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Protein

Calcium/calmodulin-dependent protein kinase type II

Gene

unc-43

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.14 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Ca2+/calmodulin binding removes an autoinhibitory regulatory segment located C-terminal to the kinase domain. This releases the catalytic activity of the enzyme and makes accessible a regulatory residue Thr-284. Phosphorylation of Thr-284 by another kinase domain within the oligomeric holoenzyme keeps CaMKII active in the absence of Ca2+/calmodulin by preventing the rebinding of the regulatory segment to the kinase domain and by increasing the affinity of calmodulin for the enzyme. Can respond to high-frequency Ca2+ pulses to become Ca2+ independent.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411ATPPROSITE-ProRule annotation1 Publication
Active sitei134 – 1341Proton acceptorCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calmodulin-dependent protein kinase activity Source: WormBase
  • ion channel binding Source: WormBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • MAPK cascade Source: WormBase
  • medium-term memory Source: WormBase
  • peptidyl-serine phosphorylation Source: WormBase
  • peptidyl-threonine phosphorylation Source: WormBase
  • positive regulation of gene expression Source: UniProtKB
  • protein phosphorylation Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 1045.
SignaLinkiO62305.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type II1 Publication (EC:2.7.11.17)
Short name:
CaM kinase II1 Publication
Alternative name(s):
Uncoordinated protein 43
Gene namesi
Name:unc-43
ORF Names:K11E8.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiK11E8.1a; CE42693; WBGene00006779; unc-43.
K11E8.1b; CE28052; WBGene00006779; unc-43.
K11E8.1d; CE28054; WBGene00006779; unc-43.
K11E8.1e; CE28055; WBGene00006779; unc-43.
K11E8.1f; CE28056; WBGene00006779; unc-43.
K11E8.1g; CE28057; WBGene00006779; unc-43.
K11E8.1h; CE28058; WBGene00006779; unc-43.
K11E8.1i; CE28059; WBGene00006779; unc-43.
K11E8.1k; CE28060; WBGene00006779; unc-43.
K11E8.1l; CE28061; WBGene00006779; unc-43.
K11E8.1m; CE35590; WBGene00006779; unc-43.
K11E8.1n; CE40979; WBGene00006779; unc-43.
K11E8.1o; CE41430; WBGene00006779; unc-43.
K11E8.1p; CE42670; WBGene00006779; unc-43.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cell projectionaxon 1 Publication
  • Perikaryon 2 Publications

  • Note: 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. Localization is regulated by tir-1 (PubMed:15625192).2 Publications

GO - Cellular componenti

  • axon cytoplasm Source: WormBase
  • neuron projection Source: WormBase
  • perikaryon Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Increased frequency of defecation, typified by a weaker repetition of the defecation motor program, an echo, 10 s after the primary motor program. Abnormal spicule protraction. Lack of tph-1 transcriptional up-regulation during learned olfactory aversion to bacteria. Reduced brood size, body length and width. Lethargic movement. A gain-of function mutation reduces locomotory activity, alters excitation of three muscle types and lengthens the period of the motor output of a behavioral clock. Both classes of mutation inhibit neurotransmitter release.6 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411K → M: Loss of kinase activity. 1 Publication
Mutagenesisi97 – 971F → E: Loss of cooperative activation of adjacent holoenzyme subunits. 2 Publications
Mutagenesisi97 – 971F → K: Increase in calcium independent kinase activity, no effect on translocation to the neurite. 2 Publications
Mutagenesisi100 – 1001I → K: Loss of cooperative activation of adjacent holoenzyme subunits. 1 Publication
Mutagenesisi108 – 1081E → K in n498gf; slight increase in calcium independent kinase activity, no effect on translocation to the neurite. Nuclear translocation of daf-16 resulting in lifespan extension. 3 Publications
Mutagenesisi134 – 1341D → N: Loss of autoinhibition and increase in binding of Ca2+/calmodulin. 2 Publications
Mutagenesisi147 – 1471K → E: Slight increase in calcium independent kinase activity, no effect on translocation to the neurite. 1 Publication
Mutagenesisi170 – 1701G → E in sy574; abnormal spicule protraction; when associated with V-665. 1 Publication
Mutagenesisi179 – 1791S → L in e408; males display locomotor and muscle seizure defects and egg laying defects. 1 Publication
Mutagenesisi200 – 2001I → K: Loss of cooperative activation of adjacent holoenzyme subunits. 1 Publication
Mutagenesisi236 – 2361D → R: Increase in calcium independent kinase activity, loss of translocation to neurites and glr-1 trafficking. 1 Publication
Mutagenesisi278 – 2792AI → DD: Decrease in binding of Ca2+/calmodulin. 1 Publication
Mutagenesisi280 – 2801H → K: Increase in calcium independent kinase activity, no effect on translocation to the neurite. 1 Publication
Mutagenesisi281 – 2811R → E: Increase in calcium independent kinase activity and translocation to an unlocalized pool in the neurite. Small decrease in glr-1 trafficking. 1 Publication
Mutagenesisi284 – 2841T → D: Constitutively activate kinase activity, increase in translocation to the neurites. 1 Publication
Mutagenesisi665 – 6651A → V in sy574; abnormal spicule protraction; when associated with E-170. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720Calcium/calmodulin-dependent protein kinase type IIPRO_0000396645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei284 – 2841Phosphothreonine; by autocatalysis1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO62305.
PRIDEiO62305.

PTM databases

iPTMnetiO62305.

Expressioni

Tissue specificityi

Expressed in the nervous system. Observed in the ADF and AWC neurons. Position in AWC neurons is regulated by microtubules. Localized to clusters in ventral cord neurites which appear to be required for glr-1 trafficking. Also present in oocytes.4 Publications

Interactioni

Subunit structurei

Dodecamer. Subunits are tightly packed around a central ring-shaped scaffold with extensive contacts between the regulatory segment of one kinase and the catalytic domain of another enabling cooperative activation of a subunit by the adjacent molecule (PubMed:16441656, PubMed:20139983). Interacts with and phosphorylates daf-16; the interaction promotes daf-16 nuclear localization. Interacts with egl-2 and tir-1 (PubMed:15625192, PubMed:21145946). Interacts with nsy-1 (PubMed:11336672).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
syx-4P914093EBI-313095,EBI-326499

GO - Molecular functioni

  • ion channel binding Source: WormBase

Protein-protein interaction databases

BioGridi43023. 8 interactions.
DIPiDIP-25971N.
DIP-58986N.
IntActiO62305. 8 interactions.
MINTiMINT-115321.

Structurei

Secondary structure

1
720
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 115Combined sources
Beta strandi12 – 2110Combined sources
Beta strandi24 – 318Combined sources
Turni32 – 343Combined sources
Beta strandi37 – 448Combined sources
Helixi45 – 473Combined sources
Helixi50 – 6516Combined sources
Beta strandi74 – 796Combined sources
Beta strandi81 – 888Combined sources
Helixi96 – 1038Combined sources
Helixi108 – 12720Combined sources
Helixi137 – 1393Combined sources
Beta strandi140 – 1467Combined sources
Beta strandi151 – 1533Combined sources
Helixi175 – 1773Combined sources
Helixi180 – 1834Combined sources
Helixi191 – 20616Combined sources
Helixi216 – 22510Combined sources
Turni232 – 2376Combined sources
Helixi240 – 24910Combined sources
Turni254 – 2563Combined sources
Helixi260 – 2634Combined sources
Helixi267 – 2704Combined sources
Helixi275 – 2773Combined sources
Helixi282 – 31029Combined sources
Helixi544 – 5474Combined sources
Helixi586 – 60419Combined sources
Helixi607 – 6137Combined sources
Beta strandi614 – 6218Combined sources
Helixi623 – 6253Combined sources
Helixi634 – 6374Combined sources
Beta strandi640 – 6423Combined sources
Beta strandi649 – 66012Combined sources
Turni661 – 6633Combined sources
Beta strandi664 – 67613Combined sources
Beta strandi682 – 69615Combined sources
Beta strandi699 – 70810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BDWX-ray1.80A/B1-543[»]
2F86X-ray2.64B/D/F/H/J/L/N540-720[»]
3KK8X-ray1.72A5-288[»]
3KK9X-ray3.21A6-287[»]
3KL8X-ray3.37A/C/E/G/I5-273[»]
ProteinModelPortaliO62305.
SMRiO62305. Positions 5-354, 586-709.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO62305.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 269258Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiO62305.
PhylomeDBiO62305.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR032710. NTF2-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 2 hits.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (15)i

Sequence statusi: Complete.

This entry describes 15 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform c1 Publication (identifier: O62305-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MMNASTKFSD NYDVKEELGK GAFSVVRRCV HKTTGLEFAA KIINTKKLSA
60 70 80 90 100
RDFQKLEREA RICRKLQHPN IVRLHDSIQE ESFHYLVFDL VTGGELFEDI
110 120 130 140 150
VAREFYSEAD ASHCIQQILE SIAYCHSNGI VHRDLKPENL LLASKAKGAA
160 170 180 190 200
VKLADFGLAI EVNDSEAWHG FAGTPGYLSP EVLKKDPYSK PVDIWACGVI
210 220 230 240 250
LYILLVGYPP FWDEDQHRLY AQIKAGAYDY PSPEWDTVTP EAKSLIDSML
260 270 280 290 300
TVNPKKRITA DQALKVPWIC NRERVASAIH RQDTVDCLKK FNARRKLKAA
310 320 330 340 350
ISAVKMVTRM SGVLRTSDST GSVASNGSTT HDASQVAGTS SQPTSPAAEV
360 370 380 390 400
YPNVLLFNPQ KFPRNCVHPF TTHPYYSPKE SSKKKLFFTL LFEVCPHTSR
410 420 430 440 450
SHILLRDNTK NIYHPYHCFT NKMSNYERAA PSSHGSSTTK KIANAIADLV
460 470 480 490 500
IRRSSPSIRR KTEADVHNSN RNRKVSAPAN LQHALVPVID VVVATGALAS
510 520 530 540 550
SSVDNLSAST SSDLGRNLLN KKEQGPPSTI KESSESSQTI DDNDSEKGGG
560 570 580 590 600
QLKHENTVVR ADGATGIVSS SNSSTASKSS STNLSAQKQD IVRVTQTLLD
610 620 630 640 650
AISCKDFETY TRLCDTSMTC FEPEALGNLI EGIEFHRFYF DGNRKNQVHT
660 670 680 690 700
TMLNPNVHII GEDAACVAYV KLTQFLDRNG EAHTRQSQES RVWSKKQGRW
710 720
VCVHVHRSTQ PSTNTTVSEF
Note: No experimental confirmation available.Curated
Length:720
Mass (Da):79,927
Last modified:October 1, 2001 - v2
Checksum:i3231366FFF81A695
GO
Isoform a1 Publication (identifier: O62305-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-490: Missing.
     491-515: VVVATGALASSSVDNLSASTSSDLG → MKNIEYWQVLLNKIFATYKIKMKQC

Note: No experimental confirmation available.Curated
Show »
Length:230
Mass (Da):25,873
Checksum:i2EAD0E576BA0619A
GO
Isoform b1 Publication (identifier: O62305-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-138: HCIQQILESIAYCHSNGIVHRDLKPE → CCIMQILDGVNYCHQRGIVHRDMKV
     139-720: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:137
Mass (Da):15,801
Checksum:iDDF4E2AD6FC2A6F4
GO
Isoform d2 Publications (identifier: O62305-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     299-314: AAISAVKMVTRMSGVL → GAILTTMIATRNLSNL
     315-514: Missing.
     548-585: Missing.

Show »
Length:482
Mass (Da):54,589
Checksum:i3870201C3162C253
GO
Isoform e2 Publications (identifier: O62305-5) [UniParc]FASTAAdd to basket

Also known as: C1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     350-364: VYPNVLLFNPQKFPR → GAILTTMIATRNLSN
     365-513: Missing.
     548-585: Missing.

Show »
Length:533
Mass (Da):59,537
Checksum:i0D8EF2D999E0B8AA
GO
Isoform f2 Publications (identifier: O62305-6) [UniParc]FASTAAdd to basket

Also known as: E1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     299-313: AAISAVKMVTRMSGV → GAILTTMIATRNLSS
     314-515: Missing.

Show »
Length:518
Mass (Da):58,067
Checksum:i14DA5EB06D2DAFF3
GO
Isoform g2 Publications (identifier: O62305-7) [UniParc]FASTAAdd to basket

Also known as: B1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     299-314: AAISAVKMVTRMSGVL → GAILTTMIATRNLSNL
     315-514: Missing.

Show »
Length:520
Mass (Da):58,264
Checksum:i7D20BF318483E085
GO
Isoform h2 Publications (identifier: O62305-8) [UniParc]FASTAAdd to basket

Also known as: D1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     350-364: VYPNVLLFNPQKFPR → GAILTTMIATRNLSN
     365-513: Missing.

Show »
Length:571
Mass (Da):63,212
Checksum:i20C754B5BFE86D01
GO
Isoform i2 Publications (identifier: O62305-9) [UniParc]FASTAAdd to basket

Also known as: H1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     299-314: AAISAVKMVTRMSGVL → GAILTTMIATRNLSNL
     315-514: Missing.
     549-550: GG → NE
     551-720: Missing.

Show »
Length:350
Mass (Da):39,384
Checksum:iE300DB75FE74E9BC
GO
Isoform k2 Publications (identifier: O62305-10) [UniParc]FASTAAdd to basket

Also known as: F1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     299-302: AAIS → VVDS
     303-720: Missing.

Show »
Length:302
Mass (Da):34,198
Checksum:i5BCA124A7458DD9F
GO
Isoform l2 Publications (identifier: O62305-11) [UniParc]FASTAAdd to basket

Also known as: G1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     299-302: AAIS → VAIC
     303-720: Missing.

Show »
Length:302
Mass (Da):34,184
Checksum:i40C0FD5A7458DD9F
GO
Isoform m1 Publication (identifier: O62305-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-414: Missing.
     415-512: PYHCFTNKMS...VDNLSASTSS → MDGLLARLKL...KPEKLEVEAD

Note: No experimental confirmation available.Curated
Show »
Length:309
Mass (Da):34,103
Checksum:i13A93D058438BA8A
GO
Isoform n1 Publication (identifier: O62305-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-505: Missing.
     506-515: LSASTSSDLG → MNFLRFSGKC

Note: No experimental confirmation available.Curated
Show »
Length:215
Mass (Da):23,941
Checksum:i392E9298ABF7375D
GO
Isoform o1 Publication (identifier: O62305-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-416: Missing.
     417-514: HCFTNKMSNY...NLSASTSSDL → MDGLLARLKL...KPEKLEVEAD
     548-585: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:269
Mass (Da):30,200
Checksum:iD1B879B53DE0A973
GO
Isoform p1 Publication (identifier: O62305-15) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-504: Missing.
     505-513: NLSASTSSD → MIATRNLSN

Note: No experimental confirmation available.Curated
Show »
Length:216
Mass (Da):23,927
Checksum:i592578E5DE7DC6B4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 505505Missing in isoform n. 1 PublicationVSP_039590Add
BLAST
Alternative sequencei1 – 504504Missing in isoform p. 1 PublicationVSP_039591Add
BLAST
Alternative sequencei1 – 490490Missing in isoform a. 1 PublicationVSP_039592Add
BLAST
Alternative sequencei1 – 416416Missing in isoform o. 1 PublicationVSP_039593Add
BLAST
Alternative sequencei1 – 414414Missing in isoform m. 1 PublicationVSP_039594Add
BLAST
Alternative sequencei113 – 13826HCIQQ…DLKPE → CCIMQILDGVNYCHQRGIVH RDMKV in isoform b. 1 PublicationVSP_039595Add
BLAST
Alternative sequencei139 – 720582Missing in isoform b. 1 PublicationVSP_039596Add
BLAST
Alternative sequencei299 – 31416AAISA…MSGVL → GAILTTMIATRNLSNL in isoform d, isoform g and isoform i. 3 PublicationsVSP_039597Add
BLAST
Alternative sequencei299 – 31315AAISA…RMSGV → GAILTTMIATRNLSS in isoform f. 2 PublicationsVSP_039598Add
BLAST
Alternative sequencei299 – 3024AAIS → VVDS in isoform k. 2 PublicationsVSP_039599
Alternative sequencei299 – 3024AAIS → VAIC in isoform l. 2 PublicationsVSP_039600
Alternative sequencei303 – 720418Missing in isoform k and isoform l. 2 PublicationsVSP_039601Add
BLAST
Alternative sequencei314 – 515202Missing in isoform f. 2 PublicationsVSP_039602Add
BLAST
Alternative sequencei315 – 514200Missing in isoform d, isoform g and isoform i. 3 PublicationsVSP_039603Add
BLAST
Alternative sequencei350 – 36415VYPNV…QKFPR → GAILTTMIATRNLSN in isoform e and isoform h. 3 PublicationsVSP_039604Add
BLAST
Alternative sequencei365 – 513149Missing in isoform e and isoform h. 3 PublicationsVSP_039605Add
BLAST
Alternative sequencei415 – 51298PYHCF…ASTSS → MDGLLARLKLGSKRKKKTSS SVKRSSRPESARQAPRDTTG SLYSNLTASSSTVSACSAPE IVVLKKEQVVLAVDHKDQVD EQKKKNEQVVKKPEKLEVEA D in isoform m. 1 PublicationVSP_039606Add
BLAST
Alternative sequencei417 – 51498HCFTN…TSSDL → MDGLLARLKLGSKRKKKTSS SVKRSSRPESARQAPRDTTG SLYSNLTASSSTVSACSAPE IVVLKKEQVVLAVDHKDQVD EQKKKNEQVVKKPEKLEVEA D in isoform o. 1 PublicationVSP_039607Add
BLAST
Alternative sequencei491 – 51525VVVAT…SSDLG → MKNIEYWQVLLNKIFATYKI KMKQC in isoform a. 1 PublicationVSP_039608Add
BLAST
Alternative sequencei505 – 5139NLSASTSSD → MIATRNLSN in isoform p. 1 PublicationVSP_039609
Alternative sequencei506 – 51510LSASTSSDLG → MNFLRFSGKC in isoform n. 1 PublicationVSP_039610
Alternative sequencei548 – 58538Missing in isoform d, isoform e and isoform o. 3 PublicationsVSP_039611Add
BLAST
Alternative sequencei549 – 5502GG → NE in isoform i. 2 PublicationsVSP_039612
Alternative sequencei551 – 720170Missing in isoform i. 2 PublicationsVSP_039613Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180735 mRNA. Translation: AAD53949.1.
AF233262 mRNA. Translation: AAF63320.1.
AF233263 mRNA. Translation: AAF63321.1.
AF233264 mRNA. Translation: AAF63322.1.
AF233265 mRNA. Translation: AAF63323.1.
AF233266 mRNA. Translation: AAF63324.1.
AF233267 mRNA. Translation: AAF63325.1.
AF255956 mRNA. Translation: AAF71543.1.
Z70279 Genomic DNA. Translation: CAA94242.3.
Z70279, AL023841 Genomic DNA. Translation: CAA94243.3.
Z70279, AL023841 Genomic DNA. Translation: CAC42322.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42323.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42324.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42325.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42326.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42327.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42328.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42329.1.
Z70279 Genomic DNA. Translation: CAE46679.1.
Z70279 Genomic DNA. Translation: CAN86910.1.
Z70279 Genomic DNA. Translation: CAO82047.1.
Z70279 Genomic DNA. Translation: CAQ58116.1.
PIRiB88809.
T23616.
RefSeqiNP_001023293.2. NM_001028122.4. [O62305-2]
NP_001023294.1. NM_001028123.3. [O62305-3]
NP_001023296.1. NM_001028125.3. [O62305-4]
NP_001023297.1. NM_001028126.3. [O62305-5]
NP_001023298.1. NM_001028127.3. [O62305-6]
NP_001023299.1. NM_001028128.3. [O62305-7]
NP_001023300.1. NM_001028129.3. [O62305-8]
NP_001023301.1. NM_001028130.3. [O62305-9]
NP_001023302.1. NM_001028131.3. [O62305-10]
NP_001023303.1. NM_001028132.3. [O62305-11]
NP_001023304.1. NM_001028133.4. [O62305-12]
NP_001122788.1. NM_001129316.2. [O62305-13]
NP_001122789.1. NM_001129317.2. [O62305-14]
NP_001129863.1. NM_001136391.2. [O62305-15]
UniGeneiCel.22903.

Genome annotation databases

GeneIDi177921.
UCSCiK11E8.1a.1. c. elegans.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180735 mRNA. Translation: AAD53949.1.
AF233262 mRNA. Translation: AAF63320.1.
AF233263 mRNA. Translation: AAF63321.1.
AF233264 mRNA. Translation: AAF63322.1.
AF233265 mRNA. Translation: AAF63323.1.
AF233266 mRNA. Translation: AAF63324.1.
AF233267 mRNA. Translation: AAF63325.1.
AF255956 mRNA. Translation: AAF71543.1.
Z70279 Genomic DNA. Translation: CAA94242.3.
Z70279, AL023841 Genomic DNA. Translation: CAA94243.3.
Z70279, AL023841 Genomic DNA. Translation: CAC42322.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42323.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42324.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42325.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42326.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42327.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42328.1.
Z70279, AL023841 Genomic DNA. Translation: CAC42329.1.
Z70279 Genomic DNA. Translation: CAE46679.1.
Z70279 Genomic DNA. Translation: CAN86910.1.
Z70279 Genomic DNA. Translation: CAO82047.1.
Z70279 Genomic DNA. Translation: CAQ58116.1.
PIRiB88809.
T23616.
RefSeqiNP_001023293.2. NM_001028122.4. [O62305-2]
NP_001023294.1. NM_001028123.3. [O62305-3]
NP_001023296.1. NM_001028125.3. [O62305-4]
NP_001023297.1. NM_001028126.3. [O62305-5]
NP_001023298.1. NM_001028127.3. [O62305-6]
NP_001023299.1. NM_001028128.3. [O62305-7]
NP_001023300.1. NM_001028129.3. [O62305-8]
NP_001023301.1. NM_001028130.3. [O62305-9]
NP_001023302.1. NM_001028131.3. [O62305-10]
NP_001023303.1. NM_001028132.3. [O62305-11]
NP_001023304.1. NM_001028133.4. [O62305-12]
NP_001122788.1. NM_001129316.2. [O62305-13]
NP_001122789.1. NM_001129317.2. [O62305-14]
NP_001129863.1. NM_001136391.2. [O62305-15]
UniGeneiCel.22903.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BDWX-ray1.80A/B1-543[»]
2F86X-ray2.64B/D/F/H/J/L/N540-720[»]
3KK8X-ray1.72A5-288[»]
3KK9X-ray3.21A6-287[»]
3KL8X-ray3.37A/C/E/G/I5-273[»]
ProteinModelPortaliO62305.
SMRiO62305. Positions 5-354, 586-709.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi43023. 8 interactions.
DIPiDIP-25971N.
DIP-58986N.
IntActiO62305. 8 interactions.
MINTiMINT-115321.

PTM databases

iPTMnetiO62305.

Proteomic databases

EPDiO62305.
PRIDEiO62305.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi177921.
UCSCiK11E8.1a.1. c. elegans.

Organism-specific databases

CTDi177921.
WormBaseiK11E8.1a; CE42693; WBGene00006779; unc-43.
K11E8.1b; CE28052; WBGene00006779; unc-43.
K11E8.1d; CE28054; WBGene00006779; unc-43.
K11E8.1e; CE28055; WBGene00006779; unc-43.
K11E8.1f; CE28056; WBGene00006779; unc-43.
K11E8.1g; CE28057; WBGene00006779; unc-43.
K11E8.1h; CE28058; WBGene00006779; unc-43.
K11E8.1i; CE28059; WBGene00006779; unc-43.
K11E8.1k; CE28060; WBGene00006779; unc-43.
K11E8.1l; CE28061; WBGene00006779; unc-43.
K11E8.1m; CE35590; WBGene00006779; unc-43.
K11E8.1n; CE40979; WBGene00006779; unc-43.
K11E8.1o; CE41430; WBGene00006779; unc-43.
K11E8.1p; CE42670; WBGene00006779; unc-43.

Phylogenomic databases

InParanoidiO62305.
PhylomeDBiO62305.

Enzyme and pathway databases

BRENDAi2.7.11.17. 1045.
SignaLinkiO62305.

Miscellaneous databases

EvolutionaryTraceiO62305.
PROiO62305.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR032710. NTF2-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 2 hits.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Diverse behavioural defects caused by mutations in Caenorhabditis elegans unc-43 CaM kinase II."
    Reiner D.J., Newton E.M., Tian H., Thomas J.H.
    Nature 402:199-203(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-108.
  2. "Biochemical properties of calcium/calmodulin-pependent protein kinase II (UNC-43) Isoforms in Caernohabditis elegans."
    Guarin E., Hernandez M.C., Gomez M., Schulman H., Nef P.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS E; F; G; H; I; K AND L).
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: Bristol N2Imported.
  4. "Lateral signaling mediated by axon contact and calcium entry regulates asymmetric odorant receptor expression in C. elegans."
    Troemel E.R., Sagasti A., Bargmann C.I.
    Cell 99:387-398(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The CaMKII UNC-43 activates the MAPKKK NSY-1 to execute a lateral signaling decision required for asymmetric olfactory neuron fates."
    Sagasti A., Hisamoto N., Hyodo J., Tanaka-Hino M., Matsumoto K., Bargmann C.I.
    Cell 105:221-232(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NSY-1.
  6. "Calcineurin, a calcium/calmodulin-dependent protein phosphatase, is involved in movement, fertility, egg laying, and growth in Caenorhabditis elegans."
    Bandyopadhyay J., Lee J., Lee J., Lee J.I., Yu J.R., Jee C., Cho J.H., Jung S., Lee M.H., Zannoni S., Singson A., Kim D.H., Koo H.S., Ahnn J.
    Mol. Biol. Cell 13:3281-3293(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Caenorhabditis elegans OSR-1 regulates behavioral and physiological responses to hyperosmotic environments."
    Solomon A., Bandhakavi S., Jabbar S., Shah R., Beitel G.J., Morimoto R.I.
    Genetics 167:161-170(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Eph and NMDA receptors control Ca2+/calmodulin-dependent protein kinase II activation during C. elegans oocyte meiotic maturation."
    Corrigan C., Subramanian R., Miller M.A.
    Development 132:5225-5237(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "A Toll-interleukin 1 repeat protein at the synapse specifies asymmetric odorant receptor expression via ASK1 MAPKKK signaling."
    Chuang C.-F., Bargmann C.I.
    Genes Dev. 19:270-281(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIR-1, SUBCELLULAR LOCATION.
  10. "The role of regulatory domain interactions in UNC-43 CaMKII localization and trafficking."
    Umemura T., Rapp P., Rongo C.
    J. Cell Sci. 118:3327-3338(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PHE-97; GLU-108; LYS-147; ASP-236; HIS-280; ARG-281 AND THR-284.
  11. "Presynaptic Ca2+/calmodulin-dependent protein kinase II modulates neurotransmitter release by activating BK channels at Caenorhabditis elegans neuromuscular junction."
    Liu Q., Chen B., Ge Q., Wang Z.W.
    J. Neurosci. 27:10404-10413(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. "Food deprivation attenuates seizures through CaMKII and EAG K+ channels."
    LeBoeuf B., Gruninger T.R., Garcia L.R.
    PLoS Genet. 3:1622-1632(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-170; SER-179 AND ALA-665.
  13. "Intestinal Ca2+ wave dynamics in freely moving C. elegans coordinate execution of a rhythmic motor program."
    Nehrke K., Denton J., Mowrey W.
    Am. J. Physiol. 294:C333-344(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  14. "Microtubule-based localization of a synaptic calcium-signaling complex is required for left-right neuronal asymmetry in C. elegans."
    Chang C., Hsieh Y.W., Lesch B.J., Bargmann C.I., Chuang C.F.
    Development 138:3509-3518(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "The effects of transient starvation persist through direct interactions between CaMKII and ether-a-go-go K+ channels in C. elegans males."
    LeBoeuf B., Guo X., Garcia L.R.
    Neuroscience 175:1-17(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EGL-2.
  16. "D1 dopamine receptor signaling is modulated by the R7 RGS protein EAT-16 and the R7 binding protein RSBP-1 in Caenoerhabditis elegans motor neurons."
    Wani K.A., Catanese M., Normantowicz R., Herd M., Maher K.N., Chase D.L.
    PLoS ONE 7:E37831-E37831(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "CAMKII and Calcineurin regulate the lifespan of Caenorhabditis elegans through the FOXO transcription factor DAF-16."
    Tao L., Xie Q., Ding Y.H., Li S.T., Peng S., Zhang Y.P., Tan D., Yuan Z., Dong M.Q.
    Elife 2:E00518-E00518(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-108.
  18. "A neuronal signaling pathway of CaMKII and Gqalpha regulates experience-dependent transcription of tph-1."
    Qin Y., Zhang X., Zhang Y.
    J. Neurosci. 33:925-935(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  19. "The Caenorhabditis elegans voltage-gated calcium channel subunits UNC-2 and UNC-36 and the calcium-dependent kinase UNC-43/CaMKII regulate neuromuscular junction morphology."
    Caylor R.C., Jin Y., Ackley B.D.
    Neural Dev. 8:10-10(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme."
    Rosenberg O.S., Deindl S., Sung R.J., Nairn A.C., Kuriyan J.
    Cell 123:849-860(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-343 OF ISOFORM I, ENZYME REGULATION, PHOSPHORYLATION AT THR-284, MUTAGENESIS OF ASP-134.
  21. "Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II."
    Rosenberg O.S., Deindl S., Comolli L.R., Hoelz A., Downing K.H., Nairn A.C., Kuriyan J.
    FEBS J. 273:682-694(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 340-482 OF ISOFORM D, SUBUNIT.
  22. "Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation."
    Chao L.H., Pellicena P., Deindl S., Barclay L.A., Schulman H., Kuriyan J.
    Nat. Struct. Mol. Biol. 17:264-272(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 5-288 OF ISOFORM E, INTERACTION WITH CALMODULIN, ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF LYS-41; PHE-97; ILE-100; ASP-134; ILE-200 AND 278-ALA-ILE-279.

Entry informationi

Entry nameiKCC2D_CAEEL
AccessioniPrimary (citable) accession number: O62305
Secondary accession number(s): A5JYT0
, A7LPH2, B3GWC8, O62304, Q21431, Q7JLT8, Q9NG91, Q9NH55, Q9NH56, Q9NH57, Q9NH58, Q9NH59, Q9NH60, Q9U6Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: October 1, 2001
Last modified: June 8, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.