117.

Gene expression databases

ArrayExpressO15117.
BgeeO15117.
CleanExHS_FYB.
GenevestigatorO15117.

Family and domain databases

InterProIPR029294. hSH3.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF14603. hSH3. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceO15117.
GeneWikiFYB.
GenomeRNAi2533.
NextBio9991.
PMAP-CutDBO15117.
PROO15117.
SOURCESearch...

Entry information

Entry nameFYB_HUMAN
AccessionPrimary (citable) accession number: O15117
Secondary accession number(s): A8K2Y8 expand/collapse secondary AC list , B4DLN2, E9PBV9, O00359, Q9NZI9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 24, 2009
Last modified: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM