Q24210 (CSKP_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	898 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat SH3 domain
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult walking behavior Inferred from mutant phenotype Ref.2. 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 male courtship behavior Inferred from mutant phenotype PubMed 21059886. Source: FlyBase neuromuscular synaptic transmission Inferred from mutant phenotype PubMed 19379781. Source: BHF-UCL regulation of cell shape Inferred from mutant phenotype PubMed 14527345. Source: FlyBase regulation of neurotransmitter secretion Inferred from direct assay PubMed 15872064. 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_component	calcium- 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_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Inferred from direct assay Ref.2. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CaMKII	Q00168	5	EBI-214423,EBI-124595
eag	Q02280	10	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 898	898	Peripheral plasma membrane protein CASK		PRO_0000094571
Regions
	Domain	12 – 278	267	Protein kinase
	Domain	343 – 397	55	L27 1
	Domain	402 – 461	60	L27 2
	Domain	495 – 576	82	PDZ
	Domain	582 – 651	70	SH3
	Domain	711 – 883	173	Guanylate kinase-like
	Nucleotide binding	18 – 26	9	ATP By similarity
	Region	306 – 316	11	Calmodulin-binding
Sites
	Active site	141	1	By similarity
	Binding site	41	1	ATP By similarity
Amino acid modifications
	Modified residue	292	1	Phosphothreonine; by autocatalysis By similarity
Natural variations
	Alternative sequence	1 – 317	317	Missing in isoform A and isoform G.		VSP_008088
	Alternative sequence	318 – 443	126	MDPLY…AAPHM → MCQHHGLTSQSLMSGGSHIS LLGSSGSSGMSGSGVGSSGQ SVPQCPAAVAAADAAMMGSN AGGHCRSLSGLSSISIPPPP PALFNPCSSALSLQQAAVTR WGPRTSCPVHSPFRVRVPNG SICSGH in isoform A and isoform G.		VSP_008089
	Alternative sequence	584	1	E → ELFRIRPAPVL in isoform A and isoform G.		VSP_008090
	Alternative sequence	663	1	Q → QGEPGAGCSAHADGCDGSA in isoform G.		VSP_041854
Experimental info
	Sequence conflict	7	1	L → V in AAC80169. Ref.1
	Sequence conflict	136	1	D → E in AAC80169. Ref.1
	Sequence conflict	463	1	L → A in AAC80169. Ref.1
	Sequence conflict	465 – 477	13	VTPPP…YLNGD → HPAPDGALPQWR in AAC80169. Ref.1
	Sequence conflict	497	1	Q → H in AAC80169. Ref.1
	Sequence conflict	523	1	I → L in AAC80169. Ref.1
	Sequence conflict	632	1	D → G in AAC80169. Ref.1
	Sequence conflict	740	1	A → V in AAC80169. Ref.1
	Sequence conflict	759	1	S → N in AAO39554. Ref.5
	Sequence conflict	886 – 892	7	HTTPQWV → DIPPRSGC in CAA63940. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified August 22, 2003. Version 4. Checksum: 5B16014EC66E0E9B	FASTA	898	100,911
	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
	Isoform A [UniParc]. Checksum: 645638C40343145C	FASTA	591	65,197
	10 20 30 40 50 60 MCQHHGLTSQ SLMSGGSHIS LLGSSGSSGM SGSGVGSSGQ SVPQCPAAVA AADAAMMGSN 70 80 90 100 110 120 AGGHCRSLSG LSSISIPPPP PALFNPCSSA LSLQQAAVTR WGPRTSCPVH SPFRVRVPNG 130 140 150 160 170 180 SICSGHQALL HSHDVVARDV YGEEALRVTP PPMVPYLNGD ELDNVEGGEL QHVTRVRLVQ 190 200 210 220 230 240 FQKNTDEPMG ITLKMTEDGR CIVARIMHGG MIHRQATLHV GDEIREINGQ PVQHQSVGQL 250 260 270 280 290 300 QRMLREARGS VTFKIVPSYR SAPPPCELFR IRPAPVLIFV RAQFDYNPLD DELIPCAQAG 310 320 330 340 350 360 ISFQVGDILQ IISKDDHHWW QARLDTVGGS AGLIPSPELQ EWRIACQTVD KTKQEQVNCS 370 380 390 400 410 420 IFGRKKKQCR DKYLAKHNAI FDTLDVVTYE EVVKVPVGDP NFQRKTLVLL GAHGVGRRHI 430 440 450 460 470 480 KNTLISKYPD KYAYPIPHTT RPAKPEEENG RSYYFVSHDE MMADIGANEY LEYGTHEDAM 490 500 510 520 530 540 YGTKLDTIRR IHTEGKMAIL DVEPQALKIL RTAEFTPYVV FIAAPSLQNI ADYDGSLERL 550 560 570 580 590 AKESEMLRQL YGHFFDLTIV NNDISETIAT LETAIDRVHT TPQWVPVSWL Y
	Isoform G [UniParc]. Checksum: 7F0A65E1DD31AD9D	FASTA	609	66,741
	10 20 30 40 50 60 MCQHHGLTSQ SLMSGGSHIS LLGSSGSSGM SGSGVGSSGQ SVPQCPAAVA AADAAMMGSN 70 80 90 100 110 120 AGGHCRSLSG LSSISIPPPP PALFNPCSSA LSLQQAAVTR WGPRTSCPVH SPFRVRVPNG 130 140 150 160 170 180 SICSGHQALL HSHDVVARDV YGEEALRVTP PPMVPYLNGD ELDNVEGGEL QHVTRVRLVQ 190 200 210 220 230 240 FQKNTDEPMG ITLKMTEDGR CIVARIMHGG MIHRQATLHV GDEIREINGQ PVQHQSVGQL 250 260 270 280 290 300 QRMLREARGS VTFKIVPSYR SAPPPCELFR IRPAPVLIFV RAQFDYNPLD DELIPCAQAG 310 320 330 340 350 360 ISFQVGDILQ IISKDDHHWW QARLDTVGGS AGLIPSPELQ EWRIACQTVD KTKQEQGEPG 370 380 390 400 410 420 AGCSAHADGC DGSAVNCSIF GRKKKQCRDK YLAKHNAIFD TLDVVTYEEV VKVPVGDPNF 430 440 450 460 470 480 QRKTLVLLGA HGVGRRHIKN TLISKYPDKY AYPIPHTTRP AKPEEENGRS YYFVSHDEMM 490 500 510 520 530 540 ADIGANEYLE YGTHEDAMYG TKLDTIRRIH TEGKMAILDV EPQALKILRT AEFTPYVVFI 550 560 570 580 590 600 AAPSLQNIAD YDGSLERLAK ESEMLRQLYG HFFDLTIVNN DISETIATLE TAIDRVHTTP QWVPVSWLY

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
PIR	S69210.
RefSeq	NP_001097862.1. NM_001104392.3. NP_524441.2. NM_079717.4. NP_732661.1. NM_169970.2. NP_732662.2. NM_169971.3.
UniGene	Dm.7404.
3D structure databases
ProteinModelPortal	Q24210.
SMR	Q24210. Positions 6-390, 403-462, 492-577, 586-893.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-19769N.
IntAct	Q24210. 6 interactions.
STRING	7227.FBpp0083559.
Proteomic databases
PaxDb	Q24210.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0084161; FBpp0083559; FBgn0013759.
GeneID	42567.
KEGG	dme:Dmel_CG6703.
Organism-specific databases
CTD	8573.
FlyBase	FBgn0013759. CASK.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00560000077048.
InParanoid	Q24210.
KO	K06103.
OMA	HEYLEYG.
OrthoDB	EOG4Q2BWF.
PhylomeDB	Q24210.
Enzyme and pathway databases
BRENDA	2.7.11.17. 1994.
SignaLink	Q24210.
Gene expression databases
Bgee	Q24210.
GermOnline	CG6703. Drosophila melanogaster.
Family and domain databases
InterPro	IPR008144. Guanylate_kin. IPR008145. Guanylate_kin/L-typ_Ca_channel. IPR020590. Guanylate_kinase_CS. IPR011009. Kinase-like_dom. IPR004172. L27. IPR014775. L27_C. IPR027417. P-loop_NTPase. IPR001478. PDZ. IPR000719. Prot_kinase_cat_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR011511. SH3_2. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00625. Guanylate_kin. 1 hit. PF02828. L27. 2 hits. PF00595. PDZ. 1 hit. PF00069. Pkinase. 1 hit. PF07653. SH3_2. 1 hit. [Graphical view]
SMART	SM00072. GuKc. 1 hit. SM00569. L27. 2 hits. SM00228. PDZ. 1 hit. SM00220. S_TKc. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50156. PDZ. 1 hit. SSF50044. SH3. 1 hit. SSF52540. SSF52540. 1 hit.
PROSITE	PS00856. GUANYLATE_KINASE_1. 1 hit. PS50052. GUANYLATE_KINASE_2. 1 hit. PS51022. L27. 2 hits. PS50106. PDZ. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	42567.
NextBio	829455.

Entry information

Entry name

CSKP_DROME

Accession

Primary (citable) accession number: Q24210
Secondary accession number(s): B5X553 , 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:	May 29, 2013
This is version 141 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project