This page contains ASEs represented as a graph of the mRNA exonic structure mapped to the protein primary sequence. Exons are shown in white with black outline. The reference form is represented above the alternative form. Coding regions are shown with blue horizontal bars. These can be interrupted by red blocks for absent regions. Below are the domains in the protein obtained from NCBI's Conserved Domain Database. Domains that are affected by the ASE are outlined in red.

Further information can be obtained in the help page

BAIAP2

• refseq_BAIAP2.F1 refseq_BAIAP2.R1 102 148
• NCBIGene 36.3 10458
• Single exon skipping, size difference: 46
• Inclusion in the protein causing a new stop codon
• Reference transcript: NM_017451

• cd SH3 57aa 8e-07 in ref transcript
  • Src homology 3 domains; SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.
• pfam IMD 220aa 5e-90 in ref transcript
  • IRSp53/MIM homology domain. The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent.
• smart SH3 61aa 8e-07 in ref transcript
  • Src homology 3 domains. Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.
• Changed! COG SbcC 220aa 0.008 in ref transcript
  • ATPase involved in DNA repair [DNA replication, recombination, and repair].

ENAH

• refseq_ENAH.F1 refseq_ENAH.R1 133 196
• NCBIGene 36.3 55740
• Single exon skipping, size difference: 63
• Exclusion in the protein (no frameshift)
• Reference transcript: NM_001008493

• cd Ena-Vasp 110aa 5e-54 in ref transcript
  • Enabled-VASP-type homology (EVH1) domain. The EVH1 domain binds to other proteins at proline rich sequences. It is found in proteins involved in cytoskeletal reorganization such as Enabled and VASP. Ena-VASP type EVH1 domains specifically recognize FPPPP motifs in the focal adhesion proteins zyxin and vinculin, and the ActA surface protein of Listeria monocytogenes. It has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.
• pfam WH1 107aa 2e-38 in ref transcript
  • WH1 domain. WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homologue. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.
• pfam VASP_tetra 40aa 3e-13 in ref transcript
  • VASP tetramerisation domain. Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerisation domain which forms a right handed alpha helical coiled coil structure.

ERBB2IP

• refseq_ERBB2IP.F1 refseq_ERBB2IP.R1 178 385
• NCBIGene 36.3 55914
• Single exon skipping, size difference: 207
• Exclusion in the protein (no frameshift)
• Reference transcript: NM_018695

• cd PDZ_signaling 60aa 3e-09 in ref transcript
  • PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.
• cd LRR_RI 162aa 2e-04 in ref transcript
  • Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
• Changed! smart PDZ 90aa 4e-10 in ref transcript
  • Domain present in PSD-95, Dlg, and ZO-1/2. Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.
• COG COG4886 348aa 3e-18 in ref transcript
  • Leucine-rich repeat (LRR) protein [Function unknown].
• COG Prc 60aa 4e-04 in ref transcript
  • Periplasmic protease [Cell envelope biogenesis, outer membrane].
• Changed! smart PDZ 90aa 6e-10 in modified transcript

MADD

• refseq_MADD.F10 refseq_MADD.R10 118 178
• NCBIGene 36.3 8567
• Single exon skipping, size difference: 60
• Exclusion in the protein (no frameshift)
• Reference transcript: NM_003682

• pfam DENN 230aa 3e-62 in ref transcript
  • DENN (AEX-3) domain. DENN (after differentially expressed in neoplastic vs normal cells) is a domain which occurs in several proteins involved in Rab- mediated processes or regulation of MAPK signalling pathways.
• pfam uDENN 91aa 2e-20 in ref transcript
  • uDENN domain. This region is always found associated with pfam02141. It is predicted to form an all beta domain.
• pfam dDENN 74aa 2e-11 in ref transcript
  • dDENN domain. This region is always found associated with pfam02141. It is predicted to form a globular domain. This domain is predicted to be completely alpha helical. Although not statistically supported it has been suggested that this domain may be similar to members of the Rho/Rac/Cdc42 GEF family.

MAP3K3

• refseq_MAP3K3.F2 refseq_MAP3K3.R2 133 226
• NCBIGene 36.3 4215
• Single exon skipping, size difference: 93
• Exclusion in the protein (no frameshift)
• Reference transcript: NM_203351

• cd STKc_MEKK3 266aa 1e-158 in ref transcript
  • Serine/threonine kinases (STKs), MAP/ERK kinase kinase 3 (MEKK3) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK3 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates extracellular signal-regulated kinase 5 (ERK5). The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy.
• cd PB1_Mekk2_3 79aa 1e-34 in ref transcript
  • The PB1 domain is present in the two mitogen-activated protein kinase kinases MEKK2 and MEKK3 which are two members of the signaling kinase cascade involved in angiogenesis and early cardiovascular development. The PB1 domain of MEKK2 (and/or MEKK3) interacts with the PB1 domain of another member of the kinase cascade Map2k5. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The MEKK2 and MEKK3 proteins contain a type II PB1 domain.
• smart S_TKc 250aa 3e-79 in ref transcript
  • Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily.
• smart PB1 77aa 6e-12 in ref transcript
  • PB1 domain. Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.
• COG SPS1 263aa 4e-30 in ref transcript
  • Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair].

MAP3K4

• refseq_MAP3K4.F1 refseq_MAP3K4.R1 139 289
• NCBIGene 36.3 4216
• Single exon skipping, size difference: 150
• Exclusion in the protein (no frameshift)
• Reference transcript: NM_005922

• cd STKc_MEKK4 260aa 1e-134 in ref transcript
  • Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK4 activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses.
• smart S_TKc 248aa 7e-73 in ref transcript
  • Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily.
• COG SPS1 267aa 3e-35 in ref transcript
  • Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair].

MAP3K7

• refseq_MAP3K7.F3 refseq_MAP3K7.R3 152 233
• NCBIGene 36.3 6885
• Single exon skipping, size difference: 81
• Exclusion in the protein (no frameshift)
• Reference transcript: NM_145331

• cd S_TKc 240aa 4e-61 in ref transcript
  • Serine/Threonine protein kinases, catalytic domain. Phosphotransferases of the serine or threonine-specific kinase subfamily. The enzymatic activity of these protein kinases is controlled by phosphorylation of specific residues in the activation segment of the catalytic domain, sometimes combined with reversible conformational changes in the C-terminal autoregulatory tail.
• smart TyrKc 242aa 3e-61 in ref transcript
  • Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily.
• pfam Mnd1 83aa 8e-04 in ref transcript
  • Mnd1 family. This family of proteins includes MND1 from Saccharomyces cerevisiae. The mnd1 protein forms a complex with hop2 to promote homologous chromosome pairing and meiotic double-strand break repair.
• COG SPS1 318aa 1e-26 in ref transcript
  • Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair].

MAP4K4

• refseq_MAP4K4.F3 refseq_MAP4K4.R3 172 265
• NCBIGene 36.3 9448
• Alternative 3-prime, size difference: 93
• Exclusion in the protein (no frameshift)
• Reference transcript: NM_145686

• cd STKc_MAP4K4_6 282aa 1e-149 in ref transcript
  • Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase kinase 4 (MAPKKKK4 or MAP4K4) and MAPKKKK6 (or MAP4K6) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAP4K4/MAP4K6 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4Ks (or MAPKKKKs) are involved in MAPK signaling pathways that are important in mediating cellular responses to extracellular signals by activating a MAPK kinase kinase (MAPKKK or MAP3K or MKKK). Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility.
• smart CNH 299aa 2e-87 in ref transcript
  • Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2. Unpublished observations.
• smart S_TKc 255aa 2e-61 in ref transcript
  • Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily.
• COG SPS1 293aa 5e-27 in ref transcript
  • Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair].
• COG ROM1 286aa 1e-06 in ref transcript
  • RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms].

MAP4K4

• refseq_MAP4K4.F5 refseq_MAP4K4.R5 136 160
• NCBIGene 36.3 9448
• Alternative 5-prime, size difference: 24
• Inclusion in the protein (no stop codon or frameshift)
• Reference transcript: NM_145686

• cd STKc_MAP4K4_6 282aa 1e-149 in ref transcript
  • Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase kinase 4 (MAPKKKK4 or MAP4K4) and MAPKKKK6 (or MAP4K6) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAP4K4/MAP4K6 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4Ks (or MAPKKKKs) are involved in MAPK signaling pathways that are important in mediating cellular responses to extracellular signals by activating a MAPK kinase kinase (MAPKKK or MAP3K or MKKK). Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility.
• Changed! smart CNH 299aa 2e-87 in ref transcript
  • Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2. Unpublished observations.
• smart S_TKc 255aa 2e-61 in ref transcript
  • Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily.
• COG SPS1 293aa 5e-27 in ref transcript
  • Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair].
• Changed! COG ROM1 286aa 1e-06 in ref transcript
  • RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms].
• Changed! smart CNH 307aa 4e-86 in modified transcript
• Changed! COG ROM1 294aa 2e-06 in modified transcript

MAPK10

• refseq_MAPK10.F1 refseq_MAPK10.R1 138 197
• NCBIGene 36.3 5602
• Single exon skipping, size difference: 59
• Exclusion in the protein causing a frameshift
• Reference transcript: NM_138982

• Changed! cd S_TKc 297aa 1e-66 in ref transcript
  • Serine/Threonine protein kinases, catalytic domain. Phosphotransferases of the serine or threonine-specific kinase subfamily. The enzymatic activity of these protein kinases is controlled by phosphorylation of specific residues in the activation segment of the catalytic domain, sometimes combined with reversible conformational changes in the C-terminal autoregulatory tail.
• Changed! smart S_TKc 284aa 1e-67 in ref transcript
  • Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily.
• Changed! PTZ PTZ00024 292aa 1e-34 in ref transcript
  • cyclin-dependent protein kinase; Provisional.
• Changed! cd S_TKc 62aa 1e-10 in modified transcript
• Changed! smart STYKc 61aa 3e-09 in modified transcript
  • Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.
• Changed! COG SPS1 59aa 0.003 in modified transcript
  • Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair].

MAPKAP1

• refseq_MAPKAP1.F3 refseq_MAPKAP1.R3 226 334
• NCBIGene 36.3 79109
• Single exon skipping, size difference: 108
• Exclusion in the protein (no frameshift)
• Reference transcript: NM_001006617

• Changed! pfam SIN1 464aa 1e-140 in ref transcript
  • Stress-activated map kinase interacting protein 1 (SIN1). This family consists of several stress-activated map kinase interacting protein 1 (MAPKAP1 OR SIN1) sequences. The fission yeast Sty1/Spc1 mitogen-activated protein (MAP) kinase is a member of the eukaryotic stress-activated MAP kinase (SAPK) family. Sin1 interacts with Sty1/Spc1. Cells lacking Sin1 display many, but not all, of the phenotypes of cells lacking the Sty1/Spc1 MAP kinase including sterility, multiple stress sensitivity and a cell-cycle delay. Sin1 is phosphorylated after stress but this is not Sty1/Spc1-dependent.
• Changed! pfam SIN1 428aa 1e-131 in modified transcript

MINK1

• refseq_MINK1.F3 refseq_MINK1.R3 136 247
• NCBIGene 36.3 50488
• Single exon skipping, size difference: 111
• Exclusion in the protein (no frameshift)
• Reference transcript: NM_153827

• cd STKc_MAP4K4_6 192aa 1e-114 in ref transcript
  • Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase kinase 4 (MAPKKKK4 or MAP4K4) and MAPKKKK6 (or MAP4K6) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAP4K4/MAP4K6 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4Ks (or MAPKKKKs) are involved in MAPK signaling pathways that are important in mediating cellular responses to extracellular signals by activating a MAPK kinase kinase (MAPKKK or MAP3K or MKKK). Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility.
• smart CNH 299aa 9e-83 in ref transcript
  • Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2. Unpublished observations.
• smart S_TKc 188aa 2e-54 in ref transcript
  • Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily.
• COG SPS1 205aa 2e-24 in ref transcript
  • Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair].
• COG ROM1 286aa 3e-08 in ref transcript
  • RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms].
• Changed! PRK PRK07764 140aa 2e-04 in modified transcript
  • DNA polymerase III subunits gamma and tau; Validated.

PTK2B

• refseq_PTK2B.F3 refseq_PTK2B.R3 102 262
• NCBIGene 36.3 2185
• Single exon skipping, size difference: 160
• Exclusion in 5'UTR
• Reference transcript: NM_173174

• cd PTKc_FAK 270aa 1e-146 in ref transcript
  • Catalytic Domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase. Protein Tyrosine Kinase (PTK) family; Focal Adhesion kinase (FAK); catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) tyr kinase that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy.
• pfam Pkinase_Tyr 233aa 5e-98 in ref transcript
  • Protein tyrosine kinase.
• pfam Focal_AT 139aa 6e-59 in ref transcript
  • Focal adhesion targeting region. Focal adhesion kinase (FAK) is a tyrosine kinase found in focal adhesions, intracellular signaling complexes that are formed following engagement of the extracellular matrix by integrins. The C-terminal 'focal adhesion targeting' (FAT) region is necessary and sufficient for localising FAK to focal adhesions. The crystal structure of FAT shows it forms a four-helix bundle that resembles those found in two other proteins involved in cell adhesion, alpha-catenin and vinculin. The binding of FAT to the focal adhesion protein, paxillin, requires the integrity of the helical bundle, whereas binding to another focal adhesion protein, talin, does not.
• smart B41 227aa 2e-31 in ref transcript
  • Band 4.1 homologues. Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.
• COG SPS1 229aa 2e-16 in ref transcript
  • Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair].