CSKP_MOUSE
ID CSKP_MOUSE Reviewed; 926 AA.
AC O70589; A2ADP8; A2ADP9; A2ADQ4; O70588; Q3UW92;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Peripheral plasma membrane protein CASK {ECO:0000305};
DE EC=2.7.11.1;
DE AltName: Full=Calcium/calmodulin-dependent serine protein kinase;
GN Name=Cask {ECO:0000312|MGI:MGI:1309489};
GN Synonyms=Lin-2 {ECO:0000303|PubMed:10846156};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=9787075; DOI=10.1006/geno.1998.5479;
RA Laverty H.G., Wilson J.B.;
RT "Murine CASK is disrupted in a sex-linked cleft palate mouse mutant.";
RL Genomics 53:29-41(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-926 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, AND INTERACTION WITH TBR1.
RX PubMed=10749215; DOI=10.1038/35005118;
RA Hsueh Y.P., Wang T.F., Yang F.C., Sheng M.;
RT "Nuclear translocation and transcription regulation by the membrane-
RT associated guanylate kinase CASK/LIN-2.";
RL Nature 404:298-302(2000).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN COMPLEX WITH APBA1 AND LIN7.
RX PubMed=10846156; DOI=10.1126/science.288.5472.1796;
RA Setou M., Nakagawa T., Seog D.-H., Hirokawa N.;
RT "Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-
RT containing vesicle transport.";
RL Science 288:1796-1802(2000).
RN [6]
RP INTERACTION WITH TSPYL2, AND IDENTIFICATION IN COMPLEX WITH TSPYL2 AND
RP TBR1.
RC STRAIN=C57BL/6J;
RX PubMed=15066269; DOI=10.1016/s0896-6273(04)00139-4;
RA Wang G.-S., Hong C.-J., Yen T.-Y., Huang H.-Y., Ou Y., Huang T.-N.,
RA Jung W.-G., Kuo T.-Y., Sheng M., Wang T.-F., Hsueh Y.-P.;
RT "Transcriptional modification by a CASK-interacting nucleosome assembly
RT protein.";
RL Neuron 42:113-128(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-570 AND SER-571 (ISOFORM 3), AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH DLG1 AND LIN7B.
RX PubMed=22337881; DOI=10.1074/jbc.m111.321216;
RA Zhang J., Yang X., Wang Z., Zhou H., Xie X., Shen Y., Long J.;
RT "Structure of an L27 domain heterotrimer from cell polarity complex
RT Patj/Pals1/Mals2 reveals mutually independent L27 domain assembly mode.";
RL J. Biol. Chem. 287:11132-11140(2012).
RN [9]
RP INTERACTION WITH NRXN1.
RX PubMed=25385611; DOI=10.1073/pnas.1416515111;
RA Li Y., Wei Z., Yan Y., Wan Q., Du Q., Zhang M.;
RT "Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem
RT reveals a highly specific assembly mechanism for the apical Crumbs
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:17444-17449(2014).
RN [10]
RP STRUCTURE BY NMR OF 405-454, AND INTERACTION WITH LIN7B.
RX PubMed=15863617; DOI=10.1073/pnas.0409346102;
RA Feng W., Long J.-F., Zhang M.;
RT "A unified assembly mode revealed by the structures of tetrameric L27
RT domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005).
CC -!- FUNCTION: Multidomain scaffolding Mg(2+)-independent protein kinase
CC that catalyzes the phosphotransfer from ATP to proteins such as NRXN1,
CC and plays a role in synaptic transmembrane protein anchoring and ion
CC channel trafficking (By similarity). Contributes to neural development
CC and regulation of gene expression via interaction with the
CC transcription factor TBR1. Binds to cell-surface proteins, including
CC amyloid precursor protein, neurexins, and syndecans. May mediate a link
CC between the extracellular matrix and the actin cytoskeleton via its
CC interaction with syndecan and with the actin/spectrin-binding protein
CC 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with
CC the motor protein KIF17 to transport vesicles containing N-methyl-D-
CC aspartate (NMDA) receptor subunit NR2B along microtubules
CC (PubMed:10846156). {ECO:0000250|UniProtKB:O14936,
CC ECO:0000269|PubMed:10749215, ECO:0000269|PubMed:10846156}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:O14936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:O14936};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Note=Unlike other protein kinases, does not require a divalent cation
CC such as magnesium for catalytic activity. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Differs from archetypal CaMK members in that the
CC kinase domain exhibits a constitutively active conformation and the
CC autoinhibitory region does not engage in direct contact with the ATP-
CC binding cleft, although it still binds Ca(2+)/CAM. {ECO:0000250}.
CC -!- SUBUNIT: CASK and LIN7 form a tripartite complex with CASKIN1 (By
CC similarity). Component of the brain-specific heterotrimeric complex
CC (LIN-10-LIN-2-LIN-7 complex) composed of at least APBA1, CASK, and
CC LIN7, which associates with the motor protein KIF17 to transport
CC vesicles along microtubules (PubMed:10846156). Forms a heterotrimeric
CC complex with DLG1 and LIN7B via their L27 domains (PubMed:22337881,
CC PubMed:15863617). Identified in a complex with ACTN4, IQGAP1, MAGI2,
CC NPHS1, SPTAN1 and SPTBN1 (By similarity). Part of a complex containing
CC CASK, TBR1 and TSPYL2 (PubMed:10749215, PubMed:15066269). Interacts
CC with WHRN (By similarity). Interacts (via the PDZ, SH3 and guanylate
CC kinase-like domains) with NRXN1 (via C-terminus) (PubMed:25385611).
CC Interacts with CASKIN1, APBA1, LIN7(A/B/C), and L27 domain of DLG1 and
CC isoform 2 of DLG4 (By similarity). Interacts with FCHSD2 (By
CC similarity). Interacts with KIRREL3 (By similarity). Interacts with
CC TBR1 (By similarity). Interacts with TSPYL2 (PubMed:15066269).
CC {ECO:0000250|UniProtKB:O14936, ECO:0000250|UniProtKB:Q62915,
CC ECO:0000269|PubMed:10749215, ECO:0000269|PubMed:10846156,
CC ECO:0000269|PubMed:15066269, ECO:0000269|PubMed:15863617,
CC ECO:0000269|PubMed:22337881, ECO:0000269|PubMed:25385611}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62915}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q62915}. Cell membrane
CC {ECO:0000250|UniProtKB:Q62915}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q62915}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=CASK-B;
CC IsoId=O70589-1; Sequence=Displayed;
CC Name=2; Synonyms=CASK-A;
CC IsoId=O70589-2; Sequence=VSP_003152, VSP_003153;
CC Name=3;
CC IsoId=O70589-3; Sequence=VSP_024614, VSP_024615;
CC Name=4;
CC IsoId=O70589-4; Sequence=VSP_024614, VSP_024616;
CC Name=5;
CC IsoId=O70589-5; Sequence=VSP_024614;
CC -!- DOMAIN: The first L27 domain binds DLG1 and the second L27 domain
CC probably binds LIN7. {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain mediates the interaction with FCHSD2.
CC {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; Y17138; CAA76647.1; -; mRNA.
DR EMBL; Y17137; CAA76646.1; -; mRNA.
DR EMBL; AL671117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK136523; BAE23024.1; -; mRNA.
DR CCDS; CCDS40878.1; -. [O70589-3]
DR CCDS; CCDS72343.1; -. [O70589-5]
DR RefSeq; NP_001271432.1; NM_001284503.1. [O70589-1]
DR RefSeq; NP_001271433.1; NM_001284504.1.
DR RefSeq; NP_001271434.1; NM_001284505.1. [O70589-5]
DR RefSeq; NP_033936.2; NM_009806.3. [O70589-3]
DR PDB; 1Y74; NMR; -; B/D=405-454.
DR PDB; 6Y9O; X-ray; 1.63 A; C=915-926.
DR PDBsum; 1Y74; -.
DR PDBsum; 6Y9O; -.
DR AlphaFoldDB; O70589; -.
DR SMR; O70589; -.
DR BioGRID; 198491; 34.
DR CORUM; O70589; -.
DR ELM; O70589; -.
DR IntAct; O70589; 20.
DR MINT; O70589; -.
DR STRING; 10090.ENSMUSP00000033321; -.
DR iPTMnet; O70589; -.
DR PhosphoSitePlus; O70589; -.
DR SwissPalm; O70589; -.
DR jPOST; O70589; -.
DR MaxQB; O70589; -.
DR PaxDb; O70589; -.
DR PeptideAtlas; O70589; -.
DR PRIDE; O70589; -.
DR ProteomicsDB; 284181; -. [O70589-1]
DR ProteomicsDB; 284182; -. [O70589-2]
DR ProteomicsDB; 284183; -. [O70589-3]
DR ProteomicsDB; 285208; -. [O70589-4]
DR ProteomicsDB; 285209; -. [O70589-5]
DR ABCD; O70589; 1 sequenced antibody.
DR Antibodypedia; 4529; 309 antibodies from 39 providers.
DR DNASU; 12361; -.
DR Ensembl; ENSMUST00000033321; ENSMUSP00000033321; ENSMUSG00000031012. [O70589-4]
DR Ensembl; ENSMUST00000115436; ENSMUSP00000111096; ENSMUSG00000031012. [O70589-3]
DR Ensembl; ENSMUST00000115438; ENSMUSP00000111098; ENSMUSG00000031012. [O70589-5]
DR GeneID; 12361; -.
DR KEGG; mmu:12361; -.
DR UCSC; uc009srp.2; mouse. [O70589-3]
DR UCSC; uc009srq.2; mouse. [O70589-1]
DR UCSC; uc012hez.2; mouse. [O70589-5]
DR CTD; 8573; -.
DR MGI; MGI:1309489; Cask.
DR VEuPathDB; HostDB:ENSMUSG00000031012; -.
DR eggNOG; KOG0033; Eukaryota.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000155600; -.
DR InParanoid; O70589; -.
DR OMA; RQAYGHY; -.
DR OrthoDB; 95102at2759; -.
DR PhylomeDB; O70589; -.
DR TreeFam; TF314263; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 12361; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Cask; mouse.
DR EvolutionaryTrace; O70589; -.
DR PRO; PR:O70589; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O70589; protein.
DR Bgee; ENSMUSG00000031012; Expressed in cortical plate and 257 other tissues.
DR ExpressionAtlas; O70589; baseline and differential.
DR Genevisible; O70589; MM.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; IDA:CACAO.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:BHF-UCL.
DR GO; GO:0060170; C:ciliary membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005652; C:nuclear lamina; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098846; C:podocyte foot; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042043; F:neurexin family protein binding; IDA:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0070509; P:calcium ion import; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0090288; P:negative regulation of cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:MGI.
DR GO; GO:0061045; P:negative regulation of wound healing; ISO:MGI.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IDA:MGI.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR CDD; cd12081; SH3_CASK; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR035473; CASK_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell membrane; Cytoplasm; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; SH3 domain; Transferase.
FT CHAIN 1..926
FT /note="Peripheral plasma membrane protein CASK"
FT /id="PRO_0000094569"
FT DOMAIN 12..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 343..398
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 402..455
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 490..571
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 612..682
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 739..911
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 305..315
FT /note="Calmodulin-binding"
FT REGION 482..909
FT /note="Required for interaction with NRXN1 (via C-terminal
FT tail)"
FT /evidence="ECO:0000250|UniProtKB:Q62915"
FT REGION 574..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /evidence="ECO:0000250"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14936"
FT MOD_RES 151
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14936"
FT MOD_RES 155
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14936"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14936"
FT VAR_SEQ 340..345
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024614"
FT VAR_SEQ 580..664
FT /note="RDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLI
FT PCKEAGIRFRVGDIIQIISKDDHNWWQGKLENS -> VISLTSLSYPNLPISSEFLTNF
FT LLMAECFCFLGNCFCCAVTTLHTNFTTKITEQKEVPPTSSALLACRYLQPFCSKIKAKY
FT RKLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9787075"
FT /id="VSP_003152"
FT VAR_SEQ 580..602
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024615"
FT VAR_SEQ 603..614
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_024616"
FT VAR_SEQ 665..926
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9787075"
FT /id="VSP_003153"
FT CONFLICT 298
FT /note="F -> L (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="N -> K (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT CONFLICT 677..679
FT /note="LQE -> IQG (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT CONFLICT 720..723
FT /note="FDQL -> LII (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="L -> S (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="Y -> C (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="Q -> R (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="Y -> F (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT CONFLICT 821..823
FT /note="ETI -> DH (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="A -> P (in Ref. 1; CAA76646/CAA76647)"
FT /evidence="ECO:0000305"
FT HELIX 406..417
FT /evidence="ECO:0007829|PDB:1Y74"
FT HELIX 423..433
FT /evidence="ECO:0007829|PDB:1Y74"
FT HELIX 435..452
FT /evidence="ECO:0007829|PDB:1Y74"
FT STRAND 922..925
FT /evidence="ECO:0007829|PDB:6Y9O"
FT MOD_RES O70589-3:570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES O70589-3:571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 926 AA; 105109 MW; ADD2008CE53E0018 CRC64;
MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK
REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH
YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV
GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR
QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA
RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL
TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP
ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGDM
DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN
GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS
VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS KDDHNWWQGK
LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW FGKKKKQYKD KYLAKHNAVF
DQLDLVTYEE VVKLPAFKRK TLVLLGAHGV GRRHIKNTLI TKHPDRFAYP IPHTTRPPKK
DEENGKNYYF VSHDQMMQDI SNNEYLEYGS HEDAMYGTKL ETIRKIHEQG LIAILDVEPQ
ALKVLRTAEF APFVVFIAAP TITPGLNEDE SLQRLQKESD VLQRTYAHYF DLTIINNEID
ETIRHLEEAV ELVCTAPQWV PVSWVY
