Phospho-Hck/Lyn (Tyr410/Tyr397) Antibody - #AF3735
製品: | Phospho-Hck/Lyn (Tyr410/Tyr397) Antibody |
カタログ: | AF3735 |
タンパク質の説明: | Rabbit polyclonal antibody to Phospho-Hck/Lyn (Tyr410/Tyr397) |
アプリケーション: | IHC |
反応性: | Human, Mouse, Rat |
分子量: | 60kD,59kD(Calculated). |
ユニプロット: | P08631 | P07948 |
RRID: | AB_2847049 |
製品説明
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
引用形式: Affinity Biosciences Cat# AF3735, RRID:AB_2847049.
折りたたみ/展開
AA407514; EC 2.7.10.2; FLJ26625; Hck 2; JTK 8; JTK8; Lck/Yes related novel protein tyrosine kinase; LYN; LYN proto oncogene, Src family tyrosine kinase; LYN_HUMAN; ONCOGENE LYN; p53Lyn; p56Lyn; Tyrosine protein kinase LYN; Tyrosine-protein kinase Lyn; V yes 1 Yamaguchi sarcoma viral related oncogene homolog; Yamaguchi sarcoma viral (v yes 1) related oncogene homolog; Bmk; Hck 1; Hck; HCK_HUMAN; Hemopoietic cell kinase; JTK9; p59-HCK/p60-HCK; p59Hck; p59HCK/p60HCK; p61Hck; Tyrosine protein kinase HCK; Tyrosine-protein kinase HCK;
免疫原
A synthesized peptide derived from human Hck/Lyn around the phosphorylation site of Tyr410/397.
Detected in monocytes and neutrophils (at protein level). Expressed predominantly in cells of the myeloid and B-lymphoid lineages. Highly expressed in granulocytes. Detected in tonsil.
P07948 LYN_HUMAN:Detected in monocytes (at protein level). Detected in placenta, and in fetal brain, lung, liver and kidney. Widely expressed in a variety of organs, tissues, and cell types such as epidermoid, hematopoietic, and neuronal cells. Expressed in primary neuroblastoma tumors.
- P08631 HCK_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIKPGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP
- P07948 LYN_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP
PTMs - P08631/P07948 基板として
Site | PTM Type | Enzyme | Source |
---|---|---|---|
G2 | Myristoylation | Uniprot | |
K9 | Ubiquitination | Uniprot | |
S11 | Phosphorylation | Uniprot | |
S13 | Phosphorylation | Uniprot | |
K20 | Ubiquitination | Uniprot | |
T30 | Phosphorylation | Uniprot | |
Y32 | Phosphorylation | P00533 (EGFR) | Uniprot |
K40 | Ubiquitination | Uniprot | |
T58 | Phosphorylation | Uniprot | |
K59 | Ubiquitination | Uniprot | |
K85 | Ubiquitination | Uniprot | |
K101 | Ubiquitination | Uniprot | |
K109 | Ubiquitination | Uniprot | |
S115 | Phosphorylation | Uniprot | |
Y117 | Phosphorylation | Uniprot | |
K132 | Ubiquitination | Uniprot | |
T135 | Phosphorylation | Uniprot | |
S149 | Phosphorylation | Uniprot | |
S158 | Phosphorylation | Uniprot | |
S164 | Phosphorylation | Uniprot | |
S166 | Phosphorylation | Uniprot | |
K181 | Ubiquitination | Uniprot | |
S187 | Phosphorylation | Uniprot | |
Y193 | Phosphorylation | Uniprot | |
Y194 | Phosphorylation | Uniprot | |
K213 | Ubiquitination | Uniprot | |
K224 | Ubiquitination | Uniprot | |
S228 | Phosphorylation | Uniprot | |
S246 | Phosphorylation | Uniprot | |
Y265 | Phosphorylation | Uniprot | |
Y266 | Phosphorylation | Uniprot | |
S269 | Phosphorylation | Uniprot | |
T276 | Phosphorylation | Uniprot | |
T281 | Phosphorylation | Uniprot | |
S283 | Phosphorylation | Uniprot | |
T296 | Phosphorylation | Uniprot | |
Y306 | Phosphorylation | Uniprot | |
Y316 | Phosphorylation | Uniprot | |
T319 | Phosphorylation | Uniprot | |
Y321 | Phosphorylation | Uniprot | |
S326 | Phosphorylation | Uniprot | |
K332 | Ubiquitination | Uniprot | |
K338 | Ubiquitination | Uniprot | |
Y397 | Phosphorylation | P07948 (LYN) | Uniprot |
T398 | Phosphorylation | Uniprot | |
K404 | Ubiquitination | Uniprot | |
T438 | Phosphorylation | Uniprot | |
Y439 | Phosphorylation | Uniprot | |
T448 | Phosphorylation | Uniprot | |
Y460 | Phosphorylation | Uniprot | |
Y473 | Phosphorylation | Uniprot | |
K477 | Ubiquitination | Uniprot | |
Y501 | Phosphorylation | Uniprot | |
T502 | Phosphorylation | Uniprot | |
T504 | Phosphorylation | Uniprot | |
Y508 | Phosphorylation | P07948 (LYN) , P41240 (CSK) , P42679 (MATK) | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
G2 | Myristoylation | Uniprot | |
K28 | Ubiquitination | Uniprot | |
T36 | Phosphorylation | Uniprot | |
Y51 | Phosphorylation | P08631 (HCK) | Uniprot |
Y89 | Phosphorylation | Uniprot | |
S111 | Phosphorylation | Uniprot | |
S119 | Phosphorylation | Uniprot | |
K124 | Ubiquitination | Uniprot | |
Y127 | Phosphorylation | Uniprot | |
Y180 | Phosphorylation | Uniprot | |
S181 | Phosphorylation | Uniprot | |
T202 | Phosphorylation | Uniprot | |
Y209 | Phosphorylation | P08631 (HCK) | Uniprot |
K228 | Acetylation | Uniprot | |
S238 | Phosphorylation | Uniprot | |
S261 | Phosphorylation | Uniprot | |
K283 | Ubiquitination | Uniprot | |
K286 | Ubiquitination | Uniprot | |
T311 | Phosphorylation | Uniprot | |
Y330 | Phosphorylation | Uniprot | |
S340 | Phosphorylation | Uniprot | |
Y411 | Phosphorylation | P08631 (HCK) | Uniprot |
T412 | Phosphorylation | Uniprot | |
K418 | Ubiquitination | Uniprot | |
S442 | Phosphorylation | Uniprot | |
S462 | Phosphorylation | Uniprot | |
S520 | Phosphorylation | Uniprot | |
Y522 | Phosphorylation | P08631 (HCK) , P42679 (MATK) | Uniprot |
PTMs - P08631/P07948 酵素として
Substrate | Site | Source |
---|---|---|
O14920 (IKBKB) | Y188 | Uniprot |
O14920 (IKBKB) | Y199 | Uniprot |
O15492 (RGS16) | Y168 | Uniprot |
O15492 (RGS16) | Y177 | Uniprot |
O43823 (AKAP8) | Y51 | Uniprot |
O43823 (AKAP8) | Y53 | Uniprot |
O43823 (AKAP8) | Y80 | Uniprot |
O43823 (AKAP8) | Y146 | Uniprot |
O43823 (AKAP8) | Y150 | Uniprot |
O43823 (AKAP8) | Y152 | Uniprot |
O43823 (AKAP8) | Y154 | Uniprot |
O43823 (AKAP8) | Y170 | Uniprot |
O43823 (AKAP8) | Y311 | Uniprot |
O43823 (AKAP8) | Y436 | Uniprot |
O43823 (AKAP8) | Y539 | Uniprot |
O60496 (DOK2) | Y271 | Uniprot |
O60496 (DOK2) | Y299 | Uniprot |
O60496 (DOK2) | Y345 | Uniprot |
O60711 (LPXN) | Y72 | Uniprot |
P00519 (ABL1) | Y70 | Uniprot |
P00519 (ABL1) | Y115 | Uniprot |
P00519 (ABL1) | Y128 | Uniprot |
P00519 (ABL1) | Y139 | Uniprot |
P00519 (ABL1) | Y172 | Uniprot |
P00519 (ABL1) | Y185 | Uniprot |
P00519 (ABL1) | Y215 | Uniprot |
P00519 (ABL1) | Y226 | Uniprot |
P00519 (ABL1) | Y393 | Uniprot |
P02730 (SLC4A1) | Y8 | Uniprot |
P02730 (SLC4A1) | Y21 | Uniprot |
P02730 (SLC4A1) | Y359 | Uniprot |
P02730 (SLC4A1) | Y904 | Uniprot |
P06493-2 (CDK1) | Y15 | Uniprot |
P07948 (LYN) | Y397 | Uniprot |
P07948 (LYN) | Y508 | Uniprot |
P11137 (MAP2) | Y67 | Uniprot |
P11274 (BCR) | Y177 | Uniprot |
P11802 (CDK4) | Y17 | Uniprot |
P11912-2 (CD79A) | Y150 | Uniprot |
P11912 (CD79A) | Y188 | Uniprot |
P12318-2 (FCGR2A) | Y280 | Uniprot |
P12318 (FCGR2A) | Y281 | Uniprot |
P12318-2 (FCGR2A) | Y287 | Uniprot |
P12318 (FCGR2A) | Y288 | Uniprot |
P12318-2 (FCGR2A) | Y303 | Uniprot |
P12318 (FCGR2A) | Y304 | Uniprot |
P13569 (CFTR) | Y512 | Uniprot |
P13569 (CFTR) | Y515 | Uniprot |
P13569 (CFTR) | Y517 | Uniprot |
P14317-1 (HCLS1) | Y222 | Uniprot |
P14317 (HCLS1) | Y378 | Uniprot |
P14317 (HCLS1) | Y397 | Uniprot |
P15391-1 (CD19) | Y409 | Uniprot |
P15391 (CD19) | Y500 | Uniprot |
P15391 (CD19) | Y531 | Uniprot |
P15941 (MUC1) | Y1229 | Uniprot |
P16885 (PLCG2) | Y743 | Uniprot |
P16885 (PLCG2) | Y753 | Uniprot |
P16885 (PLCG2) | Y759 | Uniprot |
P19174-1 (PLCG1) | Y771 | Uniprot |
P19174-2 (PLCG1) | Y783 | Uniprot |
P19235 (EPOR) | Y368 | Uniprot |
P21854 (CD72) | Y7 | Uniprot |
P21854 (CD72) | Y39 | Uniprot |
P22681 (CBL) | Y371 | Uniprot |
P24941 (CDK2) | Y15 | Uniprot |
P25490 (YY1) | Y8 | Uniprot |
P25490 (YY1) | Y254 | Uniprot |
P25490 (YY1) | Y383 | Uniprot |
P29350 (PTPN6) | Y536 | Uniprot |
P29350 (PTPN6) | Y564 | Uniprot |
P30419 (NMT1) | Y117 | Uniprot |
P30419 (NMT1) | Y180 | Uniprot |
P31994-5 (FCGR2B) | Y272 | Uniprot |
P31994-2 (FCGR2B) | Y273 | Uniprot |
P31994-4 (FCGR2B) | Y291 | Uniprot |
P31994-1 (FCGR2B) | Y292 | Uniprot |
P31995 (FCGR2C) | Y310 | Uniprot |
P32927 (CSF2RB) | Y466 | Uniprot |
P32927 (CSF2RB) | Y468 | Uniprot |
P32927 (CSF2RB) | Y822 | Uniprot |
P32927 (CSF2RB) | Y882 | Uniprot |
P33993 (MCM7) | Y600 | Uniprot |
P35354 (PTGS2) | Y120 | Uniprot |
P37840-1 (SNCA) | Y125 | Uniprot |
P40259-2 (CD79B) | Y92 | Uniprot |
P40259-2 (CD79B) | Y103 | Uniprot |
P40259 (CD79B) | Y196 | Uniprot |
P40259 (CD79B) | Y207 | Uniprot |
P42229 (STAT5A) | Y694 | Uniprot |
P42680 (TEC) | Y519 | Uniprot |
P42768 (WAS) | Y291 | Uniprot |
P43405-1 (SYK) | Y131 | Uniprot |
P43405 (SYK) | Y323 | Uniprot |
P43405 (SYK) | Y348 | Uniprot |
P43405 (SYK) | Y352 | Uniprot |
P46527 (CDKN1B) | Y88 | Uniprot |
P60484 (PTEN) | Y240 | Uniprot |
P68400 (CSNK2A1) | Y255 | Uniprot |
Q05655-1 (PRKCD) | Y52 | Uniprot |
Q05655-1 (PRKCD) | Y64 | Uniprot |
Q05655-1 (PRKCD) | Y155 | Uniprot |
Q05655-1 (PRKCD) | Y187 | Uniprot |
Q05655 (PRKCD) | Y313 | Uniprot |
Q05655 (PRKCD) | Y334 | Uniprot |
Q05655-1 (PRKCD) | Y567 | Uniprot |
Q06187 (BTK) | Y223 | Uniprot |
Q06187 (BTK) | Y551 | Uniprot |
Q12972-3 (PPP1R8) | Y40 | Uniprot |
Q12972-3 (PPP1R8) | Y111 | Uniprot |
Q12972-2 (PPP1R8) | Y122 | Uniprot |
Q12972-2 (PPP1R8) | Y193 | Uniprot |
Q12972 (PPP1R8) | Y264 | Uniprot |
Q12972 (PPP1R8) | Y335 | Uniprot |
Q13263 (TRIM28) | Y449 | Uniprot |
Q13263 (TRIM28) | Y458 | Uniprot |
Q13263 (TRIM28) | Y517 | Uniprot |
Q13291 (SLAMF1) | Y327 | Uniprot |
Q14790 (CASP8) | Y380 | Uniprot |
Q14790 (CASP8) | Y448 | Uniprot |
Q8N6F7 (GCSAM) | Y107 | Uniprot |
Q8N6F7 (GCSAM) | Y128 | Uniprot |
Q92918-1 (MAP4K1) | Y381 | Uniprot |
Q9GZY6 (LAT2) | Y95 | Uniprot |
Q9GZY6 (LAT2) | Y110 | Uniprot |
Q9GZY6 (LAT2) | Y118 | Uniprot |
Q9GZY6 (LAT2) | Y119 | Uniprot |
Q9GZY6 (LAT2) | Y136 | Uniprot |
Q9H792 (PEAK1) | Y635 | Uniprot |
Q9HBA0 (TRPV4) | Y253 | Uniprot |
Q9NWQ8 (PAG1) | Y105 | Uniprot |
Q9UN19 (DAPP1) | Y139 | Uniprot |
Q9Y6Y9 (LY96) | Y22 | Uniprot |
Q9Y6Y9 (LY96) | Y131 | Uniprot |
Substrate | Site | Source |
---|---|---|
O15350 (TP73) | Y28 | Uniprot |
O60496 (DOK2) | Y271 | Uniprot |
O60496 (DOK2) | Y299 | Uniprot |
O60496 (DOK2) | Y345 | Uniprot |
P00519 (ABL1) | Y70 | Uniprot |
P00519 (ABL1) | Y115 | Uniprot |
P00519 (ABL1) | Y128 | Uniprot |
P00519 (ABL1) | Y139 | Uniprot |
P00519 (ABL1) | Y172 | Uniprot |
P00519 (ABL1) | Y185 | Uniprot |
P00519 (ABL1) | Y215 | Uniprot |
P00519 (ABL1) | Y226 | Uniprot |
P00519 (ABL1) | Y393 | Uniprot |
P08631 (HCK) | Y51 | Uniprot |
P08631 (HCK) | Y209 | Uniprot |
P08631 (HCK) | Y411 | Uniprot |
P08631 (HCK) | Y522 | Uniprot |
P11274-1 (BCR) | Y177 | Uniprot |
P16885 (PLCG2) | Y753 | Uniprot |
P16885 (PLCG2) | Y759 | Uniprot |
P19174-1 (PLCG1) | Y771 | Uniprot |
P19174-1 (PLCG1) | Y783 | Uniprot |
P19174-1 (PLCG1) | Y1253 | Uniprot |
P22681 (CBL) | Y731 | Uniprot |
P40763-2 (STAT3) | Y704 | Uniprot |
P40763-1 (STAT3) | Y705 | Uniprot |
P42229 (STAT5A) | Y694 | Uniprot |
P42768 (WAS) | Y291 | Uniprot |
P51692 (STAT5B) | Y699 | Uniprot |
Q05655 (PRKCD) | Y313 | Uniprot |
Q13444 (ADAM15) | Y715 | Uniprot |
Q13444 (ADAM15) | Y735 | Uniprot |
Q13905 (RAPGEF1) | Y504 | Uniprot |
Q13905-3 (RAPGEF1) | Y522 | Uniprot |
Q92556-1 (ELMO1) | Y18 | Uniprot |
Q92556-2 (ELMO1) | Y31 | Uniprot |
Q92556-1 (ELMO1) | Y216 | Uniprot |
Q92556-2 (ELMO1) | Y240 | Uniprot |
Q92556-1 (ELMO1) | Y395 | Uniprot |
Q92556 (ELMO1) | Y511 | Uniprot |
Q92556 (ELMO1) | Y720 | Uniprot |
Q99062-1 (CSF3R) | Y752 | Uniprot |
Q99062-3 (CSF3R) | Y779 | Uniprot |
Q99062-1 (CSF3R) | Y787 | Uniprot |
Q99062-3 (CSF3R) | Y814 | Uniprot |
Q9UQC2 (GAB2) | Y452 | Uniprot |
研究背景
Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS.
Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation by the BCR-ABL fusion protein mediates activation of HCK. Phosphorylation at Tyr-411 increases kinase activity. Phosphorylation at Tyr-522 inhibits kinase activity. Kinase activity is not required for phosphorylation at Tyr-522, suggesting that this site is a target of other kinases.
Ubiquitinated by CBL, leading to its degradation via the proteasome.
Isoform 2 palmitoylation at position 2 requires prior myristoylation. Palmitoylation at position 3 is required for caveolar localization of isoform 2.
Lysosome. Membrane>Lipid-anchor. Cell projection>Podosome membrane>Lipid-anchor. Cytoplasm>Cytosol.
Note: Associated with specialized secretory lysosomes called azurophil granules. At least half of this isoform is found in the cytoplasm, some of this fraction is myristoylated.
Cell membrane>Lipid-anchor. Membrane>Caveola>Lipid-anchor. Cell junction>Focal adhesion. Cytoplasm>Cytoskeleton. Golgi apparatus. Cytoplasmic vesicle. Lysosome. Nucleus.
Note: 20% of this isoform is associated with caveolae. Localization at the cell membrane and at caveolae requires palmitoylation at Cys-3. Colocalizes with the actin cytoskeleton at focal adhesions.
Cytoplasmic vesicle>Secretory vesicle. Cytoplasm>Cytosol.
Detected in monocytes and neutrophils (at protein level). Expressed predominantly in cells of the myeloid and B-lymphoid lineages. Highly expressed in granulocytes. Detected in tonsil.
Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with VAV1, WAS and RAPGEF1 (By similarity). This interaction stimulates its tyrosine-kinase activity. Interacts with ARRB1 and ARRB2. Interacts with ADAM15. Interacts with FASLG. Interacts with CBL. Interacts with FCGR1A; the interaction may be indirect. Interacts with IL6ST. Interacts (via SH3 domain) with ELMO1. Interacts (via SH3 domain) with TP73. Interacts with YAP1. Interacts with ABL1 and ITGB1, and thereby recruits ABL1 to activated ITGB1. Interacts (via SH3 domain) with WDCP.
(Microbial infection) Interacts (via SH3 domain) with HEV ORF3 protein.
(Microbial infection) Interacts (via SH3 domain) with HIV-1 Nef and Vif.
The SH3 domain mediates binding to HIV-1 Nef.
Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.
Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-107'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages (By similarity). Phosphorylates CLNK (By similarity).
Ubiquitinated by CBL, leading to its degradation. Ubiquitination is SH3-dependent.
Autophosphorylated. Phosphorylated on tyrosine residues in response to KIT signaling. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A.
Cell membrane. Nucleus. Cytoplasm. Cytoplasm>Perinuclear region. Golgi apparatus. Membrane>Lipid-anchor.
Note: Accumulates in the nucleus by inhibition of CRM1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the plasma membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport. Detected on plasma membrane lipid rafts.
Detected in monocytes (at protein level). Detected in placenta, and in fetal brain, lung, liver and kidney. Widely expressed in a variety of organs, tissues, and cell types such as epidermoid, hematopoietic, and neuronal cells. Expressed in primary neuroblastoma tumors.
Interacts with TEC. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon activation of the B-cell antigen receptor. Interacts with the B-cell receptor complex. Interacts with phosphorylated THEMIS2. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3 domains) with MUC1 is stimulated by IL7 and the subsequent phosphorylation increases the binding between MUC1 and CTNNB1/beta-catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts (via SH3 domain) with CBLC, PPP1R15A and PDE4A. Interacts with TGFB1I1. Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1; identified in a complex with PAG1 and STAT3. Interacts with ABL1. Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via proline-rich region). This interaction facilitates the phosphorylation of SCIMP on 'Tyr-107', which enhances binding of SCIMP to TLR4, and consequently the phosphorylation of TLR4 in response to stimulation by lipopolysaccharide in macrophages (By similarity). Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via SH3-domain) with ANKRD54 (via ankyrin repeat region) in an activation-independent status of LYN. Forms a multiprotein complex with ANKRD54 and HCLS1. Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation. Interacts with CD36. Interacts with LYN (By similarity). Interacts with SKAP1 and FYB1; this interaction promotes the phosphorylation of CLNK (By similarity).
(Microbial infection) Interacts with Epstein-Barr virus LMP2A.
(Microbial infection) Interacts with Herpes virus saimiri tyrosine kinase interacting protein (Tip).
The protein kinase domain plays an important role in its localization in the cell membrane.
Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.
研究領域
· Environmental Information Processing > Signal transduction > NF-kappa B signaling pathway. (View pathway)
· Human Diseases > Infectious diseases: Bacterial > Epithelial cell signaling in Helicobacter pylori infection.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Human Diseases > Cancers: Overview > Viral carcinogenesis.
· Organismal Systems > Immune system > Chemokine signaling pathway. (View pathway)
· Organismal Systems > Immune system > Platelet activation. (View pathway)
· Organismal Systems > Immune system > B cell receptor signaling pathway. (View pathway)
· Organismal Systems > Immune system > Fc epsilon RI signaling pathway. (View pathway)
· Organismal Systems > Immune system > Fc gamma R-mediated phagocytosis. (View pathway)
· Organismal Systems > Nervous system > Long-term depression.
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