ID Q5JS79_HUMAN Unreviewed; 927 AA. AC Q5JS79; A6NFC6; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 3. DT 27-MAR-2024, entry version 130. DE SubName: Full=Calcium/calmodulin dependent serine protein kinase {ECO:0000313|Ensembl:ENSP00000367410.4}; GN Name=CASK {ECO:0000313|Ensembl:ENSP00000367410.4}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000367410.4, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000367410.4, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [2] {ECO:0000313|Ensembl:ENSP00000367410.4} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SIMILARITY: Belongs to the MAGUK family. CC {ECO:0000256|ARBA:ARBA00007014}. 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; AL158144; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445239; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL603754; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL627402; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF459071; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF459072; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; Q5JS79; -. DR SMR; Q5JS79; -. DR MassIVE; Q5JS79; -. DR PeptideAtlas; Q5JS79; -. DR ProteomicsDB; 63138; -. DR Antibodypedia; 4529; 342 antibodies from 39 providers. DR Ensembl; ENST00000378168.8; ENSP00000367410.4; ENSG00000147044.23. DR UCSC; uc064yqr.1; human. DR HGNC; HGNC:1497; CASK. DR VEuPathDB; HostDB:ENSG00000147044; -. DR GeneTree; ENSGT00940000155600; -. DR HOGENOM; CLU_001715_5_1_1; -. DR ChiTaRS; CASK; human. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000147044; Expressed in buccal mucosa cell and 211 other cell types or tissues. DR ExpressionAtlas; Q5JS79; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. 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. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:Q5JS79, KW ECO:0007829|MaxQB:Q5JS79}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}. FT DOMAIN 12..282 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 349..404 FT /note="L27" FT /evidence="ECO:0000259|PROSITE:PS51022" FT DOMAIN 408..461 FT /note="L27" FT /evidence="ECO:0000259|PROSITE:PS51022" FT DOMAIN 496..577 FT /note="PDZ" FT /evidence="ECO:0000259|PROSITE:PS50106" FT DOMAIN 618..688 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT DOMAIN 740..912 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000259|PROSITE:PS50052" FT REGION 580..616 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 927 AA; 105247 MW; 07A8E69C33540154 CRC64; MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEGKR WISNLKREAS ICHMLKHPHI VELLETYSSD GMLYMVFEFM DGADLCFEIV KRADAGFVYS EAVASHYMRQ ILEALRYCHD NNIIHRDVKP HCVLLASKEN SAPVKLGGFG VAIQLGESGL VAGGRVGTPH FMAPEVVKRE PYGKPVDVWG CGVILFILLS GCLPFYGTKE RLFEGIIKGK YKMNPRQWSH ISESAKDLVR RMLMLDPAER ITVYEALNHP WLKERDRYAY KIHLPETVEQ LRKFNARRKL KGAVLAAVSS HKFNSFYGDP PEELPDFSED PTSSGLLAAE RAVSQVLDSL EEIHALTDCS EKDLDFLHSV FQDQHLHTLL DLYDKINTKS SPQIRNPPSD AVQRAKEVLE EISCYPENND AKELKRILTQ PHFMALLQTH DVVAHEVYSD EALRVTPPPT SPYLNGDSPE SANGDMDMEN VTRVRLVQFQ KNTDEPMGIT LKMNELNHCI VARIMHGGMI HRQGTLHVGD EIREINGISV ANQTVEQLQK MLREMRGSIT FKIVPSYRTQ SSSCERDSPS TSRQSPANGH SSTNNSVSDL PSTTQPKGRQ IYVRAQFEYD PAKDDLIPCK EAGIRFRVGD IIQIISKDDH NWWQGKLENS KNGTAGLIPS PELQEWRVAC IAMEKTKQEQ QASCTWFGKK KKQYKDKYLA KHNADLVTYE EVVKLPAFKR KTLVLLGAHG VGRRHIKNTL ITKHPDRFAY PIPHTTRPPK KDEENGKNYY FVSHDQMMQD ISNNEYLEYG SHEDAMYGTK LETIRKIHEQ GLIAILDVEP QALKVLRTAE FAPFVVFIAA PTITPGLNED ESLQRLQKES DILQRTYAHY FDLTIINNEI DETIRHLEEA VELVCTAPQW VPVSWVY //