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Q24210 (CSKP_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peripheral plasma membrane protein CASK

Short name=dCASK
EC=2.7.11.17
Alternative name(s):
Calcium/calmodulin-dependent protein kinase
Short name=CAKI
Short name=Camguk
Gene names
Name:CASK
Synonyms:Caki, cmg
ORF Names:CG6703
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length898 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides. Functionally modulates eag potassium channels; increases eag current and whole-cell conductance. Also regulates autophosphorylation of CaMKII. Ref.7 Ref.8 Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with eag. Interacts with CaMKII. Ref.7 Ref.8

Subcellular location

Cell membrane; Peripheral membrane protein. Note: Eag recruits CASK to the plasma membrane. Ref.8

Tissue specificity

During embryogenesis, larval and pupal life, found almost exclusively in the central nervous system. In the adult head found in the lamina, the neuropil of the medulla, lobula, lobula plate and in the central brain. Ref.2

Disruption phenotype

Increases synapse-specific, activity-dependent autophosphorylation of CaMKII Thr-287. Ref.9

Sequence similarities

In the N-terminal section; belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 2 L27 domains.

Contains 1 PDZ (DHR) domain.

Contains 1 protein kinase domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAM11269.1 differs from that shown. Reason: Probable cloning artifact.

The sequence AAO39536.1 differs from that shown. Reason: Frameshift at position 114.

The sequence CAA63940.1 differs from that shown. Reason: Frameshift at positions 537 and 667.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH3 domain
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from mutant phenotype PubMed 21059886. Source: FlyBase

adult walking behavior

Inferred from mutant phenotype Ref.2. Source: FlyBase

anesthesia-resistant memory

Inferred from mutant phenotype PubMed 23543616. Source: FlyBase

border follicle cell migration

Inferred from mutant phenotype PubMed 23173089. Source: FlyBase

cell adhesion

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

establishment or maintenance of cell polarity

Non-traceable author statement PubMed 12766944. Source: FlyBase

lateral inhibition

Inferred from mutant phenotype PubMed 19363474. Source: FlyBase

locomotion

Inferred from mutant phenotype PubMed 19379781. Source: BHF-UCL

long-term memory

Inferred from mutant phenotype PubMed 23543616. Source: FlyBase

male courtship behavior

Inferred from mutant phenotype PubMed 21059886. Source: FlyBase

medium-term memory

Inferred from mutant phenotype PubMed 23543616. Source: FlyBase

neuromuscular synaptic transmission

Inferred from mutant phenotype PubMed 19379781. Source: BHF-UCL

neurotransmitter secretion

Non-traceable author statement PubMed 10798391. Source: FlyBase

positive regulation of synaptic vesicle endocytosis

Inferred from mutant phenotype PubMed 19379781. Source: FlyBase

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

regulation of cell shape

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

regulation of locomotion

Inferred from mutant phenotype PubMed 19379781. Source: FlyBase

regulation of neuromuscular synaptic transmission

Inferred from mutant phenotype PubMed 19379781. Source: FlyBase

regulation of neurotransmitter secretion

Inferred from direct assay PubMed 15872064. Source: FlyBase

regulation of synaptic growth at neuromuscular junction

Inferred from mutant phenotype PubMed 24062638. Source: FlyBase

regulation of terminal button organization

Inferred from mutant phenotype PubMed 19379781. Source: BHF-UCL

synaptic vesicle docking involved in exocytosis

Non-traceable author statement PubMed 10798391. Source: FlyBase

synaptic vesicle endocytosis

Inferred from mutant phenotype PubMed 19379781. Source: BHF-UCL

synaptic vesicle targeting

Non-traceable author statement PubMed 10798391. Source: FlyBase

   Cellular_componentcalcium- and calmodulin-dependent protein kinase complex

Inferred from sequence or structural similarity Ref.2. Source: FlyBase

neuromuscular junction

Inferred from direct assay PubMed 19379781. Source: BHF-UCL

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

type I terminal bouton

Inferred from direct assay PubMed 19379781. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin-dependent protein kinase activity

Inferred from direct assay Ref.2. Source: FlyBase

neurexin family protein binding

Inferred from physical interaction PubMed 19379781. Source: BHF-UCL

protein serine/threonine kinase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CaMKIIQ001685EBI-214423,EBI-124595
eagQ0228010EBI-214423,EBI-85304

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: Q24210-3)

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.
Isoform A (identifier: Q24210-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-317: Missing.
     318-443: MDPLYATDAD...LMRLLAAPHM → MCQHHGLTSQ...VPNGSICSGH
     584-584: E → ELFRIRPAPVL
Note: No experimental confirmation available.
Isoform G (identifier: Q24210-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-317: Missing.
     318-443: MDPLYATDAD...LMRLLAAPHM → MCQHHGLTSQ...VPNGSICSGH
     584-584: E → ELFRIRPAPVL
     663-663: Q → QGEPGAGCSAHADGCDGSA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 898898Peripheral plasma membrane protein CASK
PRO_0000094571

Regions

Domain12 – 278267Protein kinase
Domain343 – 39755L27 1
Domain402 – 46160L27 2
Domain495 – 57682PDZ
Domain582 – 65170SH3
Domain711 – 883173Guanylate kinase-like
Nucleotide binding18 – 269ATP By similarity
Region306 – 31611Calmodulin-binding

Sites

Active site1411 By similarity
Binding site411ATP By similarity

Amino acid modifications

Modified residue2921Phosphothreonine; by autocatalysis By similarity

Natural variations

Alternative sequence1 – 317317Missing in isoform A and isoform G.
VSP_008088
Alternative sequence318 – 443126MDPLY…AAPHM → MCQHHGLTSQSLMSGGSHIS LLGSSGSSGMSGSGVGSSGQ SVPQCPAAVAAADAAMMGSN AGGHCRSLSGLSSISIPPPP PALFNPCSSALSLQQAAVTR WGPRTSCPVHSPFRVRVPNG SICSGH in isoform A and isoform G.
VSP_008089
Alternative sequence5841E → ELFRIRPAPVL in isoform A and isoform G.
VSP_008090
Alternative sequence6631Q → QGEPGAGCSAHADGCDGSA in isoform G.
VSP_041854

Experimental info

Sequence conflict71L → V in AAC80169. Ref.1
Sequence conflict1361D → E in AAC80169. Ref.1
Sequence conflict4631L → A in AAC80169. Ref.1
Sequence conflict465 – 47713VTPPP…YLNGD → HPAPDGALPQWR in AAC80169. Ref.1
Sequence conflict4971Q → H in AAC80169. Ref.1
Sequence conflict5231I → L in AAC80169. Ref.1
Sequence conflict6321D → G in AAC80169. Ref.1
Sequence conflict7401A → V in AAC80169. Ref.1
Sequence conflict7591S → N in AAO39554. Ref.5
Sequence conflict886 – 8927HTTPQWV → DIPPRSGC in CAA63940. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified August 22, 2003. Version 4.
Checksum: 5B16014EC66E0E9B

FASTA898100,911
        10         20         30         40         50         60 
MTEDEILFDD VYELCEVIGK GPFSIVRRCI HRESNQQFAV KIVDVAKFTA SPGLSTADLK 

        70         80         90        100        110        120 
REATICHMLK HPHIVELLET YSSEGMLYMV FEFMEGSDLC FEVVRRAVAG FVYSEAVACH 

       130        140        150        160        170        180 
YMRQILEALR YCHENDILHR DVRPACALLA TVDNSAPVKL GGFGSAIQLP GTRETIETHG 

       190        200        210        220        230        240 
RVGCPHYMAP EVVTRRLYGK GCDVWGAGVM LHVLLSGRLP FLGSGVRLQQ SVARGRLSFE 

       250        260        270        280        290        300 
APEWKSISAN AKDLVMKMLA ANPHHRLSIT EVLDHPWIRD RDKLQRTHLA DTVEELKRYN 

       310        320        330        340        350        360 
ARRKLKGAVQ AIAGGTNMDP LYATDADMPI TGATDEWADE EAGIEAVQRI LDCLDDIYSL 

       370        380        390        400        410        420 
QDAHVDADVL RDMLRDNRLH QFLQLFDRIA ATVVTSNGRA PAAEAVGRCR DVLEQLSSTS 

       430        440        450        460        470        480 
GGNSLGGKYA KEELMRLLAA PHMQALLHSH DVVARDVYGE EALRVTPPPM VPYLNGDELD 

       490        500        510        520        530        540 
NVEGGELQHV TRVRLVQFQK NTDEPMGITL KMTEDGRCIV ARIMHGGMIH RQATLHVGDE 

       550        560        570        580        590        600 
IREINGQPVQ HQSVGQLQRM LREARGSVTF KIVPSYRSAP PPCEIFVRAQ FDYNPLDDEL 

       610        620        630        640        650        660 
IPCAQAGISF QVGDILQIIS KDDHHWWQAR LDTVGGSAGL IPSPELQEWR IACQTVDKTK 

       670        680        690        700        710        720 
QEQVNCSIFG RKKKQCRDKY LAKHNAIFDT LDVVTYEEVV KVPVGDPNFQ RKTLVLLGAH 

       730        740        750        760        770        780 
GVGRRHIKNT LISKYPDKYA YPIPHTTRPA KPEEENGRSY YFVSHDEMMA DIGANEYLEY 

       790        800        810        820        830        840 
GTHEDAMYGT KLDTIRRIHT EGKMAILDVE PQALKILRTA EFTPYVVFIA APSLQNIADY 

       850        860        870        880        890 
DGSLERLAKE SEMLRQLYGH FFDLTIVNND ISETIATLET AIDRVHTTPQ WVPVSWLY 

« Hide

Isoform A [UniParc].

Checksum: 645638C40343145C
Show »

FASTA59165,197
Isoform G [UniParc].

Checksum: 7F0A65E1DD31AD9D
Show »

FASTA60966,741

References

« Hide 'large scale' references
[1]"Camguk, Lin-2, and CASK: novel membrane-associated guanylate kinase homologs that also contain CaM kinase domains."
Dimitratos S.D., Woods D.F., Bryant P.J.
Mech. Dev. 63:127-130(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Strain: Oregon-R.
[2]"A new Drosophila Ca2+/calmodulin-dependent protein kinase (Caki) is localized in the central nervous system and implicated in walking speed."
Martin J.-R., Ollo R.
EMBO J. 15:1865-1876(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), TISSUE SPECIFICITY.
Tissue: Embryo.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
Strain: Berkeley.
Tissue: Embryo and Head.
[6]Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Strain: Berkeley.
Tissue: Embryo and Head.
[7]"Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-dependent autophosphorylation."
Lu C.S., Hodge J.J., Mehren J., Sun X.X., Griffith L.C.
Neuron 40:1185-1197(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CAMKII.
[8]"Camguk/CASK enhances Ether-a-go-go potassium current by a phosphorylation-dependent mechanism."
Marble D.D., Hegle A.P., Snyder E.D. II, Dimitratos S., Bryant P.J., Wilson G.F.
J. Neurosci. 25:4898-4907(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EAG, SUBCELLULAR LOCATION.
[9]"Activity-dependent gating of CaMKII autonomous activity by Drosophila CASK."
Hodge J.J., Mullasseril P., Griffith L.C.
Neuron 51:327-337(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U53190 mRNA. Translation: AAC80169.1.
X94264 mRNA. Translation: CAA63940.1. Frameshift.
AE014297 Genomic DNA. Translation: AAF55920.3.
AE014297 Genomic DNA. Translation: AAF55921.2.
AE014297 Genomic DNA. Translation: AAF55922.2.
AY094916 mRNA. Translation: AAM11269.1. Sequence problems.
BT003532 mRNA. Translation: AAO39536.1. Frameshift.
BT003550 mRNA. Translation: AAO39554.1.
BT046172 mRNA. Translation: ACI49771.1.
PIRS69210.
RefSeqNP_001097862.1. NM_001104392.3.
NP_524441.2. NM_079717.4.
NP_732661.1. NM_169970.2.
NP_732662.2. NM_169971.3.
UniGeneDm.7404.

3D structure databases

ProteinModelPortalQ24210.
SMRQ24210. Positions 5-462, 492-577, 586-893.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67530. 10 interactions.
DIPDIP-19769N.
IntActQ24210. 6 interactions.
STRING7227.FBpp0083559.

Protein family/group databases

TCDB9.B.106.3.2. the pock size-determining protein (psdp) family.

Proteomic databases

PaxDbQ24210.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0084161; FBpp0083559; FBgn0013759. [Q24210-3]
GeneID42567.
KEGGdme:Dmel_CG6703.

Organism-specific databases

CTD8573.
FlyBaseFBgn0013759. CASK.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00560000077048.
InParanoidQ24210.
KOK06103.
OMAHEYLEYG.
OrthoDBEOG79CXZ5.
PhylomeDBQ24210.

Enzyme and pathway databases

BRENDA2.7.11.17. 1994.
SignaLinkQ24210.

Gene expression databases

BgeeQ24210.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR011009. Kinase-like_dom.
IPR004172. L27.
IPR014775. L27_C.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00220. S_TKc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS51022. L27. 2 hits.
PS50106. PDZ. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi42567.
NextBio829455.
PROQ24210.

Entry information

Entry nameCSKP_DROME
AccessionPrimary (citable) accession number: Q24210
Secondary accession number(s): B5X553 expand/collapse secondary AC list , Q24272, Q86P03, Q86P17, Q8SX09, Q9VD77, Q9VD78, Q9VD79
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 22, 2003
Last modified: April 16, 2014
This is version 151 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase