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 27-MAR-2024, entry version 212. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 ComplexPortal; CPX-7741; LIN-10-LIN-2-LIN-7 complex, LIN7A variant. DR ComplexPortal; CPX-7742; LIN-10-LIN-2-LIN-7 complex, LIN7C variant. DR ComplexPortal; CPX-884; LIN-10-LIN-2-LIN-7 complex, LIN7B variant. DR CORUM; O70589; -. DR ELM; O70589; -. DR IntAct; O70589; 20. DR MINT; O70589; -. DR STRING; 10090.ENSMUSP00000111098; -. DR iPTMnet; O70589; -. DR PhosphoSitePlus; O70589; -. DR SwissPalm; O70589; -. DR jPOST; O70589; -. DR MaxQB; O70589; -. DR PaxDb; 10090-ENSMUSP00000033321; -. DR PeptideAtlas; 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 Pumba; O70589; -. DR ABCD; O70589; 1 sequenced antibody. DR Antibodypedia; 4529; 342 antibodies from 39 providers. DR DNASU; 12361; -. DR Ensembl; ENSMUST00000033321.11; ENSMUSP00000033321.5; ENSMUSG00000031012.18. [O70589-4] DR Ensembl; ENSMUST00000115436.9; ENSMUSP00000111096.3; ENSMUSG00000031012.18. [O70589-3] DR Ensembl; ENSMUST00000115438.10; ENSMUSP00000111098.4; ENSMUSG00000031012.18. [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 AGR; MGI:1309489; -. 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; STKWASF; -. DR OrthoDB; 2873706at2759; -. 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 82 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 261 other cell types or tissues. DR ExpressionAtlas; O70589; baseline and differential. 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: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; IBA:GO_Central. DR GO; GO:0098846; C:podocyte foot; 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:0005080; F:protein kinase C 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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:0072659; P:protein localization to plasma membrane; ISO:MGI. 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; cd00071; GMPK; 1. DR CDD; cd00992; PDZ_signaling; 1. DR CDD; cd12081; SH3_CASK; 1. DR CDD; cd14094; STKc_CASK; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 6.10.140.620; -; 1. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR Gene3D; 1.10.287.650; L27 domain; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1. DR PANTHER; PTHR23122:SF40; PERIPHERAL PLASMA MEMBRANE PROTEIN CASK; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF02828; L27; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF07653; SH3_2; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00569; L27; 2. DR SMART; SM00228; PDZ; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF101288; L27 domain; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF50044; SH3-domain; 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. DR Genevisible; O70589; MM. 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 //