| + |
PRKCD |
phosphorylation
|
ITGB2 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249120 |
Ser745 |
FEKEKLKsQWNNDNP |
Homo sapiens |
Leukocyte |
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249124 |
Thr758 |
NPLFKSAtTTVMNPK |
Homo sapiens |
Leukocyte |
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCB |
phosphorylation
|
ITGB2 |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249119 |
Ser745 |
FEKEKLKsQWNNDNP |
Homo sapiens |
|
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249122 |
Thr758 |
NPLFKSAtTTVMNPK |
Homo sapiens |
|
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCH |
phosphorylation
|
ITGB2 |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249118 |
Ser745 |
FEKEKLKsQWNNDNP |
Homo sapiens |
Leukocyte |
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249123 |
Thr758 |
NPLFKSAtTTVMNPK |
Homo sapiens |
Leukocyte |
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCD | up-regulates 
phosphorylation
|
ITGB2 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178897 |
Thr758 |
NPLFKSAtTTVMNPK |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 18550856 |
In this study, we present evidence that pkc isoforms are the major protein kinases that phosphorylate the c terminus of the integrin cd18 chain in leukocytes. Ser-745 is identified as a novel phosphorylation site in the integrin cytoplasmic domain. Additionally, we show that a thr-758-phosphorylated integrin peptide can interact with 14-3-3 proteins in leukocyte lysates |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA |
phosphorylation
|
ITGB2 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249121 |
Thr758 |
NPLFKSAtTTVMNPK |
Homo sapiens |
Leukocyte |
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249125 |
Thr760 |
LFKSATTtVMNPKFA |
Homo sapiens |
Leukocyte |
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCD | up-regulates activity
phosphorylation
|
ITGB2 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111495 |
Thr758 |
NPLFKSAtTTVMNPK |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 11700305 |
We identify catalytic domain fragments of protein kinase c (pkc) delta and pkcbetai/ii as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin cd18 chain. The sites phosphorylated in vitro were identified as ser-745 and thr-758. Pkc-mediated phosphorylation of cd18 after cell stimulation could lead to the recruitment of 14-3-3 proteins to the activated integrin, which may play a role in regulating its adhesive state or ability to signal. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITGB2 | form complex 
binding
|
AM/b2 integrin |
0.743 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253192 |
|
|
|
|
| pmid |
sentence |
| 16988024 |
Integrins are one of the major families of cell adhesion receptors (Humphries, 2000; Hynes, 2002). All integrins are non-covalently-linked, heterodimeric molecules containing an α and a β subunit. Both subunits are type I transmembrane proteins, containing large extracellular domains and mostly short cytoplasmic domains (Springer and Wang, 2004; Arnaout et al., 2005). Mammalian genomes contain 18 α subunit and 8 β subunit genes, and to date 24 different α,β combinations have been identified at the protein level. Although some subunits only appear in a single heterodimer, twelve integrins contain the β1 subunit, and five contain αV. |
|
| Publications: |
1 |
| + |
DOK1 | down-regulates activity 
binding
|
ITGB2 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257680 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19118207 |
Integrins also bind to many PTBdomain-containing proteins (Calderwood et al., 2003) – including Dok1 and integrincytoplasmic-domain-associated protein 1 (ICAP1) – and these can compete with talin for binding to integrin and so can impair activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITGB2 | form complex
binding
|
AD/b2 integrin |
0.73 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253196 |
|
|
|
|
| pmid |
sentence |
| 16988024 |
Integrins are one of the major families of cell adhesion receptors (Humphries, 2000; Hynes, 2002). All integrins are non-covalently-linked, heterodimeric molecules containing an α and a β subunit. Both subunits are type I transmembrane proteins, containing large extracellular domains and mostly short cytoplasmic domains (Springer and Wang, 2004; Arnaout et al., 2005). Mammalian genomes contain 18 α subunit and 8 β subunit genes, and to date 24 different α,β combinations have been identified at the protein level. Although some subunits only appear in a single heterodimer, twelve integrins contain the β1 subunit, and five contain αV. |
|
| Publications: |
1 |
| + |
Kindlin | up-regulates activity
binding
|
ITGB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259023 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29544897 |
Kindlins bind with β-integrin cytoplasmic tails and execute broad biological functions including directed cell migration, proliferation, differentiation and survival. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | down-regulates activity
phosphorylation
|
ITGB2 |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254740 |
|
|
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 25624455 |
PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
ITGB2 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254738 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25624455 |
PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TLN1 | up-regulates activity
binding
|
ITGB2 |
0.707 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257618 |
|
|
Mus musculus |
Blood Platelet |
| pmid |
sentence |
| 19118207 |
Over the past 10 years, the binding of talin to the cytoplasmic tail of integrin-β subunits has been established to have a key role in integrin activation. Binding of the phosphotyrosinebinding (PTB)-domain-like subdomain of the protein 4.1, ezrin, radixin, moesin (FERM) domain of talin to the conserved WxxxNP(I/L)Y motif of the β-integrin tail permits additional weaker interactions between talin and the membrane-proximal region of the tail that trigger integrin activation, probably through the disruption of inhibitory interactions between α- and β-subunit cytoplasmic tails. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ITGB1BP1 | down-regulates activity
binding
|
ITGB2 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257649 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19118207 |
Integrins also bind to many PTBdomain-containing proteins (Calderwood et al., 2003) – including Dok1 and integrincytoplasmic-domain-associated protein 1 (ICAP1) – and these can compete with talin for binding to integrin and so can impair activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITGB2 | form complex
binding
|
AX/b2 integrin |
0.823 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253194 |
|
|
|
|
| pmid |
sentence |
| 16988024 |
Integrins are one of the major families of cell adhesion receptors (Humphries, 2000; Hynes, 2002). All integrins are non-covalently-linked, heterodimeric molecules containing an α and a β subunit. Both subunits are type I transmembrane proteins, containing large extracellular domains and mostly short cytoplasmic domains (Springer and Wang, 2004; Arnaout et al., 2005). Mammalian genomes contain 18 α subunit and 8 β subunit genes, and to date 24 different α,β combinations have been identified at the protein level. Although some subunits only appear in a single heterodimer, twelve integrins contain the β1 subunit, and five contain αV. |
|
| Publications: |
1 |
| + |
ITGB2 | up-regulates activity 
|
PTK2 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257711 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITGB2 | form complex
binding
|
Av/b2 integrin |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253204 |
|
|
|
|
| pmid |
sentence |
| 16988024 |
Integrins are one of the major families of cell adhesion receptors (Humphries, 2000; Hynes, 2002). All integrins are non-covalently-linked, heterodimeric molecules containing an α and a β subunit. Both subunits are type I transmembrane proteins, containing large extracellular domains and mostly short cytoplasmic domains (Springer and Wang, 2004; Arnaout et al., 2005). Mammalian genomes contain 18 α subunit and 8 β subunit genes, and to date 24 different α,β combinations have been identified at the protein level. Although some subunits only appear in a single heterodimer, twelve integrins contain the β1 subunit, and five contain αV. |
|
| Publications: |
1 |
| + |
ITGB2 | form complex
binding
|
AL/b2 integrin |
0.912 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253190 |
|
|
|
|
| pmid |
sentence |
| 16988024 |
Integrins are one of the major families of cell adhesion receptors (Humphries, 2000; Hynes, 2002). All integrins are non-covalently-linked, heterodimeric molecules containing an α and a β subunit. Both subunits are type I transmembrane proteins, containing large extracellular domains and mostly short cytoplasmic domains (Springer and Wang, 2004; Arnaout et al., 2005). Mammalian genomes contain 18 α subunit and 8 β subunit genes, and to date 24 different α,β combinations have been identified at the protein level. Although some subunits only appear in a single heterodimer, twelve integrins contain the β1 subunit, and five contain αV. |
|
| Publications: |
1 |
| + |
PTPRG | down-regulates activity 
|
ITGB2 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254735 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation inhibits chemoattractant induced LFA-1 affinity triggering and mediated adhesion in human primary monocytes.we show that PTPRG is a novel negative regulator of LFA-1 high-affinity-state triggering and mediated arrest by chemoattractants in human primary monocytes. Notably, PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role (37). In our context, SRC appears inhibited by PTPRG activation (Table I), thus making it unlikely that the antiadhesive effect of PTPRG is mediated by SRC activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ITGB2
- 
- 