LLPS-Mum-2032
Src

▼ OVERVIEW

Status: Reviewed
Protein Name: Neuronal proto-oncogene tyrosine-protein kinase Src; Proto-oncogene c-Src; pp60c-src; p60-Src
Gene Name: Src
Ensembl Gene: ENSMUSG00000027646.15
Ensembl Protein: ENSMUSP00000105159.1
Organism: Mus musculus
Taxa ID: 10090
LLPS Type: Others
PDB: 6F3F (A) More


▼ PROPERTY


——— Disorder propensity (calculated by IUPred2A)

▼ Classification

Condensates:
CondensateDescriptionTissue/CellPMIDs
Postsynaptic density
"...We report the first direct comparison of the proteome of triplicate isolates of mouse and human cortical postsynaptic densities. The mouse postsynaptic density comprised 1556 proteins and the human one 1461."
Mouse cortex23071613

▼ FUNCTION

Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (PubMed:9344858). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation (By similarity). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (By similarity). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-738'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-226'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Involved in anchorage-independent cell growth (By similarity). Required for podosome formation (PubMed:21525037).

▼ SEQUENCE

Protein Sequence (FASTA)
1     MGSNKSKPKD  ASQRRRSLEP  SENVHGAGGA  FPASQTPSKP  ASADGHRGPS  AAFVPPAAEP  60
61    KLFGGFNSSD  TVTSPQRAGP  LAGGVTTFVA  LYDYESRTET  DLSFKKGERL  QIVNNTRKVD  120
121   VREGDWWLAH  SLSTGQTGYI  PSNYVAPSDS  IQAEEWYFGK  ITRRESERLL  LNAENPRGTF  180
181   LVRESETTKG  AYCLSVSDFD  NAKGLNVKHY  KIRKLDSGGF  YITSRTQFNS  LQQLVAYYSK  240
241   HADGLCHRLT  TVCPTSKPQT  QGLAKDAWEI  PRESLRLEVK  LGQGCFGEVW  MGTWNGTTRV  300
301   AIKTLKPGTM  SPEAFLQEAQ  VMKKLRHEKL  VQLYAVVSEE  PIYIVTEYMN  KGSLLDFLKG  360
361   ETGKYLRLPQ  LVDMSAQIAS  GMAYVERMNY  VHRDLRAANI  LVGENLVCKV  ADFGLARLIE  420
421   DNEYTARQGA  KFPIKWTAPE  AALYGRFTIK  SDVWSFGILL  TELTTKGRVP  YPGMVNREVL  480
481   DQVERGYRMP  CPPECPESLH  DLMCQCWRKE  PEERPTFEYL  QAFLEDYFTS  TEPQYQPGEN  540
541   L  541
Nucleotide CDS Sequence (FASTA)
1     ATGGGCAGCA  ACAAGAGCAA  GCCCAAGGAC  GCCAGCCAGC  GGCGCCGCAG  CCTGGAGCCC  60
61    TCGGAAAACG  TGCACGGGGC  AGGGGGCGCC  TTCCCGGCCT  CACAGACACC  GAGCAAGCCC  120
121   GCCTCCGCCG  ACGGCCACCG  CGGGCCCAGC  GCCGCCTTCG  TGCCGCCCGC  GGCCGAGCCC  180
181   AAGCTCTTCG  GAGGCTTCAA  CTCCTCGGAC  ACCGTCACCT  CCCCGCAGAG  GGCGGGGCCT  240
241   CTGGCAGGTG  GGGTGACCAC  CTTTGTGGCC  CTCTATGACT  ATGAGTCACG  GACAGAGACT  300
301   GACCTGTCCT  TCAAGAAAGG  GGAGCGGCTG  CAGATTGTCA  ATAACACAGA  GGGAGACTGG  360
361   TGGCTGGCAC  ACTCGCTGAG  CACGGGACAG  ACCGGTTACA  TCCCCAGCAA  CTATGTGGCG  420
421   CCCTCCGACT  CCATCCAGGC  TGAGGAGTGG  TACTTTGGCA  AGATCACTAG  ACGGGAATCA  480
481   GAGCGGCTGC  TGCTCAACGC  CGAGAACCCG  AGAGGGACCT  TCCTCGTGAG  GGAGAGTGAG  540
541   ACCACAAAAG  GTGCCTACTG  CCTCTCTGTA  TCCGACTTCG  ACAATGCCAA  GGGCCTAAAT  600
601   GTGAAACACT  ACAAGATCCG  CAAGCTGGAC  AGCGGCGGTT  TCTACATCAC  CTCCCGCACC  660
661   CAGTTCAACA  GCCTGCAGCA  GCTCGTGGCT  TACTACTCCA  AACATGCTGA  TGGCCTGTGT  720
721   CACCGCCTCA  CTACCGTATG  TCCCACATCC  AAGCCTCAGA  CCCAGGGATT  GGCCAAGGAT  780
781   GCGTGGGAGA  TCCCCCGGGA  GTCCCTGCGG  CTGGAGGTCA  AGCTGGGCCA  GGGTTGCTTC  840
841   GGAGAGGTGT  GGATGGGGAC  CTGGAACGGC  ACCACGAGGG  TTGCCATCAA  AACTCTGAAG  900
901   CCAGGCACCA  TGTCCCCAGA  GGCCTTCCTG  CAGGAGGCCC  AAGTCATGAA  GAAACTGAGG  960
961   CACGAGAAAC  TGGTGCAGCT  GTATGCTGTG  GTGTCGGAAG  AACCCATTTA  CATTGTGACA  1020
1021  GAGTACATGA  ACAAGGGGAG  TCTGCTGGAC  TTTCTCAAGG  GGGAAACGGG  CAAATATTTG  1080
1081  CGGCTACCCC  AGCTGGTGGA  CATGTCTGCT  CAGATCGCTT  CAGGCATGGC  CTATGTGGAG  1140
1141  CGGATGAACT  ATGTGCACCG  GGACCTTCGA  GCCGCCAATA  TCCTAGTAGG  GGAGAACCTG  1200
1201  GTGTGCAAAG  TGGCCGACTT  TGGGTTGGCC  CGGCTCATAG  AAGACAACGA  ATACACAGCC  1260
1261  CGGCAAGGTG  CCAAATTCCC  CATCAAGTGG  ACCGCCCCTG  AAGCTGCTCT  GTACGGCAGG  1320
1321  TTCACCATCA  AGTCGGATGT  GTGGTCCTTT  GGGATTCTGC  TGACCGAGCT  CACCACTAAG  1380
1381  GGAAGAGTGC  CCTATCCTGG  GATGGTGAAC  CGTGAGGTTC  TGGACCAGGT  GGAGCGGGGC  1440
1441  TACCGGATGC  CTTGTCCCCC  CGAGTGCCCC  GAGTCCCTGC  ATGACCTTAT  GTGCCAGTGC  1500
1501  TGGCGGAAGG  AGCCCGAGGA  GCGGCCCACC  TTCGAGTACC  TGCAGGCCTT  CCTGGAAGAC  1560
1561  TACTTTACGT  CCACTGAGCC  ACAGTACCAG  CCCGGGGAGA  ACCTATAG  1608

▼ KEYWORD

ID
Family
3D-structure
ATP-binding
Cell adhesion
Cell cycle
Cell membrane
Complete proteome
Cytoplasm
Cytoskeleton
Immunity
Kinase
Lipoprotein
Membrane
Mitochondrion
Mitochondrion inner membrane
Myristate
Nucleotide-binding
Nucleus
Phosphoprotein
Proto-oncogene
Reference proteome
SH2 domain
SH3 domain
Transferase
Tyrosine-protein kinase
Ubl conjugation

▼ GENE ONTOLOGY

ID
Classification
Description
Cellular Component
Actin filament
Cellular Component
Caveola
Cellular Component
Cytoplasm
Cellular Component
Cytosol
Cellular Component
Extrinsic component of cytoplasmic side of plasma membrane
Cellular Component
Glutamatergic synapse
Cellular Component
Late endosome
Cellular Component
Lysosome
Cellular Component
Membrane
Cellular Component
Mitochondrial inner membrane
Cellular Component
Mitochondrion
Cellular Component
Neuron projection
Cellular Component
Nucleoplasm
Cellular Component
Nucleus
Cellular Component
Perinuclear region of cytoplasm
Cellular Component
Plasma membrane
Cellular Component
Podosome
Cellular Component
Postsynaptic density
Cellular Component
Postsynaptic specialization, intracellular component
Cellular Component
Ruffle membrane
Molecular Function
ATP binding
Molecular Function
Cell adhesion molecule binding
Molecular Function
Connexin binding
Molecular Function
Enzyme binding
Molecular Function
Ephrin receptor binding
Molecular Function
Estrogen receptor binding
Molecular Function
Growth factor receptor binding
Molecular Function
Heme binding
Molecular Function
Insulin receptor binding
Molecular Function
Integrin binding
Molecular Function
Ion channel binding
Molecular Function
Kinase activity
Molecular Function
Kinase binding
Molecular Function
Non-membrane spanning protein tyrosine kinase activity
Molecular Function
Phosphoprotein binding
Molecular Function
Protein C-terminus binding
Molecular Function
Protein domain specific binding
Molecular Function
Protein kinase activity
Molecular Function
Protein kinase binding
Molecular Function
Protein kinase C binding
Molecular Function
Protein tyrosine kinase activity
Molecular Function
Protein-containing complex binding
Molecular Function
Scaffold protein binding
Molecular Function
SH2 domain binding
Molecular Function
Signaling receptor binding
Molecular Function
Ubiquitin protein ligase binding
Biological Process
Activation of protein kinase B activity
Biological Process
Adherens junction organization
Biological Process
Angiotensin-activated signaling pathway involved in heart process
Biological Process
Bone resorption
Biological Process
Branching involved in mammary gland duct morphogenesis
Biological Process
Cell cycle
Biological Process
Cell differentiation
Biological Process
Cell migration
Biological Process
Cell population proliferation
Biological Process
Cell-cell adhesion
Biological Process
Cellular response to fatty acid
Biological Process
Cellular response to fluid shear stress
Biological Process
Cellular response to hydrogen peroxide
Biological Process
Cellular response to hypoxia
Biological Process
Cellular response to insulin stimulus
Biological Process
Cellular response to lipopolysaccharide
Biological Process
Cellular response to peptide hormone stimulus
Biological Process
Cellular response to platelet-derived growth factor stimulus
Biological Process
Cellular response to progesterone stimulus
Biological Process
Cellular response to reactive oxygen species
Biological Process
Cellular response to transforming growth factor beta stimulus
Biological Process
Epidermal growth factor receptor signaling pathway
Biological Process
Forebrain development
Biological Process
Integrin-mediated signaling pathway
Biological Process
Intracellular signal transduction
Biological Process
Negative regulation of anoikis
Biological Process
Negative regulation of apoptotic process
Biological Process
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
Biological Process
Negative regulation of extrinsic apoptotic signaling pathway
Biological Process
Negative regulation of focal adhesion assembly
Biological Process
Negative regulation of intrinsic apoptotic signaling pathway
Biological Process
Negative regulation of mitochondrial depolarization
Biological Process
Negative regulation of protein homooligomerization
Biological Process
Negative regulation of telomerase activity
Biological Process
Negative regulation of telomere maintenance via telomerase
Biological Process
Negative regulation of transcription, DNA-templated
Biological Process
Neurotrophin TRK receptor signaling pathway
Biological Process
Odontogenesis
Biological Process
Oogenesis
Biological Process
Osteoclast development
Biological Process
Peptidyl-serine phosphorylation
Biological Process
Peptidyl-tyrosine autophosphorylation
Biological Process
Peptidyl-tyrosine phosphorylation
Biological Process
Phosphorylation
Biological Process
Positive regulation of apoptotic process
Biological Process
Positive regulation of canonical Wnt signaling pathway
Biological Process
Positive regulation of cell adhesion
Biological Process
Positive regulation of cyclin-dependent protein serine/threonine kinase activity
Biological Process
Positive regulation of cytokine secretion
Biological Process
Positive regulation of DNA biosynthetic process
Biological Process
Positive regulation of epithelial cell migration
Biological Process
Positive regulation of ERK1 and ERK2 cascade
Biological Process
Positive regulation of gene expression
Biological Process
Positive regulation of glucose metabolic process
Biological Process
Positive regulation of insulin receptor signaling pathway
Biological Process
Positive regulation of intracellular signal transduction
Biological Process
Positive regulation of lamellipodium morphogenesis
Biological Process
Positive regulation of MAP kinase activity
Biological Process
Positive regulation of ovarian follicle development
Biological Process
Positive regulation of peptidyl-tyrosine phosphorylation
Biological Process
Positive regulation of phosphatidylinositol 3-kinase activity
Biological Process
Positive regulation of platelet-derived growth factor receptor-beta signaling pathway
Biological Process
Positive regulation of podosome assembly
Biological Process
Positive regulation of protein autophosphorylation
Biological Process
Positive regulation of protein kinase B signaling
Biological Process
Positive regulation of protein localization to nucleus
Biological Process
Positive regulation of protein processing
Biological Process
Positive regulation of protein serine/threonine kinase activity
Biological Process
Positive regulation of protein transport
Biological Process
Positive regulation of small GTPase mediated signal transduction
Biological Process
Positive regulation of smooth muscle cell migration
Biological Process
Positive regulation of transcription, DNA-templated
Biological Process
Primary ovarian follicle growth
Biological Process
Progesterone receptor signaling pathway
Biological Process
Protein autophosphorylation
Biological Process
Protein destabilization
Biological Process
Protein phosphorylation
Biological Process
Regulation of caveolin-mediated endocytosis
Biological Process
Regulation of cell projection assembly
Biological Process
Regulation of cell-cell adhesion
Biological Process
Regulation of early endosome to late endosome transport
Biological Process
Regulation of epithelial cell migration
Biological Process
Regulation of intracellular estrogen receptor signaling pathway
Biological Process
Regulation of postsynaptic neurotransmitter receptor activity
Biological Process
Regulation of protein binding
Biological Process
Response to acidic pH
Biological Process
Response to electrical stimulus
Biological Process
Response to interleukin-1
Biological Process
Response to mechanical stimulus
Biological Process
Response to mineralocorticoid
Biological Process
Response to nutrient levels
Biological Process
Response to virus
Biological Process
Stress fiber assembly
Biological Process
Substrate adhesion-dependent cell spreading
Biological Process
Transcytosis
Biological Process
Transforming growth factor beta receptor signaling pathway
Biological Process
Transmembrane receptor protein tyrosine kinase signaling pathway
Biological Process
Uterus development

▼ KEGG


▼ ORTHOLOGY

DrLLPS IDOrganismIdentityE-valueScore
LLPS-Pap-2515Pan paniscus99.560.0 956
LLPS-Ran-2557Rattus norvegicus99.450.01123
LLPS-Pat-0192Pan troglodytes98.890.01102
LLPS-Hos-4827Homo sapiens98.890.01102
LLPS-Mal-3995Mandrillus leucophaeus98.710.01100
LLPS-Chs-2554Chlorocebus sabaeus98.710.01098
LLPS-Maf-4116Macaca fascicularis98.710.01100
LLPS-Aon-3625Aotus nancymaae98.340.01097
LLPS-Tag-2197Taeniopygia guttata98.10.0 870
LLPS-Ict-4453Ictidomys tridecemlineatus97.970.01088
LLPS-Cas-3823Carlito syrichta97.970.01086
LLPS-Otg-2338Otolemur garnettii97.970.01092
LLPS-Caj-4394Callithrix jacchus97.60.01081
LLPS-Gog-3202Gorilla gorilla97.60.01080
LLPS-Rhb-2714Rhinopithecus bieti97.60.01082
LLPS-Loa-4417Loxodonta africana97.60.01105
LLPS-Mea-3680Mesocricetus auratus97.420.01093
LLPS-Fud-1380Fukomys damarensis97.240.0 957
LLPS-Cap-0475Cavia porcellus97.230.01071
LLPS-Poa-1909Pongo abelii96.930.01093
LLPS-Myl-4188Myotis lucifugus96.870.01090
LLPS-Mup-4148Mustela putorius furo96.860.01087
LLPS-Aim-1577Ailuropoda melanoleuca96.860.01087
LLPS-Caf-2899Canis familiaris96.860.01087
LLPS-Urm-1272Ursus maritimus96.860.01086
LLPS-Paa-0503Papio anubis96.750.01090
LLPS-Mam-3642Macaca mulatta96.750.01090
LLPS-Man-2015Macaca nemestrina96.750.01090
LLPS-Cea-3856Cercocebus atys96.560.01088
LLPS-Dio-4081Dipodomys ordii96.320.01080
LLPS-Fec-0156Felis catus96.020.01093
LLPS-Eqc-3924Equus caballus95.958e-41 160
LLPS-Orc-3946Oryctolagus cuniculus95.40.01061
LLPS-Ova-2328Ovis aries95.250.01074
LLPS-Bot-1432Bos taurus94.890.01068
LLPS-Sus-3143Sus scrofa94.810.01088
LLPS-Fia-1852Ficedula albicollis94.270.01060
LLPS-Nol-1392Nomascus leucogenys94.110.01014
LLPS-Gaga-2157Gallus gallus94.090.01059
LLPS-Meg-2240Meleagris gallopavo94.090.01058
LLPS-Sah-3984Sarcophilus harrisii92.980.01041
LLPS-Pes-3669Pelodiscus sinensis92.610.01039
LLPS-Mod-3280Monodelphis domestica91.850.01048
LLPS-Anc-2987Anolis carolinensis91.130.01019
LLPS-Xet-3905Xenopus tropicalis86.740.0 968
LLPS-Lac-3266Latimeria chalumnae85.920.0 958
LLPS-Dar-2736Danio rerio82.690.0 921
LLPS-Ora-1852Ornithorhynchus anatinus82.470.0 816
LLPS-Tar-2335Takifugu rubripes81.50.0 917
LLPS-Orn-3990Oreochromis niloticus81.310.0 917
LLPS-Pof-2508Poecilia formosa81.130.0 919
LLPS-Scm-3820Scophthalmus maximus81.090.0 919
LLPS-Leo-0211Lepisosteus oculatus81.060.0 911
LLPS-Orl-1941Oryzias latipes80.940.0 912
LLPS-Xim-2950Xiphophorus maculatus80.760.0 916
LLPS-Ten-0896Tetraodon nigroviridis80.760.0 904
LLPS-Tut-1237Tursiops truncatus80.580.0 815
LLPS-Icp-3800Ictalurus punctatus80.550.0 907
LLPS-Asm-0921Astyanax mexicanus80.540.0 907
LLPS-Gaa-0948Gasterosteus aculeatus80.220.0 898
LLPS-Scf-0121Scleropages formosus78.310.0 872
LLPS-Anp-2845Anas platyrhynchos75.360.0 764
LLPS-Cii-1366Ciona intestinalis69.720.0 677
LLPS-Ere-0346Erinaceus europaeus67.132e-157 461