SRC/Proto-oncogene c-Src  Protein, Antibody, ELISA Kit, cDNA Clone

발현 숙주: Baculovirus-Insect Cells  
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10755-H20B-50
10755-H20B-20
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발현 숙주: Baculovirus-Insect Cells  
  • Slide 1
50311-M20B-50
50311-M20B-20
50 µg 
20 µg 
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SRC/Proto-oncogene c-Src Related Area

SRC/Proto-oncogene c-Src 관련 경로

SRC/Proto-oncogene c-Src 요약 및 단백질 정보

SRC/Proto-oncogene c-Src 배경

유전자 요약: This c-SRC gene is highly similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this c-SRC gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase. Mutations in this c-SRC gene could be involved in the malignant progression of colon cancer. Two transcript variants encoding the same protein have been found for this c-SRC gene. [provided by RefSeq, Jul 2008]
General information above from NCBI
촉매 활성: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-ProRule:PRU10028}.
효소 조절: ENZYME REGULATION: Phosphorylation by CSK at Tyr-530 inhibits kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced by heme. Further phosphorylation by CDK1 partially reactivates CSK-inactivated SRC and facilitates complete reactivation by protein tyrosine phosphatase PTPRC. Integrin engagement stimulates kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and pseudosubstrate-based peptide inhibitors like CIYKYYF act as inhibitors. Phosphorylation at Tyr-419 increases kinase activity. {ECO:0000269|PubMed:14632929, ECO:0000269|PubMed:21036157, ECO:0000269|PubMed:7929427, ECO:0000269|PubMed:8759729, ECO:0000269|PubMed:9571170}.
하부단위 구조: Interacts with DDEF1/ASAP1; via the SH3 domain. Interacts with CCPG1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ERBB2, STAT1 and PNN. Interacts with DDR1, DDR2 and DAB2. Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2. Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin. Interacts with RALGPS1; via the SH3 domain. Interacts with HEV ORF3 protein; via the SH3 domain. Interacts with CAV2 (tyrosine phosphorylated form). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with ARRB1 and ARRB2. Interacts with SRCIN1. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and ESR1 (dimethylated on arginine). Interacts with FASLG. Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with PDGFRA (tyrosine phosphorylated). Interacts with CSF1R. Interacts (via SH2 and SH3 domain) with TNK2. Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain). Interacts with TRAF3 (via RING-type zinc finger domain). Interacts with DDX58, MAVS and TBK1. Interacts (via SH2 domain) with GNB2L1/RACK1; the interaction is enhanced by tyrosine phosphorylation of GNB2L1 and inhibits SRC activity. Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration. Interacts with FCAMR. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Interacts with TRAP1. Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at Tyr-419. {ECO:0000269|PubMed:10747847, ECO:0000269|PubMed:10753943, ECO:0000269|PubMed:11152665, ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:11518702, ECO:0000269|PubMed:12091389, ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:15504032, ECO:0000269|PubMed:15851033, ECO:0000269|PubMed:16479011, ECO:0000269|PubMed:17202804, ECO:0000269|PubMed:17293535, ECO:0000269|PubMed:17525734, ECO:0000269|PubMed:18024423, ECO:0000269|PubMed:18657504, ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:21309750, ECO:0000269|PubMed:21411625, ECO:0000269|PubMed:22888118, ECO:0000269|PubMed:23564345, ECO:0000269|PubMed:8759729, ECO:0000269|PubMed:9584165, ECO:0000269|PubMed:9924018}.
도메인: The SH2 and SH3 domains are important for the intramolecular and intermolecular interactions that regulate catalytic activity, localization, and substrate recruitment.
세포하 위치: Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasm, cytoskeleton. Note=Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain.
조직 특이성: Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues.
번역 후: Myristoylated at Gly-2, and this is essential for targeting to membranes. {ECO:0000269|PubMed:7525268}.; Dephosphorylated at Tyr-530 by PTPRJ (By similarity). Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity. {ECO:0000250, ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:21442427, ECO:0000269|PubMed:22888118, ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:7525268}.; S-nitrosylation is important for activation of its kinase activity. {ECO:0000250}.; Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation. {ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:22888118, ECO:0000269|PubMed:6273838}.
질병과의 관련성: DISEASE: Note=SRC kinase activity has been shown to be increased in several tumor tissues and tumor cell lines such as colon carcinoma cells.
염기서열 유사성: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 protein kinase domain. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 SH2 domain. {ECO:0000255|PROSITE-ProRule:PRU00191}.; Contains 1 SH3 domain. {ECO:0000255|PROSITE-ProRule:PRU00192}.
General information above from UniProt

Proto-oncogene tyrosine-protein kinase SRC is a hydrophobic protein belonging to the SRC family kinase including nine members that is a family of non-receptor tyrosine kinases. SRC protein may exist in different forms: C-SRC and V-SRC. C-SRC is only activated under certain circumstances where it is required such as growth factor signaling, while V-SRC is a constitutively active as opposed to normal SRC (C-SRC). Thus, V-SRC is an instructive example of an oncogene protein kinase whereas C-SRC is a proto-oncogene protein kinase. Inhibition of SRC with NR2A tyrosine phosphorylation mediated by PSD-95 may contribute to the lithium-induced downregulation of NMDA receptor function and provide neuroprotection against excitotoxicity.

SRC/Proto-oncogene c-Src 대체 이름

ASV,SRC1,c-SRC,p60-Src, [homo-sapiens]
ASV,c-SRC,p60-Src,RP5-823N20.1,SRC,SRC1, [human]
AW259666,pp60c-src,RP23-169M4.1,Src, [mouse]
AW259666,pp60c-src, [mus-musculus]

SRC/Proto-oncogene c-Src 관련 연구

  • Juan Ma. et al., 2003, Neuroscience Letters. 348 (3): 185-189.
  • Czernilofsky AP. et al., 1980, Nature. 287: 198-203.
  • Beischlag TV. et al., 2002, Molecular and cellular biology. 22 (12): 4319-33.
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