Details for: FYN
Gene ID: 2534
Gene Type: Protein-coding - A gene that serves as a template for producing a messenger RNA (mRNA) molecule, which is then translated into a functional protein.
Symbol: FYN
Ensembl ID: ENSG00000010810
Description: FYN proto-oncogene, Src family tyrosine kinase
Selected Context(s): Overall
Cell Significance Landscape
Associated with
Significant Cells
Cell Significance Index (CSI) scores for the chosen context(s)
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CSI 74.6rCSI 50.26%PRS 70.61
-
CSI 41.17rCSI 56.33%PRS 52.09
-
CSI 40.84rCSI 74.21%PRS 50.34
-
CSI 40.27rCSI 67.59%PRS 40.05
-
CSI 37.74rCSI 66.66%PRS 39.08
-
CSI 36.46rCSI 81.75%PRS 40.79
-
CSI 35.63rCSI 48.68%PRS 59.64
-
CSI 34.43rCSI 73.36%PRS 29.82
-
CSI 31.69rCSI 69.72%PRS 40.7
-
CSI 30.55rCSI 36.49%PRS 39.89
-
CSI 29.46rCSI 47.38%PRS 42.32
-
CSI 29.16rCSI 20.3%PRS 72.69
-
CSI 27.75rCSI 38.43%PRS 59.68
-
CSI 27.71rCSI 55.25%PRS 75.69
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CSI 26.6rCSI 21.12%PRS 79.34
-
CSI 26.5rCSI 32.11%PRS 46.52
-
CSI 26.34rCSI 64.02%PRS 38.76
-
CSI 25.92rCSI 32.24%PRS 38.19
-
CSI 25.32rCSI 19.16%PRS 71.38
-
CSI 24.89rCSI 28.74%PRS 51.28
-
CSI 23.27rCSI 20.23%PRS 68.28
-
CSI 22.41rCSI 28.76%PRS 55.27
-
CSI 22.15rCSI 69.29%PRS 44.18
-
CSI 22.05rCSI 28.2%PRS 80.86
-
CSI 21.54rCSI 16.38%PRS 70.54
-
CSI 21rCSI 20.21%PRS 58.08
-
CSI 19.91rCSI 17.44%PRS 67.75
-
CSI 19.39rCSI 12.92%PRS 78.8
-
CSI 18.5rCSI 16.27%PRS 45.82
-
CSI 18.4rCSI 54.3%PRS 61.06
-
CSI 17.28rCSI 62.19%PRS 38.53
-
CSI 16.52rCSI 12.41%PRS 62.73
-
CSI 16.33rCSI 36.08%PRS 44.33
-
CSI 16.15rCSI 12.11%PRS 85.25
-
CSI 16.1rCSI 60.86%PRS 40.92
-
CSI 15.56rCSI 19.38%PRS 68.65
-
CSI 15.23rCSI 10.93%PRS 72.04
-
CSI 15.21rCSI 12.02%PRS 44.77
-
CSI 15.12rCSI 47.24%PRS 41.54
-
CSI 14.72rCSI 13.7%PRS 58
-
CSI 14.54rCSI 49.82%PRS 47.27
-
CSI 14.19rCSI 18.3%PRS 41.23
-
CSI 14.14rCSI 24.46%PRS 48
-
CSI 14.02rCSI 16.47%PRS 85.67
-
CSI 13.78rCSI 36.71%PRS 47.84
-
CSI 13.05rCSI 13.63%PRS 81.11
-
CSI 12.42rCSI 19.81%PRS 50.74
-
CSI 12.16rCSI 10.43%PRS 65.95
-
CSI 12rCSI 8.89%PRS 50.55
-
CSI 11.96rCSI 9.66%PRS 68.39
-
CSI 11.95rCSI 30.36%PRS 52.34
-
CSI 11.92rCSI 9.68%PRS 58.41
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CSI 11.78rCSI 10.82%PRS 66.47
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CSI 11.68rCSI 44.07%PRS 45.1
-
CSI 11.67rCSI 48.41%PRS 62.59
-
CSI 11.46rCSI 64.75%PRS 43.28
-
CSI 11.03rCSI 9.69%PRS 63.03
-
CSI 10.84rCSI 13.92%PRS 51.19
-
CSI 10.74rCSI 24.79%PRS 47.48
-
CSI 10.72rCSI 20.44%PRS 73.28
-
CSI 10.72rCSI 15.29%PRS 60.33
-
CSI 10.66rCSI 47.36%PRS 57.09
-
CSI 10.49rCSI 14.57%PRS 56.78
-
CSI 10.39rCSI 7.78%PRS 72.74
-
CSI 10.19rCSI 7.16%PRS 76.92
-
CSI 9.98rCSI 6.94%PRS 68.44
-
CSI 9.87rCSI 32.12%PRS 58.92
-
CSI 9.8rCSI 9.64%PRS 80.2
-
CSI 9.78rCSI 11.33%PRS 70.54
-
CSI 9.74rCSI 57.35%PRS 41.44
-
CSI 9.74rCSI 17.07%PRS 49.98
-
CSI 9.6rCSI 18.77%PRS 89.62
-
CSI 9.57rCSI 12.02%PRS 85.65
-
CSI 9.48rCSI 12.92%PRS 49.95
-
CSI 9.42rCSI 17%PRS 80.43
-
CSI 9.38rCSI 67.03%PRS 51.72
-
CSI 9rCSI 13.04%PRS 73.83
-
CSI 8.9rCSI 21.39%PRS 66.05
-
CSI 8.47rCSI 17.18%PRS 37.88
-
CSI 8.42rCSI 6.55%PRS 75.72
-
CSI 8.31rCSI 6.66%PRS 78.5
-
CSI 8.23rCSI 6.34%PRS 57.8
-
CSI 8.22rCSI 14.06%PRS 76.32
-
CSI 8.15rCSI 14.64%PRS 50.89
-
CSI 8.03rCSI 6.92%PRS 64.02
-
CSI 7.89rCSI 35.27%PRS 42.25
-
CSI 7.89rCSI 58.02%PRS 44.86
-
CSI 7.85rCSI 38.68%PRS 69.17
-
CSI 7.83rCSI 21.53%PRS 71.19
-
CSI 7.83rCSI 15.72%PRS 47.05
-
CSI 7.68rCSI 21.84%PRS 56.18
-
CSI 7.5rCSI 30.56%PRS 53.01
-
CSI 7.49rCSI 47.95%PRS 60.94
-
CSI 7.34rCSI 10.38%PRS 63.8
-
CSI 7.32rCSI 11.04%PRS 61.39
-
CSI 7.27rCSI 24.62%PRS 50.89
-
CSI 7.27rCSI 6.72%PRS 77.48
-
CSI 7.25rCSI 8.66%PRS 77.56
-
CSI 7.22rCSI 19.28%PRS 49.31
-
CSI 7.21rCSI 19.02%PRS 66.75
-
CSI 0.2rCSI 2.0%PRS 71.2%
-
CSI 0.3rCSI 3.9%PRS 74.0%
-
CSI 0.3rCSI 2.4%PRS 71.7%
-
CSI 0.4rCSI 4.0%PRS 86.5%
-
CSI 0.5rCSI 5.4%PRS 85.0%
-
CSI 0.5rCSI 2.1%PRS 72.4%
-
CSI 0.6rCSI 1.1%PRS 60.5%
-
CSI 0.6rCSI 4.4%PRS 76.0%
-
CSI 0.7rCSI 2.5%PRS 88.5%
-
CSI 0.7rCSI 4.5%PRS 49.8%
-
CSI 0.8rCSI 5.2%PRS 54.2%
-
CSI 0.8rCSI 14.5%PRS 89.0%
-
CSI 0.8rCSI 0.7%PRS 54.6%
-
CSI 0.8rCSI 1.3%PRS 55.9%
-
CSI 0.8rCSI 4.8%PRS 67.5%
-
CSI 0.9rCSI 2.4%PRS 55.0%
-
CSI 0.9rCSI 5.4%PRS 67.5%
-
CSI 0.9rCSI 3.8%PRS 69.8%
-
CSI 1.0rCSI 4.7%PRS 74.8%
-
CSI 1.0rCSI 1.8%PRS 66.9%
-
CSI 1.1rCSI 1.1%PRS 61.3%
-
CSI 1.1rCSI 1.7%PRS 59.8%
-
CSI 1.2rCSI 13.1%PRS 49.4%
-
CSI 1.2rCSI 18.6%PRS 62.8%
-
CSI 1.2rCSI 22.9%PRS 74.8%
-
CSI 1.2rCSI 4.7%PRS 73.6%
-
CSI 1.3rCSI 4.7%PRS 67.6%
-
CSI 1.4rCSI 3.3%PRS 69.6%
-
CSI 1.4rCSI 8.2%PRS 77.7%
-
CSI 1.4rCSI 1.6%PRS 47.9%
-
CSI 1.4rCSI 3.2%PRS 55.8%
-
CSI 1.4rCSI 11.7%PRS 51.1%
-
CSI 1.5rCSI 2.0%PRS 77.7%
-
CSI 1.5rCSI 8.2%PRS 73.9%
-
CSI 1.5rCSI 1.5%PRS 48.3%
-
CSI 1.5rCSI 4.0%PRS 75.0%
-
CSI 1.6rCSI 8.3%PRS 53.0%
-
CSI 1.8rCSI 5.3%PRS 56.6%
-
CSI 1.8rCSI 5.8%PRS 63.4%
-
CSI 1.8rCSI 2.6%PRS 48.0%
-
CSI 1.8rCSI 7.2%PRS 58.2%
-
CSI 1.8rCSI 11.8%PRS 76.5%
-
CSI 1.9rCSI 5.5%PRS 81.7%
-
CSI 1.9rCSI 2.7%PRS 54.2%
-
CSI 1.9rCSI 1.5%PRS 59.1%
-
CSI 1.9rCSI 16.6%PRS 45.4%
-
CSI 2.0rCSI 5.5%PRS 53.7%
-
CSI 2.0rCSI 4.3%PRS 76.4%
-
CSI 2.1rCSI 2.5%PRS 55.8%
-
CSI 2.1rCSI 19.5%PRS 69.6%
-
CSI 2.2rCSI 8.5%PRS 34.9%
-
CSI 2.2rCSI 5.3%PRS 89.4%
-
CSI 2.3rCSI 14.9%PRS 55.4%
-
CSI 2.3rCSI 14.3%PRS 40.5%
-
CSI 2.3rCSI 2.9%PRS 64.1%
-
CSI 2.3rCSI 2.3%PRS 60.5%
-
CSI 2.3rCSI 2.9%PRS 59.8%
-
CSI 2.4rCSI 6.1%PRS 66.4%
-
CSI 2.4rCSI 2.1%PRS 62.6%
-
CSI 2.4rCSI 4.6%PRS 87.3%
-
CSI 2.5rCSI 10.9%PRS 71.1%
-
CSI 2.6rCSI 35.2%PRS 86.0%
-
CSI 2.6rCSI 7.0%PRS 87.7%
-
CSI 2.7rCSI 6.2%PRS 77.3%
-
CSI 2.7rCSI 21.0%PRS 54.9%
-
CSI 2.8rCSI 8.9%PRS 56.6%
-
CSI 2.8rCSI 4.1%PRS 52.0%
-
CSI 2.8rCSI 17.5%PRS 73.9%
-
CSI 2.9rCSI 3.2%PRS 74.1%
-
CSI 2.9rCSI 8.2%PRS 77.3%
-
CSI 2.9rCSI 6.6%PRS 57.6%
-
CSI 3.0rCSI 41.8%PRS 49.6%
-
CSI 3.0rCSI 11.0%PRS 77.3%
-
CSI 3.1rCSI 73.5%PRS 40.3%
-
CSI 3.1rCSI 73.6%PRS 39.3%
-
CSI 3.2rCSI 23.8%PRS 52.1%
-
CSI 3.2rCSI 64.8%PRS 49.2%
-
CSI 3.2rCSI 6.2%PRS 84.4%
-
CSI 3.2rCSI 7.7%PRS 67.0%
-
CSI 3.2rCSI 4.9%PRS 58.5%
-
CSI 3.3rCSI 16.3%PRS 70.2%
-
CSI 3.3rCSI 13.4%PRS 56.5%
-
CSI 3.3rCSI 67.6%PRS 50.5%
-
CSI 3.3rCSI 5.9%PRS 66.5%
-
CSI 3.3rCSI 11.0%PRS 45.3%
-
CSI 3.4rCSI 4.6%PRS 65.7%
-
CSI 3.5rCSI 5.1%PRS 63.3%
-
CSI 3.5rCSI 16.8%PRS 57.0%
-
CSI 3.6rCSI 9.3%PRS 53.0%
-
CSI 3.7rCSI 7.9%PRS 57.7%
-
CSI 3.7rCSI 10.8%PRS 47.9%
-
CSI 3.8rCSI 6.0%PRS 50.2%
-
CSI 3.8rCSI 12.6%PRS 43.7%
-
CSI 3.8rCSI 4.1%PRS 61.9%
-
CSI 3.8rCSI 10.0%PRS 57.5%
-
CSI 3.8rCSI 9.9%PRS 84.2%
-
CSI 3.9rCSI 27.3%PRS 50.0%
-
CSI 3.9rCSI 8.1%PRS 60.5%
-
CSI 3.9rCSI 12.1%PRS 67.4%
-
CSI 4.0rCSI 68.3%PRS 81.7%
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Network Configuration
Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.
Legend:
- Query Gene
-
Node Color (Target Cell CSI, relative to current network):
- Very High
- High
- Medium
- Low
- Very Low
- CSI N/A
- Node Size: Proportional to Target Cell CSI magnitude
- STRING PPI Edge
- Shared Pathway Edge (ONTOLOGY)
Other Information
This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.
Genular Protein ID: 3205760051
Symbol: FYN_HUMAN
Name: Tyrosine-protein kinase Fyn
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 3099169
Title: Isolation and oncogenic potential of a novel human src-like gene.
PubMed ID: 3099169
PubMed ID: 3526330
Title: Yes-related protooncogene, syn, belongs to the protein-tyrosine kinase family.
PubMed ID: 3526330
PubMed ID: 7822789
Title: Human p59fyn(T) regulates OKT3-induced calcium influx by a mechanism distinct from PIP2 hydrolysis in Jurkat T cells.
PubMed ID: 7822789
PubMed ID: 19054851
Title: Human protein factory for converting the transcriptome into an in vitro-expressed proteome.
PubMed ID: 19054851
DOI: 10.1038/nmeth.1273
PubMed ID: 14574404
Title: The DNA sequence and analysis of human chromosome 6.
PubMed ID: 14574404
DOI: 10.1038/nature02055
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 1699196
Title: In vivo phosphorylation and membrane association of the fyn proto-oncogene product in IM-9 human lymphoblasts.
PubMed ID: 1699196
PubMed ID: 1533589
Title: Regulation of the p59fyn protein tyrosine kinase by the CD45 phosphotyrosine phosphatase.
PubMed ID: 1533589
PubMed ID: 8394019
Title: Src-homology 3 domain of protein kinase p59fyn mediates binding to phosphatidylinositol 3-kinase in T cells.
PubMed ID: 8394019
PubMed ID: 8206991
Title: Dual myristylation and palmitylation of Src family member p59fyn affects subcellular localization.
PubMed ID: 8206991
PubMed ID: 7568038
Title: p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine kinase ITK: implications for T-cell costimulation.
PubMed ID: 7568038
PubMed ID: 9038210
Title: Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes.
PubMed ID: 9038210
PubMed ID: 9360983
Title: Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates.
PubMed ID: 9360983
PubMed ID: 9207119
Title: Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production.
PubMed ID: 9207119
PubMed ID: 9741627
Title: A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth.
PubMed ID: 9741627
PubMed ID: 10196263
Title: Altered expression of tyrosine kinases of the Src and Syk families in human T-cell leukemia virus type 1-infected T-cell lines.
PubMed ID: 10196263
PubMed ID: 10498895
Title: Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity.
PubMed ID: 10498895
PubMed ID: 10790433
Title: Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation.
PubMed ID: 10790433
PubMed ID: 11005864
Title: T-cell receptor antagonists induce Vav phosphorylation by selective activation of Fyn kinase.
PubMed ID: 11005864
PubMed ID: 11162638
Title: Activated Fyn phosphorylates alpha-synuclein at tyrosine residue 125.
PubMed ID: 11162638
PubMed ID: 11518702
Title: The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK.
PubMed ID: 11518702
PubMed ID: 11536198
Title: Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates oligodendrocyte differentiation.
PubMed ID: 11536198
DOI: 10.1002/neu.1066
PubMed ID: 12218089
Title: Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells.
PubMed ID: 12218089
PubMed ID: 12788081
Title: p250GAP, a neural RhoGAP protein, is associated with and phosphorylated by Fyn.
PubMed ID: 12788081
PubMed ID: 14761972
Title: Regulation of TRPC6 channel activity by tyrosine phosphorylation.
PubMed ID: 14761972
PubMed ID: 15557120
Title: Phosphorylation of DCC by Fyn mediates Netrin-1 signaling in growth cone guidance.
PubMed ID: 15557120
PubMed ID: 14707117
Title: Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein (WASp) tyrosine phosphorylation is required for coupling T cell antigen receptor engagement to WASp effector function and T cell activation.
PubMed ID: 14707117
DOI: 10.1084/jem.20030976
PubMed ID: 14757743
Title: Unc119, a novel activator of Lck/Fyn, is essential for T cell activation.
PubMed ID: 14757743
DOI: 10.1084/jem.20030589
PubMed ID: 15489916
Title: Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation.
PubMed ID: 15489916
PubMed ID: 15536091
Title: Fyn phosphorylates human MAP-2c on tyrosine 67.
PubMed ID: 15536091
PubMed ID: 15537652
Title: Regulation of ultraviolet B-induced phosphorylation of histone H3 at serine 10 by Fyn kinase.
PubMed ID: 15537652
PubMed ID: 16387660
Title: Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation.
PubMed ID: 16387660
PubMed ID: 16841086
Title: Src-family tyrosine kinase fyn phosphorylates phosphatidylinositol 3-kinase enhancer-activating Akt, preventing its apoptotic cleavage and promoting cell survival.
PubMed ID: 16841086
PubMed ID: 17925405
Title: Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain.
PubMed ID: 17925405
PubMed ID: 17194753
Title: Specific phosphorylation of p120-catenin regulatory domain differently modulates its binding to RhoA.
PubMed ID: 17194753
DOI: 10.1128/mcb.01974-06
PubMed ID: 18056706
Title: Regulation of FynT function by dual domain docking on PAG/Cbp.
PubMed ID: 18056706
PubMed ID: 18258597
Title: Neph1, a component of the kidney slit diaphragm, is tyrosine-phosphorylated by the Src family tyrosine kinase and modulates intracellular signaling by binding to Grb2.
PubMed ID: 18258597
PubMed ID: 18088087
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19807924
Title: Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening.
PubMed ID: 19807924
PubMed ID: 19179337
Title: Phosphorylation of nephrin triggers Ca2+ signaling by recruitment and activation of phospholipase C-{gamma}1.
PubMed ID: 19179337
PubMed ID: 19652227
Title: Semaphorin3A signaling mediated by Fyn-dependent tyrosine phosphorylation of collapsin response mediator protein 2 at tyrosine 32.
PubMed ID: 19652227
PubMed ID: 19369195
Title: Large-scale proteomics analysis of the human kinome.
PubMed ID: 19369195
PubMed ID: 20028775
Title: The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402 and 580 occurs via a distinct mechanism than other receptor systems.
PubMed ID: 20028775
DOI: 10.1189/jlb.0409227
PubMed ID: 20100835
Title: Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm.
PubMed ID: 20100835
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 22080863
Title: T cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in mice.
PubMed ID: 22080863
DOI: 10.1172/jci59492
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 27335501
Title: ARAP, a novel adaptor protein, is required for TCR signaling and integrin-mediated adhesion.
PubMed ID: 27335501
PubMed ID: 7687536
Title: Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin.
PubMed ID: 7687536
DOI: 10.2210/pdb1shf/pdb
PubMed ID: 7664083
Title: High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
PubMed ID: 7664083
DOI: 10.1038/nsb0894-546
PubMed ID: 8961927
Title: Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase.
PubMed ID: 8961927
DOI: 10.1021/bi9620969
PubMed ID: 8681387
Title: Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain.
PubMed ID: 8681387
PubMed ID: 8805554
Title: Solution structure and peptide binding of the SH3 domain from human Fyn.
PubMed ID: 8805554
PubMed ID: 9351806
Title: The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.
PubMed ID: 9351806
PubMed ID: 12545174
PubMed ID: 17344846
Title: Patterns of somatic mutation in human cancer genomes.
PubMed ID: 17344846
DOI: 10.1038/nature05610
Sequence Information:
- Length: 537
- Mass: 60762
- Checksum: 4A1E443A4B5A0977
- Sequence:
MGCVQCKDKE ATKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL LDFLKDGEGR ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQSFL EDYFTATEPQ YQPGENL