Product: Phospho-Hck/Lyn (Tyr410/Tyr397) Antibody
Catalog: AF3735
Description: Rabbit polyclonal antibody to Phospho-Hck/Lyn (Tyr410/Tyr397)
Application: IHC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 60kD,59kD(Calculated).
Uniprot: P08631 | P07948
RRID: AB_2847049

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Product Info

Source:
Rabbit
Application:
IHC 1:50-1:200
*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.

Reactivity:
Human,Mouse,Rat
Clonality:
Polyclonal
Specificity:
Phospho-Hck/Lyn (Tyr410/Tyr397) Antibody detects endogenous levels of Hck/Lyn only when phosphorylated at Tyr410/397.
RRID:
AB_2847049
Cite Format: Affinity Biosciences Cat# AF3735, RRID:AB_2847049.
Conjugate:
Unconjugated.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

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;

Immunogens

Immunogen:

A synthesized peptide derived from human Hck/Lyn around the phosphorylation site of Tyr410/397.

Uniprot:
Gene(ID):
Expression:
P08631 HCK_HUMAN:

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.

Sequence:
MGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIKPGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP

MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP

PTMs - P08631/P07948 As Substrate

Site PTM Type Enzyme
G2 Myristoylation
K9 Ubiquitination
S11 Phosphorylation
S13 Phosphorylation
K20 Ubiquitination
T30 Phosphorylation
Y32 Phosphorylation P00533 (EGFR)
K40 Ubiquitination
T58 Phosphorylation
K59 Ubiquitination
K85 Ubiquitination
K101 Ubiquitination
K109 Ubiquitination
S115 Phosphorylation
Y117 Phosphorylation
K132 Ubiquitination
T135 Phosphorylation
S149 Phosphorylation
S158 Phosphorylation
S164 Phosphorylation
S166 Phosphorylation
K181 Ubiquitination
S187 Phosphorylation
Y193 Phosphorylation
Y194 Phosphorylation
K213 Ubiquitination
K224 Ubiquitination
S228 Phosphorylation
S246 Phosphorylation
Y265 Phosphorylation
Y266 Phosphorylation
S269 Phosphorylation
T276 Phosphorylation
T281 Phosphorylation
S283 Phosphorylation
T296 Phosphorylation
Y306 Phosphorylation
Y316 Phosphorylation
T319 Phosphorylation
Y321 Phosphorylation
S326 Phosphorylation
K332 Ubiquitination
K338 Ubiquitination
Y397 Phosphorylation P07948 (LYN)
T398 Phosphorylation
K404 Ubiquitination
T438 Phosphorylation
Y439 Phosphorylation
T448 Phosphorylation
Y460 Phosphorylation
Y473 Phosphorylation
K477 Ubiquitination
Y501 Phosphorylation
T502 Phosphorylation
T504 Phosphorylation
Y508 Phosphorylation P07948 (LYN) , P41240 (CSK) , P42679 (MATK)
Site PTM Type Enzyme
G2 Myristoylation
K28 Ubiquitination
T36 Phosphorylation
Y51 Phosphorylation P08631 (HCK)
Y89 Phosphorylation
S111 Phosphorylation
S119 Phosphorylation
K124 Ubiquitination
Y127 Phosphorylation
Y180 Phosphorylation
S181 Phosphorylation
T202 Phosphorylation
Y209 Phosphorylation P08631 (HCK)
K228 Acetylation
S238 Phosphorylation
S261 Phosphorylation
K283 Ubiquitination
K286 Ubiquitination
T311 Phosphorylation
Y330 Phosphorylation
S340 Phosphorylation
Y411 Phosphorylation P08631 (HCK)
T412 Phosphorylation
K418 Ubiquitination
S442 Phosphorylation
S462 Phosphorylation
S520 Phosphorylation
Y522 Phosphorylation P08631 (HCK) , P42679 (MATK)

PTMs - P08631/P07948 As Enzyme

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

Research Backgrounds

Function:

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.

PTMs:

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.

Subcellular Location:

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.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

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.

Subunit Structure:

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.

Family&Domains:

The SH3 domain mediates binding to HIV-1 Nef.

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Function:

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).

PTMs:

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.

Subcellular Location:

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.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

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.

Subunit Structure:

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).

Family&Domains:

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.

Research Fields

· 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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