Reviewed,
UniProtKB/Swiss-Prot Q95M30 (HCK_MACFA)
Last modified
February 9, 2010.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Tyrosine-protein kinase HCK EC=2.7.10.2 Alternative name(s): Hemopoietic cell kinase p56-HCK | ||
| Gene names |
| ||
| Organism | Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey) | ||
| Taxonomic identifier | 9541 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
Protein attributes
| Sequence length | 504 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | May serve as part of a signaling pathway coupling the Fc receptor to the activation of the respiratory burst. May also contribute to neutrophil migration and may regulate the degranulation process of neutrophils By similarity. |
| Catalytic activity | ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. |
| Subcellular location | Membrane; Peripheral membrane protein By similarity. |
| Sequence similarities | Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Domain | SH2 domain SH3 domain |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase Tyrosine-protein kinase |
| PTM | Lipoprotein Myristate Palmitate Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activityInferred from electronic annotation. Source: EC protein bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 504 | 503 | Tyrosine-protein kinase HCK | PRO_0000088103 | |||||
Regions | |||||||||
| Domain | 56 – 116 | 61 | SH3 | ||||||
| Domain | 122 – 219 | 98 | SH2 | ||||||
| Domain | 240 – 493 | 254 | Protein kinase | ||||||
| Nucleotide binding | 246 – 254 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 359 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 268 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 15 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 30 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 105 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 180 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 187 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 308 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 389 | 1 | Phosphotyrosine; by autocatalysis By similarity | ||||||
| Modified residue | 440 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 493 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 498 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 500 | 1 | Phosphotyrosine By similarity | ||||||
| Lipidation | 2 | 1 | N-myristoyl glycine By similarity | ||||||
| Lipidation | 3 | 1 | S-palmitoyl cysteine By similarity | ||||||
Sequences
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References
| [1] | Picard C. Thesis (2001), University of Marseille, France Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ320181 mRNA. Translation: CAC44031.1. |
3D structure databases | |
| SMR | Q95M30. Positions 56-116, 59-504. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q95M30. |
Enzyme and pathway databases | |
| BRENDA | 2.7.10.2. 3438. |
Family and domain databases | |
| InterPro | IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR000980. SH2. IPR001452. SH3_domain. IPR020473. SH3_region. IPR020748. Tyr_kinase_non-rcpt_Hck. IPR020635. Tyr_Pkinase_cat_dom. IPR020685. Tyr_prot_kinase. IPR008266. Tyr_prot_kinase_AS. [Graphical view] |
| Gene3D | G3DSA:3.30.505.10. SH2. 1 hit. |
| PANTHER | PTHR23256:SF259. Tyr_kinase_non-rcpt_Hck. 1 hit. PTHR23256. Tyr_prot_kinase. 1 hit. |
| Pfam | PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view] |
| PRINTS | PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. |
| SMART | SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view] |
| PROSITE | PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50001. SH2. 1 hit. PS50002. SH3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HCK_MACFA | ||||||||
| Accession | Primary (citable) accession number: Q95M30 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


