UniProt ID | KCC2D_CAEEL | |
---|---|---|
UniProt AC | O62305 | |
Protein Name | Calcium/calmodulin-dependent protein kinase type II {ECO:0000303|PubMed:10647014} | |
Gene Name | unc-43 | |
Organism | Caenorhabditis elegans. | |
Sequence Length | 720 | |
Subcellular Localization | Cytoplasm . Cell projection, axon . Perikaryon . Localizes at or near the Golgi apparatus (PubMed:16079277). Localizes to post-synaptic regions and is enriched in punctate structures in axons of AWC neurons where it co-localizes with tir-1. Localizat | |
Protein Description | Acts in the signaling of a variety of pathways and processes. Phosphorylates 'Ser-319' of daf-16 in response to stress signals, such as heat, starvation and oxidation, which plays a role in prolonging lifespan. Required for viability under chronic osmotic stress in which it acts downstream of osr-1. Has roles in locomotion, oocyte maturation, brood size, egg laying, defecation, meiotic maturation and neuronal cell fate specification. Required for the regulation of synaptic density and neuromuscular junction morphology. Regulates the synaptic trafficking of glr-1. Bidirectional modulator of neurotransmitter release with negative modulatory effects mainly mediated via slo-1 activation. Involved in activation of ADF neurons and increased tph-1 transcription following exposure to pathogenic bacteria which leads to learned olfactory aversion to the bacteria. Implicated in the muscle regulation of spicule protraction. In conjunction with egl-2 has a role in the suppression of mating behavior under food deprivation to encourage foraging. Involved in restricting str-2 expression to only one of the two AWC neurons. May suppress the functional response to an internal pacemaker, perhaps by modulating the activity of the IP3 receptor.. | |
Protein Sequence | MMNASTKFSDNYDVKEELGKGAFSVVRRCVHKTTGLEFAAKIINTKKLSARDFQKLEREARICRKLQHPNIVRLHDSIQEESFHYLVFDLVTGGELFEDIVAREFYSEADASHCIQQILESIAYCHSNGIVHRDLKPENLLLASKAKGAAVKLADFGLAIEVNDSEAWHGFAGTPGYLSPEVLKKDPYSKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKSLIDSMLTVNPKKRITADQALKVPWICNRERVASAIHRQDTVDCLKKFNARRKLKAAISAVKMVTRMSGVLRTSDSTGSVASNGSTTHDASQVAGTSSQPTSPAAEVYPNVLLFNPQKFPRNCVHPFTTHPYYSPKESSKKKLFFTLLFEVCPHTSRSHILLRDNTKNIYHPYHCFTNKMSNYERAAPSSHGSSTTKKIANAIADLVIRRSSPSIRRKTEADVHNSNRNRKVSAPANLQHALVPVIDVVVATGALASSSVDNLSASTSSDLGRNLLNKKEQGPPSTIKESSESSQTIDDNDSEKGGGQLKHENTVVRADGATGIVSSSNSSTASKSSSTNLSAQKQDIVRVTQTLLDAISCKDFETYTRLCDTSMTCFEPEALGNLIEGIEFHRFYFDGNRKNQVHTTMLNPNVHIIGEDAACVAYVKLTQFLDRNGEAHTRQSQESRVWSKKQGRWVCVHVHRSTQPSTNTTVSEF | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
8 (in isoform 15) | Phosphorylation | - | 12.89 | 19530675 | |
24 (in isoform 15) | Phosphorylation | - | 21.11 | 28854356 | |
277 | Phosphorylation | CNRERVASAIHRQDT CCHHHHHHHHHHHHH | 25.54 | 30078680 | |
284 | Phosphorylation | SAIHRQDTVDCLKKF HHHHHHHHHHHHHHH | 15.20 | 9851916 | |
302 | Phosphorylation | RKLKAAISAVKMVTR HHHHHHHHHHHHHHH | 23.45 | 19530675 | |
303 (in isoform 9) | Phosphorylation | - | 9.99 | 19530675 | |
303 (in isoform 7) | Phosphorylation | - | 9.99 | 19530675 | |
303 (in isoform 6) | Phosphorylation | - | 9.99 | 19530675 | |
303 (in isoform 4) | Phosphorylation | - | 9.99 | 19530675 | |
304 (in isoform 9) | Phosphorylation | - | 3.07 | 19530675 | |
304 (in isoform 7) | Phosphorylation | - | 3.07 | 19530675 | |
304 (in isoform 6) | Phosphorylation | - | 3.07 | 19530675 | |
304 (in isoform 4) | Phosphorylation | - | 3.07 | 19530675 | |
312 (in isoform 9) | Phosphorylation | - | 17.09 | 18806794 | |
312 (in isoform 7) | Phosphorylation | - | 17.09 | 18806794 | |
312 (in isoform 4) | Phosphorylation | - | 17.09 | 18806794 | |
328 (in isoform 9) | Phosphorylation | - | 34.09 | 28854356 | |
328 (in isoform 7) | Phosphorylation | - | 34.09 | 28854356 | |
328 (in isoform 4) | Phosphorylation | - | 34.09 | 28854356 | |
354 (in isoform 8) | Phosphorylation | - | 4.20 | 18806794 | |
354 (in isoform 5) | Phosphorylation | - | 4.20 | 18806794 | |
355 (in isoform 8) | Phosphorylation | - | 6.01 | 19530675 | |
355 (in isoform 5) | Phosphorylation | - | 6.01 | 19530675 | |
363 (in isoform 8) | Phosphorylation | - | 33.34 | 28854356 | |
363 (in isoform 5) | Phosphorylation | - | 33.34 | 28854356 | |
379 (in isoform 8) | Phosphorylation | - | 65.37 | 28854356 | |
379 (in isoform 5) | Phosphorylation | - | 65.37 | 28854356 | |
528 | Phosphorylation | KKEQGPPSTIKESSE CCCCCCCCCHHCCCC | 45.99 | 28854356 | |
529 | Phosphorylation | KEQGPPSTIKESSES CCCCCCCCHHCCCCC | 41.67 | 19530675 | |
533 | Phosphorylation | PPSTIKESSESSQTI CCCCHHCCCCCCCCC | 34.11 | 19060867 | |
534 | Phosphorylation | PSTIKESSESSQTID CCCHHCCCCCCCCCC | 42.46 | 19060867 | |
536 | Phosphorylation | TIKESSESSQTIDDN CHHCCCCCCCCCCCC | 29.69 | 28854356 | |
537 | Phosphorylation | IKESSESSQTIDDND HHCCCCCCCCCCCCC | 27.56 | 28854356 | |
539 | Phosphorylation | ESSESSQTIDDNDSE CCCCCCCCCCCCCCC | 28.46 | 19530675 | |
545 | Phosphorylation | QTIDDNDSEKGGGQL CCCCCCCCCCCCCCC | 47.68 | 19530675 | |
557 | Phosphorylation | GQLKHENTVVRADGA CCCCCCCEEEECCCC | 19.86 | 30078680 | |
569 | Phosphorylation | DGATGIVSSSNSSTA CCCCEEEECCCCCCC | 26.57 | 30078680 | |
570 | Phosphorylation | GATGIVSSSNSSTAS CCCEEEECCCCCCCC | 23.73 | 18806794 | |
571 | Phosphorylation | ATGIVSSSNSSTASK CCEEEECCCCCCCCC | 32.97 | 19530675 | |
573 | Phosphorylation | GIVSSSNSSTASKSS EEEECCCCCCCCCCC | 30.89 | 19060867 | |
574 | Phosphorylation | IVSSSNSSTASKSSS EEECCCCCCCCCCCC | 32.04 | 19060867 | |
575 | Phosphorylation | VSSSNSSTASKSSST EECCCCCCCCCCCCC | 34.47 | 19060867 | |
579 | Phosphorylation | NSSTASKSSSTNLSA CCCCCCCCCCCCCCH | 27.33 | 30078680 | |
580 | Phosphorylation | SSTASKSSSTNLSAQ CCCCCCCCCCCCCHH | 44.94 | 30078680 | |
581 | Phosphorylation | STASKSSSTNLSAQK CCCCCCCCCCCCHHH | 28.53 | 30078680 | |
582 | Phosphorylation | TASKSSSTNLSAQKQ CCCCCCCCCCCHHHH | 41.97 | 30078680 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of KCC2D_CAEEL !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KCC2D_CAEEL !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of KCC2D_CAEEL !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
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Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Structure of the autoinhibited kinase domain of CaMKII and SAXSanalysis of the holoenzyme."; Rosenberg O.S., Deindl S., Sung R.J., Nairn A.C., Kuriyan J.; Cell 123:849-860(2005). Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-343 OF ISOFORM I, ENZYMEREGULATION, PHOSPHORYLATION AT THR-284, AND MUTAGENESIS OF ASP-134. |