HCK (hematopoietic cell kinase) is a non-receptor, Src-family protein tyrosine kinase expressed mainly in myeloid and B-lymphoid hematopoietic cells. It is lipid-anchored (N-myristoylated and palmitoylated) to the cytoplasmic face of cellular membranes and exists as two translation-start isoforms, p59Hck (predominantly plasma membrane, caveolae, focal adhesions, cytosol) and p61Hck (lysosomes/azurophil granules). Held inactive by intramolecular SH3/SH2 interactions, it is activated downstream of Fc receptors, integrins and cytokine receptors, where it phosphorylates substrates such as CBL, VAV1 and WAS to drive phagocytosis, secretory-lysosome mobilization, degranulation, the NADPH-oxidase respiratory burst, and actin-cytoskeleton/podosome reorganization. Its SH2 domain binds phosphotyrosine and its SH3 domain engages partners including TP73.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001784 phosphotyrosine residue binding | IPI PMID:20624904 Tarp regulates early Chlamydia-induced host cell survival th... | ACCEPT | Summary: The HCK SH2 domain binds phosphotyrosine-containing ligands. Reason: HCK has a canonical SH2 domain; it is included among the human SH2/phosphotyrosine- binding domains profiled for phosphopeptide recognition. Supporting Evidence: PMID:20624904 a protein microarray comprising virtually all human SRC homology 2 (SH2) and phosphotyrosine binding domains |
| GO:0002522 leukocyte migration involved in immune response | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Leukocyte migration involved in immune response. Reason: HCK contributes to phagocyte migration during immune responses; a downstream process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt cell adhesion and migration |
| GO:0002758 innate immune response-activating signaling pathway | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Innate immune response-activating signaling pathway. Reason: HCK transduces activating signals in innate immunity; a downstream immune process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt regulation of innate immune responses |
| GO:0002758 innate immune response-activating signaling pathway | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Innate immune response-activating signaling pathway. Reason: HCK transduces activating signals in innate immunity; a downstream immune process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt regulation of innate immune responses |
| GO:0002862 negative regulation of inflammatory response to antigenic stimulus | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Negative regulation of inflammatory response to antigenic stimulus. Reason: HCK can dampen inflammatory output in some contexts; a specific non-core regulatory process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Plays a role in the release of inflammatory |
| GO:0002862 negative regulation of inflammatory response to antigenic stimulus | TAS Reactome:R-HSA-9664323 | KEEP AS NON CORE | Summary: Negative regulation of inflammatory response to antigenic stimulus. Reason: HCK can dampen inflammatory output in some contexts; a specific non-core regulatory process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Plays a role in the release of inflammatory |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: Protein kinase activity; HCK is specifically a tyrosine kinase. Reason: The InterPro kinase-domain mapping is correct but general; HCK is a protein tyrosine kinase, a term already asserted experimentally. Proposed replacements: protein tyrosine kinase activity Supporting Evidence: file:human/HCK/HCK-uniprot.txt Non-receptor tyrosine-protein kinase found in hematopoietic |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:10861086 Differential involvement of Src family kinases in Fc gamma r... | ACCEPT | Summary: HCK catalyses protein tyrosine phosphorylation. Reason: Multiple experimental studies show HCK tyrosine-kinase activity (e.g. phosphorylation of Cbl), and UniProt curates the EC 2.7.10.2 reaction. Supporting Evidence: PMID:10092522 Hematopoietic cell kinase (Hck) is a member of the Src-family of protein tyrosine kinases PMID:10092522 Hck phosphorylates Cbl in vitro |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:16921024 Differential kinase requirements in human and mouse Fc-gamma... | ACCEPT | Summary: HCK catalyses protein tyrosine phosphorylation. Reason: Multiple experimental studies show HCK tyrosine-kinase activity (e.g. phosphorylation of Cbl), and UniProt curates the EC 2.7.10.2 reaction. Supporting Evidence: PMID:10092522 Hematopoietic cell kinase (Hck) is a member of the Src-family of protein tyrosine kinases PMID:10092522 Hck phosphorylates Cbl in vitro |
| GO:0004713 protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: HCK catalyses protein tyrosine phosphorylation. Reason: Multiple experimental studies show HCK tyrosine-kinase activity (e.g. phosphorylation of Cbl), and UniProt curates the EC 2.7.10.2 reaction. Supporting Evidence: PMID:10092522 Hematopoietic cell kinase (Hck) is a member of the Src-family of protein tyrosine kinases PMID:10092522 Hck phosphorylates Cbl in vitro |
| GO:0004713 protein tyrosine kinase activity | IMP PMID:10092522 The proto-oncogene p120(Cbl) is a downstream substrate of th... | ACCEPT | Summary: HCK catalyses protein tyrosine phosphorylation. Reason: Multiple experimental studies show HCK tyrosine-kinase activity (e.g. phosphorylation of Cbl), and UniProt curates the EC 2.7.10.2 reaction. Supporting Evidence: PMID:10092522 Hematopoietic cell kinase (Hck) is a member of the Src-family of protein tyrosine kinases PMID:10092522 Hck phosphorylates Cbl in vitro |
| GO:0004713 protein tyrosine kinase activity | TAS PMID:3496523 Identification of a human gene (HCK) that encodes a protein-... | ACCEPT | Summary: HCK catalyses protein tyrosine phosphorylation. Reason: Multiple experimental studies show HCK tyrosine-kinase activity (e.g. phosphorylation of Cbl), and UniProt curates the EC 2.7.10.2 reaction. Supporting Evidence: PMID:10092522 Hematopoietic cell kinase (Hck) is a member of the Src-family of protein tyrosine kinases PMID:10092522 Hck phosphorylates Cbl in vitro |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-9664261 | ACCEPT | Summary: HCK catalyses protein tyrosine phosphorylation. Reason: Multiple experimental studies show HCK tyrosine-kinase activity (e.g. phosphorylation of Cbl), and UniProt curates the EC 2.7.10.2 reaction. Supporting Evidence: PMID:10092522 Hematopoietic cell kinase (Hck) is a member of the Src-family of protein tyrosine kinases PMID:10092522 Hck phosphorylates Cbl in vitro |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: HCK is a non-membrane-spanning (Src-family, cytoplasmic) tyrosine kinase. Reason: This is the most specific molecular-function term for a Src-family kinase and matches the phylogenetic placement (IBA) and EC 2.7.10.2. Supporting Evidence: PMID:10092522 Hematopoietic cell kinase (Hck) is a member of the Src-family of protein tyrosine kinases |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | IEA GO_REF:0000003 | ACCEPT | Summary: HCK is a non-membrane-spanning (Src-family, cytoplasmic) tyrosine kinase. Reason: This is the most specific molecular-function term for a Src-family kinase and matches the phylogenetic placement (IBA) and EC 2.7.10.2. Supporting Evidence: PMID:10092522 Hematopoietic cell kinase (Hck) is a member of the Src-family of protein tyrosine kinases |
| GO:0005102 signaling receptor binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: HCK binds signaling receptors (FLT3, IL6ST, FCGR1A) via its SH2/SH3 domains. Reason: Receptor binding mediates HCK recruitment downstream of immune receptors; it supports but is distinct from the core catalytic function. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Interacts (via SH2 domain) with FLT3 |
| GO:0005515 protein binding | IPI PMID:11278465 The tyrosine kinase Hck is an inhibitor of HIV-1 replication... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:11278465 The tyrosine kinase Hck is an inhibitor of HIV-1 replication... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:11741929 Phosphorylation-dependent interactions between ADAM15 cytopl... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:12029088 Identification of novel SH3 domain ligands for the Src famil... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:12029088 Identification of novel SH3 domain ligands for the Src famil... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:12029088 Identification of novel SH3 domain ligands for the Src famil... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:12029088 Identification of novel SH3 domain ligands for the Src famil... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:12029088 Identification of novel SH3 domain ligands for the Src famil... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:12029088 Identification of novel SH3 domain ligands for the Src famil... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:14993658 The hepatitis C virus NS5A protein binds to members of the S... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:14993658 The hepatitis C virus NS5A protein binds to members of the S... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:15784897 Further studies on hepatitis C virus NS5A-SH3 domain interac... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:15784897 Further studies on hepatitis C virus NS5A-SH3 domain interac... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:16374509 Identification of preferred protein interactions by phage-di... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:16374509 Identification of preferred protein interactions by phage-di... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:16374509 Identification of preferred protein interactions by phage-di... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:16636290 Targeting AMAP1 and cortactin binding bearing an atypical sr... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:17141806 Solution structure of a Hck SH3 domain ligand complex reveal... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:17141806 Solution structure of a Hck SH3 domain ligand complex reveal... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:18042718 Protein protein interaction inhibition (2P2I) combining high... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:19234535 Src kinase Hck association with the WASp and mDia1 cytoskele... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:20670214 Identification and biophysical assessment of the molecular r... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:22641034 Structural recognition mechanisms between human Src homology... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:22641034 Structural recognition mechanisms between human Src homology... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:22939624 Quantitative analysis of HSP90-client interactions reveals p... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:23397142 Analysis of protein-protein interactions in cross-talk pathw... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:23397142 Analysis of protein-protein interactions in cross-talk pathw... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:24860872 Analysis of 5-lipoxygenase phosphorylation on molecular leve... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:25036101 Identification of SH3 domain proteins interacting with the c... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:25469238 Molecular characterization of WDCP, a novel fusion partner f... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:25825872 Preferred SH3 domain partners of ADAM metalloproteases inclu... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:25825872 Preferred SH3 domain partners of ADAM metalloproteases inclu... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:32226298 Nucleotide binding domain and leucine-rich repeat pyrin doma... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005515 protein binding | IPI PMID:7859737 Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains ... | REMOVE | Summary: Generic protein binding from many pairwise interaction studies and screens. Reason: Bare protein binding is uninformative and removed under the protein-binding policy. HCK's informative binding activities are captured by phosphotyrosine residue binding and signaling receptor binding, and its substrates by its kinase activity; removal does not dispute the interactions. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: ATP binding supports the kinase reaction. Reason: ATP is the phosphate donor for the kinase activity; a required cofactor-binding property rather than the core function itself. Supporting Evidence: file:human/HCK/HCK-uniprot.txt L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Nuclear localization reported for an HCK isoform. Reason: A fraction of HCK is detected in the nucleus (consistent with TP73 regulation), a peripheral location relative to its membrane-proximal signaling role. Supporting Evidence: PMID:11904303 p59Hck isoform induces F-actin reorganization |
| GO:0005764 lysosome | IDA PMID:15998323 Activation of the lysosome-associated p61Hck isoform trigger... | KEEP AS NON CORE | Summary: p61Hck associates with lysosomes/azurophil granules. Reason: The p61Hck isoform is lysosome-associated and drives secretory-lysosome functions; a genuine but isoform-specific, non-core location. Supporting Evidence: PMID:15998323 p59Hck and p61Hck, present at the plasma membrane |
| GO:0005764 lysosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: p61Hck associates with lysosomes/azurophil granules. Reason: The p61Hck isoform is lysosome-associated and drives secretory-lysosome functions; a genuine but isoform-specific, non-core location. Supporting Evidence: PMID:15998323 p59Hck and p61Hck, present at the plasma membrane |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Golgi apparatus localization (subcellular-location mapping). Reason: Reported among HCK isoform 2 locations; peripheral to the core membrane-signaling role. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Golgi apparatus |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: A substantial pool of HCK is cytosolic. Reason: At least half of p59Hck is cytoplasmic; cytosolic localization is well established. Supporting Evidence: file:human/HCK/HCK-uniprot.txt At least half of this isoform is found in the cytoplasm |
| GO:0005829 cytosol | IEA GO_REF:0000120 | ACCEPT | Summary: A substantial pool of HCK is cytosolic. Reason: At least half of p59Hck is cytoplasmic; cytosolic localization is well established. Supporting Evidence: file:human/HCK/HCK-uniprot.txt At least half of this isoform is found in the cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-200858 | ACCEPT | Summary: A substantial pool of HCK is cytosolic. Reason: At least half of p59Hck is cytoplasmic; cytosolic localization is well established. Supporting Evidence: file:human/HCK/HCK-uniprot.txt At least half of this isoform is found in the cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029459 | ACCEPT | Summary: A substantial pool of HCK is cytosolic. Reason: At least half of p59Hck is cytoplasmic; cytosolic localization is well established. Supporting Evidence: file:human/HCK/HCK-uniprot.txt At least half of this isoform is found in the cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664261 | ACCEPT | Summary: A substantial pool of HCK is cytosolic. Reason: At least half of p59Hck is cytoplasmic; cytosolic localization is well established. Supporting Evidence: file:human/HCK/HCK-uniprot.txt At least half of this isoform is found in the cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664275 | ACCEPT | Summary: A substantial pool of HCK is cytosolic. Reason: At least half of p59Hck is cytoplasmic; cytosolic localization is well established. Supporting Evidence: file:human/HCK/HCK-uniprot.txt At least half of this isoform is found in the cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9674816 | ACCEPT | Summary: A substantial pool of HCK is cytosolic. Reason: At least half of p59Hck is cytoplasmic; cytosolic localization is well established. Supporting Evidence: file:human/HCK/HCK-uniprot.txt At least half of this isoform is found in the cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9705738 | ACCEPT | Summary: A substantial pool of HCK is cytosolic. Reason: At least half of p59Hck is cytoplasmic; cytosolic localization is well established. Supporting Evidence: file:human/HCK/HCK-uniprot.txt At least half of this isoform is found in the cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9707977 | ACCEPT | Summary: A substantial pool of HCK is cytosolic. Reason: At least half of p59Hck is cytoplasmic; cytosolic localization is well established. Supporting Evidence: file:human/HCK/HCK-uniprot.txt At least half of this isoform is found in the cytoplasm |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | TOO GENERAL | Summary: Cytoskeleton localization; HCK colocalizes with actin. Reason: The specific term actin filament is asserted (IDA) for this gene; the bare cytoskeleton term is entailed by it and adds no information. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Colocalizes with the actin |
| GO:0005884 actin filament | IDA PMID:15998323 Activation of the lysosome-associated p61Hck isoform trigger... | KEEP AS NON CORE | Summary: HCK localizes to actin filaments/podosomes. Reason: p61Hck triggers actin-rich podosome structures and HCK colocalizes with the actin cytoskeleton; a genuine but non-core location. Supporting Evidence: PMID:15998323 bona fide podosome rosettes |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | MODIFY | Summary: HCK (p59 isoform) is anchored at the plasma membrane, on its cytoplasmic face. Reason: p59Hck is lipid-anchored to the plasma membrane, the principal site where it couples immune receptors to downstream signaling; this matches the Src-family IBA placement. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Propagation Review Root cause: TERM SCOPING PROBLEM Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:15998323 p59Hck and p61Hck, present at the plasma membrane |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | MODIFY | Summary: HCK (p59 isoform) is anchored at the plasma membrane, on its cytoplasmic face. Reason: p59Hck is lipid-anchored to the plasma membrane, the principal site where it couples immune receptors to downstream signaling; this matches the Src-family IBA placement. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:15998323 p59Hck and p61Hck, present at the plasma membrane |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | MODIFY | Summary: HCK (p59 isoform) is anchored at the plasma membrane, on its cytoplasmic face. Reason: p59Hck is lipid-anchored to the plasma membrane, the principal site where it couples immune receptors to downstream signaling; this matches the Src-family IBA placement. The more specific supported term the gene already carries is cytoplasmic side of plasma membrane (GO:0009898) -- the protein is lipid-anchored or recruited to the inner (cytoplasmic) leaflet and faces the cytosol, not the cell exterior. Proposed replacements: cytoplasmic side of plasma membrane Supporting Evidence: PMID:15998323 p59Hck and p61Hck, present at the plasma membrane |
| GO:0005901 caveola | IDA PMID:7791757 Myristoylation and differential palmitoylation of the HCK pr... | KEEP AS NON CORE | Summary: A fraction of p59Hck resides in caveolae. Reason: Palmitoylation targets HCK to caveolar membrane microdomains; a specific membrane subcompartment that is non-core. Supporting Evidence: PMID:7791757 including the organelles known as caveolae |
| GO:0005901 caveola | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: A fraction of p59Hck resides in caveolae. Reason: Palmitoylation targets HCK to caveolar membrane microdomains; a specific membrane subcompartment that is non-core. Supporting Evidence: PMID:7791757 including the organelles known as caveolae |
| GO:0005925 focal adhesion | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Active p59Hck localizes to focal adhesions. Reason: Constitutively active p59Hck is found at focal adhesion sites and colocalizes with the actin cytoskeleton there; relevant to adhesion/migration but non-core. Supporting Evidence: PMID:11904303 p59Hck(ca) was found at focal adhesion sites |
| GO:0005925 focal adhesion | IMP PMID:11904303 p59Hck isoform induces F-actin reorganization to form protru... | KEEP AS NON CORE | Summary: Active p59Hck localizes to focal adhesions. Reason: Constitutively active p59Hck is found at focal adhesion sites and colocalizes with the actin cytoskeleton there; relevant to adhesion/migration but non-core. Supporting Evidence: PMID:11904303 p59Hck(ca) was found at focal adhesion sites |
| GO:0006468 protein phosphorylation | TAS PMID:3496523 Identification of a human gene (HCK) that encodes a protein-... | MODIFY | Summary: Protein phosphorylation; HCK specifically phosphorylates tyrosine. Reason: Correct but general; HCK performs peptidyl-tyrosine phosphorylation, a term already asserted for this gene. Proposed replacements: peptidyl-tyrosine phosphorylation Supporting Evidence: PMID:10092522 Hck phosphorylates Cbl in vitro |
| GO:0006952 defense response | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Defense response (broad immune process). Reason: Consistent with HCK's innate-immune role but very general; retained as non-core. Supporting Evidence: file:human/HCK/HCK-uniprot.txt regulation of innate immune responses |
| GO:0007155 cell adhesion | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Cell adhesion. Reason: HCK contributes to phagocyte adhesion downstream of integrins; a peripheral process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt cell adhesion and migration |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Participation in cell-surface receptor tyrosine kinase signaling. Reason: HCK acts downstream of receptor tyrosine kinases (e.g. EGFR/ERBB, KIT, FLT3) as a cytoplasmic effector; a non-core signaling context. Supporting Evidence: file:human/HCK/HCK-uniprot.txt transmits signals from cell surface receptors |
| GO:0007229 integrin-mediated signaling pathway | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Integrin-mediated signaling. Reason: HCK acts downstream of integrins ITGB1/ITGB2; peripheral to its core kinase function. Supporting Evidence: file:human/HCK/HCK-uniprot.txt integrins, such as ITGB1 and ITGB2 |
| GO:0007498 mesoderm development | TAS PMID:3453117 Novel protein-tyrosine kinase gene (hck) preferentially expr... | MARK AS OVER ANNOTATED | Summary: Mesoderm development, from the hck gene-characterization paper. Reason: The cited reference reports hck as a hematopoietic-lineage tyrosine kinase; mesoderm development is an indirect, lineage-of-origin inference and over-annotates HCK's function. Supporting Evidence: PMID:3453117 novel human protein-tyrosine kinase gene (hck) that is primarily expressed in hematopoietic cells |
| GO:0008284 positive regulation of cell population proliferation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Positive regulation of cell proliferation. Reason: Activated HCK transforms fibroblasts and promotes proliferation/survival in hematopoietic contexts; a downstream, non-core outcome. Supporting Evidence: PMID:10092522 Fibroblasts that are transformed with an activated allele of Hck |
| GO:0008284 positive regulation of cell population proliferation | IMP PMID:10092522 The proto-oncogene p120(Cbl) is a downstream substrate of th... | KEEP AS NON CORE | Summary: Positive regulation of cell proliferation. Reason: Activated HCK transforms fibroblasts and promotes proliferation/survival in hematopoietic contexts; a downstream, non-core outcome. Supporting Evidence: PMID:10092522 Fibroblasts that are transformed with an activated allele of Hck |
| GO:0008289 lipid binding | EXP PMID:31877324 Membrane Anchoring of Hck Kinase via the Intrinsically Disor... | KEEP AS NON CORE | Summary: The SH4-U region of HCK binds membrane lipids for anchoring. Reason: Experimental neutron-reflectometry work shows HCK membrane anchoring via its intrinsically disordered, lipid-modified SH4-U region; lipid binding localizes the kinase but is not its catalytic function. Supporting Evidence: PMID:31877324 Membrane Anchoring of Hck Kinase via the Intrinsically Disordered SH4 |
| GO:0008360 regulation of cell shape | IMP PMID:10092522 The proto-oncogene p120(Cbl) is a downstream substrate of th... | KEEP AS NON CORE | Summary: Regulation of cell shape. Reason: HCK remodels the actin cytoskeleton and membrane protrusions, affecting cell shape; peripheral to the catalytic core. Supporting Evidence: file:human/HCK/HCK-uniprot.txt formation of podosomes and cell protrusions |
| GO:0009898 cytoplasmic side of plasma membrane | IMP PMID:11904303 p59Hck isoform induces F-actin reorganization to form protru... | ACCEPT | Summary: HCK is anchored to the cytoplasmic (inner) face of the plasma membrane. Reason: IMP localizes active p59Hck to the cytoplasmic side of the plasma membrane; this inner-leaflet position is where HCK couples immune receptors to signaling. HCK has no extracellular domain. Supporting Evidence: PMID:11904303 p59Hck(ca) was found at focal adhesion sites |
| GO:0016020 membrane | IEA GO_REF:0000044 | TOO GENERAL | Summary: Membrane is the generic parent of the asserted plasma membrane localization. Reason: HCK is specifically anchored to the plasma membrane (and its cytoplasmic side), terms already asserted; bare membrane is entailed by them. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Membrane; Lipid-anchor |
| GO:0018108 peptidyl-tyrosine phosphorylation | IMP PMID:10092522 The proto-oncogene p120(Cbl) is a downstream substrate of th... | ACCEPT | Summary: HCK phosphorylates tyrosine residues on substrate proteins. Reason: Direct output of HCK catalytic activity, shown experimentally (e.g. Cbl, autophosphorylation). Supporting Evidence: PMID:10092522 Hck phosphorylates Cbl in vitro |
| GO:0019221 cytokine-mediated signaling pathway | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Cytokine-mediated signaling. Reason: HCK acts downstream of cytokine receptors (IFNG, IL2, IL6, IL8); a non-core context. Supporting Evidence: file:human/HCK/HCK-uniprot.txt the receptors for |
| GO:0030133 transport vesicle | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Transport vesicle localization. Reason: Reported among HCK's vesicular locations; peripheral. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Cytoplasmic vesicle |
| GO:0030154 cell differentiation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Cell differentiation (broad, IBA). Reason: A general Src-family process term; retained as non-core. Supporting Evidence: PMID:3496523 Expression in granulocytic and monocytic leukemia cells increases after the cells have been induced to differentiate |
| GO:0030838 positive regulation of actin filament polymerization | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Positive regulation of actin filament polymerization. Reason: HCK drives actin polymerization during podosome/protrusion formation; a specific downstream process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Promotes reorganization of the actin cytoskeleton and actin |
| GO:0031410 cytoplasmic vesicle | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Cytoplasmic vesicle localization. Reason: Reported among HCK isoform locations; peripheral. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Cytoplasmic vesicle |
| GO:0031663 lipopolysaccharide-mediated signaling pathway | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: LPS-mediated signaling. Reason: HCK participates in innate responses to bacterial LPS; a non-core signaling context. Supporting Evidence: file:human/HCK/HCK-uniprot.txt regulation of innate immune responses |
| GO:0032956 regulation of actin cytoskeleton organization | IMP PMID:11904303 p59Hck isoform induces F-actin reorganization to form protru... | KEEP AS NON CORE | Summary: Regulation of actin cytoskeleton organization. Reason: Strongly supported by IMP (active HCK reorganizes F-actin); a specific downstream process rather than the catalytic core. Supporting Evidence: PMID:11904303 triggered reorganization of the actin cytoskeleton |
| GO:0035556 intracellular signal transduction | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Intracellular signal transduction. Reason: General signaling term consistent with HCK's role; retained as non-core. Supporting Evidence: file:human/HCK/HCK-uniprot.txt transmits signals from cell surface receptors |
| GO:0035556 intracellular signal transduction | IMP PMID:11904303 p59Hck isoform induces F-actin reorganization to form protru... | KEEP AS NON CORE | Summary: Intracellular signal transduction. Reason: General signaling term consistent with HCK's role; retained as non-core. Supporting Evidence: file:human/HCK/HCK-uniprot.txt transmits signals from cell surface receptors |
| GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis | IEA GO_REF:0000117 | ACCEPT | Summary: Fc-gamma receptor signaling pathway in phagocytosis. Reason: HCK is a Src-family kinase acting immediately downstream of Fc-gamma receptors to drive phagocytosis, a defining function; supported experimentally and in Reactome. Supporting Evidence: PMID:10861086 Differential involvement of Src family kinases in Fc gamma receptor-mediated phagocytosis file:human/HCK/HCK-uniprot.txt Acts downstream of receptors that bind the Fc region of immunoglobulins |
| GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis | TAS Reactome:R-HSA-2029480 | ACCEPT | Summary: Fc-gamma receptor signaling pathway in phagocytosis. Reason: HCK is a Src-family kinase acting immediately downstream of Fc-gamma receptors to drive phagocytosis, a defining function; supported experimentally and in Reactome. Supporting Evidence: PMID:10861086 Differential involvement of Src family kinases in Fc gamma receptor-mediated phagocytosis file:human/HCK/HCK-uniprot.txt Acts downstream of receptors that bind the Fc region of immunoglobulins |
| GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis | TAS Reactome:R-HSA-9664422 | ACCEPT | Summary: Fc-gamma receptor signaling pathway in phagocytosis. Reason: HCK is a Src-family kinase acting immediately downstream of Fc-gamma receptors to drive phagocytosis, a defining function; supported experimentally and in Reactome. Supporting Evidence: PMID:10861086 Differential involvement of Src family kinases in Fc gamma receptor-mediated phagocytosis file:human/HCK/HCK-uniprot.txt Acts downstream of receptors that bind the Fc region of immunoglobulins |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:17535448 Regulation of p73 by Hck through kinase-dependent and indepe... | KEEP AS NON CORE | Summary: Negative regulation of apoptosis via TP73. Reason: HCK interacts with and phosphorylates TP73, inhibiting TP73-mediated apoptosis; a specific, non-core regulatory role. Supporting Evidence: PMID:17535448 SH3 domain of Hck interacts with p73 file:human/HCK/HCK-uniprot.txt TP73-mediated apoptosis |
| GO:0043299 leukocyte degranulation | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Leukocyte degranulation. Reason: HCK mediates degranulation/secretory-lysosome mobilization in phagocytes; a key but downstream immune output. Supporting Evidence: file:human/HCK/HCK-uniprot.txt mediates mobilization of secretory lysosomes |
| GO:0045121 membrane raft | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Membrane raft localization. Reason: HCK partitions into raft/caveolar microdomains via palmitoylation; a non-core location. Supporting Evidence: PMID:7791757 including the organelles known as caveolae |
| GO:0045728 respiratory burst after phagocytosis | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Respiratory burst after phagocytosis. Reason: HCK activates NADPH oxidase to produce the respiratory burst following phagocytosis; a downstream immune output. Supporting Evidence: file:human/HCK/HCK-uniprot.txt activation of NADPH oxidase to bring about the |
| GO:0046777 protein autophosphorylation | IMP PMID:10092522 The proto-oncogene p120(Cbl) is a downstream substrate of th... | ACCEPT | Summary: Protein autophosphorylation. Reason: HCK autophosphorylates (Tyr-411 activation loop), a core regulatory property of the kinase. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Phosphorylation at Tyr-411 is required for optimal activity |
| GO:0050727 regulation of inflammatory response | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Regulation of inflammatory response. Reason: HCK modulates release of inflammatory molecules; a downstream immune process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt Plays a role in the release of inflammatory |
| GO:0050764 regulation of phagocytosis | IMP PMID:11904303 p59Hck isoform induces F-actin reorganization to form protru... | KEEP AS NON CORE | Summary: Regulation of phagocytosis. Reason: HCK regulates Fc-receptor phagocytosis; supported by IMP but a downstream process relative to the catalytic core. Supporting Evidence: PMID:11904303 phagocytosis, cell migration, and lysosome mobilization |
| GO:0050900 leukocyte migration | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Leukocyte migration. Reason: HCK contributes to phagocyte migration; a downstream immune process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt cell adhesion and migration |
| GO:0060333 type II interferon-mediated signaling pathway | TAS PMID:18538446 Hematopoietic cell kinase (Hck) isoforms and phagocyte dutie... | KEEP AS NON CORE | Summary: Type II interferon (IFN-gamma)-mediated signaling. Reason: HCK acts downstream of the IFNG receptor; a non-core signaling context. Supporting Evidence: file:human/HCK/HCK-uniprot.txt the receptors for |
| GO:0071345 cellular response to cytokine stimulus | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Cellular response to cytokine stimulus. Reason: General cytokine-response term consistent with HCK signaling; non-core. Supporting Evidence: file:human/HCK/HCK-uniprot.txt the receptors for |
| GO:0071396 cellular response to lipid | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Cellular response to lipid. Reason: Consistent with HCK's role downstream of LPS; a general non-core process. Supporting Evidence: file:human/HCK/HCK-uniprot.txt regulation of innate immune responses |
| GO:0071801 regulation of podosome assembly | IDA PMID:15998323 Activation of the lysosome-associated p61Hck isoform trigger... | KEEP AS NON CORE | Summary: Regulation of podosome assembly. Reason: Active p61Hck triggers de novo podosome (rosette) biogenesis; a specific, well- supported downstream process. Supporting Evidence: PMID:15998323 bona fide podosome rosettes |
| GO:0120035 regulation of plasma membrane bounded cell projection organization | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Regulation of plasma membrane bounded cell projection organization. Reason: HCK drives membrane protrusion/podosome formation; the general version of its actin-remodelling role, retained as non-core. Supporting Evidence: file:human/HCK/HCK-uniprot.txt formation of podosomes and cell protrusions |
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Download this section (compressed HTML)Q: Which substrate-phosphorylation events uniquely require HCK versus other myeloid Src-family kinases (LYN, FGR) in Fc-receptor phagocytosis?
Q: How do the lipid modifications and the SH4-U region partition p59Hck versus p61Hck between the plasma membrane and lysosomes to produce their distinct phenotypes?
Experiment: Phosphoproteomics of HCK-null versus reconstituted phagocytes after Fc-gamma receptor engagement to map the HCK-specific substrate network.
Type: proteomics
Experiment: Live-cell imaging of palmitoylation-deficient HCK to test the requirement of membrane/caveolar targeting for podosome formation and the respiratory burst.
Type: cell biology
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