KCC2D_CAEEL - dbPTM
KCC2D_CAEEL - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
8 (in isoform 15)Phosphorylation-12.8919530675
24 (in isoform 15)Phosphorylation-21.1128854356
277PhosphorylationCNRERVASAIHRQDT
CCHHHHHHHHHHHHH
25.5430078680
284PhosphorylationSAIHRQDTVDCLKKF
HHHHHHHHHHHHHHH
15.209851916
302PhosphorylationRKLKAAISAVKMVTR
HHHHHHHHHHHHHHH
23.4519530675
303 (in isoform 9)Phosphorylation-9.9919530675
303 (in isoform 7)Phosphorylation-9.9919530675
303 (in isoform 6)Phosphorylation-9.9919530675
303 (in isoform 4)Phosphorylation-9.9919530675
304 (in isoform 9)Phosphorylation-3.0719530675
304 (in isoform 7)Phosphorylation-3.0719530675
304 (in isoform 6)Phosphorylation-3.0719530675
304 (in isoform 4)Phosphorylation-3.0719530675
312 (in isoform 9)Phosphorylation-17.0918806794
312 (in isoform 7)Phosphorylation-17.0918806794
312 (in isoform 4)Phosphorylation-17.0918806794
328 (in isoform 9)Phosphorylation-34.0928854356
328 (in isoform 7)Phosphorylation-34.0928854356
328 (in isoform 4)Phosphorylation-34.0928854356
354 (in isoform 8)Phosphorylation-4.2018806794
354 (in isoform 5)Phosphorylation-4.2018806794
355 (in isoform 8)Phosphorylation-6.0119530675
355 (in isoform 5)Phosphorylation-6.0119530675
363 (in isoform 8)Phosphorylation-33.3428854356
363 (in isoform 5)Phosphorylation-33.3428854356
379 (in isoform 8)Phosphorylation-65.3728854356
379 (in isoform 5)Phosphorylation-65.3728854356
528PhosphorylationKKEQGPPSTIKESSE
CCCCCCCCCHHCCCC
45.9928854356
529PhosphorylationKEQGPPSTIKESSES
CCCCCCCCHHCCCCC
41.6719530675
533PhosphorylationPPSTIKESSESSQTI
CCCCHHCCCCCCCCC
34.1119060867
534PhosphorylationPSTIKESSESSQTID
CCCHHCCCCCCCCCC
42.4619060867
536PhosphorylationTIKESSESSQTIDDN
CHHCCCCCCCCCCCC
29.6928854356
537PhosphorylationIKESSESSQTIDDND
HHCCCCCCCCCCCCC
27.5628854356
539PhosphorylationESSESSQTIDDNDSE
CCCCCCCCCCCCCCC
28.4619530675
545PhosphorylationQTIDDNDSEKGGGQL
CCCCCCCCCCCCCCC
47.6819530675
557PhosphorylationGQLKHENTVVRADGA
CCCCCCCEEEECCCC
19.8630078680
569PhosphorylationDGATGIVSSSNSSTA
CCCCEEEECCCCCCC
26.5730078680
570PhosphorylationGATGIVSSSNSSTAS
CCCEEEECCCCCCCC
23.7318806794
571PhosphorylationATGIVSSSNSSTASK
CCEEEECCCCCCCCC
32.9719530675
573PhosphorylationGIVSSSNSSTASKSS
EEEECCCCCCCCCCC
30.8919060867
574PhosphorylationIVSSSNSSTASKSSS
EEECCCCCCCCCCCC
32.0419060867
575PhosphorylationVSSSNSSTASKSSST
EECCCCCCCCCCCCC
34.4719060867
579PhosphorylationNSSTASKSSSTNLSA
CCCCCCCCCCCCCCH
27.3330078680
580PhosphorylationSSTASKSSSTNLSAQ
CCCCCCCCCCCCCHH
44.9430078680
581PhosphorylationSTASKSSSTNLSAQK
CCCCCCCCCCCCHHH
28.5330078680
582PhosphorylationTASKSSSTNLSAQKQ
CCCCCCCCCCCHHHH
41.9730078680

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCC2D_CAEEL !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCC2D_CAEEL

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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