Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyProtein kinase-like (PK-like)8069259 3000066 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyProtein kinase-like (PK-like)8069259 3000066 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF07714e4v0gA1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: PF07714ECOD (1.6)
BPF07714e4v0gB1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: PF07714ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.30.200.20 Alpha Beta 2-Layer Sandwich Phosphorylase Kinase domain 1CATH (4.3.0)
A1.10.510.10 Mainly Alpha Orthogonal Bundle Transferase(Phosphotransferase) domain 1CATH (4.3.0)
B3.30.200.20 Alpha Beta 2-Layer Sandwich Phosphorylase Kinase domain 1CATH (4.3.0)
B1.10.510.10 Mainly Alpha Orthogonal Bundle Transferase(Phosphotransferase) domain 1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF07714Protein tyrosine and serine/threonine kinase (PK_Tyr_Ser-Thr)Protein tyrosine and serine/threonine kinaseProtein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosph ...Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [1]; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.
Domain
PF07714Protein tyrosine and serine/threonine kinase (PK_Tyr_Ser-Thr)Protein tyrosine and serine/threonine kinaseProtein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosph ...Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [1]; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
TYROSINE-PROTEIN KINASE JAK3
TYROSINE-PROTEIN KINASE JAK3

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR000299FERM domainDomain
IPR016251Tyrosine-protein kinase, non-receptor Jak/Tyk2Family
IPR008266Tyrosine-protein kinase, active siteActive Site
IPR020635Tyrosine-protein kinase, catalytic domainDomain
IPR000719Protein kinase domainDomain
IPR041381JAK1-3/TYK2, pleckstrin homology-like domainDomain
IPR017441Protein kinase, ATP binding siteBinding Site
IPR036860SH2 domain superfamilyHomologous Superfamily
IPR020775Tyrosine-protein kinase, non-receptor Jak3Family
IPR000980SH2 domainDomain
IPR011993PH-like domain superfamilyHomologous Superfamily
IPR001245Serine-threonine/tyrosine-protein kinase, catalytic domainDomain
IPR041046JAK, FERM F2 lobe domainDomain
IPR019749Band 4.1 domainDomain
IPR011009Protein kinase-like domain superfamilyHomologous Superfamily
IPR041155FERM F1 lobe ubiquitin-like domainDomain
IPR000299FERM domainDomain
IPR016251Tyrosine-protein kinase, non-receptor Jak/Tyk2Family
IPR008266Tyrosine-protein kinase, active siteActive Site
IPR020635Tyrosine-protein kinase, catalytic domainDomain
IPR000719Protein kinase domainDomain
IPR041381JAK1-3/TYK2, pleckstrin homology-like domainDomain
IPR017441Protein kinase, ATP binding siteBinding Site
IPR036860SH2 domain superfamilyHomologous Superfamily
IPR020775Tyrosine-protein kinase, non-receptor Jak3Family
IPR000980SH2 domainDomain
IPR011993PH-like domain superfamilyHomologous Superfamily
IPR001245Serine-threonine/tyrosine-protein kinase, catalytic domainDomain
IPR041046JAK, FERM F2 lobe domainDomain
IPR019749Band 4.1 domainDomain
IPR011009Protein kinase-like domain superfamilyHomologous Superfamily
IPR041155FERM F1 lobe ubiquitin-like domainDomain

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosP52333
PharosP52333

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
PTR Parent Component: TYR

RESIDAA0039

PSI-MOD :  O4'-phospho-L-tyrosine MOD:00048
PTR Parent Component: TYR

RESIDAA0039 , AA0039

PSI-MOD :  O4'-phospho-L-tyrosine MOD:00048 , O4'-phospho-L-tyrosine MOD:00048