Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  FYN-binding protein  

UniProtKB / Swiss-Prot ID :  FYB_HUMAN

Gene Name (Synonyms) : 
FYB, SLAP130  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus (By similarity). 

Protein 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. 

Protein Sequence MAKYNTGGNPTEDVSVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPAGPSNVPKFGSPKPPVAVKPSS...
Predicted Secondary Structure CCCCCCCCCCHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
51P -> L (in dbSNP:rs1642515). VAR_056880
332K -> R (in dbSNP:rs3749741). VAR_056881
672V -> F (in dbSNP:rs379707). VAR_060592
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
3N6-acetyllysine--MAKYNTG
--CCCCCCC
37.42HPRD
Link-
3N6-acetyllysine--MAKYNTG
--CCCCCCC
37.42Phosphositeplus
Link-
3N6-acetyllysine.--MAKYNTG
--CCCCCCC
37.42UniProtKB
Link-
4Phosphotyrosine-MAKYNTGG
-CCCCCCCC
14.39Phosphositeplus
Link-
46PhosphoserineQGNASPPAG
CCCCCCCCC
35.10HPRD
Link-
46PhosphoserineQGNASPPAG
CCCCCCCCC
35.10PhosphoELM
Link-
46PhosphoserineQGNASPPAG
CCCCCCCCC
35.10Phosphositeplus
Link-
46PhosphoserineQGNASPPAG
CCCCCCCCC
35.10SysPTM
Link-
46Phosphoserine.QGNASPPAG
CCCCCCCCC
35.10UniProtKB
Link-
149N6-acetyllysineDHDLKPLGP
CCCCCCCCC
44.23HPRD
Link-
149N6-acetyllysineDHDLKPLGP
CCCCCCCCC
44.23Phosphositeplus
Link-
149N6-acetyllysine.DHDLKPLGP
CCCCCCCCC
44.23UniProtKB
Link-
158PhosphothreonineKSGPTPPTS
CCCCCCCCC
45.48HPRD
Link-
158PhosphothreonineKSGPTPPTS
CCCCCCCCC
45.48PhosphoELM
Link-
158PhosphothreonineKSGPTPPTS
CCCCCCCCC
45.48Phosphositeplus
Link-
158PhosphothreonineKSGPTPPTS
CCCCCCCCC
45.48SysPTM
Link-
158Phosphothreonine.KSGPTPPTS
CCCCCCCCC
45.48UniProtKB
Link-
161PhosphothreoninePTPPTSENE
CCCCCCCCC
50.29HPRD
Link-
161PhosphothreoninePTPPTSENE
CCCCCCCCC
50.29Phosphositeplus
Link-
209PhosphoserineSTENSHEDE
CCCCCCCCC
23.25Phosphositeplus
Link-
265N6-acetyllysineGVVLKPAAS
CCCCCCCCC
22.47HPRD
Link-
265N6-acetyllysineGVVLKPAAS
CCCCCCCCC
22.47Phosphositeplus
Link-
265N6-acetyllysine.GVVLKPAAS
CCCCCCCCC
22.47UniProtKB
Link-
425N6-acetyllysinePRNIKPPFD
CCCCCCCCE
50.62HPRD
Link-
425N6-acetyllysinePRNIKPPFD
CCCCCCCCE
50.62Phosphositeplus
Link-
425N6-acetyllysine.PRNIKPPFD
CCCCCCCCE
50.62UniProtKB
Link-
446Caspase cleavage aspartic acidVTHSDGAGN
CCCCCCCCC
43.27Phosphositeplus
Link-
457PhosphoserineEEQDSEGET
HHCCCCCCC
47.39Phosphositeplus
Link-
457Phosphoserine.EEQDSEGET
HHCCCCCCC
47.39UniProtKB
Link-
559PhosphotyrosineARGSYGYIK
CCCCCCEEE
19.44Phosphositeplus
Link-
571PhosphotyrosineVEIDYDSLK
EEECHHHHH
17.06HPRD
Link-
571PhosphotyrosineVEIDYDSLK
EEECHHHHH
17.06PhosphoELM
Link-
571PhosphotyrosineVEIDYDSLK
EEECHHHHH
17.06Phosphositeplus
Link-
571PhosphotyrosineVEIDYDSLK
EEECHHHHH
17.06SysPTM
Link-
571Phosphotyrosine.VEIDYDSLK
EEECHHHHH
17.06UniProtKB
Link-
573PhosphoserineIDYDSLKLK
ECHHHHHHH
22.60HPRD
Link-
573PhosphoserineIDYDSLKLK
ECHHHHHHH
22.60PhosphoELM
Link-
573PhosphoserineIDYDSLKLK
ECHHHHHHH
22.60Phosphositeplus
Link-
573PhosphoserineIDYDSLKLK
ECHHHHHHH
22.60SysPTM
Link-
573Phosphoserine.IDYDSLKLK
ECHHHHHHH
22.60UniProtKB
Link-
595PhosphotyrosineDQEVYDDVA
HHHHHHHHH
12.98Phosphositeplus
Link-
595Phosphotyrosine (FYN)DQEVYDDVA
HHHHHHHHH
12.98HPRD
Link-
595Phosphotyrosine (Fyn;Fyn)DQEVYDDVA
HHHHHHHHH
12.98PhosphoELM
Link-
626Caspase cleavage aspartic acidDDIYDGIEE
HHHHCCCCC
52.51Phosphositeplus
Link-
651PhosphotyrosineGDEVYDDVD
HHHHHHHCC
12.36Phosphositeplus
Link-
651Phosphotyrosine (FYN)GDEVYDDVD
HHHHHHHCC
12.36HPRD
Link-
651Phosphotyrosine (Fyn;Fyn)GDEVYDDVD
HHHHHHHCC
12.36PhosphoELM
Link-
651Phosphotyrosine.GDEVYDDVD
HHHHHHHCC
12.36UniProtKB
Link-
711PhosphothreonineVLYSTKVTT
EEEEEEECC
18.90HPRD
Link
711Phosphothreonine.VLYSTKVTT
EEEEEEECC
18.90UniProtKB
Link
755PhosphotyrosineEEGKYGYVL
CCCCCCCCH
25.25HPRD
Link
755PhosphotyrosineEEGKYGYVL
CCCCCCCCH
25.25Phosphositeplus
Link
757PhosphotyrosineGKYGYVLRS
CCCCCCHHH
8.01HPRD
Link
757PhosphotyrosineGKYGYVLRS
CCCCCCHHH
8.01Phosphositeplus
Link
771PhosphotyrosineDGEIYDDIA
CCCHHHCCC
11.85Phosphositeplus
Link-
776Caspase cleavage aspartic acidDDIADGCIY
HCCCCCEEE
53.48Phosphositeplus
Link-
780PhosphotyrosineDGCIYDND
CCEEECCC
16.87Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SH21A_HUMANphysical interactionMINT-56628MINT15096483
FYN_HUMANphysical interactionMINT-16564MINT9207119
FYN_HUMANphysical interactionMINT-16565MINT9207119
FYN_HUMANphysical interactionMINT-16566MINT9207119
LCP2_HUMANphysical interactionMINT-15245MINT9207119
LCP2_HUMANphysical interactionMINT-15244MINT9207119
WASP_HUMANin vivoHPRD:04107HPRD10747096
SH21A_HUMANin vitro
in vivo
HPRD:04107HPRD12458214
LCP2_HUMANin vitroHPRD:04107HPRD10497204
9115214
9207119
VASP_HUMANin vivoHPRD:04107HPRD10747096
EVL_HUMANin vivoHPRD:04107HPRD10747096
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-149; LYS-265 ANDLYS-425, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; THR-158; TYR-571 ANDSER-573, AND MASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-571, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-711, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-457; TYR-571;SER-573 AND TYR-651, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures