The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Phosphorylase Kinase; domain 1
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 65935: cAMP-dependent protein kinase catalytic subunit al...

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 20 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Protein serine/threonine kinase activity GO:0004674
Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
2 P05132 (/TAS) P22612 (/TAS)
CAMP-dependent protein kinase activity GO:0004691
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of cAMP.
2 P05132 (/IDA) P21137 (/IDA)
CAMP-dependent protein kinase activity GO:0004691
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of cAMP.
2 P05132 (/TAS) P22612 (/TAS)
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
1 P05132 (/IDA)
Protein kinase activity GO:0004672
Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
1 P05132 (/IDA)
Protein serine/threonine kinase activity GO:0004674
Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
1 P22612 (/EXP)
Protein serine/threonine kinase activity GO:0004674
Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
1 P05132 (/IDA)
Protein serine/threonine kinase activity GO:0004674
Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
1 P05132 (/IMP)
Protein serine/threonine kinase activity GO:0004674
Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
1 P05132 (/ISO)
CAMP-dependent protein kinase activity GO:0004691
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of cAMP.
1 P05132 (/ISO)
Protein serine/threonine/tyrosine kinase activity GO:0004712
Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
1 P05132 (/ISO)
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
1 P05132 (/IPI)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 P05132 (/IDA)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 P05132 (/IMP)
Protein kinase binding GO:0019901
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
1 P05132 (/ISO)
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
1 P05132 (/IPI)
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
1 P05132 (/IMP)
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
1 P05132 (/ISO)
Protein kinase A regulatory subunit binding GO:0034237
Interacting selectively and non-covalently with one or both of the regulatory subunits of protein kinase A.
1 P05132 (/IPI)
Protein kinase A regulatory subunit binding GO:0034237
Interacting selectively and non-covalently with one or both of the regulatory subunits of protein kinase A.
1 P05132 (/ISO)

There are 33 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Protein phosphorylation GO:0006468
The process of introducing a phosphate group on to a protein.
2 P05132 (/IDA) P21137 (/IDA)
Mesoderm formation GO:0001707
The process that gives rise to the mesoderm. This process pertains to the initial formation of the structure from unspecified parts.
1 P05132 (/IGI)
Neural tube closure GO:0001843
The last step in the formation of the neural tube, where the paired neural folds are brought together and fuse at the dorsal midline.
1 P05132 (/IGI)
Stimulatory C-type lectin receptor signaling pathway GO:0002223
Any series of molecular signals generated as a consequence of binding to a C-type lectin receptor capable of cellular activation.
1 P22612 (/TAS)
Renal water homeostasis GO:0003091
Renal process involved in the maintenance of an internal steady state of water in the body.
1 P22612 (/TAS)
MRNA processing GO:0006397
Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
1 P05132 (/ISO)
Spermatogenesis GO:0007283
The process of formation of spermatozoa, including spermatocytogenesis and spermiogenesis.
1 P22612 (/TAS)
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
1 P22612 (/TAS)
Male gonad development GO:0008584
The process whose specific outcome is the progression of the male gonad over time, from its formation to the mature structure.
1 P22612 (/TAS)
Peptidyl-serine phosphorylation GO:0018105
The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
1 P05132 (/IDA)
Peptidyl-serine phosphorylation GO:0018105
The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
1 P05132 (/IMP)
Peptidyl-serine phosphorylation GO:0018105
The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
1 P05132 (/ISO)
Peptidyl-threonine phosphorylation GO:0018107
The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine.
1 P05132 (/IDA)
Triglyceride catabolic process GO:0019433
The chemical reactions and pathways resulting in the breakdown of a triglyceride, any triester of glycerol.
1 P05132 (/TAS)
Activation of protein kinase A activity GO:0034199
Any process that initiates the activity of the inactive enzyme protein kinase A.
1 P22612 (/TAS)
High-density lipoprotein particle assembly GO:0034380
The non-covalent aggregation and arrangement of proteins and lipids to form a high-density lipoprotein particle.
1 P22612 (/TAS)
Cellular response to heat GO:0034605
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
1 P05132 (/ISO)
Cellular response to heat GO:0034605
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
1 P05132 (/ISS)
Intracellular signal transduction GO:0035556
The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
1 P05132 (/TAS)
Regulation of osteoblast differentiation GO:0045667
Any process that modulates the frequency, rate or extent of osteoblast differentiation.
1 P05132 (/ISO)
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
1 P05132 (/IDA)
Positive regulation of protein export from nucleus GO:0046827
Any process that activates or increases the frequency, rate or extent of directed movement of proteins from the nucleus into the cytoplasm.
1 P05132 (/IMP)
Sperm capacitation GO:0048240
A process required for sperm to reach fertilization competence. Sperm undergo an incompletely understood series of morphological and molecular maturational processes, termed capacitation, involving, among other processes, protein tyrosine phosphorylation and increased intracellular calcium.
1 P05132 (/IDA)
Modulation of synaptic transmission GO:0050804
Any process that modulates the frequency or amplitude of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse. Amplitude, in this case, refers to the change in postsynaptic membrane potential due to a single instance of synaptic transmission.
1 P05132 (/IMP)
Regulation of proteasomal protein catabolic process GO:0061136
Any process that modulates the rate, frequency, or extent of the chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome.
1 P05132 (/ISO)
Regulation of protein processing GO:0070613
Any process that modulates the frequency, rate or extent of protein processing, any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein.
1 P05132 (/IGI)
Positive regulation of cell cycle arrest GO:0071158
Any process that increases the rate, frequency, or extent of cell cycle arrest, the process in which the cell cycle is halted during one of the normal phases.
1 P05132 (/IDA)
Cellular response to glucose stimulus GO:0071333
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucose stimulus.
1 P05132 (/ISO)
Cellular response to parathyroid hormone stimulus GO:0071374
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a parathyroid hormone stimulus.
1 P05132 (/IMP)
Cellular response to glucagon stimulus GO:0071377
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucagon stimulus.
1 P22612 (/TAS)
Positive regulation of oocyte maturation GO:1900195
Any process that activates or increases the frequency, rate or extent of oocyte maturation.
1 P21137 (/IMP)
Negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning GO:1901621
Any process that stops, prevents or reduces the frequency, rate or extent of smoothened signaling pathway involved in dorsal/ventral neural tube patterning.
1 P05132 (/IGI)
Regulation of bicellular tight junction assembly GO:2000810
Any process that modulates the frequency, rate or extent of tight junction assembly.
1 P05132 (/ISO)

There are 29 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
2 P05132 (/TAS) P22612 (/TAS)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
2 P05132 (/TAS) P22612 (/TAS)
Acrosomal vesicle GO:0001669
A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome.
1 P05132 (/IDA)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 P05132 (/IDA)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 P05132 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P05132 (/IDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P05132 (/ISO)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
1 P05132 (/IDA)
Centrosome GO:0005813
A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
1 P05132 (/ISO)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
1 P22612 (/IDA)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
1 P05132 (/ISO)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
1 P05132 (/IDA)
CAMP-dependent protein kinase complex GO:0005952
An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer.
1 P05132 (/IMP)
CAMP-dependent protein kinase complex GO:0005952
An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer.
1 P21137 (/ISS)
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
1 P05132 (/ISO)
Nucleotide-activated protein kinase complex GO:0031588
A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae).
1 P05132 (/ISO)
Neuromuscular junction GO:0031594
The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.
1 P05132 (/IDA)
Sperm flagellum GO:0036126
A microtubule-based flagellum (or cilium) that is part of a sperm, a mature male germ cell that develops from a spermatid.
1 P05132 (/IDA)
Dendritic spine GO:0043197
A small, membranous protrusion from a dendrite that forms a postsynaptic compartment - typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable including \thin\, \stubby\, \mushroom\, and \branched\, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity.
1 P05132 (/IDA)
Plasma membrane raft GO:0044853
A membrane raft that is part of the plasma membrane.
1 P05132 (/ISO)
Intercellular bridge GO:0045171
A direct connection between the cytoplasm of two cells that is formed following the completion of cleavage furrow ingression during cell division. They are usually present only briefly prior to completion of cytokinesis. However, in some cases, such as the bridges between germ cells during their development, they become stabilised.
1 P22612 (/IDA)
Intercellular bridge GO:0045171
A direct connection between the cytoplasm of two cells that is formed following the completion of cleavage furrow ingression during cell division. They are usually present only briefly prior to completion of cytokinesis. However, in some cases, such as the bridges between germ cells during their development, they become stabilised.
1 P05132 (/ISO)
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
1 P05132 (/ISO)
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
1 P05132 (/ISS)
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
1 P05132 (/ISO)
Sperm midpiece GO:0097225
The highly organized segment of the sperm flagellum which begins at the connecting piece and is characterized by the presence of 9 outer dense fibers (ODFs) that lie outside each of the 9 outer axonemal microtubule doublets and by a sheath of mitochondria that encloses the ODFs and the axoneme; the midpiece terminates about one-fourth of the way down the sperm flagellum at the annulus, which marks the beginning of the principal piece.
1 P05132 (/ISO)
Sperm midpiece GO:0097225
The highly organized segment of the sperm flagellum which begins at the connecting piece and is characterized by the presence of 9 outer dense fibers (ODFs) that lie outside each of the 9 outer axonemal microtubule doublets and by a sheath of mitochondria that encloses the ODFs and the axoneme; the midpiece terminates about one-fourth of the way down the sperm flagellum at the annulus, which marks the beginning of the principal piece.
1 P05132 (/ISS)
Ciliary base GO:0097546
Area of the cilium (also called flagellum) where the basal body and the axoneme are anchored to the plasma membrane. The ciliary base encompasses the distal part of the basal body, transition fibers and transition zone and is structurally and functionally very distinct from the rest of the cilium. In this area proteins are sorted and filtered before entering the cilium, and many ciliary proteins localize specifically to this area.
1 P05132 (/IDA)
Ciliary base GO:0097546
Area of the cilium (also called flagellum) where the basal body and the axoneme are anchored to the plasma membrane. The ciliary base encompasses the distal part of the basal body, transition fibers and transition zone and is structurally and functionally very distinct from the rest of the cilium. In this area proteins are sorted and filtered before entering the cilium, and many ciliary proteins localize specifically to this area.
1 P22612 (/TAS)