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O15117

- FYB_HUMAN

UniProt

O15117 - FYB_HUMAN

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Protein

FYN-binding protein

Gene

FYB

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

Functioni

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.3 Publications

GO - Molecular functioni

  1. receptor binding Source: UniProtKB

GO - Biological processi

  1. immune response Source: ProtInc
  2. intracellular signal transduction Source: ProtInc
  3. NLS-bearing protein import into nucleus Source: ProtInc
  4. protein phosphorylation Source: ProtInc
  5. signal transduction Source: ProtInc
  6. T cell receptor signaling pathway Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_12623. Generation of second messenger molecules.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinkiO15117.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:FYB
Synonyms:SLAP130
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:4036. FYB.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28452.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 783782FYN-binding proteinPRO_0000087396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei3 – 31N6-acetyllysine1 Publication
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei46 – 461Phosphoserine2 Publications
Modified residuei457 – 4571Phosphoserine1 Publication
Modified residuei571 – 5711Phosphotyrosine1 Publication
Modified residuei573 – 5731Phosphoserine1 Publication
Modified residuei651 – 6511Phosphotyrosine1 Publication

Post-translational modificationi

T-cell receptor ligation leads to increased tyrosine phosphorylation.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO15117.
PaxDbiO15117.
PRIDEiO15117.

2D gel databases

OGPiO15117.

PTM databases

PhosphoSiteiO15117.

Miscellaneous databases

PMAP-CutDBO15117.

Expressioni

Tissue specificityi

Expressed in hematopoietic tissues such as myeloid and T-cells, spleen and thymus. Not expressed in B-cells, nor in non-lymphoid tissues.

Gene expression databases

BgeeiO15117.
CleanExiHS_FYB.
ExpressionAtlasiO15117. baseline and differential.
GenevestigatoriO15117.

Organism-specific databases

HPAiCAB025336.
HPA026796.

Interactioni

Subunit structurei

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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FYNP062412EBI-1753267,EBI-515315
LCP2Q130945EBI-1753267,EBI-346946
NCK1P163333EBI-1753267,EBI-389883
SKAP1Q86WV16EBI-1753267,EBI-2477305

Protein-protein interaction databases

BioGridi108809. 13 interactions.
DIPiDIP-42204N.
IntActiO15117. 26 interactions.
MINTiMINT-1176058.
STRINGi9606.ENSP00000316460.

Structurei

Secondary structure

1
783
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi498 – 5047Combined sources
Beta strandi514 – 5207Combined sources
Beta strandi526 – 5283Combined sources
Beta strandi537 – 5415Combined sources
Beta strandi546 – 5483Combined sources
Beta strandi551 – 5533Combined sources
Beta strandi559 – 5624Combined sources
Helixi564 – 5663Combined sources
Beta strandi567 – 5693Combined sources
Helixi572 – 5754Combined sources
Helixi690 – 6989Combined sources
Beta strandi736 – 75015Combined sources
Turni751 – 7533Combined sources
Beta strandi754 – 7596Combined sources
Helixi760 – 7623Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RI9NMR-A683-771[»]
2GTJNMR-A486-579[»]
2GTONMR-A486-579[»]
ProteinModelPortaliO15117.
SMRiO15117. Positions 506-579, 689-765.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15117.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini514 – 57057SH3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni348 – 448101Interaction with SKAP1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili456 – 50752Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi462 – 4654SH2-bindingSequence Analysis
Motifi469 – 50537Nuclear localization signalSequence AnalysisAdd
BLAST
Motifi595 – 5984SH2-binding; to LCP2
Motifi625 – 6284SH2-binding; to FYN
Motifi674 – 70027Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi355 – 3606Poly-Pro
Compositional biasi393 – 3975Poly-Pro
Compositional biasi617 – 6204Poly-Pro

Sequence similaritiesi

Contains 1 SH3 domain.Curated

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG18948.
GeneTreeiENSGT00530000063460.
HOGENOMiHOG000008686.
HOVERGENiHBG005774.
InParanoidiO15117.
KOiK17698.
OMAiACCDVKG.
OrthoDBiEOG70W3CP.
PhylomeDBiO15117.
TreeFamiTF337003.

Family and domain databases

InterProiIPR029294. hSH3.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF14603. hSH3. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform FYB-120 (identifier: O15117-1) [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
MAKYNTGGNP TEDVSVNSRP FRVTGPNSSS GIQARKNLFN NQGNASPPAG
60 70 80 90 100
PSNVPKFGSP KPPVAVKPSS EEKPDKEPKP PFLKPTGAGQ RFGTPASLTT
110 120 130 140 150
RDPEAKVGFL KPVGPKPINL PKEDSKPTFP WPPGNKPSLH SVNQDHDLKP
160 170 180 190 200
LGPKSGPTPP TSENEQKQAF PKLTGVKGKF MSASQDLEPK PLFPKPAFGQ
210 220 230 240 250
KPPLSTENSH EDESPMKNVS SSKGSPAPLG VRSKSGPLKP AREDSENKDH
260 270 280 290 300
AGEISSLPFP GVVLKPAASR GGPGLSKNGE EKKEDRKIDA AKNTFQSKIN
310 320 330 340 350
QEELASGTPP ARFPKAPSKL TVGGPWGQSQ EKEKGDKNSA TPKQKPLPPL
360 370 380 390 400
FTLGPPPPKP NRPPNVDLTK FHKTSSGNST SKGQTSYSTT SLPPPPPSHP
410 420 430 440 450
ASQPPLPASH PSQPPVPSLP PRNIKPPFDL KSPVNEDNQD GVTHSDGAGN
460 470 480 490 500
LDEEQDSEGE TYEDIEASKE REKKREKEEK KRLELEKKEQ KEKEKKEQEI
510 520 530 540 550
KKKFKLTGPI QVIHLAKACC DVKGGKNELS FKQGEQIEII RITDNPEGKW
560 570 580 590 600
LGRTARGSYG YIKTTAVEID YDSLKLKKDS LGAPSRPIED DQEVYDDVAE
610 620 630 640 650
QDDISSHSQS GSGGIFPPPP DDDIYDGIEE EDADDGFPAP PKQLDMGDEV
660 670 680 690 700
YDDVDTSDFP VSSAEMSQGT NVGKAKTEEK DLKKLKKQEK EEKDFRKKFK
710 720 730 740 750
YDGEIRVLYS TKVTTSITSK KWGTRDLQVK PGESLEVIQT TDDTKVLCRN
760 770 780
EEGKYGYVLR SYLADNDGEI YDDIADGCIY DND
Length:783
Mass (Da):85,387
Last modified:November 24, 2009 - v2
Checksum:i4EE28EF12AA0E457
GO
Isoform FYB-130 (identifier: O15117-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     636-636: G → GSTLQVQEKSNTWSWGILKMLKGKDDRKKSIREKPKVSDSDNNEGSS

Show »
Length:829
Mass (Da):90,606
Checksum:iBDDEE1977674BC65
GO
Isoform 3 (identifier: O15117-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:839
Mass (Da):91,651
Checksum:i3EB9A0C1FF816B6B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271N → S in BAF83092. (PubMed:14702039)Curated
Sequence conflicti273 – 2731P → L in AAC51300. (PubMed:9115214)Curated
Sequence conflicti275 – 2751L → V in AAB62226. (PubMed:9207119)Curated
Sequence conflicti541 – 5411R → C in BAF83092. (PubMed:14702039)Curated
Sequence conflicti674 – 6741K → E in BAF83092. (PubMed:14702039)Curated
Sequence conflicti729 – 7291V → A in BAF83092. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511P → L.
Corresponds to variant rs1642515 [ dbSNP | Ensembl ].
VAR_056880
Natural varianti332 – 3321K → R.
Corresponds to variant rs3749741 [ dbSNP | Ensembl ].
VAR_056881
Natural varianti672 – 6721V → F.6 Publications
Corresponds to variant rs379707 [ dbSNP | Ensembl ].
VAR_060592

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDGKADVKSLM in isoform 3. 1 PublicationVSP_047288
Alternative sequencei636 – 6361G → GSTLQVQEKSNTWSWGILKM LKGKDDRKKSIREKPKVSDS DNNEGSS in isoform FYB-130 and isoform 3. 3 PublicationsVSP_042309

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS47200.1. [O15117-1]
CCDS54848.1. [O15117-2]
RefSeqiNP_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]
UniGeneiHs.370503.
Hs.691768.

Genome annotation databases

EnsembliENST00000351578; ENSP00000316460; ENSG00000082074. [O15117-1]
ENST00000505428; ENSP00000427114; ENSG00000082074. [O15117-2]
ENST00000512982; ENSP00000425845; ENSG00000082074. [O15117-2]
ENST00000515010; ENSP00000426346; ENSG00000082074. [O15117-1]
GeneIDi2533.
KEGGihsa:2533.
UCSCiuc003jls.3. human. [O15117-1]
uc003jlt.3. human. [O15117-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS47200.1. [O15117-1 ]
CCDS54848.1. [O15117-2 ]
RefSeqi NP_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 ]
UniGenei Hs.370503.
Hs.691768.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RI9 NMR - A 683-771 [» ]
2GTJ NMR - A 486-579 [» ]
2GTO NMR - A 486-579 [» ]
ProteinModelPortali O15117.
SMRi O15117. Positions 506-579, 689-765.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108809. 13 interactions.
DIPi DIP-42204N.
IntActi O15117. 26 interactions.
MINTi MINT-1176058.
STRINGi 9606.ENSP00000316460.

PTM databases

PhosphoSitei O15117.

2D gel databases

OGPi O15117.

Proteomic databases

MaxQBi O15117.
PaxDbi O15117.
PRIDEi O15117.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000351578 ; ENSP00000316460 ; ENSG00000082074 . [O15117-1 ]
ENST00000505428 ; ENSP00000427114 ; ENSG00000082074 . [O15117-2 ]
ENST00000512982 ; ENSP00000425845 ; ENSG00000082074 . [O15117-2 ]
ENST00000515010 ; ENSP00000426346 ; ENSG00000082074 . [O15117-1 ]
GeneIDi 2533.
KEGGi hsa:2533.
UCSCi uc003jls.3. human. [O15117-1 ]
uc003jlt.3. human. [O15117-2 ]

Organism-specific databases

CTDi 2533.
GeneCardsi GC05M039112.
H-InvDB HIX0024785.
HGNCi HGNC:4036. FYB.
HPAi CAB025336.
HPA026796.
MIMi 602731. gene.
neXtProti NX_O15117.
PharmGKBi PA28452.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG18948.
GeneTreei ENSGT00530000063460.
HOGENOMi HOG000008686.
HOVERGENi HBG005774.
InParanoidi O15117.
KOi K17698.
OMAi ACCDVKG.
OrthoDBi EOG70W3CP.
PhylomeDBi O15117.
TreeFami TF337003.

Enzyme and pathway databases

Reactomei REACT_12623. Generation of second messenger molecules.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinki O15117.

Miscellaneous databases

EvolutionaryTracei O15117.
GeneWikii FYB.
GenomeRNAii 2533.
NextBioi 9991.
PMAP-CutDB O15117.
PROi O15117.
SOURCEi Search...

Gene expression databases

Bgeei O15117.
CleanExi HS_FYB.
ExpressionAtlasi O15117. baseline and differential.
Genevestigatori O15117.

Family and domain databases

InterProi IPR029294. hSH3.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF14603. hSH3. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiFYB_HUMAN
AccessioniPrimary (citable) accession number: O15117
Secondary accession number(s): A8K2Y8
, B4DLN2, E9PBV9, O00359, Q9NZI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 24, 2009
Last modified: October 29, 2014
This is version 141 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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