A0A994J7X8 · A0A994J7X8_HUMAN
- ProteinCalcium/calmodulin-dependent protein kinase type II subunit delta
- GeneCAMK2D
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids523 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | sarcolemma | |
Cellular Component | sarcoplasmic reticulum membrane | |
Molecular Function | ATP binding | |
Molecular Function | calcium/calmodulin-dependent protein kinase activity | |
Molecular Function | calmodulin binding | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCalcium/calmodulin-dependent protein kinase type II subunit delta
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A994J7X8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane, sarcolemma ; Peripheral membrane protein
Sarcoplasmic reticulum membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 311 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 235 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 276 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 277 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 280 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 306 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 307 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 315 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 319 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 376 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 382 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 517 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-272 | Protein kinase | ||||
Sequence: YQLFEELGKGAFSVVRRCMKIPTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPAKRITASEALKHPWI | ||||||
Compositional bias | 348-378 | Polar residues | ||||
Sequence: TSPKENIPTPALEPQTTVIHNPDGNKESTES | ||||||
Region | 348-386 | Disordered | ||||
Sequence: TSPKENIPTPALEPQTTVIHNPDGNKESTESSNTTIEDE |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length523
- Mass (Da)58,998
- Last updated2023-05-03 v1
- Checksum59FD5E07C9A62DDF
Computationally mapped potential isoform sequences
There are 22 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q13557 | KCC2D_HUMAN | CAMK2D | 499 | ||
E9PBG7 | E9PBG7_HUMAN | CAMK2D | 512 | ||
H0Y9J2 | H0Y9J2_HUMAN | CAMK2D | 182 | ||
D6R938 | D6R938_HUMAN | CAMK2D | 498 | ||
H0Y9C2 | H0Y9C2_HUMAN | CAMK2D | 194 | ||
A0A8V8TPJ8 | A0A8V8TPJ8_HUMAN | CAMK2D | 512 | ||
A0A8V8TPK3 | A0A8V8TPK3_HUMAN | CAMK2D | 491 | ||
A0A8V8TPM4 | A0A8V8TPM4_HUMAN | CAMK2D | 347 | ||
A0A8V8TQ10 | A0A8V8TQ10_HUMAN | CAMK2D | 71 | ||
A0A8V8TPY4 | A0A8V8TPY4_HUMAN | CAMK2D | 491 | ||
E9PF82 | E9PF82_HUMAN | CAMK2D | 533 | ||
A0A8V8TN60 | A0A8V8TN60_HUMAN | CAMK2D | 491 | ||
A0A8V8TN65 | A0A8V8TN65_HUMAN | CAMK2D | 512 | ||
A0A8V8TN88 | A0A8V8TN88_HUMAN | CAMK2D | 477 | ||
A0A8V8TNA1 | A0A8V8TNA1_HUMAN | CAMK2D | 511 | ||
A0A8V8TNA7 | A0A8V8TNA7_HUMAN | CAMK2D | 492 | ||
A0A8V8TND4 | A0A8V8TND4_HUMAN | CAMK2D | 523 | ||
A0A8V8TNN4 | A0A8V8TNN4_HUMAN | CAMK2D | 119 | ||
A0A8V8TNN9 | A0A8V8TNN9_HUMAN | CAMK2D | 344 | ||
A0A8V8TNR6 | A0A8V8TNR6_HUMAN | CAMK2D | 255 | ||
A0A994J5B0 | A0A994J5B0_HUMAN | CAMK2D | 503 | ||
A0A994J516 | A0A994J516_HUMAN | CAMK2D | 503 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 348-378 | Polar residues | ||||
Sequence: TSPKENIPTPALEPQTTVIHNPDGNKESTES |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC004056 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC004168 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC093900 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC107386 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |